|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-5149 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 8562.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12316 1 MNAEDSLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEG 160
Cdd:PRK12316 81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 161 PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
Cdd:PRK12316 161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 241 EYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVG 320
Cdd:PRK12316 241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 321 VPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYN 400
Cdd:PRK12316 321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 401 HQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQA 480
Cdd:PRK12316 401 HQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 481 SVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA 560
Cdd:PRK12316 481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 561 DRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWL 638
Cdd:PRK12316 561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLgrKLPLAAGVQVLDLDRPAAWL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 639 ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:PRK12316 641 EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 719 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:PRK12316 721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 799 NLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP 878
Cdd:PRK12316 801 NLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 879 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGDW 958
Cdd:PRK12316 881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 959 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDD 1038
Cdd:PRK12316 961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDD 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1039 NFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAA-KAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQH 1117
Cdd:PRK12316 1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQH 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAE-QAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:PRK12316 1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAApQAGEVLWQRQAASEEELLALCEEAQRSLDL 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:PRK12316 1201 EQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARAEELDYW 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:PRK12316 1281 QAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGH 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1357 GREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNY 1436
Cdd:PRK12316 1361 GREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNY 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1437 LGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:PRK12316 1441 LGQFDRQFDEAALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHC 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1517 LDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQ 1595
Cdd:PRK12316 1521 CDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEaGDYINQLRVDVQGLDPDRFRAAWQ 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1596 ATLDAHEILRSGFLWKDGWPQPLQVVFEQatLELRLA--------PPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLAN 1667
Cdd:PRK12316 1601 ATVDRHEILRSGFLWQDGLEQPLQVIHKQ--VELPFAeldwrgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGE 1678
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1668 GRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQART 1747
Cdd:PRK12316 1679 GRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAART 1758
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1748 EQP--GQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINT 1825
Cdd:PRK12316 1759 EDGqvGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINT 1838
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1826 LPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSN 1904
Cdd:PRK12316 1839 LPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQgAPAGLVFGRVSN 1918
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1905 HEQTNYPLTLGVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEA 1984
Cdd:PRK12316 1919 HEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEA 1998
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1985 LPRG-GVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:PRK12316 1999 YPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGST 2142
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDTAPAVQLAGENLAYVIYTSGST 2158
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVT 2222
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT 2238
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2223 ILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQ--AVQAEAWFNAYGPTEAVITPLAWHCRAQEGGA--- 2297
Cdd:PRK12316 2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAweALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaay 2318
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2298 PAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVE 2377
Cdd:PRK12316 2319 VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVE 2398
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2378 YLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMrgEDLLAELRTWLAGRLPAYMQP 2457
Cdd:PRK12316 2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAA--EDLLAELRAWLAARLPAYMVP 2476
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2458 TAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSR 2537
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSR 2556
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2538 LRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK12316 2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGV 2636
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRL 2697
Cdd:PRK12316 2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRL 2716
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2698 LALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL 2777
Cdd:PRK12316 2717 LALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERL 2796
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2778 GAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN 2857
Cdd:PRK12316 2797 GGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN 2876
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2858 RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQ 2937
Cdd:PRK12316 2877 RAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA 2956
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2938 DAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 3017
Cdd:PRK12316 2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDA 3036
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3018 EERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMER 3097
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVER 3116
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3098 SIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwfEDYSEANPDIHL 3177
Cdd:PRK12316 3117 SLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD---ENYAEANPAIRT 3193
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 3257
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273
|
3290 3300 3310 3320 3330 3340 3350 3360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqagLYNLYGPTEAAIDV 3337
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITV 3350
|
3370 3380 3390 3400 3410 3420 3430 3440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGD 3417
Cdd:PRK12316 3351 THWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
|
3450 3460 3470 3480 3490 3500 3510 3520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASL 3510
|
3530 3540 3550 3560 3570 3580 3590 3600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVS 3576
Cdd:PRK12316 3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
|
3610 3620 3630 3640 3650 3660 3670 3680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3577 IQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREA 3656
Cdd:PRK12316 3591 LQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670
|
3690 3700 3710 3720 3730 3740 3750 3760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLV 3736
Cdd:PRK12316 3671 LDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLA 3750
|
3770 3780 3790 3800 3810 3820 3830 3840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3737 DMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLE 3816
Cdd:PRK12316 3751 TLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQ 3830
|
3850 3860 3870 3880 3890 3900 3910 3920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3817 GAPAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREEL 3896
Cdd:PRK12316 3831 GVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDL 3910
|
3930 3940 3950 3960 3970 3980 3990 4000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3897 FADIDLSRTVGWFTSLFPVRLSPVADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFD 3976
Cdd:PRK12316 3911 FADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFD 3990
|
4010 4020 4030 4040 4050 4060 4070 4080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3977 AQFD-EMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSP 4055
Cdd:PRK12316 3991 GSFDeEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAE 4070
|
4090 4100 4110 4120 4130 4140 4150 4160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4056 RHGATPSDFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALD 4135
Cdd:PRK12316 4071 RHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALD 4150
|
4170 4180 4190 4200 4210 4220 4230 4240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4136 RHAILRSGFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLI 4215
Cdd:PRK12316 4151 RHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLI 4230
|
4250 4260 4270 4280 4290 4300 4310 4320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4216 YTHHHILLDGWSNAQLLSEVLESYAGRSPEQPrDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTS 4295
Cdd:PRK12316 4231 YTNHHILMDGWSNSQLLGEVLERYSGRPPAQP-GGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRS 4309
|
4330 4340 4350 4360 4370 4380 4390 4400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4296 ANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPV 4375
Cdd:PRK12316 4310 ANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPV 4389
|
4410 4420 4430 4440 4450 4460 4470 4480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4376 VVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQ 4455
Cdd:PRK12316 4390 IATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQ 4469
|
4490 4500 4510 4520 4530 4540 4550 4560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4456 TNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPA 4535
Cdd:PRK12316 4470 TNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549
|
4570 4580 4590 4600 4610 4620 4630 4640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4536 TPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK12316 4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
|
4650 4660 4670 4680 4690 4700 4710 4720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMP 4695
Cdd:PRK12316 4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
|
4730 4740 4750 4760 4770 4780 4790 4800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4696 KGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGV 4775
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLV 4789
|
4810 4820 4830 4840 4850 4860 4870 4880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4776 FPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPI 4855
Cdd:PRK12316 4790 FPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPI 4869
|
4890 4900 4910 4920 4930 4940 4950 4960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
|
4970 4980 4990 5000 5010 5020 5030 5040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEY 5015
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEY 5029
|
5050 5060 5070 5080 5090 5100 5110 5120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5016 MVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQV 5095
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
|
5130 5140 5150 5160 5170
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 5096 TARMQSEVGVELPLAALFQTESLQAYAELAAAQTSSNDTDFDDLREFMSELEAI 5149
Cdd:PRK12316 5110 TSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLEELLSELEEI 5163
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1520-5126 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 4310.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1520 RHRGVTPSDFPLAglsqtqldelsldpdSVRDIY---PLSPMQQGMLF---HSLHGTEGDYVNQLRMDiGGLDPDRFRAA 1593
Cdd:PRK12467 29 QEEGVSFANLPIP---------------QVRSAFeriPLSYAQERQWFlwqLDPDSAAYNIPTALRLR-GELDVSALRRA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1594 WQATLDAHEILRSGFLWKDGwpQPLQVVFEQA--TLELRLAPPGSDPQRQA------EAEREAGFDPARAPLQRLVLVPL 1665
Cdd:PRK12467 93 FDALVARHESLRTRFVQDEE--GFRQVIDASLslTIPLDDLANEQGRARESqieayiNEEVARPFDLANGPLLRVRLLRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1666 ANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEV--AATVGRYRDYI----GWLQGRDAMATEFFWRDRLA-- 1733
Cdd:PRK12467 171 ADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSaysqGREPslPALPIQYADYAiwqrSWLEAGERERQLAYWQEQLGge 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1734 --SLEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAE 1811
Cdd:PRK12467 251 htVLELPTDRPRPAVPSYRGARLRVD-LPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1812 lpGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDI------QRWAGHggEALFDsiLVFENFP 1885
Cdd:PRK12467 330 --ETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLvealqpERSLSH--SPLFQ--VMFNHQN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1886 VAEALRQAPAD----LEFSTPSNHEQT-NYPLTLGVTLGER-LSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAA 1959
Cdd:PRK12467 404 TATGGRDREGAqlpgLTVEELSWARHTaQFDLALDTYESAQgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1960 LGELALLDAGERQEALRDWQAPLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA 2039
Cdd:PRK12467 484 LGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2040 LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA--WPA 2117
Cdd:PRK12467 564 LVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPAdlLCG 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2118 SADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGA 2197
Cdd:PRK12467 644 YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGA 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2198 RVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGEA--WDASLLTQQAVQAEAWFN 2274
Cdd:PRK12467 724 TLHLLPPDCaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-PQRALVCGGEAlqVDLLARVRALGPGARLIN 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 AYGPTEAVITPLAWHCR--AQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVAD 2352
Cdd:PRK12467 803 HYGPTETTVGVSTYELSdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2353 PFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLV--- 2429
Cdd:PRK12467 883 PFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaa 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2430 GRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEAL 2509
Cdd:PRK12467 963 VADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADV 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2510 LGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHA 2589
Cdd:PRK12467 1043 LKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYA 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2590 QQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLE--DCAG 2667
Cdd:PRK12467 1123 QERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPllLAAD 1202
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2668 ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLK 2747
Cdd:PRK12467 1203 KDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALP 1282
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2748 LQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPF 2827
Cdd:PRK12467 1283 IQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLF 1362
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2828 MLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFE 2907
Cdd:PRK12467 1363 MLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFE 1442
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2908 QLVDALQPERNLSHSPLFQVMYNHQSGERQD-AQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEART 2986
Cdd:PRK12467 1443 QLVEALQPERSLSHSPLFQVMFNHQRDDHQAqAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEAST 1522
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2987 VERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDY 3066
Cdd:PRK12467 1523 IERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTY 1602
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3067 AELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL- 3145
Cdd:PRK12467 1603 GELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLq 1682
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 -KLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV 3224
Cdd:PRK12467 1683 aRLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVV 1762
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3225 LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCS 3303
Cdd:PRK12467 1763 LQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQmDEQVEHPLSLRRVVCG 1842
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3304 GEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELY 3380
Cdd:PRK12467 1843 GEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCrrkDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELY 1922
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3381 LAGQGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 3459
Cdd:PRK12467 1923 LGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3460 REAAVLAVDG---RQLVGYVVLESES--------GDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:PRK12467 2003 REAVVIAQDGangKQLVAYVVPTDPGlvdddeaqVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3529 QAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQQTVQGLARV 3607
Cdd:PRK12467 2083 DASELQQaYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAV 2162
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3608 ARVG-AAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT 3686
Cdd:PRK12467 2163 AQEGdGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGG 2242
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3687 WHAEH-AEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLED 3765
Cdd:PRK12467 2243 WSAMHrAPEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLED 2322
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3766 LQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQGALEQRFATSVQSRFDR 3845
Cdd:PRK12467 2323 LQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQRRHAASVTTHLDS 2402
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3846 SLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLSPVADLGE 3925
Cdd:PRK12467 2403 EWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLAT 2482
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3926 SLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFDAQFD--EMALLDPAGESAGAEMDPGAPLD 4003
Cdd:PRK12467 2483 SIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDaeKQALFVPSGEFSGAEQSEEAPLG 2562
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4004 NWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARLDALPVALEE 4083
Cdd:PRK12467 2563 NWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDRLPVAVGD 2642
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4084 VEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQRQL 4163
Cdd:PRK12467 2643 IEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVVYKQARL 2722
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4164 PFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRS 4243
Cdd:PRK12467 2723 PFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQP 2802
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4244 PeQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGVGEHLREVDATATARLRDFARRHQV 4323
Cdd:PRK12467 2803 P-PAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRV 2881
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4324 TLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQE 4403
Cdd:PRK12467 2882 TLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFE 2961
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4404 HTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQTNYPLALALGGGDSLSLQFSYDRGLFPA 4483
Cdd:PRK12467 2962 HTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDA 3041
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4484 ATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPATPLVHQRVAERARMAPDAVAVIFDEEKL 4563
Cdd:PRK12467 3042 AAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQL 3121
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSH 4643
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH 3201
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4644 LLERLPIPEGLSCLSVDREEEWaGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDC 4723
Cdd:PRK12467 3202 LLEQLPAPAGDTALTLDRLDLN-GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDR 3280
|
3290 3300 3310 3320 3330 3340 3350 3360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4724 ELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERdGNPPPVRVYCFG 4803
Cdd:PRK12467 3281 VLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG-ADCASLDIYVFG 3359
|
3370 3380 3390 3400 3410 3420 3430 3440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4804 GDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELY 4883
Cdd:PRK12467 3360 GEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELY 3439
|
3450 3460 3470 3480 3490 3500 3510 3520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4884 LGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PRK12467 3440 IGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
|
3530 3540 3550 3560 3570 3580 3590 3600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4964 REAVVVAQPGAVGQQLVGYVVAQEPavadspeaQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQP 5043
Cdd:PRK12467 3520 REAVVLARDGAGGKQLVAYVVPADP--------QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
3610 3620 3630 3640 3650 3660 3670 3680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5044 DASlLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQtesLQAYAE 5123
Cdd:PRK12467 3592 DAK-GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMS---APTIAE 3667
|
...
gi 2310915810 5124 LAA 5126
Cdd:PRK12467 3668 LAG 3670
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
41-2771 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 3393.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 41 PAGVSSAERDR---LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRgaDDSLAQ 117
Cdd:PRK12467 1105 QPALPDVDRDQplpLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ--EDGRTR 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 118 APLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEE 197
Cdd:PRK12467 1183 QVIHPVGSLTLEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDE 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 198 FSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSI 277
Cdd:PRK12467 1263 LVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFEL 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 278 EPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATL 357
Cdd:PRK12467 1343 PPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQL 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 358 LAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEAldSVAGLSFGQLDWKSRTTQFDLSLDT 437
Cdd:PRK12467 1423 LQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQA--QLPGLSVESLSWESQTAQFDLTLDT 1500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 438 YEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLF 517
Cdd:PRK12467 1501 YESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLI 1580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 518 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 597
Cdd:PRK12467 1581 EDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPR 1660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 598 ERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRH 675
Cdd:PRK12467 1661 ERLAYMIEDSGIELLLTQSHLqaRLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRH 1740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 676 SALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSML 755
Cdd:PRK12467 1741 GALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSML 1820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 756 QAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRPIGN 831
Cdd:PRK12467 1821 QQLLQmDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCrrkDLEGRDSVPIGQPIAN 1900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:PRK12467 1901 LSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQV 1980
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 911 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG---RQLVGYVVLESEG--------GDWREALAAHLAASLPEYMVPAQW 979
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQGGVREAVVIAQDGangKQLVAYVVPTDPGlvdddeaqVALRAILKNHLKASLPEYMVPAHL 2060
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 980 LALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQ 1059
Cdd:PRK12467 2061 VFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQ 2140
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1060 AGLQLSPRDLFQHQNIRSLAL--AAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGR 1137
Cdd:PRK12467 2141 AGIRFTPKDLFQHQTVQSLAAvaQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEA 2220
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1138 ALERLQAQHDALRLRFREERGAWHQAY--AEQAGEP-LWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQ 1214
Cdd:PRK12467 2221 ALQALLVHHDALRLGFVQEDGGWSAMHraPEQERRPlLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQ 2300
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1215 RLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD----LGPRSSSYQTWSRHL--HEQAGARLDELDYWQAQLHDAPHALP 1288
Cdd:PRK12467 2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGqpvkLPAKTSAFKAWAERLqtYAASAALADELGYWQAQLQGASTELP 2380
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1289 CENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLS 1368
Cdd:PRK12467 2381 CDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLT 2460
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1369 RTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNYLGRFDRQFDGA- 1447
Cdd:PRK12467 2461 RTVGWFTSLYPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDAEk 2540
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1448 -ALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHCLDPRHRGVTP 1526
Cdd:PRK12467 2541 qALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTP 2620
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1527 SDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQATLDAHEILR 1605
Cdd:PRK12467 2621 SDFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGaGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILR 2700
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1606 SGFLWKDGWPQPLQVVFEQATLELRLAPPGSDPQRQ------AEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHI 1679
Cdd:PRK12467 2701 SGFLWDGELEEPLQVVYKQARLPFSRLDWRDRADLEqaldalAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHI 2780
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1680 LMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLAR--QARTEQP--GQGEH 1755
Cdd:PRK12467 2781 LMDGWSGSQLLGEVLQRYFGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARalYPAPAEAvaGHGAH 2860
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1756 LRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQ 1835
Cdd:PRK12467 2861 YLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAE 2940
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1836 QSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSNHEQTNYPLTL 1914
Cdd:PRK12467 2941 QTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQgAPSGLRFGAVSSREQTNYPLTL 3020
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1915 GVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEALPRG-GVAAA 1993
Cdd:PRK12467 3021 AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSErLVHQL 3100
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:PRK12467 3181 RERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHG 3260
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:PRK12467 3261 ALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQ 3340
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 QAEElrHAGRRIA-VRTCILGGEAWDASllTQQAVQAEA----WFNAYGPTEAVITPLAWHC-RAQEGGAPA--IGRALG 2305
Cdd:PRK12467 3341 FAED--AGGADCAsLDIYVFGGEAVPPA--AFEQVKRKLkprgLTNGYGPTEAVVTVTLWKCgGDAVCEAPYapIGRPVA 3416
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK12467 3417 GRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQ 3496
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSS 2465
Cdd:PRK12467 3497 VKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADP--QGDWRETLRDHLAASLPDYMVPAQLLVLAA 3574
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2466 LPLNANGKLDRKALPKVDAAARRqAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELD 2545
Cdd:PRK12467 3575 MPLGPNGKVDRKALPDPDAKGSR-EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLK 3653
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2546 VPLRILFERPVLADFAASLESQAASVAPVLQVlprvaelplshaqqrmwflwklepesaayhlpsvlhvrgvldqAALQQ 2625
Cdd:PRK12467 3654 LSLRDLMSAPTIAELAGYSPLGDVPVNLLLDL-------------------------------------------NRLET 3690
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2626 AFDWLVLRHETLRTRFEEvdgqarqtilanMPLRIVLEdcagaseatlrqrvaeeirqpfdlargpllrvrllalaGQEH 2705
Cdd:PRK12467 3691 GFPALFCRHEGLGTVFDY------------EPLAVILE--------------------------------------GDRH 3720
|
2730 2740 2750 2760 2770 2780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2706 VLVITQHHIVSDGWSmqvmvDELLQAYAaarrgeqptlaplkLQYADYAAWHRAWLDSGEGARQLD 2771
Cdd:PRK12467 3721 VLGLTCRHLLDDGWQ-----DTSLQAMA--------------VQYADYILWQQAKGPYGLLGWSLG 3767
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1583-5149 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 2990.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRL----APPGSDPQRQAEAEREAG----FDPAR 1654
Cdd:PRK05691 708 GELDEAALRASFQRLVERHESLRTRFYERDG--VALQRIDAQGEFALQRidlsDLPEAEREARAAQIREEEarqpFDLEK 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1655 APLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQ--EVAATVGRYRDYIGW----LQGRDAMAT 1724
Cdd:PRK05691 786 GPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAaacqGQtaELAPLPLGYADYGAWqrqwLAQGEAARQ 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1725 EFFWRDRLAS----LEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVA 1800
Cdd:PRK05691 866 LAYWKAQLGDeqpvLELATDHPRSARQAHSAARYSLR-VDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIR 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1801 FGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILV 1880
Cdd:PRK05691 945 IGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMF 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1881 FENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGE--RLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQA 1958
Cdd:PRK05691 1023 NHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRngRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQR 1102
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1959 ALGELALLDAGERQEaLRDW-QAPLEAlPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVA 2037
Cdd:PRK05691 1103 ALGDVQLLDAAERAQ-LAQWgQAPCAP-AQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGP 1180
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2038 EALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLET---AA 2114
Cdd:PRK05691 1181 DVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSlhlDS 1260
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2115 WPASAdtrPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLL 2194
Cdd:PRK05691 1261 WPSQA---PGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLI 1337
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2195 AGARVLL-GDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGEAWDASLLTQ--QAVQAEA 2271
Cdd:PRK05691 1338 TGCRLVLaGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT-SLRRLFSGGEALPAELRNRvlQRLPQVQ 1416
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 WFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVA 2351
Cdd:PRK05691 1417 LHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP 1496
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 DPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGR 2431
Cdd:PRK05691 1497 DPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGE 1576
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2432 DAMrgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGepPREGLERSVAAIWEALLG 2511
Cdd:PRK05691 1577 AGQ--EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVE--PRTELQQQIAAIWREVLG 1652
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2512 VEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASL----ESQAASVAPVLQVLPRVAELPLS 2587
Cdd:PRK05691 1653 LPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVariqAAGERNSQGAIARVDRSQPVPLS 1732
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2588 HAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAG 2667
Cdd:PRK05691 1733 YSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSA 1812
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2668 ASEATLRQRVAE----EIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTL 2743
Cdd:PRK05691 1813 LPADARQQRLQQladsEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPL 1892
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2744 APLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREG 2823
Cdd:PRK05691 1893 EPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRG 1972
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2824 VTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQD 2903
Cdd:PRK05691 1973 LTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQD 2052
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2904 LPFEQLVDALQPERNLSHSPLFQVMYNHQSGE-RQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLF 2982
Cdd:PRK05691 2053 LPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLF 2132
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2983 EARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEE 3062
Cdd:PRK05691 2133 DEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQ 2212
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:PRK05691 2213 TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSD 2292
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHL-----KLPlaQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG 3217
Cdd:PRK05691 2293 RALfealgELP--AGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG 2370
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3218 LGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAKLVALINREGVDTLHFVP---SMLQAFLQDEDVASc 3294
Cdd:PRK05691 2371 MRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-QWGAEEICQLIREQQVSILGFTPsygSQLAQWLAGQGEQL- 2448
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3295 tSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAidVTHWTC-----VEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:PRK05691 2449 -PVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETV--VMPLAClapeqLEEGAASVPIGRVVGARVAYILDADLA 2525
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 3448
Cdd:PRK05691 2526 LVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGE 2605
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3449 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLESESGD------WREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:PRK05691 2606 IESRLLEHPAVREAVVLALDtpsGKQLAGYLVSAVAGQDdeaqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTANGK 2685
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3520 LDRKALPRPQ-AAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQ 3598
Cdd:PRK05691 2686 LDRRALPAPDpELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQH 2765
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3599 QTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRL 3678
Cdd:PRK05691 2766 QTVQTLAAVATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRL 2845
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3679 RFHETDGTWHAEHAEATlGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVS 3758
Cdd:PRK05691 2846 RFSQADGRWQAEYRAVT-AQELLWQVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVS 2924
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3759 WRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQGALEQRFATS 3838
Cdd:PRK05691 2925 WRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQT 3004
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3839 VQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLS 3918
Cdd:PRK05691 3005 VSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLT 3084
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3919 P----VADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGA 3994
Cdd:PRK05691 3085 PapgdDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQAPITFNYLGQFDQSFASDALFRPLDEPAGP 3164
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3995 EMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARL 4074
Cdd:PRK05691 3165 AHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQL 3244
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4075 DALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDV-SGLDIPRFRAAWQSALDRHAILRSGFAWQ-GELQq 4152
Cdd:PRK05691 3245 DALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRInSALDPERFAQAWQAVVARHEALRASFSWNaGETM- 3323
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4153 pLQIVYRQRQLPFAEEDLSQAANRDAAL--LALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQ 4230
Cdd:PRK05691 3324 -LQVIHKPGRTPIDYLDWRGLPEDGQEQrlQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSL 3402
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4231 LLSEVLESYA----GRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLveALAQPGLTSANG------VG 4300
Cdd:PRK05691 3403 LMNDFFEIYTalgeGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPI--PSDRPFLREHAGdsggmvVG 3480
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4301 EHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLa 4380
Cdd:PRK05691 3481 DCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQL- 3559
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4381 PQ----MTLDELLQGLQRQNLALREQEHTPLFELQRWAGF-GGEAVFDNLLVFENYPVD-EVLERSSAGGVRFGAVAMHe 4454
Cdd:PRK05691 3560 PAagqrCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELpKGQPLFDSLFVFENAPVEvSVLDRAQSLNASSDSGRTH- 3638
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4455 qTNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYP 4534
Cdd:PRK05691 3639 -TNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYP 3717
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4535 A----TPLVHQRVAERarmaPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK05691 3718 LeqsyVRLFEAQVAAH----PQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKA 3793
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER-LPIPEGLSC-----LSVDREEEWAGFPAHDPEVALHGDNLAY 4684
Cdd:PRK05691 3794 GAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQaRALLDELGCanrprLLVWEEVQAGEVASHNPGIYSGPDNLAY 3873
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTY 4763
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHdPQGLL 3953
|
3290 3300 3310 3320 3330 3340 3350 3360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVTVGVFPPVYLQQL--AEHAERDGnpppVRVYCFGGDAVAQasyDLAWRALKpKY----LFNGYGPTETVVTP 4837
Cdd:PRK05691 3954 AHVQAQGITVLESVPSLIQGMlaEDRQALDG----LRWMLPTGEAMPP---ELARQWLQ-RYpqigLVNAYGPAECSDDV 4025
|
3370 3380 3390 3400 3410 3420 3430 3440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4838 LLWKARAGDACGaAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLY 4917
Cdd:PRK05691 4026 AFFRVDLASTRG-SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLY 4104
|
3450 3460 3470 3480 3490 3500 3510 3520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAqepavADSPEAQ 4997
Cdd:PRK05691 4105 RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVP-----HQTVLAQ 4179
|
3530 3540 3550 3560 3570 3580 3590 3600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4998 AECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQ-QVYVAPRSDLEQQVAGIWAEVLQLQQV 5076
Cdd:PRK05691 4180 GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQsQAYLAPRNELEQTLATIWADVLKVERV 4259
|
3610 3620 3630 3640 3650 3660 3670
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 5077 GLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAE----LAAAQTSsnDTDFDDLREFMSELEAI 5149
Cdd:PRK05691 4260 GVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEyiegLAGSAID--EQKVDRLSDLMAELEGL 4334
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-2570 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 2320.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 25 LETLRGEGIDFSLFPIpAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLR 104
Cdd:PRK05691 1705 VARIQAAGERNSQGAI-ARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLR 1783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 105 TVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHI 184
Cdd:PRK05691 1784 TTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHI 1863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 185 VSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPV 264
Cdd:PRK05691 1864 VTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPP 1943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 265 VPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVL 344
Cdd:PRK05691 1944 VQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVL 2023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 345 RSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLvaDIEALDSVAGLSFGQLDW 424
Cdd:PRK05691 2024 RCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRW--EFQQSRQLAGMTVEYLVN 2101
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 425 KSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATA 504
Cdd:PRK05691 2102 DARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEA 2181
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 505 AEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKA 584
Cdd:PRK05691 2182 GEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 585 GGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL-----KLPlaQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVI 659
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALfealgELP--AGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLI 2339
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAKLVEL 739
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-QWGAEEICQL 2418
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 740 INREGVDTLHFVP---SMLQAFLQDEDVASctSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAidVTHWTC- 815
Cdd:PRK05691 2419 IREQQVSILGFTPsygSQLAQWLAGQGEQL--PVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETV--VMPLACl 2494
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 816 ----VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGD 890
Cdd:PRK05691 2495 apeqLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGD 2574
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESEGGD------WREA 961
Cdd:PRK05691 2575 LVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDtpsGKQLAGYLVSAVAGQDdeaqaaLREA 2654
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 962 LAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFF 1041
Cdd:PRK05691 2655 LKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFF 2734
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1042 SLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLAL-AAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQHWNQ 1120
Cdd:PRK05691 2735 ELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAvATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQ 2814
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1121 SLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEP-LWRRQAGSEEALLALCEEAQRSLDLEQG 1199
Cdd:PRK05691 2815 ALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQElLWQVTVADFAECAALFADAQRSLDLQQG 2894
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGP----RSSSYQTWSRHLHEQAGAR--LDEL 1273
Cdd:PRK05691 2895 PLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPalpaKTSAFRDWAARLQAYAGSEslREEL 2974
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1274 DYWQAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQL 1353
Cdd:PRK05691 2975 GWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQL 3054
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1354 EGHGREDLGEAIDLSRTVGWFTSLFPVRLTPA----ADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQ 1429
Cdd:PRK05691 3055 EGHGREALFDDIDLTRSVGWFTSAYPLRLTPApgddAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQ 3134
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1430 PRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYAREL 1509
Cdd:PRK05691 3135 APITFNYLGQFDQSFASDALFRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAEL 3214
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1510 HALIEHCLDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSL--HGTeGDYVNQLRMDI-GGLD 1586
Cdd:PRK05691 3215 QALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLlePGT-GLYYMQDRYRInSALD 3293
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1587 PDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQATLELR------LAPPGSDPQRQA--EAEREAGFDPARAPLQ 1658
Cdd:PRK05691 3294 PERFAQAWQAVVARHEALRASFSWNAG-ETMLQVIHKPGRTPIDyldwrgLPEDGQEQRLQAlhKQEREAGFDLLNQPPF 3372
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1659 RLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEVAATVG-RYRDYIGWLQGRDAMATEFFWRDRLA 1733
Cdd:PRK05691 3373 HLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTalgeGREAQLPVPpRYRDYIGWLQRQDLAQARQWWQDNLR 3452
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1734 SLEMPTRLA--RQARTEQPGQ------GEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATV 1805
Cdd:PRK05691 3453 GFERPTPIPsdRPFLREHAGDsggmvvGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTV 3532
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1806 AGRPAELPGIEAQIGLFINTLPV-IAAPQPQQ--SVADYLQGMQALNLALREHEHTPLYDIQRWAG-HGGEALFDSILVF 1881
Cdd:PRK05691 3533 AGRPVSMPQMQRTVGLFINSIALrVQLPAAGQrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSElPKGQPLFDSLFVF 3612
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1882 ENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGERLSLQYVYARRDFDAADI----AELDRHLLHLLQRMaetpQ 1957
Cdd:PRK05691 3613 ENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVerllGEFKRLLLALVQGF----H 3688
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1958 AALGELALLDAGERQEALRDWQAPLEALP-RGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVV 2036
Cdd:PRK05691 3689 GDLSELPLLGEQERDFLLDGCNRSERDYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVG 3768
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2037 AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAER-------LPCPAEVERLP 2109
Cdd:PRK05691 3769 VDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQaralldeLGCANRPRLLV 3848
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2110 LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQL 2189
Cdd:PRK05691 3849 WEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQF 3928
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2190 FVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHA--GRRIAVRTcilgGEAWDASLLTQ-- 2264
Cdd:PRK05691 3929 LAAPLFGARVeIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAldGLRWMLPT----GEAMPPELARQwl 4004
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2265 QAVQAEAWFNAYGPTEAV--ITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRP 2342
Cdd:PRK05691 4005 QRYPQIGLVNAYGPAECSddVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDP 4084
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2343 GQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGP 2422
Cdd:PRK05691 4085 LRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGK 4164
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2423 LLAAYLVGRDAMRGED-LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVD-AAARRQAGEPPREGLER 2500
Cdd:PRK05691 4165 HLVGYLVPHQTVLAQGaLLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDiGQLQSQAYLAPRNELEQ 4244
|
2570 2580 2590 2600 2610 2620 2630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2501 SVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASLESQAAS 2570
Cdd:PRK05691 4245 TLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGS 4314
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-1397 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1520.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12467 1 MDNNVALRIARRFITLPLEKRRLYLEKMQEEGVSFANLPIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 81 NGPLDRQALERAFASLVQRHETLRTVFpRGADDSLAQAPL-QRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCE 159
Cdd:PRK12467 81 RGELDVSALRRAFDALVARHESLRTRF-VQDEEGFRQVIDaSLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 160 GPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQ 239
Cdd:PRK12467 160 GPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 240 LEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRV 319
Cdd:PRK12467 240 LAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 320 GVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMY 399
Cdd:PRK12467 320 GVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 400 NHQPLVADIE--ALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLEN 477
Cdd:PRK12467 400 NHQNTATGGRdrEGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 478 PQASVDSLPMLDAEERGQLLEGWNATAAEYpLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG 557
Cdd:PRK12467 480 PRRRLGELPLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 558 IGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQAD 635
Cdd:PRK12467 559 VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLlaQLPVPAGLRSLCLDEPA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 636 AWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP 715
Cdd:PRK12467 639 DLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 716 LMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQA 795
Cdd:PRK12467 719 LASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 796 GLYNLYGPTEAAIDVTHWTCVEEGKD--TVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAER 873
Cdd:PRK12467 799 RLINHYGPTETTVGVSTYELSDEERDfgNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAER 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 874 FVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG---RQLVGYV 949
Cdd:PRK12467 879 FVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGdagLQLVAYL 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 950 VLE-----SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEI 1024
Cdd:PRK12467 959 VPAavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAI 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1025 WQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNI----RSLALAAKAGAATAEQGPASGEVA 1099
Cdd:PRK12467 1039 WADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLagfaQAVAAQQQGAQPALPDVDRDQPLP 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQ--RWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYaeQAGEPLWRRQA 1177
Cdd:PRK12467 1119 LSYAQerQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVI--HPVGSLTLEEP 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1178 GS------EEALLALCE-EAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD--- 1247
Cdd:PRK12467 1197 LLlaadkdEAQLKVYVEaEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGqsl 1276
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1248 ----LGPRSSSYQTWSRHLHEqAGARLDELDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAP 1321
Cdd:PRK12467 1277 qlpaLPIQYADYAVWQRQWMD-AGERARQLAYWKAQLggEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 1322 AAYRTqVNDLLLTALARATCRWSGDASVLVQLEGHGREDLgeaiDLSRTVGWF--TSLFPVRLTPAADLGESLKAIKE 1397
Cdd:PRK12467 1356 REGVT-LFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA----ETEGLIGFFvnTQVLRAEVDGQASFQQLLQQVKQ 1428
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1990-3880 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1327.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALV----CGDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSfDLVVGLLGILKAGA 2063
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRfladDPGEGvvLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGP-DYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPA-----ERLAYMLRDSGARWLICQETLAERLpcpAEVERLPLETAAW--------PASADTRPLPEVAGE 2130
Cdd:PRK05691 90 IAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPEllcvdtldPALAEAWQEPALQPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--VGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLGDAGQW 2207
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2208 SAQHLA--DEVERHAVTILDLPP-AYL-------QQQAEELRHAGRRIAVRtcilGGEAWDASLLTQQA-------VQAE 2270
Cdd:PRK05691 247 LERPLRwlEAISEYGGTISGGPDfAYRlcservsESALERLDLSRWRVAYS----GSEPIRQDSLERFAekfaacgFDPD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2271 AWFNAYGPTEAVITpLAWHCRAQegGAPAI---GRALGARRA----------C----------ILDAA-LQPCAPGMIGE 2326
Cdd:PRK05691 323 SFFASYGLAEATLF-VSGGRRGQ--GIPALeldAEALARNRAepgtgsvlmsCgrsqpghavlIVDPQsLEVLGDNRVGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2327 LYIGGQCLARGYLGRPGQTAERFVadpfSGSGERLYRTGDLARYRvDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:PRK05691 400 IWASGPSIAHGYWRNPEASAKTFV----EHDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2407 YVAEAAVVAL-----DGVGGPLLAAYlVGRDAMR---GEDLLAELRTWLAgrlPAYMQPTAWQVL---SSLPLNANGKLD 2475
Cdd:PRK05691 475 EVVRKGRVAAfavnhQGEEGIGIAAE-ISRSVQKilpPQALIKSIRQAVA---EACQEAPSVVLLlnpGALPKTSSGKLQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2476 RKA---------------LPKVDAAARRQAGEPPREgLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQ 2540
Cdd:PRK05691 551 RSAcrlrladgsldsyalFPALQAVEAAQTAASGDE-LQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRD 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2541 DLELDVPLRILFERPVLADFAASLESQAASVAPV---LQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK05691 630 ELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAqaaIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGE 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMP---LRIVLEDCAGAS-EATLRQRVAEEIRQPFDLARGPLL 2693
Cdd:PRK05691 710 LDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEfalQRIDLSDLPEAErEARAAQIREEEARQPFDLEKGPLL 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2694 RVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYW 2773
Cdd:PRK05691 790 RVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYW 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2774 RERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPI 2853
Cdd:PRK05691 870 KAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPN 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2854 ANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERnlsHSPLFQVMYNHQS 2933
Cdd:PRK05691 950 ANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAR---EQGLFQVMFNHQQ 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2934 GERQDA-QVDGLHIESFAWDGAAAQFDLALDTWETPDG-LGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDS 3011
Cdd:PRK05691 1027 RDLSALrRLPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGD 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3012 LPMLDAEERGQLLEgWNATAAEyPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLV 3091
Cdd:PRK05691 1107 VQLLDAAERAQLAQ-WGQAPCA-PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCV 1184
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3092 GVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL--KLPLAQGVQRIDLDRGApwFEDYS 3169
Cdd:PRK05691 1185 AIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLleRLPQAEGVSAIALDSLH--LDSWP 1262
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3170 EANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 3249
Cdd:PRK05691 1263 SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRL 1342
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 3329
Cdd:PRK05691 1343 VLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYG 1422
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3330 PTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-A 3408
Cdd:PRK05691 1423 PTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeD 1502
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3409 GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL---AVDGRQLVGYVVLESESGDW 3485
Cdd:PRK05691 1503 GARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLvreGAAGAQLVGYYTGEAGQEAE 1582
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3486 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQtHVAPQNEMERRIAAVWADVLKLEEVGATDN 3565
Cdd:PRK05691 1583 AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQRE-HVEPRTELQQQIAAIWREVLGLPRVGLRDD 1661
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3566 FFALGGDSIVSIQVVSRCR-AAGIQFTPKDLFQQQTVQGLA-RVARVGAAVQME-QGPVS----GETVLLPF--QRLFF- 3635
Cdd:PRK05691 1662 FFALGGHSLLATQIVSRTRqACDVELPLRALFEASELGAFAeQVARIQAAGERNsQGAIArvdrSQPVPLSYsqQRMWFl 1741
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3636 EQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATlGGALLWR-----AEAVDRQ 3710
Cdd:PRK05691 1742 WQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDS-GLRMDWQdfsalPADARQQ 1820
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3711 ALESLC-EESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG-EAP--RLPGKTS 3786
Cdd:PRK05691 1821 RLQQLAdSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDrESPlePLPVQYL 1900
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3787 PFKAWAGRVSEHARGESmkaQLQFWRELL--EGAPAELPCEHPQGAleqrfatsVQS------RFDrsLTERLLKQAPAA 3858
Cdd:PRK05691 1901 DYSVWQRQWLESGERQR---QLDYWKAQLgnEHPLLELPADRPRPP--------VQShrgelyRFD--LSPELAARVRAF 1967
|
2010 2020
....*....|....*....|....*
gi 2310915810 3859 YRTQVNDLLLT---ALARVVCRWSG 3880
Cdd:PRK05691 1968 NAQRGLTLFMTmtaTLAALLYRYSG 1992
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
53-1297 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1241.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 53 SYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCS 132
Cdd:PRK05691 679 SLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 133 GLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPG 212
Cdd:PRK05691 759 DLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAE 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 213 LPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQ 292
Cdd:PRK05691 839 LAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAH 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 293 GLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQ 372
Cdd:PRK05691 919 QATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQ 998
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 373 DLPFERLVEAFKVERSlshSPLFQVMYNHQPlvADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYE-KGGRLYAALTYA 451
Cdd:PRK05691 999 DLPFEQLVEALPQARE---QGLFQVMFNHQQ--RDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEdRNGRLTLSFDYA 1073
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 452 TDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEgWNATAAEyPLQRGVHRLFEEQVERTPTAPALA 531
Cdd:PRK05691 1074 AELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQ-WGQAPCA-PAQAWLPELLNEQARQTPERIALV 1151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 532 FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK05691 1152 WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVEL 1231
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 612 LLSQSHL--KLPLAQGVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAY 689
Cdd:PRK05691 1232 LLTQSHLleRLPQAEGVSAIALDSLH--LDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATY 1309
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 690 GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTS 769
Cdd:PRK05691 1310 ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTS 1389
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 770 LKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:PRK05691 1390 LRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVA 1469
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 850 GELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:PRK05691 1470 GELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA 1549
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 929 HPWVREAAVL---AVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSV 1005
Cdd:PRK05691 1550 QPGVAQAAVLvreGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1006 AQagYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRSLALAAKA 1084
Cdd:PRK05691 1630 RE--HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFAEQVAR 1707
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1085 GAATAE---QGPA-----SGEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFR 1154
Cdd:PRK05691 1708 IQAAGErnsQGAIarvdrSQPVPLSYSQQrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFP 1787
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1155 EERGAWHQAYAEQAGEPLWRRQAGSEEA------LLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDG 1227
Cdd:PRK05691 1788 SVDGVPVQQVAEDSGLRMDWQDFSALPAdarqqrLQQLAdSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEG 1867
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1228 VSWRILLEDLQRLY----ADLDADLGP---RSSSYQTWSRHLHEqAGARLDELDYWQAQLHDApH---ALPCENPHGALE 1297
Cdd:PRK05691 1868 WAMDIFARELGALYeaflDDRESPLEPlpvQYLDYSVWQRQWLE-SGERQRQLDYWKAQLGNE-HpllELPADRPRPPVQ 1945
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
39-1340 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 1146.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 39 PIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQA 118
Cdd:COG1020 7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 119 PLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEF 198
Cdd:COG1020 87 QPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 199 SRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIE 278
Cdd:COG1020 167 LRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:COG1020 247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTY 438
Cdd:COG1020 327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELEL---PGLTLEPLELDSGTAKFDLTLTVV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 439 EKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFE 518
Cdd:COG1020 404 ETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 519 EQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:COG1020 484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 599 RQAYMLEDSGVQLLLSQSHLKLPLAQ-GVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:COG1020 564 RLAYMLEDAGARLVLTQSALAARLPElGVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:COG1020 642 LVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 758 FLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCY 835
Cdd:COG1020 722 LL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANTRVY 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:COG1020 801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 915 LRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:COG1020 881 FRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 991 GKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLF 1070
Cdd:COG1020 961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLF 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1071 QHQNIRSLALAAKAGAATAEQGPASGEV--ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDA 1148
Cdd:COG1020 1041 LAAAAAAAAAAAAAAAAAAAAPLAAAAAplPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLA 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1149 LRLRFREERGAWHQ---------AYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLV 1219
Cdd:COG1020 1121 LLAALRARRAVRQEgprlrllvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLL 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1220 IHHLAVDGVSWRILLEDLQRLYADLDADLG------PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPH 1293
Cdd:COG1020 1201 LLLLLLLLLLLLLLLLLLLLLLLLAAAAAAllalalLLALLALAALLALAALAALAAALLALALALLALALLLLALALLL 1280
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*..
gi 2310915810 1294 GALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARAT 1340
Cdd:COG1020 1281 PALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2567-3875 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 1139.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2567 QAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDG 2646
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2647 QARQTI----LANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQ 2722
Cdd:COG1020 81 RPVQVIqpvvAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2723 VMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQR 2802
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2803 LDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGL 2882
Cdd:COG1020 241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2883 AFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLAL 2962
Cdd:COG1020 321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2963 DTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHR 3042
Cdd:COG1020 401 TVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:COG1020 481 LFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQ-GVQRIDLDrgAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:COG1020 561 PAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALD--ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVE 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:COG1020 639 HRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSL 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDAVPIGRPIANL 3359
Cdd:COG1020 719 LRALL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANT 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:COG1020 798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPL 3514
Cdd:COG1020 878 IRGFRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3515 SPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSR--CRAAGIQFTP 3592
Cdd:COG1020 958 TGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARaaRLLLLLLLLL 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3593 KDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEH 3672
Cdd:COG1020 1038 LLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3673 HDALRLRFHETDGTWHAEHAE-------ATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRL 3745
Cdd:COG1020 1118 LLALLAALRARRAVRQEGPRLrllvalaAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3746 LLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCE 3825
Cdd:COG1020 1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALA 1277
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3826 HPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVV 3875
Cdd:COG1020 1278 LLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1534-2838 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 888.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1534 LSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTEGDYVNQLRMDIGGLDPDRFRAAWQATLDAHEILRSGFLWKDG 1613
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1614 WPQPLQVVFEQATLELRL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNA 1687
Cdd:COG1020 81 RPVQVIQPVVAAPLPVVVllvdleALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1688 QLLAEVLQRYAGQEVAATVG----------RYRDYIGWLQGRDAMATEFFWRDRLAS----LEMPTRLARQARTEQPGqG 1753
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPlpplpiqyadYALWQREWLQGEELARQLAYWRQQLAGlpplLELPTDRPRPAVQSYRG-A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1754 EHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQ 1833
Cdd:COG1020 240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1834 PQQSVADYLQGMQALNLALREHEHTPLYDIQRWAG----HGGEALFDSILVFENFPVAEaLRQAPADLEFsTPSNHEQTN 1909
Cdd:COG1020 318 GDPSFAELLARVRETLLAAYAHQDLPFERLVEELQperdLSRNPLFQVMFVLQNAPADE-LELPGLTLEP-LELDSGTAK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1910 YPLTLGVT-LGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEALPRG 1988
Cdd:COG1020 396 FDLTLTVVeTGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1989 G-VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:COG1020 476 AtLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKG 2147
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKG 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDL 2226
Cdd:COG1020 635 VMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALAELLARHRVTVLNL 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 PPAYLQQQAEELRHAGRRiaVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAVITPLAWHCRA--QEGGAPAIGR 2302
Cdd:COG1020 715 TPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRRwrARLPGARLVNLYGPTETTVDSTYYEVTPpdADGGSVPIGR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2303 ALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRA 2382
Cdd:COG1020 793 PIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2383 DQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQ 2461
Cdd:COG1020 873 DDQVKIRGFRIELGEIEAALLQHPGVREAVVVAReDAPGDKRLVAYVVPEAG--AAAAAALLRLALALLLPPYMVPAAVV 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2462 VLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQD 2541
Cdd:COG1020 951 LLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLL 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2542 LELDVPLRILFERPVLADFAASLE-SQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQ 2620
Cdd:COG1020 1031 LLLLLLLLLFLAAAAAAAAAAAAAaAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2621 AALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLAL 2700
Cdd:COG1020 1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2701 AGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAE 2780
Cdd:COG1020 1191 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALA 1270
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2781 QPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLL 2838
Cdd:COG1020 1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4069-5130 |
0e+00 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 835.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4069 LDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRSGFAWQG 4148
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4149 ELQQPLQIVyRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSN 4228
Cdd:COG1020 81 RPVQVIQPV-VAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4229 AQLLSEVLESY-----AGRSPEQPRDGRYSDYIAW----LQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGv 4299
Cdd:COG1020 160 GLLLAELLRLYlaayaGAPLPLPPLPIQYADYALWqrewLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4300 GEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTL 4379
Cdd:COG1020 239 ARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4380 APQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGF----GGEAVFDNLLVFENYPVDEVlersSAGGVRFGAVAMHEQ 4455
Cdd:COG1020 317 SGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPerdlSRNPLFQVMFVLQNAPADEL----ELPGLTLEPLELDSG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4456 T-NYPLALALG-GGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGY 4533
Cdd:COG1020 393 TaKFDLTLTVVeTGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:COG1020 473 PADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPiPEGLSCLSVDrEEEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:COG1020 553 YVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALD-ALALAAEPATNPPVPVTPDDLAYVIYTSGSTG 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVT 4772
Cdd:COG1020 631 RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALAELLARHRVT 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4773 VGVFPPVYLQQLAEHAERDgnPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcGAAY 4852
Cdd:COG1020 711 VLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDA-DGGS 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVD 4932
Cdd:COG1020 788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLE 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqlktALRERL 5012
Cdd:COG1020 868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRL-------ALALLL 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLA 5092
Cdd:COG1020 941 PPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLL 1020
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 2310915810 5093 IQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQTS 5130
Cdd:COG1020 1021 LALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAA 1058
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4058-5128 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 817.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4058 GATPSDFPLagldqarldalPVALEEVEDIyPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDR 4136
Cdd:PRK12467 32 GVSFANLPI-----------PQVRSAFERI-PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGeLDVSALRRAFDALVAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4137 HAILRSGFAWQGElqQPLQIVYRQRQLPFAEEDLS--QAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHL 4214
Cdd:PRK12467 100 HESLRTRFVQDEE--GFRQVIDASLSLTIPLDDLAneQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4215 IYTHHHILLDGWSNAQLLSEVLESYA----GRSPEQPR-DGRYSDYIAWlQRQDAAATE-----AFWREQMAALDEPTRL 4284
Cdd:PRK12467 178 VVTLHHIISDGWSMRVLVEELVQLYSaysqGREPSLPAlPIQYADYAIW-QRSWLEAGErerqlAYWQEQLGGEHTVLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4285 VEALAQPGLTSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpaDLPGVEN 4364
Cdd:PRK12467 257 PTDRPRPAVPSYRG-ARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR--NRVETER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4365 QVGLFINTLPVVVTLAPQMTLDELLQGLQRQnlALREQEHTPL-FE-----LQRWAGFGGEAVFDnllVFENYPVD---- 4434
Cdd:PRK12467 334 LIGFFVNTQVLKAEVDPQASFLELLQQVKRT--ALGAQAHQDLpFEqlveaLQPERSLSHSPLFQ---VMFNHQNTatgg 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4435 EVLERSSAGGVRFGAVAMHEQTNYpLALALGGGDS---LSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDL 4511
Cdd:PRK12467 409 RDREGAQLPGLTVEELSWARHTAQ-FDLALDTYESaqgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGEL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4512 QMLEKAELSAIGAIWNRSDSGYpATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVA 4591
Cdd:PRK12467 488 PLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVG 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4592 IAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDR-EEEWAGFPA 4670
Cdd:PRK12467 567 IAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEpADLLCGYSG 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVL 4750
Cdd:PRK12467 647 HNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLH 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IRD-DSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNPPPVRVYCFGGDAVAQASYDLaWRALKPKY-LFNGY 4828
Cdd:PRK12467 727 LLPpDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLAR-VRALGPGArLINHY 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GPTETVVTPLLWKARaGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP 4908
Cdd:PRK12467 805 GPTETTVGVSTYELS-DEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDP 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4909 FGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVaqeP 4988
Cdd:PRK12467 884 FGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLV---P 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4989 AVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWA 5068
Cdd:PRK12467 961 AAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWA 1040
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5069 EVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQ 5128
Cdd:PRK12467 1041 DVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ 1100
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2577-3606 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 747.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2577 VLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANM 2656
Cdd:PRK10252 1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2657 PL----RIVLEDCAGAsEATLRQRVAEEIRQPFDLARG-PLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQA 2731
Cdd:PRK10252 81 TFplpeIIDLRTQPDP-HAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2732 YAAARRGEQP---TLAPLKLQYADYAAWhRAwldSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALP 2808
Cdd:PRK10252 160 YCAWLRGEPTpasPFTPFADVVEEYQRY-RA---SEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2809 VPLSEELLACARreGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLL 2888
Cdd:PRK10252 236 DGAFRQLAAQAS--GVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2889 GRVREAALGAQAHQDLPFEQLVDAL---QPERNLsHSPLFQVM---YNHQSGERQdAQVDGLhiesfawdGAAAQFDLAL 2962
Cdd:PRK10252 314 TRLAAQLKKMRRHQRYDAEQIVRDSgraAGDEPL-FGPVLNIKvfdYQLDFPGVQ-AQTHTL--------ATGPVNDLEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2963 DTW-ETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERgQLLEGWNATAAEYPLQRgVH 3041
Cdd:PRK10252 384 ALFpDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEIPETT-LS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK10252 462 ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEdySEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:PRK10252 542 YPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVG 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:PRK10252 620 QTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSM 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLQDEDV----ASCTSLKRIVCSGEALPADaQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA-----VPI 3352
Cdd:PRK10252 700 LAAFVASLTPegarQSCASLRQVFCSGEALPAD-LCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAvrgssVPI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGR 3432
Cdd:PRK10252 779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGR 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGRQLVGYVVLESESGDWREALAAHLAASLPEYMV 3502
Cdd:PRK10252 859 SDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaatggDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMV 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3503 PAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSR 3582
Cdd:PRK10252 939 PVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQ 1018
|
1050 1060
....*....|....*....|....*
gi 2310915810 3583 CRAA-GIQFTPKDLFQQQTVQGLAR 3606
Cdd:PRK10252 1019 LSRQfARQVTPGQVMVASTVAKLAT 1043
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
52-1070 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 744.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGaDDSLAQ--APLQRPLEVAFE 129
Cdd:PRK10252 10 LVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQwvDPALTFPLPEII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 130 DCSGLPEAEQEARLReeAQRESLQPFDLCEG-PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG 208
Cdd:PRK10252 89 DLRTQPDPHAAAQAL--MQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 209 AE-PGLPALPIQ--YADYALWQRSwlEAGEQERQleYWRGKLGERHPVLELPtdhPRPVVPSYRGSRY-EFSIEPALAEA 284
Cdd:PRK10252 167 EPtPASPFTPFAdvVEEYQRYRAS--EAWQRDAA--FWAEQRRQLPPPASLS---PAPLPGRSASADIlRLKLEFTDGAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:PRK10252 240 RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 365 VLGAQAHQDLPFERLV-EAFKV--ERSLsHSPLFQV-MYNHQPLVADIEALDSVagLSFGQLDwksrttqfDLSLDTY-E 439
Cdd:PRK10252 320 LKKMRRHQRYDAEQIVrDSGRAagDEPL-FGPVLNIkVFDYQLDFPGVQAQTHT--LATGPVN--------DLELALFpD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 440 KGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERgQLLEGWNATAAEYPLQRgVHRLFEE 519
Cdd:PRK10252 389 EHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEIPETT-LSALVAQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 520 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK10252 467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 600 QAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENhAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALS 679
Cdd:PRK10252 547 LKMMLEDARPSLLITTADQ-LPRFADVPDLTSLCYNAPLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 680 NRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL 759
Cdd:PRK10252 625 NRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFV 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 760 QDEDV----ASCTSLKRIVCSGEALPADaQQQVFAKLPQAGLYNLYGPTEAAIDVTHW-TCVEEGK----DTVPIGRPIG 830
Cdd:PRK10252 705 ASLTPegarQSCASLRQVFCSGEALPAD-LCREWQQLTGAPLHNLYGPTEAAVDVSWYpAFGEELAavrgSSVPIGYPVW 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 831 NLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:PRK10252 784 NTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 911 KLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWL 980
Cdd:PRK10252 864 KIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaatggDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLL 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 981 ALERMPLSPNGKLDRKALPAPEVSVAQAGySAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA 1060
Cdd:PRK10252 944 QLDQLPLSANGKLDRKALPLPELKAQVPG-RAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQ 1022
|
1050
....*....|.
gi 2310915810 1061 -GLQLSPRDLF 1070
Cdd:PRK10252 1023 fARQVTPGQVM 1033
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
4551-5041 |
0e+00 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 716.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLlthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17649 81 EDSGAGLL------------------------------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR-HGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd17649 125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVReLGVTVLDLPPAYLQQLAEEAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4790 R--DGNPPPVRVYCFGGDAVaqaSYDLAWRALK-PKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYI 4866
Cdd:cd17649 205 RtgDGRPPSLRLYIFGGEAL---SPELLRRWLKaPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGF 4946
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4947 RIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEpavadsPEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRA------AAAQPELRAQLRTALRASLPDYMVPAHLVFLAR 435
|
490
....*....|....*
gi 2310915810 5027 MPLTPNGKLDRKGLP 5041
Cdd:cd17649 436 LPLTPNGKLDRKALP 450
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
2002-2480 |
0e+00 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 696.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQEtlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17649 81 EDSGAGLLLTHH-----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQW-SAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd17649 126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWaSADELAEMVRELGVTVLDLPPAYLQQLAEEADR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 --AGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPA---IGRALGARRACILDAA 2315
Cdd:cd17649 206 tgDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd17649 286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd17649 366 GEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
....*
gi 2310915810 2476 RKALP 2480
Cdd:cd17649 446 RKALP 450
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
525-998 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 652.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd05930 81 EDSGAKLVLTDP------------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV 764
Cdd:cd05930 125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 765 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCYILDGNLE 842
Cdd:cd05930 205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 843 PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 922
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 923 EARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05930 365 EAALLAHPGVREAAVVAREdgdgEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
3052-3525 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 652.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd05930 81 EDSGAKLVLT------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDV 3291
Cdd:cd05930 125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:cd05930 205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 3449
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3450 EARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05930 365 EAALLAHPGVREAAVVAREdgdgEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
3041-3525 |
0e+00 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 652.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA--LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPS 3280
Cdd:cd17646 159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-EEGKDAVPIGRPIANL 3359
Cdd:cd17646 239 MLRVFLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRgPAETPSVPIGRPVPNT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd17646 318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGD-----WREalaaHLAASLPEYMVPAQWLALE 3510
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARAapagAARLVGYVVPAAGAAGpdtaaLRA----HLAERLPEYMVPAAFVVLD 473
|
490
....*....|....*
gi 2310915810 3511 RMPLSPNGKLDRKAL 3525
Cdd:cd17646 474 ALPLTANGKLDRAAL 488
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
2583-3005 |
0e+00 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 650.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAG----ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19531 81 VDLSGlpeaEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2739 EQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19531 161 RPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19531 241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYA 2978
Cdd:cd19531 321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
|
410 420
....*....|....*....|....*..
gi 2310915810 2979 TDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19531 401 TDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
514-998 |
0e+00 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 650.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 EYPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA--LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS 753
Cdd:cd17646 159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 754 MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-EEGKDTVPIGRPIGNL 832
Cdd:cd17646 239 MLRVFLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRgPAETPSVPIGRPVPNT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd17646 318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 913 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGD-----WREalaaHLAASLPEYMVPAQWLALE 983
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARAapagAARLVGYVVPAAGAAGpdtaaLRA----HLAERLPEYMVPAAFVVLD 473
|
490
....*....|....*
gi 2310915810 984 RMPLSPNGKLDRKAL 998
Cdd:cd17646 474 ALPLTANGKLDRAAL 488
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
52-478 |
0e+00 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 649.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPrgaddSLAQAPLQR-----PLEV 126
Cdd:cd19531 4 LSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFV-----EVDGEPVQVilpplPLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19531 79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 207 TGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:cd19531 159 AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:cd19531 239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYA 446
Cdd:cd19531 319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALEL---PGLTVEPLEVDSGTAKFDLTLSLTETDGGLRG 395
|
410 420 430
....*....|....*....|....*....|..
gi 2310915810 447 ALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19531 396 SLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
515-1002 |
0e+00 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 566.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 595 YPEERQAYMLEDSGVQLLLSQSHLKLPLAqGVQRIDLDQADAWLENHAENNPgIELNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIA-FIGLIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPKGVMIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 675 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSM 754
Cdd:cd17655 159 HRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 755 LQaFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEAAIDVTHWTCVEEG--KDTVPIGRPIGN 831
Cdd:cd17655 239 LK-LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETdqQVSVPIGKPLGN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd17655 318 TRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 912 LRGLRIELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESE--GGDWREalaaHLAASLPEYMVPAQWLALERM 985
Cdd:cd17655 398 IRGYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEKElpVAQLRE----FLARELPDYMIPSYFIKLDEI 473
|
490
....*....|....*..
gi 2310915810 986 PLSPNGKLDRKALPAPE 1002
Cdd:cd17655 474 PLTPNGKVDRKALPEPD 490
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
4551-5040 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 563.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRahlllthshllerlpipeglsclsvdreeewagfpahdPEVAL-HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd05930 81 EDSG--------------------------------------AKLVLtDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLAEHA 4788
Cdd:cd05930 123 LWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdPEALADLLAEEGITVLHLTPSLLRLLLQEL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 ErDGNPPPVRVYCFGGDAVaqaSYDLA--WRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAaYMPIGTLLGNRSGY 4865
Cdd:cd05930 203 E-LAALPSLRLVLVGGEAL---PPDLVrrWRELLPGaRLVNLYGPTEATVDATYYRVPPDDEEDG-RVPIGRPIPNTRVY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05930 278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd05930 357 YRIELGEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDE--------EELRAHLAERLPDYMVPSAFVVL 428
|
490
....*....|....*.
gi 2310915810 5025 ARMPLTPNGKLDRKGL 5040
Cdd:cd05930 429 DALPLTPNGKVDRKAL 444
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
4087-4504 |
2.53e-180 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 561.05 E-value: 2.53e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQLPF 4165
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEG-LGEPLQVVLKDRKLPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAANRDAALLALAAAER--ERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA--- 4240
Cdd:cd19543 80 RELDLSHLSEAEQEAELEALAEEdrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 -GRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGlTSANGVGEHLREVDATATARLRDFAR 4319
Cdd:cd19543 160 eGQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADA-DGSYEPGEVSFELSAELTARLQELAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4320 RHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLAL 4399
Cdd:cd19543 239 QHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4400 REQEHTPLFELQRWAGfGGEAVFDNLLVFENYPVDEVLER-SSAGGVRFGAVAMHEQTNYPLALALGGGDSLSLQFSYDR 4478
Cdd:cd19543 319 REHEYVPLYEIQAWSE-GKQALFDHLLVFENYPVDESLEEeQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDA 397
|
410 420
....*....|....*....|....*.
gi 2310915810 4479 GLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19543 398 EVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
3042-3528 |
5.52e-179 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 560.41 E-value: 5.52e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLA--QGVQRIDLDRGapwfedYSEANPDIHLDGE--NLAYVIYTSGSTGKPKG 3197
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIAfiGLIDLLDEDTI------YHEESENLEPVSKsdDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3198 AGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHF 3277
Cdd:cd17655 155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 VPSMLQaFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEAAIDVTHWTCVEEG--KDAVPIGR 3354
Cdd:cd17655 235 TPAHLK-LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETdqQVSVPIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRID 3434
Cdd:cd17655 314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESE--SGDWREalaaHLAASLPEYMVPAQWLA 3508
Cdd:cd17655 394 HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEKElpVAQLRE----FLARELPDYMIPSYFIK 469
|
490 500
....*....|....*....|
gi 2310915810 3509 LERMPLSPNGKLDRKALPRP 3528
Cdd:cd17655 470 LDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
2002-2479 |
8.76e-178 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 554.83 E-value: 8.76e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd05930 81 EDSGAKLVLTD------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQW-SAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd05930 125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRkDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRiAVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAVITPLAWHCRAQE--GGAPAIGRALGARRACILDAAL 2316
Cdd:cd05930 205 AALP-SLRLVLVGGEALPPDLVRRwrELLPGARLVNLYGPTEATVDATYYRVPPDDeeDGRVPIGRPIPNTRVYVLDENL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIG 2396
Cdd:cd05930 284 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP-GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAReDGDGEKRLVAYVVPDEG--GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440
|
....
gi 2310915810 2476 RKAL 2479
Cdd:cd05930 441 RKAL 444
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1097-1516 |
4.98e-174 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 543.38 E-value: 4.98e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEqAGEPLWRRQ 1176
Cdd:cd19534 1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRG-DVEELFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AGS------EEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLG- 1249
Cdd:cd19534 80 VVDlsslaqAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 --PRSSSYQTWSRHLHEQAG--ARLDELDYWQAQLHDAPHALPCENPHgalENRHERKLVLTLDAERTRQLLQEAPAAYR 1325
Cdd:cd19534 160 plPSKTSFQTWAELLAEYAQspALLEELAYWRELPAADYWGLPKDPEQ---TYGDARTVSFTLDEEETEALLQEANAAYR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1326 TQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAA--DLGESLKAIKEQLRGVP 1403
Cdd:cd19534 237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLRRIP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1404 DKGVGYGLLRYLAGEEAAtRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELS 1483
Cdd:cd19534 317 NKGIGYGILRYLTPEGTK-RLAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGGQLV 395
|
410 420 430
....*....|....*....|....*....|...
gi 2310915810 1484 LHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:cd19534 396 ITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
3624-4051 |
4.50e-173 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 540.69 E-value: 4.50e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3624 ETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGgalLWR 3703
Cdd:cd19534 1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEE---LFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3704 AEAVD------RQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGE 3777
Cdd:cd19534 78 LEVVDlsslaqAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3778 APRLPGKTSpFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQgalEQRFATSVQSRFDRSLTERLLKQAPA 3857
Cdd:cd19534 158 PIPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQ---TYGDARTVSFTLDEEETEALLQEANA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3858 AYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLSPVA--DLGESLKAIKEQLR 3935
Cdd:cd19534 234 AYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3936 AIPDKGLGYGLLRYLAGEESARvLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDG 4015
Cdd:cd19534 314 RIPNKGIGYGILRYLTPEGTKR-LAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGG 392
|
410 420 430
....*....|....*....|....*....|....*.
gi 2310915810 4016 ELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFC 4051
Cdd:cd19534 393 QLVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
3042-3525 |
2.30e-168 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 529.47 E-value: 2.30e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALD---AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSnRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLhFVPSM 3281
Cdd:cd12117 158 HRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHW--TCVEEGKDAVPIGRPIANL 3359
Cdd:cd12117 236 LFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHvvTELDEVAGSIPIGRPIANT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd12117 316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd12117 396 RGFRIELGEIEAALRAHPGVREAVVVVREDaggdKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLT 473
|
490
....*....|
gi 2310915810 3516 PNGKLDRKAL 3525
Cdd:cd12117 474 ANGKVDRRAL 483
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
515-998 |
7.26e-168 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 527.92 E-value: 7.26e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 595 YPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADawlENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEAL---DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 675 HSALSnRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSM 754
Cdd:cd12117 158 HRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 755 LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHW--TCVEEGKDTVPIGRPIGNL 832
Cdd:cd12117 236 LFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHvvTELDEVAGSIPIGRPIANT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd12117 316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 913 RGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLS 988
Cdd:cd12117 396 RGFRIELGEIEAALRAHPGVREAVVVVREDaggdKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLT 473
|
490
....*....|
gi 2310915810 989 PNGKLDRKAL 998
Cdd:cd12117 474 ANGKVDRRAL 483
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1552-1956 |
1.82e-166 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 521.38 E-value: 1.82e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQATLEL 1629
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGsGAYVEQMVITLeGPLDPDRFRAAWQAVVDRHPILRTSFVW-EGLGEPLQVVLKDRKLPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RLAPPGSDP--------QRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA--- 1698
Cdd:cd19543 80 RELDLSHLSeaeqeaelEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1699 -GQEVA-ATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQARTEQ---PGQGEHLRELDPQTTRQLASFAQG 1773
Cdd:cd19543 160 eGQPPSlPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADAdgsYEPGEVSFELSAELTARLQELARQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1774 QKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALR 1853
Cdd:cd19543 240 HGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1854 EHEHTPLYDIQRWAGhGGEALFDSILVFENFPVAEALR--QAPADLEFSTPSNHEQTNYPLTLGVTLGERLSLQYVYARR 1931
Cdd:cd19543 320 EHEYVPLYEIQAWSE-GKQALFDHLLVFENYPVDESLEeeQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAE 398
|
410 420
....*....|....*....|....*
gi 2310915810 1932 DFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19543 399 VFDEATIERLLGHLRRVLEQVAANP 423
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
3066-3464 |
2.30e-163 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 511.81 E-value: 2.30e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSH 3144
Cdd:TIGR01733 2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3145 LKLPLAQGVQRIDLDRGAPWFEDYSEAN---PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 3221
Cdd:TIGR01733 82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3222 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 3300
Cdd:TIGR01733 162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3301 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:TIGR01733 241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400
|
....*....
gi 2310915810 3456 HPWVREAAV 3464
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
3044-3526 |
3.16e-163 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 514.97 E-value: 3.16e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSQSHLkLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPAL-AGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQ 3283
Cdd:cd17651 160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3284 AFLQDEDVASCTS--LKRIVCSGEALPADAQ-QQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGK--DAVPIGRPIAN 3358
Cdd:cd17651 240 ALAEHGRPLGVRLaaLRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAwpAPPPIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 LACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:cd17651 320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPL 3514
Cdd:cd17651 400 IRGFRIELGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
|
490
....*....|..
gi 2310915810 3515 SPNGKLDRKALP 3526
Cdd:cd17651 480 TPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
539-937 |
1.23e-162 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 509.88 E-value: 1.23e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSH 617
Cdd:TIGR01733 2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 618 LKLPLAQGVQRIDLDQADAWLENHAENN---PGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:TIGR01733 82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 695 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 773
Cdd:TIGR01733 162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 774 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:TIGR01733 241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 851 ELYLAGRGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400
|
....*....
gi 2310915810 929 HPWVREAAV 937
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
3052-3526 |
2.60e-162 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 510.76 E-value: 2.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17649 81 EDSGAGLLLTH-----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD-ED 3290
Cdd:cd17649 126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3291 VASCT--SLKRIVCSGEALPAD--AQQQVFAKLpqagLYNLYGPTEAAIDVTHWTCVEEGKDA---VPIGRPIANLACYI 3363
Cdd:cd17649 206 TGDGRppSLRLYIFGGEALSPEllRRWLKAPVR----LFNAYGPTEATVTPLVWKCEAGAARAgasMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 3442
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3443 RIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLE--SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 3517
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRaaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441
|
....*....
gi 2310915810 3518 GKLDRKALP 3526
Cdd:cd17649 442 GKLDRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
517-999 |
3.83e-162 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 511.89 E-value: 3.83e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 597 EERQAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPAL-AGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 677 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 756
Cdd:cd17651 160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 757 AFLQDEDVASCTS--LKRIVCSGEALPADAQ-QQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGK--DTVPIGRPIGN 831
Cdd:cd17651 240 ALAEHGRPLGVRLaaLRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAwpAPPPIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd17651 320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 912 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPL 987
Cdd:cd17651 400 IRGFRIELGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
|
490
....*....|..
gi 2310915810 988 SPNGKLDRKALP 999
Cdd:cd17651 480 TPNGKLDRRALP 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
525-999 |
2.34e-161 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 508.06 E-value: 2.34e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17649 81 EDSGAGLLLTH-----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD-ED 763
Cdd:cd17649 126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 764 VASCT--SLKRIVCSGEALPAD--AQQQVFAKLpqagLYNLYGPTEAAIDVTHWTCVEEGKD---TVPIGRPIGNLGCYI 836
Cdd:cd17649 206 TGDGRppSLRLYIFGGEALSPEllRRWLKAPVR----LFNAYGPTEATVTPLVWKCEAGAARagaSMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 916 RIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLE--SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRaaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441
|
....*....
gi 2310915810 991 GKLDRKALP 999
Cdd:cd17649 442 GKLDRKALP 450
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
4121-5133 |
2.67e-161 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 538.86 E-value: 2.67e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4121 LDIPRFRAAWQSALDRHAILRSGFAwqGELQQPLQIVYRQRQLPFAE-EDLSQAANRDAALLALAAAERERGFELQRA-P 4198
Cdd:PRK10252 42 LDAPLLARAVVAGLAEADTLRMRFT--EDNGEVWQWVDPALTFPLPEiIDLRTQPDPHAAAQALMQADLQQDLRVDSGkP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4199 LLRLLLVKTAEgEHHLIY-THHHILLDGWSNAQLLSEVLESYAGRSPEQPRDGR--------YSDYIAWLQRQDAAATEA 4269
Cdd:PRK10252 120 LVFHQLIQLGD-NRWYWYqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASpftpfadvVEEYQRYRASEAWQRDAA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4270 FWREQMAALDEPTRLVEALAqPGLTSANGVGEHLREVDATATARLRdfARRHQVTLNTLVQAGWALLLQRYTGQHTVVFG 4349
Cdd:PRK10252 199 FWAEQRRQLPPPASLSPAPL-PGRSASADILRLKLEFTDGAFRQLA--AQASGVQRPDLALALVALWLGRLCGRMDYAAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4350 ATVSGRpadLPGVENQV-GLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGF--GGEAVFD--- 4423
Cdd:PRK10252 276 FIFMRR---LGSAALTAtGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGpvl 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4424 NLLVFENYP----VDEVLERSSAGGVRfgavamheqtNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEA 4499
Cdd:PRK10252 353 NIKVFDYQLdfpgVQAQTHTLATGPVN----------DLELALFPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQ 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4500 FAEHPQRRLVDLQMLEKAELSAIgAIWNRSDSGYPATPLVhQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHAL 4579
Cdd:PRK10252 423 FAADPALLCGDVDILLPGEYAQL-AQVNATAVEIPETTLS-ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLL 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4580 IARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSV 4659
Cdd:PRK10252 501 RERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCY 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4660 DreEEWAGfPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGW 4739
Cdd:PRK10252 581 N--APLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEF 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4740 MHPLINGARVLI------RDdslwlPERTYAEMHRHGVTVGVFPP----VYLQQLAEHAERDGNPPPVRVYCfGGDAVAQ 4809
Cdd:PRK10252 658 FWPFIAGAKLVMaepeahRD-----PLAMQQFFAEYGVTTTHFVPsmlaAFVASLTPEGARQSCASLRQVFC-SGEALPA 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4810 ASYDLaWRALKPKYLFNGYGPTETVVTPLLWKARAGD--ACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGE 4887
Cdd:PRK10252 732 DLCRE-WQQLTGAPLHNLYGPTEAAVDVSWYPAFGEElaAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGI 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4888 GVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PRK10252 811 QLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAV 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4968 VVAQ-------PGAVGQQLVGYVVAQEPAVADSPeaqaecraQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK10252 890 THACvinqaaaTGGDARQLVGYLVSQSGLPLDTS--------ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5041 PQPDASlLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQA 5120
Cdd:PRK10252 962 PLPELK-AQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAK 1040
|
1050
....*....|...
gi 2310915810 5121 YAELAAAQTSSND 5133
Cdd:PRK10252 1041 LATLLDAEEDESR 1053
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1583-2567 |
1.59e-160 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 536.55 E-value: 1.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATL------ELRLAPpgsDPQRQA----EAEREAGFDP 1652
Cdd:PRK10252 40 GELDAPLLARAVVAGLAEADTLRMRFTEDNG--EVWQWVDPALTFplpeiiDLRTQP---DPHAAAqalmQADLQQDLRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1653 ARA-PLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG---------------QEVAATVGRYRDYIGWL 1716
Cdd:PRK10252 115 DSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrgeptpaspftpfADVVEEYQRYRASEAWQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1717 QGRDamatefFWRDRLASLEMPTRLARQARTEQPGQGEHLR---ELDPQTTRQLASFAQGQKVT--LNTLVqAAWallLQ 1791
Cdd:PRK10252 195 RDAA------FWAEQRRQLPPPASLSPAPLPGRSASADILRlklEFTDGAFRQLAAQASGVQRPdlALALV-ALW---LG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1792 RHCGQETVAFGATVAGRpaeLPGIEAQI-GLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGH- 1869
Cdd:PRK10252 265 RLCGRMDYAAGFIFMRR---LGSAALTAtGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRa 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1870 -GGEALFDSILVFENFPVAEALRQAPADLEF--STPSNHeqtnypLTLGVTLGERLSLqyvyaRRDFDAA----DIAELD 1942
Cdd:PRK10252 342 aGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTlaTGPVND------LELALFPDEHGGL-----SIEILANpqryDEATLI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1943 RH---LLHLLQRMAETPQAALGELALLDAGERQEaLRDWQAPLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAEL 2019
Cdd:PRK10252 411 AHaerLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2020 DMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL 2099
Cdd:PRK10252 490 REQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRF 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2100 PCPAEVErlPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFAS 2179
Cdd:PRK10252 570 ADVPDLT--SLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTP 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2180 ISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPP----AYLQQQAEELRHAGRRiAVRTCILGG 2254
Cdd:PRK10252 648 CSFDVSVWEFFWPFIAGAKlVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPsmlaAFVASLTPEGARQSCA-SLRQVFCSG 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 EAWDASL--LTQQAVQAEAwFNAYGPTEAVITPLAWHCRAQEGGAPA-----IGRALGARRACILDAALQPCAPGMIGEL 2327
Cdd:PRK10252 727 EALPADLcrEWQQLTGAPL-HNLYGPTEAAVDVSWYPAFGEELAAVRgssvpIGYPVWNTGLRILDARMRPVPPGVAGDL 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2328 YIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:PRK10252 806 YLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPD 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2408 VAEAAVVAL-------DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PRK10252 885 VEQAVTHACvinqaaaTGGDARQLVGYLVSQSGLPLD--TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALP 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2481 KVDAAARRqAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADF 2560
Cdd:PRK10252 963 LPELKAQV-PGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKL 1041
|
....*..
gi 2310915810 2561 AASLESQ 2567
Cdd:PRK10252 1042 ATLLDAE 1048
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1992-2479 |
3.34e-158 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 500.65 E-value: 3.34e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1992 AAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2072 YPAERLAYMLRDSGARWLICQETLAERLpcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVS 2151
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTTADLAARL--PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2152 QAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDA-GQWSAQHLADEVERHAVTILDLPPAY 2230
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPgGHRDPAYLAALIREHGVTTCHFVPSM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEELRhAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF-NAYGPTEAVITPLAWHCRAQEGGAP-AIGRALGARR 2308
Cdd:cd17646 240 LRVFLAEPA-AGSCASLRRVFCSGEALPPELAARFLALPGAELhNLYGPTEAAIDVTHWPVRGPAETPSvPIGRPVPNTR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17646 319 LYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF-GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARaAPAGAARLVGYVVPAAGAAGPD-TAALRAHLAERLPEYMVPAAFVVLDALP 476
|
490
....*....|..
gi 2310915810 2468 LNANGKLDRKAL 2479
Cdd:cd17646 477 LTANGKLDRAAL 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1994-2480 |
5.20e-157 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 497.25 E-value: 5.20e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELA-VELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17651 160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATlVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 QQAEELRHAGRRI-AVRTCILGGEAWDASLLTQQAVQAE---AWFNAYGPTEA-VITplAWHCRAQEGGAPA---IGRAL 2304
Cdd:cd17651 240 ALAEHGRPLGVRLaALRYLLTGGEQLVLTEDLREFCAGLpglRLHNHYGPTEThVVT--ALSLPGDPAAWPApppIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2305 GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGsGERLYRTGDLARYRVDGQVEYLGRADQ 2384
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLGRADD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2385 QIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamRGEDLLAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17651 397 QVKIRGFRIELGEIEAALARHPGVREAVVLAReDRPGEKRLVAYVVGDP--EAPVDAAELRAALATHLPEYMVPSAFVLL 474
|
490
....*....|....*..
gi 2310915810 2464 SSLPLNANGKLDRKALP 2480
Cdd:cd17651 475 DALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
3052-3525 |
1.45e-155 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 492.19 E-value: 1.45e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA---AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD--E 3289
Cdd:cd12116 158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAgwQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLkrivCSGEALPADAQQQVFAKLpqAGLYNLYGPTEAAIDVThWTCVEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:cd12116 238 GRAGLTAL----CGGEALPPDLAARLLSRV--GSLWNLYGPTETTIWST-AARVTAAAGPIPIGRPLANTQVYVLDAALR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 3448
Cdd:cd12116 311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3449 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd12116 391 IEAALAAHPGVAQAAVVVREdggDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
4540-5040 |
1.10e-154 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 490.25 E-value: 1.10e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4620 EYPRERLLYMMQDSRAHLLLTHSHLLERLPipeGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVA 4699
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLP---AGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4700 VSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFPP 4778
Cdd:cd17646 158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 VYLQQLAEHAERDGNPPPVRVYCfGGDAVAQASYDLaWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAayMPIGTL 4858
Cdd:cd17646 238 SMLRVFLAEPAAGSCASLRRVFC-SGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPS--VPIGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17646 314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGALEFLGRSD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQ-PGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMV 5017
Cdd:cd17646 393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARaAPAGAARLVGYVVPAAGAAGPDTAA-------LRAHLAERLPEYMV 465
|
490 500
....*....|....*....|...
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd17646 466 PAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
3052-3526 |
3.00e-154 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 486.76 E-value: 3.00e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17652 81 ADARPALLLTTP------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAfLQDEDV 3291
Cdd:cd17652 125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-LPPDDL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASctsLKRIVCSGEALPADAQQQvFAklPQAGLYNLYGPTEAAIDVThWTCVEEGKDAVPIGRPIANLACYILDGNLEPV 3371
Cdd:cd17652 204 PD---LRTLVVAGEACPAELVDR-WA--PGRRMINAYGPTETTVCAT-MAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3372 PVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3451 ARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 3526
Cdd:cd17652 357 AALTEHPGVAEAVVVVRDdrpgDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
525-998 |
3.54e-153 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 485.26 E-value: 3.54e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLenhAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAA---APAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD--E 762
Cdd:cd12116 158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAgwQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 763 DVASCTSLkrivCSGEALPADAQQQVFAKLpqAGLYNLYGPTEAAIDVThWTCVEEGKDTVPIGRPIGNLGCYILDGNLE 842
Cdd:cd12116 238 GRAGLTAL----CGGEALPPDLAARLLSRV--GSLWNLYGPTETTIWST-AARVTAAAGPIPIGRPLANTQVYVLDAALR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 843 PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 921
Cdd:cd12116 311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 922 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLES----EGGDWREalaaHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd12116 391 IEAALAAHPGVAQAAVVVREdggDRRLVAYVVLKAgaapDAAALRA----HLRATLPAYMVPSAFVRLDALPLTANGKLD 466
|
....
gi 2310915810 995 RKAL 998
Cdd:cd12116 467 RKAL 470
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1992-2479 |
3.89e-153 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 485.55 E-value: 3.89e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1992 AAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2072 YPAERLAYMLRDSGARWLICQETLAERLPCPaevERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVS 2151
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGL---EVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2152 QAALVAHCQaAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAY 2230
Cdd:cd12117 158 HRGVVRLVK-NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTlLDPDALGALIAEEGVTVLWLTAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEElrHAGRRIAVRTCILGGEAWDASLLtQQAVQAEA---WFNAYGPTE-------AVITPLawhcrAQEGGAPAI 2300
Cdd:cd12117 237 FNQLADE--DPECFAGLRELLTGGEVVSPPHV-RRVLAACPglrLVNGYGPTEnttfttsHVVTEL-----DEVAGSIPI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2301 GRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLG 2380
Cdd:cd12117 309 GRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF-GPGERLYRTGDLARWLPDGRLEFLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2381 RADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGP-LLAAYLVGRDAMRgedlLAELRTWLAGRLPAYMQPTA 2459
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDkRLVAYVVAEGALD----AAELRAFLRERLPAYMVPAA 463
|
490 500
....*....|....*....|
gi 2310915810 2460 WQVLSSLPLNANGKLDRKAL 2479
Cdd:cd12117 464 FVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
525-999 |
6.82e-153 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 482.91 E-value: 6.82e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17652 81 ADARPALLLTTP------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAfLQDEDV 764
Cdd:cd17652 125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-LPPDDL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 765 ASctsLKRIVCSGEALPADAQQQvFAklPQAGLYNLYGPTEAAIDVThWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPV 844
Cdd:cd17652 204 PD---LRTLVVAGEACPAELVDR-WA--PGRRMINAYGPTETTVCAT-MAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 845 PVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 924 ARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 999
Cdd:cd17652 357 AALTEHPGVAEAVVVVRDdrpgDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
4541-5040 |
1.69e-152 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 484.01 E-value: 1.69e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAHLLLTHSHLLERLpipeGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAV 4700
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRA----GGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4701 SHGPLIAhiVATGERY-EMTPEDCELHFMSFAFDGS-HEGWMhPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTV---- 4773
Cdd:cd12117 157 THRGVVR--LVKNTNYvTLGPDDRVLQTSPLAFDAStFEIWG-ALLNGARlVLAPKGTLLDPDALGALIAEEGVTVlwlt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4774 -GVFppvylQQLAEHAER--DGnpppVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGA 4850
Cdd:cd12117 234 aALF-----NQLADEDPEcfAG----LRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4851 AyMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGV 4930
Cdd:cd12117 305 S-IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPDGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4931 VDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVAdspeaqaecrAQLKTALR 5009
Cdd:cd12117 383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGdKRLVAYVVAEGALDA----------AELRAFLR 452
|
490 500 510
....*....|....*....|....*....|.
gi 2310915810 5010 ERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12117 453 ERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1994-2483 |
2.20e-151 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 481.06 E-value: 2.20e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRplPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLE--PVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17655 161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 qqaeELRHAGRRIA--VRTCILGGEAWDASL---LTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQ--EGGAPAIGRALG 2305
Cdd:cd17655 241 ----LLDAADDSEGlsLKHLIVGGEALSTELakkIIELFGTNPTITNAYGPTETTVDASIYQYEPEtdQQVSVPIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:cd17655 317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFV-PGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRdamrgEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARkDEQGQNYLCAYIVSE-----KELpVAQLREFLARELPDYMIPSYFIKL 470
|
490 500
....*....|....*....|
gi 2310915810 2464 SSLPLNANGKLDRKALPKVD 2483
Cdd:cd17655 471 DEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
4541-5044 |
2.29e-151 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 481.06 E-value: 2.29e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAhlllTHSHLLERLPIPEGLSCLsVDREEEWAG--FPAHDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:cd17655 81 YPEERIQYILEDSGA----DILLTQSHLQPPIAFIGL-IDLLDEDTIyhEESENLEPVSKSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFP 4777
Cdd:cd17655 156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEhaERDGNPPPVRVYCFGGDAVaqaSYDLAWRALKPKY----LFNGYGPTETVVTPLLWKARAGDACGaAYM 4853
Cdd:cd17655 236 PAHLKLLDA--ADDSEGLSLKHLIVGGEAL---STELAKKIIELFGtnptITNAYGPTETTVDASIYQYEPETDQQ-VSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4854 PIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDY 4933
Cdd:cd17655 310 PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAVAdspeaqaecrAQLKTALRERL 5012
Cdd:cd17655 389 LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNyLCAYIVSEKELPV----------AQLREFLAREL 458
|
490 500 510
....*....|....*....|....*....|..
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDRKGLPQPD 5044
Cdd:cd17655 459 PDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
2002-2479 |
4.43e-151 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 479.09 E-value: 4.43e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLPCPAeveRLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGL---PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAG-QWSAQHLADEVERHAVTILDLPPAYLQQ--QAEEL 2238
Cdd:cd12116 158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMllDAGWQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2239 RHAGRRIAVrtcilGGEAWDASLLTQQAVQAEAWFNAYGPTEAVItplaWHCRAQ---EGGAPAIGRALGARRACILDAA 2315
Cdd:cd12116 238 GRAGLTALC-----GGEALPPDLAARLLSRVGSLWNLYGPTETTI----WSTAARvtaAAGPIPIGRPLANTQVYVLDAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd12116 389 GEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPD--AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466
|
....
gi 2310915810 2476 RKAL 2479
Cdd:cd12116 467 RKAL 470
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
2002-2480 |
1.09e-150 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 476.74 E-value: 1.09e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17652 81 ADARPALLLTT------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAYLQQ-QAEELr 2239
Cdd:cd17652 125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEElLPGEPLADLLREHRITHVTLPPAALAAlPPDDL- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2240 hagrrIAVRTCILGGEAWDASLLTQQAVqAEAWFNAYGPTEAVITPLAWHCRAqEGGAPAIGRALGARRACILDAALQPC 2319
Cdd:cd17652 204 -----PDLRTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCATMAGPLP-GGGVPPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2320 APGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIE 2399
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2400 SQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKA 2478
Cdd:cd17652 357 AALTEHPGVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPTA--AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
..
gi 2310915810 2479 LP 2480
Cdd:cd17652 435 LP 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
3040-3525 |
4.13e-150 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 475.65 E-value: 4.13e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQSHlklplaqgvqridldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAG 3199
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD------------------------------------DLAYVIYTSGSTGRPKGVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd12115 125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3280 SMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaaiDVTHWTCVE---EGKDAVPIGRPI 3356
Cdd:cd12115 200 SAAAELLRHDALP--ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYSTVAPvppGASGEVSIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:cd12115 275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
|
490
....*....|...
gi 2310915810 3513 PLSPNGKLDRKAL 3525
Cdd:cd12115 435 PLTPNGKIDRSAL 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
4551-5041 |
1.29e-149 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 473.66 E-value: 1.29e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRahlllthshllerlpipeglsclsvdreeewagfpahdPEVAL-HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd17652 81 ADAR--------------------------------------PALLLtTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEM-HRHGVTVGVFPPVYLQQLAEha 4788
Cdd:cd17652 123 AAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLlREHRITHVTLPPAALAALPP-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 erdGNPPPVRVYCFGGDAVAQAsydLAWRALKPKYLFNGYGPTETVVtpllWKARAGDACGAAYMPIGTLLGNRSGYILD 4868
Cdd:cd17652 201 ---DDLPDLRTLVVAGEACPAE---LVDRWAPGRRMINAYGPTETTV----CATMAGPLPGGGVPPIGRPVPGTRVYVLD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd17652 271 ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQ-PGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd17652 351 ELGEVEAALTEHPGVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPT--------AAELRAHLAERLPGYMVPAAFVVLDAL 422
|
490
....*....|....
gi 2310915810 5028 PLTPNGKLDRKGLP 5041
Cdd:cd17652 423 PLTPNGKLDRRALP 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
513-998 |
7.52e-149 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 471.80 E-value: 7.52e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PEYPEERQAYMLEDSGVQLLLSQSHlklplaqgvqridldqadawlenhaennpgielngeNLAYVIYTSGSTGKPKGAG 672
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD------------------------------------DLAYVIYTSGSTGRPKGVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVP 752
Cdd:cd12115 125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 753 SMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaaiDVTHWTCVE---EGKDTVPIGRPI 829
Cdd:cd12115 200 SAAAELLRHDALP--ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYSTVAPvppGASGEVSIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 830 GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:cd12115 275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 910 VKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERM 985
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
|
490
....*....|...
gi 2310915810 986 PLSPNGKLDRKAL 998
Cdd:cd12115 435 PLTPNGKIDRSAL 447
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
4551-5040 |
1.33e-148 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 471.41 E-value: 1.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSrahlllthshllerlpipeGLSCLSVDreeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17643 81 ADS-------------------GPSLLLTD------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGS-HEGWMhPLINGARVLIRD-DSLWLPERTYAEMHRHGVTV-GVFPPVYLQQLAEH 4787
Cdd:cd17643 124 ATQRWFGFNEDDVWTLFHSYAFDFSvWEIWG-ALLHGGRLVVVPyEVARSPEDFARLLRDEGVTVlNQTPSAFYQLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4788 AERDGNPPPVRVYCFGGDAvaqasydLAWRALKPKY---------LFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTL 4858
Cdd:cd17643 203 DRDGRDPLALRYVIFGGEA-------LEAAMLRPWAgrfgldrpqLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17643 276 LPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQepavadspEAQAECRAQLKTALRERLPEYMV 5017
Cdd:cd17643 356 EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTrLVAYVVAD--------DGAAADIAELRALLKELLPDYMV 427
|
490 500
....*....|....*....|...
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd17643 428 PARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
4543-5041 |
2.32e-148 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 472.21 E-value: 2.32e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHSHLLERLPIPEGLscLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVA--VTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAHIVATGERYEMTPEDCELHFMSFAFDGS-HEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSvQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAEHAERDGNPPP-VRVYCFGGDAVAQASYDLAW-RALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAyMPIGTLL 4859
Cdd:cd17651 239 RALAEHGRPLGVRLAaLRYLLTGGEQLVLTEDLREFcAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAP-PPIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4860 GNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELEFLGRADD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaecrAQLKTALRERLPEYMVP 5018
Cdd:cd17651 397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGeKRLVAYVVGDPEAPVDA--------AELRAALATHLPEYMVP 468
|
490 500
....*....|....*....|...
gi 2310915810 5019 SHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17651 469 SAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
513-999 |
1.37e-147 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 468.84 E-value: 1.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PEYPEERQAYMLEDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielnGENLAYVIYTSGSTGKPKGAG 672
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVP 752
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 753 SMLQAFLQDEDVASCT---SLKRIVCSGEA-LPADAQQ--QVFAKLPQagLYNLYGPTEAAIDVT--HWTCVEEGKDT-V 823
Cdd:cd17644 206 AYWHLLVLELLLSTIDlpsSLRLVIVGGEAvQPELVRQwqKNVGNFIQ--LINVYGPTEATIAATvcRLTQLTERNITsV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 824 PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA--GERMYRTGDLARYRADGVIE 901
Cdd:cd17644 284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 902 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESEGGDWREALAAHLAASLPEYMVPA 977
Cdd:cd17644 364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
|
490 500
....*....|....*....|..
gi 2310915810 978 QWLALERMPLSPNGKLDRKALP 999
Cdd:cd17644 444 AFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
3040-3526 |
1.65e-147 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 468.84 E-value: 1.65e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQshlklplaqgvqridldrgapwfedyseanpdihldGENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3280 SMLQAFLQDEDVASCT---SLKRIVCSGEA-LPADAQQ--QVFAKLPQagLYNLYGPTEAAIDVT--HWTCVEEGK-DAV 3350
Cdd:cd17644 206 AYWHLLVLELLLSTIDlpsSLRLVIVGGEAvQPELVRQwqKNVGNFIQ--LINVYGPTEATIAATvcRLTQLTERNiTSV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3351 PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA--GERMYRTGDLARYRADGVIE 3428
Cdd:cd17644 284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3429 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESESGDWREALAAHLAASLPEYMVPA 3504
Cdd:cd17644 364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
|
490 500
....*....|....*....|..
gi 2310915810 3505 QWLALERMPLSPNGKLDRKALP 3526
Cdd:cd17644 444 AFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
3052-3525 |
1.75e-147 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 467.94 E-value: 1.75e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17643 81 ADSGPSLLLT------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DE 3289
Cdd:cd17643 125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaaDR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLKRIVCSGEALPADAQQQVFAK--LPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDAVPIGRPIANLACYIL 3364
Cdd:cd17643 205 DGRDPLALRYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAAdlpAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3365 DGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVREDEPgdtrLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444
|
....*.
gi 2310915810 3520 LDRKAL 3525
Cdd:cd17643 445 LDRAAL 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
525-998 |
7.44e-147 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 466.40 E-value: 7.44e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielnGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17643 81 ADSGPSLLLTD------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DE 762
Cdd:cd17643 125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaaDR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 763 DVASCTSLKRIVCSGEALPADAQQQVFAK--LPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDTVPIGRPIGNLGCYIL 837
Cdd:cd17643 205 DGRDPLALRYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAAdlpAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 838 DGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 917 IELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVREDEPgdtrLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444
|
....*.
gi 2310915810 993 LDRKAL 998
Cdd:cd17643 445 LDRAAL 450
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
2584-3005 |
5.24e-146 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 463.05 E-value: 5.24e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLE 2663
Cdd:cd19540 2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2664 dCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTL 2743
Cdd:cd19540 82 -VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2744 APLKLQYADYAAWHRAWLDS-----GEGARQLDYWRERLgAEQP-VLELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19540 161 APLPVQYADYALWQRELLGDeddpdSLAARQLAYWRETL-AGLPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:cd19540 240 LAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLAL------DTWETPDGL 2971
Cdd:cd19540 320 AFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFtlterrDADGAPAGL 399
|
410 420 430
....*....|....*....|....*....|....
gi 2310915810 2972 GAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19540 400 TGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
4551-5040 |
1.87e-143 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 457.14 E-value: 1.87e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLTHSHLLERLPipegLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd12116 81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd12116 157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRdPEALARLIEAHSITVMQATPATWRMLLDAGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4790 RdgNPPPVRVYCfGGDAVAQasyDLAWRAL-KPKYLFNGYGPTETVVtpllWKARAGDACGAAYMPIGTLLGNRSGYILD 4868
Cdd:cd12116 237 Q--GRAGLTALC-GGEALPP---DLAARLLsRVGSLWNLYGPTETTI----WSTAARVTAAAGPIPIGRPLANTQVYVLD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd12116 307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMP 5028
Cdd:cd12116 387 ELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPD--------AAALRAHLRATLPAYMVPSAFVRLDALP 458
|
490
....*....|..
gi 2310915810 5029 LTPNGKLDRKGL 5040
Cdd:cd12116 459 LTANGKLDRKAL 470
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
2015-2413 |
5.16e-141 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 447.87 E-value: 5.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAERLPCPAEVERLP---LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP 2170
Cdd:TIGR01733 81 ALASRLAGLVLPVILLdplELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 GDCQLQFASISFDAAAEQLFVPLLAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiaVR 2248
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVppEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALAS--LR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 TCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAW-HCRAQEGGAPA--IGRALGARRACILDAALQPCAPGM 2323
Cdd:TIGR01733 239 LVILGGEALTPALVDrwRARGPGARLINLYGPTETTVWSTATlVDPDDAPRESPvpIGRPLANTRLYVLDDDLRPVPVGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2324 IGELYIGGQCLARGYLGRPGQTAERFVADPFSGS-GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
|
410
....*....|.
gi 2310915810 2403 LAHPYVAEAAV 2413
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
2002-2479 |
5.84e-141 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 449.45 E-value: 5.84e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIcqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17643 81 ADSGPSLLL------------------------------TDP------DDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQW---SAQHLADEVERHAVTILD-LPPAYLQQQAEE 2237
Cdd:cd17643 125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVP--YEvarSPEDFARLLRDEGVTVLNqTPSAFYQLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2238 LRHAGRRIAVRTCILGGEAWDASLLTQQAV----QAEAWFNAYGPTEAviTPLAWHCRAQEGGAPA-----IGRALGARR 2308
Cdd:cd17643 203 DRDGRDPLALRYVIFGGEALEAAMLRPWAGrfglDRPQLVNMYGITET--TVHVTFRPLDAADLPAaaaspIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGV-GGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVIVREDEpGDTRLVAYVVADDG--AAADIAELRALLKELLPDYMVPARYVPLDALP 438
|
490
....*....|..
gi 2310915810 2468 LNANGKLDRKAL 2479
Cdd:cd17643 439 LTVNGKLDRAAL 450
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
52-478 |
3.37e-140 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 446.48 E-value: 3.37e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaqAPLQRPLEVAfEDC 131
Cdd:cd19540 4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDG-----GPYQVVLPAA-EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 132 SGLP-----EAEQEARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19540 78 PDLTvvdvtEDELAARLAEAARR----GFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 207 TGAEPGLPALPIQYADYALWQRSWL-----EAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19540 154 AGRAPDWAPLPVQYADYALWQRELLgdeddPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:cd19540 234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 362 KDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVAdieALDSVAGLSFGQLDWKSRTTQFDLSL------ 435
Cdd:cd19540 314 RETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAA---ATLELPGLTVEPVPVDTGVAKFDLSFtlterr 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2310915810 436 DTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19540 391 DADGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
524-999 |
1.96e-138 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 443.45 E-value: 1.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 524 TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 604 LEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENhaENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQED--TSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 684 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSMLQAFLQDE- 762
Cdd:cd17656 159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSEr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 763 ----DVASCtsLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGK--DTVPIGRPIGNLGCYI 836
Cdd:cd17656 238 efinRFPTC--VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEipELPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 917 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVMEQELNI--SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
....*..
gi 2310915810 993 LDRKALP 999
Cdd:cd17656 473 VDRKALP 479
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
3051-3526 |
5.48e-138 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 441.91 E-value: 5.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3051 TPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDYSeaNPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 3210
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTS--NIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3211 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLhFVPSMLQAFLQDE- 3289
Cdd:cd17656 159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSEr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 ----DVASCtsLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGK--DAVPIGRPIANLACYI 3363
Cdd:cd17656 238 efinRFPTC--VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEipELPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVMEQELNI--SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
....*..
gi 2310915810 3520 LDRKALP 3526
Cdd:cd17656 473 VDRKALP 479
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1994-2480 |
8.12e-137 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 438.02 E-value: 8.12e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17644 6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17644 86 QERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVMIEHQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQH-LADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17644 130 SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEdFVQYIQQWQLTVLSLPPAYWH 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 QQAEELRHAGRRI--AVRTCILGGEAWDASLLTQ-QAVQAE--AWFNAYGPTEAVITPLAWHCRAQEGGA---PAIGRAL 2304
Cdd:cd17644 210 LLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQwQKNVGNfiQLINVYGPTEATIAATVCRLTQLTERNitsVPIGRPI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2305 GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGS-GERLYRTGDLARYRVDGQVEYLGRAD 2383
Cdd:cd17644 290 ANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSeSERLYKTGDLARYLPDGNIEYLGRID 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2384 QQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedLLAELRTWLAGRLPAYMQPTAWQV 2462
Cdd:cd17644 370 NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVReDQPGNKRLVAYIVPHYEESP--STVELRQFLKAKLPDYMIPSAFVV 447
|
490
....*....|....*...
gi 2310915810 2463 LSSLPLNANGKLDRKALP 2480
Cdd:cd17644 448 LEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1994-2479 |
2.68e-136 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 435.59 E-value: 2.68e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd12115 85 PERLRFILEDAQARLVLTD------------------------------------PDDLAYVIYTSGSTGRPKGVAIEHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagqwSAQHLADEVERHAVTILDLPPAYLqq 2233
Cdd:cd12115 129 NAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVPSAA-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 qAEELRHAGRRIAVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACI 2311
Cdd:cd12115 203 -AELLRHDALPASVRVVNLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2312 LDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:cd12115 282 LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF-GPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:cd12115 361 RIELGEIEAALRSIPGVREAVVVAIgDAAGERRLVAYIVAEPGAAG--LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTP 438
|
....*....
gi 2310915810 2471 NGKLDRKAL 2479
Cdd:cd12115 439 NGKIDRSAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
4539-5041 |
1.50e-134 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 431.47 E-value: 1.50e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSrahlllthshllerlpipeGLSCLSVDREeewagfpahdpevalhgdNLAYVIYTSGSTGMPKGV 4698
Cdd:cd17644 82 PNYPQERLTYILEDA-------------------QISVLLTQPE------------------NLAYVIYTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFP 4777
Cdd:cd17644 125 MIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSsLEDFVQYIQQWQLTVLSLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEHAERDGNPPP--VRVYCFGGDAVAQASYDLAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMP 4854
Cdd:cd17644 205 PAYWHLLVLELLLSTIDLPssLRLVIVGGEAVQPELVRQWQKNVGNFiQLINVYGPTEATIAATVCRLTQLTERNITSVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGSRLYRSGDLTRGRADGVVDY 4933
Cdd:cd17644 285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADSPEaqaecraqLKTALRERL 5012
Cdd:cd17644 365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNkRLVAYIVPHYEESPSTVE--------LRQFLKAKL 436
|
490 500
....*....|....*....|....*....
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17644 437 PDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
4564-4968 |
3.17e-133 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 425.14 E-value: 3.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLPI--PEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:TIGR01733 81 ALASRLAGlvLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAE--MHRHGVTVGVFPPVYLQQLAEHAERDgnPPPVR 4798
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAalIAEHPVTVLNLTPSLLALLAAALPPA--LASLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4799 VYCFGGDAVAQASYDlAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVG 4877
Cdd:TIGR01733 239 LVILGGEALTPALVD-RWRARGPGaRLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4878 VAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 2310915810 4957 LREHPAVREAVV 4968
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
514-999 |
1.34e-131 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 421.96 E-value: 1.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 EYPEERQAYMLEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNP------------------------------------DDLAYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVdTLHFVPS 753
Cdd:cd17645 125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 754 ML-QAFLQDEDvascTSLKRIVCSGEALpadaqqQVFAKLPQAgLYNLYGPTEAAIDVTHWTcVEEGKDTVPIGRPIGNL 832
Cdd:cd17645 204 GAaEQFMQLDN----QSLRVLLTGGDKL------KKIERKGYK-LVNNYGPTENTVVATSFE-IDKPYANIPIGKPIDNT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd17645 272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 913 RGLRIELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESEGGdwREALAAHLAASLPEYMVPAQWLALERMPLS 988
Cdd:cd17645 352 RGYRIEPGEIEPFLMNHPLIELAAVLAKedaDGRKyLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALPLT 429
|
490
....*....|.
gi 2310915810 989 PNGKLDRKALP 999
Cdd:cd17645 430 ANGKVDRKALP 440
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
3041-3526 |
1.65e-131 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 421.58 E-value: 1.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNP------------------------------------DDLAYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVdTLHFVPS 3280
Cdd:cd17645 125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 ML-QAFLQDEDvascTSLKRIVCSGEALpadaqqQVFAKLPQAgLYNLYGPTEAAIDVTHWTcVEEGKDAVPIGRPIANL 3359
Cdd:cd17645 204 GAaEQFMQLDN----QSLRVLLTGGDKL------KKIERKGYK-LVNNYGPTENTVVATSFE-IDKPYANIPIGKPIDNT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd17645 272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESESGdwREALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd17645 352 RGYRIEPGEIEPFLMNHPLIELAAVLAKedaDGRKyLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALPLT 429
|
490
....*....|.
gi 2310915810 3516 PNGKLDRKALP 3526
Cdd:cd17645 430 ANGKVDRKALP 440
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
4539-5040 |
3.56e-128 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 412.48 E-value: 3.56e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSRAHLllthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:cd12115 81 PAYPPERLRFILEDAQARL-------------------------------------VLTDPDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYemTPEDCE--LHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEmhrhGVTVGVF 4776
Cdd:cd12115 124 AIEHRNAAAFLQWAAAAF--SAEELAgvLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAA----EVTLINT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4777 PPVYLQQLAEHaerDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETV----VTPLlwkaragDACGAAY 4852
Cdd:cd12115 198 VPSAAAELLRH---DALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTtystVAPV-------PPGASGE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVD 4932
Cdd:cd12115 268 VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPDGLLE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADspeaqaecRAQLKTALRER 5011
Cdd:cd12115 347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGErRLVAYIVAEPGAAGL--------VEDLRRHLGTR 418
|
490 500
....*....|....*....|....*....
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12115 419 LPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
3052-3525 |
7.06e-128 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 411.48 E-value: 7.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17650 81 EDSGAKLLLTQP------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--D 3288
Cdd:cd17650 125 WRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyvY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAG-LYNLYGPTEAAIDVTHWTCV---EEGKDAVPIGRPIANLACYIL 3364
Cdd:cd17650 205 RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYYEEGrdpLGDSANVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3365 DGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 3444
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3445 ELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVlESESGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVREDKggeaRLCAYVV-AAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 2310915810 3521 DRKAL 3525
Cdd:cd17650 443 DRRAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
525-998 |
6.73e-127 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 408.78 E-value: 6.73e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17650 81 EDSGAKLLLTQP------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--D 761
Cdd:cd17650 125 WRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyvY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 762 EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAG-LYNLYGPTEAAIDVTHWTCV---EEGKDTVPIGRPIGNLGCYIL 837
Cdd:cd17650 205 RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYYEEGrdpLGDSANVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 838 DGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 917
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 918 ELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVlESEGGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVREDKggeaRLCAYVV-AAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 2310915810 994 DRKAL 998
Cdd:cd17650 443 DRRAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
4551-5040 |
9.97e-125 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 402.62 E-value: 9.97e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAhlllthshllerlpipeglsclsvdreeewagfpahdPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPlIAHIV 4710
Cdd:cd17650 81 EDSGA-------------------------------------KLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRN-VAHAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGER-YEMTPEDCE-LHFMSFAFDGSHEGWMHPLINGARVLI-RDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEH 4787
Cdd:cd17650 123 HAWRReYELDSFPVRlLQMASFSFDVFAGDFARSLLNGGTLVIcPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4788 AERDG-NPPPVRVYCFGGDAVAQASY-DLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGY 4865
Cdd:cd17650 203 VYRNGlDLSAMRLLIVGSDGCKAQDFkTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd17650 283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKIRG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAqepavADSPEAqaecrAQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd17650 362 FRIELGEIESQLARHPAIDEAVVAVREDKGGEaRLCAYVVA-----AATLNT-----AELRAFLAKELPSYMIPSYYVQL 431
|
490
....*....|....*.
gi 2310915810 5025 ARMPLTPNGKLDRKGL 5040
Cdd:cd17650 432 DALPLTPNGKVDRRAL 447
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
52-478 |
4.50e-124 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 400.10 E-value: 4.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPrgADDSLaqaPLQRPLEVAfEDC 131
Cdd:cd19538 4 LSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFP--EEDGV---PYQLILEED-EAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 132 SGL-----PEAEQEARLREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19538 78 PKLeikevDEEELESEINEAVR----YPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 207 TGAEPGLPALPIQYADYALWQRSWLEAGEQ-----ERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19538 154 KGEAPELAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:cd19538 234 HQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 362 KDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMY---NHQPLVADIEALDSVAGLSfgqldwKSRTTQFDLSLD-- 436
Cdd:cd19538 314 KETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLalqNTPQPSLDLPGLEAKLELR------TVGSAKFDLTFElr 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2310915810 437 ---TYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19538 388 eqyNDGTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
3052-3525 |
7.93e-124 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 401.26 E-value: 7.93e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHlklPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd12114 81 ADAGARLVLTDGP---DAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPS---MLQAFLQD 3288
Cdd:cd12114 158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCtSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKD--AVPIGRPIANLACYILDG 3366
Cdd:cd12114 238 AQALLP-SLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDwrSIPYGRPLANQRYRVLDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3367 NLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 3446
Cdd:cd12114 317 RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3447 GEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESE-SGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVLGdpgGKRLAAFVVPDNDgTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
...
gi 2310915810 3523 KAL 3525
Cdd:cd12114 475 AAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
3040-3525 |
4.97e-123 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 398.84 E-value: 4.97e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQSHlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTSSP-----------------------------------SDAAYVIFTSGSTGKPKGVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd05918 126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--PSEEDRLNDLAGFINRLRVTWAFLTP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3280 SMLqAFLQDEDVascTSLKRIVCSGEALpadaQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVEEGkDAVPIGRPIAN 3358
Cdd:cd05918 204 SVA-RLLDPEDV---PSLRTLVLGGEAL----TQSDVDTwADRVRLINAYGPAECTIAATVSPVVPST-DPRNIGRPLGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 lACYILD-GNLE-PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP-------FVAGERMYRTGDLARYRADGVIEY 3429
Cdd:cd05918 275 -TCWVVDpDNHDrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3430 AGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV------DGRQLVGYVVLESESGDWREALAAHLAASL----- 3497
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDefral 433
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2310915810 3498 ------------PEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05918 434 vaelrsklrqrlPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
525-998 |
8.06e-123 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 398.18 E-value: 8.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQShlklPLAQGVQRIDLDQADAWLENHAEN-NPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd12114 81 ADAGARLVLTDG----PDAQLDVAVFDVLILDLDALAAPApPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 684 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS---MLQAFLQ 760
Cdd:cd12114 157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 761 DEDVASCtSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPI--GRPIGNLGCYILD 838
Cdd:cd12114 237 AAQALLP-SLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 839 GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIE 918
Cdd:cd12114 316 PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 919 LGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESEG-GDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd12114 394 LGEIEAALQAHPGVARAVVVVLGdpgGKRLAAFVVPDNDGtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473
|
....
gi 2310915810 995 RKAL 998
Cdd:cd12114 474 RAAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
513-998 |
2.13e-122 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 397.30 E-value: 2.13e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PEYPEERQAYMLEDSGVQLLLSQSHlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAG 672
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTSSP-----------------------------------SDAAYVIFTSGSTGKPKGVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHRDPAKLVELINREGVDTLHFVP 752
Cdd:cd05918 126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--PSEEDRLNDLAGFINRLRVTWAFLTP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 753 SMLqAFLQDEDVascTSLKRIVCSGEALpadaQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVEEGkDTVPIGRPIGN 831
Cdd:cd05918 204 SVA-RLLDPEDV---PSLRTLVLGGEAL----TQSDVDTwADRVRLINAYGPAECTIAATVSPVVPST-DPRNIGRPLGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 832 lGCYILD-GNLE-PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP-------FVAGERMYRTGDLARYRADGVIEY 902
Cdd:cd05918 275 -TCWVVDpDNHDrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 903 AGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV------DGRQLVGYVVLESEGGDWREALAAHLAASL----- 970
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDefral 433
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2310915810 971 ------------PEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05918 434 vaelrsklrqrlPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
2583-3005 |
2.92e-122 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 394.71 E-value: 2.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19538 1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAgASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPT 2742
Cdd:cd19538 81 EIKE-VDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2743 LAPLKLQYADYAAWHRAWLDSGEG-----ARQLDYWRERLgAEQPV-LELPADRVRPAQASGRGQRLDMALPVPLSEELL 2816
Cdd:cd19538 160 LAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQL-AGLPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2817 ACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAAL 2896
Cdd:cd19538 239 QLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2897 GAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWE-----TPDGL 2971
Cdd:cd19538 319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREqyndgTPNGI 398
|
410 420 430
....*....|....*....|....*....|....
gi 2310915810 2972 GAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19538 399 EGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
525-999 |
5.49e-121 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 392.15 E-value: 5.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 604 LEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd17648 81 LEDTGARVVITNS------------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 684 WMQQAYGLGVGDT--VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFlqd 761
Cdd:cd17648 125 SLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 762 eDVASCTSLKRIVCSGEALpadaQQQVFAKLPQ--AGL-YNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILD 838
Cdd:cd17648 202 -DLARLPHLKRVDAAGEEF----TAPVFEKLRSrfAGLiINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 839 GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE--------RMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:cd17648 277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 911 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG---------RQLVGYVVLESEGGDWREaLAAHLAASLPEYMVPAQWLA 981
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriqKYLVGYYLPEPGHVPESD-LLSFLRAKLPRYMVPARLVR 435
|
490
....*....|....*...
gi 2310915810 982 LERMPLSPNGKLDRKALP 999
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
3052-3526 |
6.66e-121 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 391.76 E-value: 6.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 3210
Cdd:cd17648 81 LEDTGARVVITNS------------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3211 WMQQAYGLGVGDT--VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFlqd 3288
Cdd:cd17648 125 SLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 eDVASCTSLKRIVCSGEALpadaQQQVFAKLPQ--AGL-YNLYGPTEAAidVTHWTCVEEGKDAV--PIGRPIANLACYI 3363
Cdd:cd17648 202 -DLARLPHLKRVDAAGEEF----TAPVFEKLRSrfAGLiINAYGPTETT--VTNHKRFFPGDQRFdkSLGRPVRNTKCYV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE--------RMYRTGDLARYRADGVIEYAGRIDH 3435
Cdd:cd17648 275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3436 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG---------RQLVGYVVLESESGDWREaLAAHLAASLPEYMVPAQW 3506
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriqKYLVGYYLPEPGHVPESD-LLSFLRAKLPRYMVPARL 433
|
490 500
....*....|....*....|
gi 2310915810 3507 LALERMPLSPNGKLDRKALP 3526
Cdd:cd17648 434 VRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
3042-3525 |
8.60e-121 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 390.52 E-value: 8.60e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTD----------------------------------SPDDLAYIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaapgdhRDPAKLVALINREgVDTLHFVPSM 3281
Cdd:cd17653 127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFlqdeDVASCTSLKRIVCSGEALPADAqqqVFAKLPQAGLYNLYGPTEAAIDVTHwTCVEEGkDAVPIGRPIANLAC 3361
Cdd:cd17653 200 LSTL----SPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTM-TELLPG-QPVTIGKPIPNSTC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3362 YILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd17653 271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3442 LRIELGEIEAR-LLEHPWVREAAVLAVDGRqLVGYVVLESESGDwreALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17653 351 FRINLEEIEEVvLQSQPEVTQAAAIVVNGR-LVAFVTPETVDVD---GLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
....*
gi 2310915810 3521 DRKAL 3525
Cdd:cd17653 427 DRKAL 431
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1994-2479 |
7.66e-120 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 389.98 E-value: 7.66e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd05918 5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd05918 85 LQRLQEILQDTGAKVVLT-----------------------------SSP------SDAAYVIFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-------LLGDagqwsaqhLADEVERHAVTILDL 2226
Cdd:cd05918 130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLcipseedRLND--------LAGFINRLRVTWAFL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 PPAYLQQ-QAEELRHagrriaVRTCILGGEAWDASLLTQqavqaeaW------FNAYGPTEAVItplawHCRAQEGGAPA 2299
Cdd:cd05918 202 TPSVARLlDPEDVPS------LRTLVLGGEALTQSDVDT-------WadrvrlINAYGPAECTI-----AATVSPVVPST 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2300 ----IGRALGARrACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPF------SGSGERLYRTGDL 2367
Cdd:cd05918 264 dprnIGRPLGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2368 ARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL----DGVGGPLLAAYLVGRDAMRG------- 2436
Cdd:cd05918 343 VRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpkDGSSSPQLVAFVVLDGSSSGsgdgdsl 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2437 --------EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05918 423 flepsdefRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
515-998 |
1.46e-119 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 387.05 E-value: 1.46e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 595 YPEERQAYMLEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTD----------------------------------SPDDLAYIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 675 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaapgdhRDPAKLVELINREgVDTLHFVPSM 754
Cdd:cd17653 127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 755 LQAFlqdeDVASCTSLKRIVCSGEALPADAqqqVFAKLPQAGLYNLYGPTEAAIDVTHwTCVEEGkDTVPIGRPIGNLGC 834
Cdd:cd17653 200 LSTL----SPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTM-TELLPG-QPVTIGKPIPNSTC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 835 YILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:cd17653 271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 915 LRIELGEIEAR-LLEHPWVREAAVLAVDGRqLVGYVVLESEGGDwreALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17653 351 FRINLEEIEEVvLQSQPEVTQAAAIVVNGR-LVAFVTPETVDVD---GLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
....*
gi 2310915810 994 DRKAL 998
Cdd:cd17653 427 DRKAL 431
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
4539-5040 |
1.03e-116 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 380.73 E-value: 1.03e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSRAhlllthshllerlpipeglsclsvdreeewagfpahdpEVAL--HGDNLAYVIYTSGSTGMPK 4696
Cdd:cd05918 81 PSHPLQRLQEILQDTGA--------------------------------------KVVLtsSPSDAAYVIFTSGSTGKPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4697 GVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGS-HEGWMhPLINGARVLI-RDDSLW--LPErtyaEMHRHGVT 4772
Cdd:cd05918 123 GVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSiLEIFT-TLAAGGCLCIpSEEDRLndLAG----FINRLRVT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4773 VGVFPPVYLQQLaehaeRDGNPPPVRVYCFGGDAVAQASYDlAWrALKPKyLFNGYGPTE----TVVTPLLWKARAGDac 4848
Cdd:cd05918 198 WAFLTPSVARLL-----DPEDVPSLRTLVLGGEALTQSDVD-TW-ADRVR-LINAYGPAEctiaATVSPVVPSTDPRN-- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4849 gaaympIGTLLGNRSgYILD--GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF------GAPGSRLYRSG 4920
Cdd:cd05918 268 ------IGRPLGATC-WVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVA----QPGAVGQQLVGYVVA----------Q 4986
Cdd:cd05918 341 DLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpKDGSSSPQLVAFVVLdgsssgsgdgD 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4987 EPAVADSPEAQAECRaQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05918 421 SLFLEPSDEFRALVA-ELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
2002-2479 |
1.30e-116 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 380.46 E-value: 1.30e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLPCPAEVERLPLETAAWPasaDTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAP---APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWS-AQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd12114 158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRdPAHWAELIERHGVTLWNSVPALLEMLLDVLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYG-PTEAVITPLAWHCRAQEGGAPAI--GRALGARRACILDAA 2315
Cdd:cd12114 238 AQALLPsLRLVLLSGDWIPLDLPARlRALAPDARLISLGgATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLDPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd12114 318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGeDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTP-IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473
|
....
gi 2310915810 2476 RKAL 2479
Cdd:cd12114 474 RAAL 477
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
52-497 |
4.11e-115 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 375.13 E-value: 4.11e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:pfam00668 7 LSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQEN----GEPVQvileeRPFEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:pfam00668 83 EIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 207 TGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:pfam00668 163 KGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:pfam00668 242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQ--PLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:pfam00668 322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQnyLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 445 YAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLL 497
Cdd:pfam00668 402 TIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
2002-2479 |
4.17e-115 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 374.88 E-value: 4.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIcqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAAlVAHCQA 2161
Cdd:cd17650 81 EDSGAKLLL------------------------------TQP------EDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 A-ARTYGVgpgDCQ----LQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQA 2235
Cdd:cd17650 124 AwRREYEL---DSFpvrlLQMASFSFDVFAGDFARSLLNGGTlVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2236 EELRHAGRRI-AVRTCILGGE---AWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWH---CRAQEGGAPAIGRALGARR 2308
Cdd:cd17650 201 AYVYRNGLDLsAMRLLIVGSDgckAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEegrDPLGDSANVPIGRPLPNTA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17650 281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPL-LAAYLVGRDAMRgedlLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17650 360 RGFRIELGEIESQLARHPAIDEAVVAVREDKGGEArLCAYVVAAATLN----TAELRAFLAKELPSYMIPSYYVQLDALP 435
|
490
....*....|..
gi 2310915810 2468 LNANGKLDRKAL 2479
Cdd:cd17650 436 LTPNGKVDRRAL 447
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
3048-3525 |
3.14e-114 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 372.35 E-value: 3.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3127
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3128 AYMLEDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSN 3207
Cdd:cd05945 81 REILDAAKPALLIA------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ 3287
Cdd:cd05945 125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3288 DE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVT--HWT-CVEEGKDAVPIGRPIANLACY 3362
Cdd:cd05945 205 SPtfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTyiEVTpEVLDGYDRLPIGYAKPGAKLV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3363 ILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 3442
Cdd:cd05945 285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3443 RIELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVLESESGDWREALAAHL-AASLPEYMVPAQWLALERMPLSPN 3517
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGekvtELIAFVVPKPGAEAGLTKAIKAElAERLPPYMIPRRFVYLDELPLNAN 441
|
....*...
gi 2310915810 3518 GKLDRKAL 3525
Cdd:cd05945 442 GKIDRKAL 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
3044-3440 |
7.10e-114 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 370.10 E-value: 7.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGE-ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLP--------LAQGVQRIDLDRGAPWFEDYSEAN---------PDIHLDGENLAYV 3185
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPVLKEEPLPEEakpadvpppPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAY----GLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPGDHRDP 3260
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT 3338
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3339 H-WTCVEEGKDAVPIGRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTG 3416
Cdd:pfam00501 320 TpLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
|
410 420
....*....|....*....|....
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLR 3440
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1994-2480 |
1.28e-113 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 370.35 E-value: 1.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17645 84 GERIAYMLADSSAKILLTN------------------------------------PDDLAYVIYTSGSTGLPKGVMIEHH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17645 128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALhVVPSERRLDLDALNDYFNQEGITISFLPTGAAE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 QQAEELRHAgrriaVRTCILGGEAwdaslLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPaIGRALGARRACIL 2312
Cdd:cd17645 208 QFMQLDNQS-----LRVLLTGGDK-----LKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIP-IGKPIDNTRVYIL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:cd17645 277 DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV-PGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2393 IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdllaELRTWLAGRLPAYMQPTAWQVLSSLPLNAN 2471
Cdd:cd17645 356 IEPGEIEPFLMNHPLIELAAVLAKeDADGRKYLVAYVTAPEEIPHE----ELREWLKNDLPDYMIPTYFVHLKALPLTAN 431
|
....*....
gi 2310915810 2472 GKLDRKALP 2480
Cdd:cd17645 432 GKVDRKALP 440
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
517-913 |
6.09e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 367.41 E-value: 6.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 517 FEEQVERTPTAPALAFGE-ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 596 PEERQAYMLEDSGVQLLLSQSHLKLP--------LAQGVQRIDLDQADAWLE---------NHAENNPGIELNGENLAYV 658
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPVLKEeplpeeakpADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 659 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAY----GLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPGDHRDP 733
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 734 AKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT 811
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 812 HWTCVEEGKDTVP-IGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTG 889
Cdd:pfam00501 320 TPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
|
410 420
....*....|....*....|....
gi 2310915810 890 DLARYRADGVIEYAGRIDHQVKLR 913
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
521-998 |
7.88e-113 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 368.11 E-value: 7.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 601 AYMLEDSGVQLLLSqshlklplaqgvqridlDQADawlenhaennpgielngenLAYVIYTSGSTGKPKGAGNRHSALSN 680
Cdd:cd05945 81 REILDAAKPALLIA-----------------DGDD-------------------NAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 681 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ 760
Cdd:cd05945 125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 761 DE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVT--HWT-CVEEGKDTVPIGRPIGNLGCY 835
Cdd:cd05945 205 SPtfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTyiEVTpEVLDGYDRLPIGYAKPGAKLV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd05945 285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 916 RIELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVLESEGGDWREALAAHL-AASLPEYMVPAQWLALERMPLSPN 990
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGekvtELIAFVVPKPGAEAGLTKAIKAElAERLPPYMIPRRFVYLDELPLNAN 441
|
....*...
gi 2310915810 991 GKLDRKAL 998
Cdd:cd05945 442 GKIDRKAL 449
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
4551-5041 |
1.33e-111 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 364.80 E-value: 1.33e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVG-PEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYM 4629
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4630 MQDSRAhlllthshlleRLPIPEGlsclsvdreeewagfpahdpevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd17648 81 LEDTGA-----------RVVITNS--------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCE--LHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLaE 4786
Cdd:cd17648 124 TSLSERYFGRDNGDEavLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFdPDRFYAYINREKVTYLSGTPSVLQQY-D 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4787 HAERdgnpPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcgaAYMPIGTLLGNRSGYI 4866
Cdd:cd17648 203 LARL----PHLKRVDAAGEEFTAPVFE-KLRSRFAGLIINAYGPTETTVTNHKRFFPGDQR---FDKSLGRPVRNTKCYV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPG-------SRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd17648 275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ------LVGYVVAQEPAVADSpeaqaecraQLKTALRERLP 5013
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkyLVGYYLPEPGHVPES---------DLLSFLRAKLP 425
|
490 500
....*....|....*....|....*...
gi 2310915810 5014 EYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17648 426 RYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
2002-2480 |
1.87e-111 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 365.64 E-value: 1.87e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLPCPAEVERL--PLETAAWPASADTrplpEVAGETLAYVIYTSGSTGQPKGVAV---SQAALV 2156
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKSTILLedPSISQEDTSNIDY----INNSDDLLYIIYTSGTTGKPKGVQLehkNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHcqaaARTY-GVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:cd17656 158 HF----EREKtNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 AEElRHAGRRIA--VRTCILGGEAWDASLLTQQAVQAE--AWFNAYGPTEA-VITPLAWHCRAQEGGAPAIGRALGARRA 2309
Cdd:cd17656 234 FSE-REFINRFPtcVKHIITAGEQLVITNEFKEMLHEHnvHLHNHYGPSEThVVTTYTINPEAEIPELPPIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2310 CILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:cd17656 313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFD-PNERMYRTGDLARYLPDGNIEFLGRADHQVKIR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2390 GFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDllaeLRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSEAVVLDKaDDKGEKYLCAYFVMEQELNISQ----LREYLAKQLPEYMIPSFFVPLDQLPL 467
|
490
....*....|..
gi 2310915810 2469 NANGKLDRKALP 2480
Cdd:cd17656 468 TPNGKVDRKALP 479
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
4551-5040 |
7.52e-111 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 363.90 E-value: 7.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEValhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP----DDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLI------RDDSLWlpertyAE-MHRHGVTVGVFPPVYLQQ 4783
Cdd:cd12114 157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpdearrRDPAHW------AElIERHGVTLWNSVPALLEM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4784 LAEHAERDGNPPP-VRVYCFGGDAVAQasyDLA--WRALKPK-YLFNGYGPTETVVTPLLWKARAGDAcGAAYMPIGTLL 4859
Cdd:cd12114 231 LLDVLEAAQALLPsLRLVLLSGDWIPL---DLParLRALAPDaRLISLGGATEASIWSIYHPIDEVPP-DWRSIPYGRPL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4860 GNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgaPGSRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd12114 307 ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMVPS 5019
Cdd:cd12114 384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDA-------LRAFLAQTLPAYMIPS 456
|
490 500
....*....|....*....|.
gi 2310915810 5020 HLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12114 457 RVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
4540-5041 |
2.31e-110 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 360.72 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4620 EYPRERLLYMMQDSRAHLllthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVA 4699
Cdd:cd17645 81 DYPGERIAYMLADSSAKI-------------------------------------LLTNPDDLAYVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4700 VSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLP-ERTYAEMHRHGVTVGVFPp 4778
Cdd:cd17645 124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDlDALNDYFNQEGITISFLP- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 vylQQLAEHAERDGNPPpVRVYCFGGDAVAQASYdlawralKPKYLFNGYGPTETVVTPLLWKARAGDACgaayMPIGTL 4858
Cdd:cd17645 203 ---TGAAEQFMQLDNQS-LRVLLTGGDKLKKIER-------KGYKLVNNYGPTENTVVATSFEIDKPYAN----IPIGKP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17645 268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAvadSPEAqaecraqLKTALRERLPEYMV 5017
Cdd:cd17645 347 QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKyLVAYVTAPEEI---PHEE-------LREWLKNDLPDYMI 416
|
490 500
....*....|....*....|....
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17645 417 PTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
4551-5041 |
9.89e-107 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 351.78 E-value: 9.89e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGfpaHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDT---SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARV-LIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhaE 4789
Cdd:cd17656 159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS--E 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4790 RDGNPP---PVRVYCFGGDAVAQAsyDLAWRALKPK--YLFNGYGPTET-VVTplLWKARAGDACgAAYMPIGTLLGNRS 4863
Cdd:cd17656 237 REFINRfptCVKHIITAGEQLVIT--NEFKEMLHEHnvHLHNHYGPSEThVVT--TYTINPEAEI-PELPPIGKPISNTW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4864 GYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:cd17656 312 IYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQVKI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4944 RGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAqEPAVADSpeaqaecraQLKTALRERLPEYMVPSHLL 5022
Cdd:cd17656 391 RGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKyLCAYFVM-EQELNIS---------QLREYLAKQLPEYMIPSFFV 460
|
490
....*....|....*....
gi 2310915810 5023 FLARMPLTPNGKLDRKGLP 5041
Cdd:cd17656 461 PLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
4551-5040 |
4.62e-106 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 348.14 E-value: 4.62e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17653 11 PDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLllthshllerlpipeglsCLSVDReeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17653 91 RTSGATL------------------LLTTDS-----------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDdslwlPERTYAEMHRhgvTVGVFP--PVYLQQLaeha 4788
Cdd:cd17653 136 QPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD-----PSDPFAHVAR---TVDALMstPSILSTL---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 eRDGNPPPVRVYCFGGDAVAQasyDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcgaayMPIGTLLGNRSGYILD 4868
Cdd:cd17653 204 -SPQDFPNLKTIFLGGEAVPP---SLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQP-----VTIGKPIPNSTCYILD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd17653 275 ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEAR-LREHPAVREAVVVaqpgAVGQQLVGYVVaqePAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd17653 354 NLEEIEEVvLQSQPEVTQAAAI----VVNGRLVAFVT---PETVDV--------DGLRSELAKHLPSYAVPDRIIALDSF 418
|
490
....*....|...
gi 2310915810 5028 PLTPNGKLDRKGL 5040
Cdd:cd17653 419 PLTANGKVDRKAL 431
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1990-2490 |
6.61e-106 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 348.34 E-value: 6.61e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawpasadtrplpevagetlAYVIYTSGSTGQPKGVA 2149
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2150 VSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLGDAgqWSAQHLADEVERHAVTILDLPP 2228
Cdd:COG0318 120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2229 AYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGA 2306
Cdd:COG0318 198 TMLARLLRHPEFARYDLSsLRLVVSGGAPLPPELLERfEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQI 2386
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIVGRKKDMI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2387 KIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLS 2464
Cdd:COG0318 350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVpDEKWGERVVAFVVLRP---GAELdAEELRAFLRERLARYKVPRRVEFVD 426
|
490 500
....*....|....*....|....*.
gi 2310915810 2465 SLPLNANGKLDRKALPKVDAAARRQA 2490
Cdd:COG0318 427 ELPRTASGKIDRRALRERYAAGALEA 452
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
2002-2480 |
1.48e-105 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 347.47 E-value: 1.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARG-VVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETlaerlpcpaeverlpletaawpasadtrplpevageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQ 2160
Cdd:cd17648 81 LEDTGARVVITNST------------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2161 AAARTYGV-GPGD-CQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQaeE 2237
Cdd:cd17648 125 SLSERYFGrDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKlVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--D 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2238 LrhaGRRIAVRTCILGGEAWDASLLTQQAVQ-AEAWFNAYGPTEAVITPlawHCRAQEGGAP---AIGRALGARRACILD 2313
Cdd:cd17648 203 L---ARLPHLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTETTVTN---HKRFFPGDQRfdkSLGRPVRNTKCYVLN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2314 AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPF-------SGSGERLYRTGDLARYRVDGQVEYLGRADQQI 2386
Cdd:cd17648 277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqeraRGRNARLYKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2387 KIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPL--LAAYLVGRDAMRGEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVGYYLPEPGHVpESDLLSFLRAKLPRYMVPARLVRL 436
|
490
....*....|....*..
gi 2310915810 2464 SSLPLNANGKLDRKALP 2480
Cdd:cd17648 437 EGIPVTINGKLDVRALP 453
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3040-3534 |
4.11e-105 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 346.03 E-value: 4.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAG 3199
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFV 3278
Cdd:COG0318 120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPI 3356
Cdd:COG0318 197 PTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:COG0318 276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:COG0318 349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPdekwGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
|
490 500
....*....|....*....|..
gi 2310915810 3513 PLSPNGKLDRKALpRPQAAAGQ 3534
Cdd:COG0318 429 PRTASGKIDRRAL-RERYAAGA 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
4547-5040 |
6.50e-105 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 345.39 E-value: 6.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LyMMQDsrahlllthshllerlpipeglsclsvdreeewagfpAHDPEVALH-GDNLAYVIYTSGSTGMPKGVAVSHGPL 4705
Cdd:cd05945 81 R-EILD-------------------------------------AAKPALLIAdGDDNAYIIFTSGSTGRPKGVQISHDNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4706 IAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQL 4784
Cdd:cd05945 123 VSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4785 AEHAERD-GNPPPVRVYCFGGDA--VAQASydlAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLG 4860
Cdd:cd05945 203 LLSPTFTpESLPSLRHFLFCGEVlpHKTAR---ALQQRFPDaRIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4861 NRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:cd05945 280 GAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYVVAQepavadsPEAQAECRAQLKTALRERLPEYMVPS 5019
Cdd:cd05945 356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKYkGEKVTELIAFVVPK-------PGAEAGLTKAIKAELAERLPPYMIPR 428
|
490 500
....*....|....*....|.
gi 2310915810 5020 HLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05945 429 RFVYLDELPLNANGKIDRKAL 449
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
2583-3024 |
1.53e-104 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 344.70 E-value: 1.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF-EEVDGQARQTILANMPLRIV 2661
Cdd:pfam00668 4 EYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILEERPFELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2662 LEDCAGASEATLRQRVAEEIR----QPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARR 2737
Cdd:pfam00668 84 IIDISDLSESEEEEAIEAFIQrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2738 GEQPTLAPLKlQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:pfam00668 164 GEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:pfam00668 243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVD-------GLHIESFAWDgaAAQFDLALDTWETPDG 2970
Cdd:pfam00668 323 AEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEefqlselDLSVSSVIEE--EAKYDLSLTASERGGG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2971 LGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLL 3024
Cdd:pfam00668 401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4539-5042 |
1.72e-104 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 344.49 E-value: 1.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSrahlllthshllerlpipeglsclsvdreeewagfpahDPEVALHgdnlAYVIYTSGSTGMPKGV 4698
Cdd:COG0318 81 PRLTAEELAYILEDS--------------------------------------GARALVT----ALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFP 4777
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFGV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTET--VVTpllwkARAGDACGAAYMP 4854
Cdd:COG0318 197 PTMLARLLRHPEFARyDLSSLRLVVSGGAPLPPELLE-RFEERFGVRIVEGYGLTETspVVT-----VNPEDPGERRPGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvPDPFgapgsrlYRSGDLTRGRADGVVDYL 4934
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLP 5013
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKwGERVVAFVVLRPGAELD--------AEELRAFLRERLA 414
|
490 500
....*....|....*....|....*....
gi 2310915810 5014 EYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1993-2479 |
8.49e-104 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 341.60 E-value: 8.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1993 AFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2073 PAERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawPASADTrplpevagetLAYVIYTSGSTGQPKGVAVSQ 2152
Cdd:cd17653 82 PSARIQAILRTSGATLLLT------------------------TDSPDD----------LAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2153 AALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGD-AGQWsaQHLADEVERHAVT--ILD-LPP 2228
Cdd:cd17653 128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADpSDPF--AHVARTVDALMSTpsILStLSP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2229 AYLQQqaeelrhagrriaVRTCILGGEAWDASLLtqqavqaEAW------FNAYGPTEAVITPLAWHCRAqeGGAPAIGR 2302
Cdd:cd17653 206 QDFPN-------------LKTIFLGGEAVPPSLL-------DRWspgrrlYNAYGPTECTISSTMTELLP--GQPVTIGK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2303 ALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRA 2382
Cdd:cd17653 264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2383 DQQIKIRGFRIEIGEIESQLLA-HPYVAEAAVVAldgVGGPLLAayLVGRDAMRGEDLLAELRTwlagRLPAYMQPTAWQ 2461
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIV---VNGRLVA--FVTPETVDVDGLRSELAK----HLPSYAVPDRII 413
|
490
....*....|....*...
gi 2310915810 2462 VLSSLPLNANGKLDRKAL 2479
Cdd:cd17653 414 ALDSFPLTANGKVDRKAL 431
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
513-1000 |
9.61e-104 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 342.18 E-value: 9.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PEYPEERQAYMLEDSGVQLLLSqshlklplaqgvqridldqadawlenhaennpgielngenlAYVIYTSGSTGKPKGAG 672
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFV 751
Cdd:COG0318 120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 752 PSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPI 829
Cdd:COG0318 197 PTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 830 GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:COG0318 276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 910 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERM 985
Cdd:COG0318 349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPdekwGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
|
490
....*....|....*
gi 2310915810 986 PLSPNGKLDRKALPA 1000
Cdd:COG0318 429 PRTASGKIDRRALRE 443
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
2585-3005 |
3.51e-102 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 336.66 E-value: 3.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTIL----ANMPLR 2659
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILppgpAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2660 IVLeDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19539 83 DLS-DPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPvLELPADRVRPAQASGRGQRLDMALPVPLSEELLACA 2819
Cdd:cd19539 162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2820 RREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQ 2899
Cdd:cd19539 241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2900 AHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQS---GERQDAQVDGLHIESFAWDGAAaqFDLALDTWETPDGLGAALT 2976
Cdd:cd19539 321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNapaGELELAGGLSYTEGSDIPDGAK--FDLNLTVTEEGTGLRGSLG 398
|
410 420
....*....|....*....|....*....
gi 2310915810 2977 YATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19539 399 YATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
49-478 |
3.29e-100 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 330.88 E-value: 3.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 49 RDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPL---QRPLE 125
Cdd:cd19539 1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILppgPAPLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 126 VAFEDCSGL-PEAEQEARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSA 204
Cdd:cd19539 81 VRDLSDPDSdRERRLEELLRERESR----GFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 205 YATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPvLELPTDHPRPVVPSYRGSRYEFSIEPALAEA 284
Cdd:cd19539 157 RRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:cd19539 236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 365 VLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVAdiEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:cd19539 316 LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPA--GELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGL 393
|
410 420 430
....*....|....*....|....*....|....
gi 2310915810 445 YAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19539 394 RGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1998-2479 |
1.94e-97 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 323.82 E-value: 1.94e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 AYMLRDSGARWLIcqetlaerlpcpaeverlpletaawpasadtrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05945 81 REILDAAKPALLI------------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2158 HCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQA- 2235
Cdd:cd05945 125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2236 EELRHAGRRIAVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAWHCR----AQEGGAPaIGRALGARRA 2309
Cdd:cd05945 205 SPTFTPESLPSLRHFLFCGEVLPHKTARalQQRFPDARIYNTYGPTEATVAVTYIEVTpevlDGYDRLP-IGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2310 CILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:cd05945 284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2390 GFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:cd05945 360 GYRIELEEIEAALRQVPGVKEAVVVPKyKGEKVTELIAFVVPKPGAE-AGLTKAIKAELAERLPPYMIPRRFVYLDELPL 438
|
490
....*....|.
gi 2310915810 2469 NANGKLDRKAL 2479
Cdd:cd05945 439 NANGKIDRKAL 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1994-2389 |
3.17e-92 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 307.70 E-value: 3.17e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGD-EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2073 PAERLAYMLRDSGARWLICQETL--------AERLPCPAEVERL---------PLETAAWPASADTRPLPEVAGETLAYV 2135
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLdrdpvlkeePLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2136 IYTSGSTGQPKGVAVSQAALVAHCQAAARTY----GVGPGDCQLQFASISFDAAAE-QLFVPLLAGAR-VLLGDAGQWSA 2209
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATvVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVTILDLPPAYLQQQAEELRHAG-RRIAVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAviTPLA 2287
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRaLLSSLRLVLSGGAPLPPELARRfRELFGGALVNGYGLTET--TGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRAQEG---GAPAIGRALGARRACILDAA-LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgeRLYR 2363
Cdd:pfam00501 319 TTPLPLDEdlrSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYR 391
|
410 420
....*....|....*....|....*.
gi 2310915810 2364 TGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:pfam00501 392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
4543-4944 |
1.22e-91 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 305.78 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDE-EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 PRERLLYMMQDSRA------HLLLTHSHLLERLPIPEGLSCLSVDR----------EEEWAGFPAHDPEVALHGDNLAYV 4685
Cdd:pfam00501 81 PAEELAYILEDSGAkvlitdDALKLEELLEALGKLEVVKLVLVLDRdpvlkeeplpEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4686 IYTSGSTGMPKGVAVSHGPLIA----HIVATGERYEMTPEDCELHFMSFAFDGSHEGWMH-PLINGAR-VLIRDDSLWLP 4759
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGATvVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4760 ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVaQASYDLAWRALKPKYLFNGYGPTETvvTPL 4838
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALlSSLRLVLSGGAPL-PPELARRFRELFGGALVNGYGLTET--TGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAAYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgsRLY 4917
Cdd:pfam00501 318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWY 390
|
410 420
....*....|....*....|....*..
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIR 4944
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
2773-3624 |
4.23e-88 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 320.09 E-value: 4.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2773 WRERLGAeQPVLELPADRVRPAQASGRGQRLDMALPvplSEELLACArreGVTPFMLLLASFQVLLKRYSGQSDIRVGVP 2852
Cdd:TIGR03443 2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLP---SAEVTAGG---GSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2853 IANRNRAeverligffvntQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNL-SHSPLFQVMYNH 2931
Cdd:TIGR03443 75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAFQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2932 QSGERQDAQVDGLHIesfawdgaaaqfDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDS 3011
Cdd:TIGR03443 143 APDNQQTTYSTGSTT------------DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3012 LPMLDAEERGQLLE-----GWnataAEYplqRG-VHRLFEEQVER---------TPTAPALAFGEERLDYAELNRRANRL 3076
Cdd:TIGR03443 211 VSLITPSQKSLLPDptkdlDW----SGF---RGaIHDIFADNAEKhpdrtcvveTPSFLDPSSKTRSFTYKQINEASNIL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3077 AHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA-YM----------LEDSGV--------- 3136
Cdd:TIGR03443 284 AHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiYLsvakpralivIEKAGTldqlvrdyi 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 ----ELLLSQSHLKLpLAQGvqriDLDRGAPWFEDYSEANPDIHLDGENLAYVI---------YTSGSTGKPKGAGNRHS 3203
Cdd:TIGR03443 364 dkelELRTEIPALAL-QDDG----SLVGGSLEGGETDVLAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGD--TVLQ---KTPFSFDVsvwefFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFV 3278
Cdd:TIGR03443 439 SLAYYFPWMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLT 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQaFLQDEDVASCTSLKRIVCSGEALPA-DAQQ-QVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGK 3347
Cdd:TIGR03443 514 PAMGQ-LLSAQATTPIPSLHHAFFVGDILTKrDCLRlQTLA--ENVCIVNMYGTTETQRAVSYFeipsrssdsTFLKNLK 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3348 DAVPIGRPIANLACYILDGN--LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE--------------- 3410
Cdd:TIGR03443 591 DVMPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkpere 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3411 -------RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQ-LVGYVVLE 3479
Cdd:TIGR03443 671 fwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrrdKDEEPtLVSYIVPQ 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3480 SESGDWREALAAHLAASL--------------------------PEYMVPAQWLALERMPLSPNGKLDRKALPRPQ---- 3529
Cdd:TIGR03443 751 DKSDELEEFKSEVDDEESsdpvvkglikyrklikdireylkkklPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaql 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3530 AAAGQTHVAPQ-----NEMERRIAAVWADVL--KLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDL-FQQQTV 3601
Cdd:TIGR03443 831 AAVAKNRSASAadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLiFKSPTI 910
|
970 980
....*....|....*....|....
gi 2310915810 3602 QGLAR-VARVGAAVQMEQGPVSGE 3624
Cdd:TIGR03443 911 KGFAKeVDRLKKGEELADEGDSEI 934
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2583-3005 |
2.18e-87 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 293.93 E-value: 2.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPlRIVL 2662
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTV-RFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEATLRQRVAEEI----RQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19066 80 EIIDLRNLADPEARLLELIdqiqQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2739 eQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19066 160 -KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHI--ESFAWDGaAAQFDLALDTWETPDG-LGAAL 2975
Cdd:cd19066 319 IEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFttPVYTSSE-GTVFDLDLEASEDPDGdLLLRL 397
|
410 420 430
....*....|....*....|....*....|
gi 2310915810 2976 TYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19066 398 EYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
52-297 |
2.52e-86 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 283.47 E-value: 2.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLwhlEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDslaqaPLQR-----PLEV 126
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGE-----PVQRidpdaDLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:COG4908 73 EVVDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 207 TGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:COG4908 153 EGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALK 232
|
250
....*....|.
gi 2310915810 287 GTARRQGLTLF 297
Cdd:COG4908 233 ALAKAHGATVN 243
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2583-2998 |
1.18e-85 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 289.16 E-value: 1.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGA--SEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG-E 2739
Cdd:cd20483 81 IDLSEAadPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGrD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL-GAEQPVLELP-ADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd20483 161 LATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLeGIPDASKLLPfAKAERPPVKDYERSTVEATLDKELLARMKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:cd20483 241 ICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQ-SGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPD-GLGAAL 2975
Cdd:cd20483 321 AYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvHGKFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDgGLDLRL 400
|
410 420
....*....|....*....|...
gi 2310915810 2976 TYATDLFEARTVERMARHWQNLL 2998
Cdd:cd20483 401 EFSTTLYDSADMERFLDNFVTFL 423
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
52-478 |
1.30e-85 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 288.92 E-value: 1.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGaDDSLAQAPLQRPLEVAFEDC 131
Cdd:cd19066 4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLDKTVRFRIEII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 132 SGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGaEP 211
Cdd:cd19066 83 DLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ-KP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARR 291
Cdd:cd19066 162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 292 QGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAH 371
Cdd:cd19066 242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 372 QDLPFERLVEAFKVERSLSHSPLFQVMYNHQplvADIEALDSVAGLSFGQLDWKSR-TTQFDLSLDTYE-KGGRLYAALT 449
Cdd:cd19066 322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFK---NNQQQLGKTGGFIFTTPVYTSSeGTVFDLDLEASEdPDGDLLLRLE 398
|
410 420
....*....|....*....|....*....
gi 2310915810 450 YATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19066 399 YSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2585-3005 |
2.68e-85 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 288.06 E-value: 2.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLED 2664
Cdd:cd20484 3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2665 CAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLA 2744
Cdd:cd20484 83 ISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2745 PLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGV 2824
Cdd:cd20484 163 SSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2825 TPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDL 2904
Cdd:cd20484 243 NLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2905 PFEQLVDALQPERNLSHSPLFQVMYNHQ----SGERQDAQ-----------VDGLHIEsfawdgaaAQFDLALDTWETPD 2969
Cdd:cd20484 323 PFPAMVRDLNIPRSQANSPVFQVAFFYQnflqSTSLQQFLaeyqdvlsiefVEGIHQE--------GEYELVLEVYEQED 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 2310915810 2970 GLGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd20484 395 RFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
518-998 |
8.59e-85 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 289.35 E-value: 8.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 518 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 597
Cdd:TIGR01734 7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 598 ERQAYMLEDSGVQLLLSQSHLKLPlAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:TIGR01734 87 ERIEMIIEAAGPELVIHTAELSID-AVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQISHDN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:TIGR01734 166 LVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVDM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 758 FLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDTVPIG--RPIG 830
Cdd:TIGR01734 246 CLLDPNFNQenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEildQYPRLPIGfaKPDM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 831 NLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRaDGVIEYAGRIDHQV 910
Cdd:TIGR01734 326 NL--FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGTIT-DGQLFYQGRLDFQI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 911 KLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR--QLVGYVVLESEGGDwREALAAHL-----AASLPEYMVPAQWL 980
Cdd:TIGR01734 400 KLHGYRIELEDIEFNLRQSSYIESAVVVPKynkDHKveYLIAAIVPETEDFE-KEFQLTKAikkelKKSLPAYMIPRKFI 478
|
490
....*....|....*...
gi 2310915810 981 ALERMPLSPNGKLDRKAL 998
Cdd:TIGR01734 479 YRDQLPLTANGKIDRKAL 496
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
517-1003 |
7.96e-84 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 286.41 E-value: 7.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 597 EERQAYMLEDSGVQLLLSQSHLKLpLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:PRK04813 88 AERIEMIIEVAKPSLIIATEELPL-EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 677 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDH---RDPAKLVELINREGVDTLHFVPS 753
Cdd:PRK04813 167 NLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVAL---PKdmtANFKQLFETLPQLPINVWVSTPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 754 MLQAFLQDEDVASCT--SLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcVE------EGKDTVPI 825
Cdd:PRK04813 244 FADMCLLDPSFNEEHlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTS---IEitdemlDQYKRLPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 826 GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLArYRADGVIEYAGR 905
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAG-YLEDGLLFYQGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 906 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR--QLVGYVVLEsEGGDWREALAAHL-----AASLPEYMVP 976
Cdd:PRK04813 397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDHKvqYLIAYVVPK-EEDFEREFELTKAikkelKERLMEYMIP 475
|
490 500
....*....|....*....|....*..
gi 2310915810 977 AQWLALERMPLSPNGKLDRKALpAPEV 1003
Cdd:PRK04813 476 RKFIYRDSLPLTPNGKIDRKAL-IEEV 501
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2585-3005 |
8.25e-84 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 283.58 E-value: 8.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF--EEVDGQARQTILANMPLRIVL 2662
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEAtlrQRVAEEIRQ-PFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAaarrgeQP 2741
Cdd:cd19532 83 VQISDEAEV---EEEFERLKNhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN------GQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLEL---PADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19532 154 PLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAARIKEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19532 234 SRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGlGAALTYA 2978
Cdd:cd19532 314 LAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEGEEFEDARTPYDLSLDIIDNPDG-DCLLTLK 392
|
410 420
....*....|....*....|....*....
gi 2310915810 2979 T--DLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19532 393 VqsSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
252-1054 |
8.87e-84 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 306.61 E-value: 8.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 252 PVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTarrqglTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAev 331
Cdd:TIGR03443 10 TLSVLPHDYLRPANNRLVEATYSLQLPSAEVTAGGGS------TPFIILLAAFAALVYRLTGDEDIVLGTSSNKSGRP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 332 egliglfvntQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSL-SHSPLFQVMYNHQPLVAdiea 410
Cdd:TIGR03443 82 ----------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAFQDAPDNQ---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 411 LDSVAglsfgqldwKSRTTqfDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 490
Cdd:TIGR03443 148 QTTYS---------TGSTT--DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 491 EERGQLLE-----GWnataAEYplqRG-VHRLFEEQVER---------TPTAPALAFGEERLDYAELNRRANRLAHALIE 555
Cdd:TIGR03443 217 SQKSLLPDptkdlDW----SGF---RGaIHDIFADNAEKhpdrtcvveTPSFLDPSSKTRSFTYKQINEASNILAHYLLK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 556 RGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA-YM----------LEDSGVqllLSQSHLK----- 619
Cdd:TIGR03443 290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiYLsvakpralivIEKAGT---LDQLVRDyidke 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 620 LPLAQGVQRIDLdQADAWLENHAENN-------PGIELNGENLAYVI---------YTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:TIGR03443 367 LELRTEIPALAL-QDDGSLVGGSLEGgetdvlaPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 684 WMQQAYGLGVGD--TVLQ---KTPFSFDVsvwefFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQaF 758
Cdd:TIGR03443 446 WMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQ-L 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 759 LQDEDVASCTSLKRIVCSGEALPA-DAQQ-QVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDTVPIGR 827
Cdd:TIGR03443 520 LSAQATTPIPSLHHAFFVGDILTKrDCLRlQTLA--ENVCIVNMYGTTETQRAVSYFeipsrssdsTFLKNLKDVMPAGK 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 828 PIGNLGCYILDGN--LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE---------------------- 883
Cdd:TIGR03443 598 GMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkperefwlgprd 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 884 RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQ-LVGYVVLESEGGDWR 959
Cdd:TIGR03443 678 RLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrrdKDEEPtLVSYIVPQDKSDELE 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 960 EALAAHLAASL--------------------------PEYMVPAQWLALERMPLSPNGKLDRKALPAPEVS-VAQAGYSA 1012
Cdd:TIGR03443 758 EFKSEVDDEESsdpvvkglikyrklikdireylkkklPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAqLAAVAKNR 837
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 1013 PRNAV-------ERTLAEIWQDLL--GVERVGLDDNFFSLGGDSIVSIQVV 1054
Cdd:TIGR03443 838 SASAAdeeftetEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMI 888
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
3044-3525 |
1.04e-83 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 286.41 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSQSHLKLpLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:PRK04813 88 AERIEMIIEVAKPSLIIATEELPL-EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDH---RDPAKLVALINREGVDTLHFVPS 3280
Cdd:PRK04813 167 NLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVAL---PKdmtANFKQLFETLPQLPINVWVSTPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVASCT--SLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcVE------EGKDAVPI 3352
Cdd:PRK04813 244 FADMCLLDPSFNEEHlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTS---IEitdemlDQYKRLPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLArYRADGVIEYAGR 3432
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAG-YLEDGLLFYQGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR--QLVGYVVLESESGDwREALAAHL-----AASLPEYMVP 3503
Cdd:PRK04813 397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDHKvqYLIAYVVPKEEDFE-REFELTKAikkelKERLMEYMIP 475
|
490 500
....*....|....*....|..
gi 2310915810 3504 AQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK04813 476 RKFIYRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
3045-3525 |
1.22e-83 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 285.88 E-value: 1.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3045 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 3124
Cdd:TIGR01734 7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3125 ERQAYMLEDSGVELLLSQSHLKLP-LAQGVQRIDLDRGApwFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:TIGR01734 87 ERIEMIIEAAGPELVIHTAELSIDaVGTQIITLSALEQA--ETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQISHD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQ 3283
Cdd:TIGR01734 165 NLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3284 AFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA---VPIG--RPI 3356
Cdd:TIGR01734 245 MCLLDPNFNQenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQyprLPIGfaKPD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLacYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 3436
Cdd:TIGR01734 325 MNL--FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGTIT-DGQLFYQGRLDFQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR--QLVGYVVLESESGDwREALAAHL-----AASLPEYMVPAQW 3506
Cdd:TIGR01734 399 IKLHGYRIELEDIEFNLRQSSYIESAVVVPKynkDHKveYLIAAIVPETEDFE-KEFQLTKAikkelKKSLPAYMIPRKF 477
|
490
....*....|....*....
gi 2310915810 3507 LALERMPLSPNGKLDRKAL 3525
Cdd:TIGR01734 478 IYRDQLPLTANGKIDRKAL 496
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
4084-4519 |
2.06e-83 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 283.46 E-value: 2.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4084 VEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQgELQQPLQIVYRQRQ 4162
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGeLDPERLEKALQELINRHDALRTVFIRQ-ENGEPVQVILEERP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4163 LPFAEEDLSQAANRDAALL--ALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA 4240
Cdd:pfam00668 80 FELEIIDISDLSESEEEEAieAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 ----GRSPEQPRDGRYSDYIAWLQR----QDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATATA 4312
Cdd:pfam00668 160 qllkGEPLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKG-DRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4313 RLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGL 4392
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4393 QRQNLALREQEHTPLFELQR----WAGFGGEAVFDNLLVFENYPVDEVLE---RSSAGGVRFGaVAMHEQTNYPLAL-AL 4464
Cdd:pfam00668 317 QEDLLSAEPHQGYPFGDLVNdlrlPRDLSRHPLFDPMFSFQNYLGQDSQEeefQLSELDLSVS-SVIEEEAKYDLSLtAS 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4465 GGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQML---EKAEL 4519
Cdd:pfam00668 396 ERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLsdaEKQKL 453
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
52-478 |
9.49e-81 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 274.96 E-value: 9.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDC 131
Cdd:cd20484 4 LSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 132 SGLPEAEQEARLREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEP 211
Cdd:cd20484 84 SSLKESEIIAYLREKAK----EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARR 291
Cdd:cd20484 160 TLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 292 QGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAH 371
Cdd:cd20484 240 QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 372 QDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLV--ADIEALDSV--AGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAA 447
Cdd:cd20484 320 AAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLqsTSLQQFLAEyqDVLSIEFVEGIHQEGEYELVLEVYEQEDRFTLN 399
|
410 420 430
....*....|....*....|....*....|.
gi 2310915810 448 LTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd20484 400 IKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
52-478 |
6.86e-79 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 269.46 E-value: 6.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:cd19543 4 LSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGL----GEPLQvvlkdRKLPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19543 80 RELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 207 TGAEPGLPALPiQYADYAlwqrSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:cd19543 160 EGQPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNrAEVEGL---IGLFVNTQVLRSVFDGRTSVATLLAGLKD 363
Cdd:cd19543 235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 364 TVLGAQAHQDLPferLVEAFKveRSLSHSPLFQ--VMYNHQPLVADIEALDSVAGLSFGQLDWKSRtTQFDLSLDTYEkG 441
Cdd:cd19543 314 QQLELREHEYVP---LYEIQA--WSEGKQALFDhlLVFENYPVDESLEEEQDEDGLRITDVSAEEQ-TNYPLTVVAIP-G 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 2310915810 442 GRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19543 387 EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
52-471 |
9.65e-79 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 269.13 E-value: 9.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDC 131
Cdd:cd20483 4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 132 SGlpEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEP 211
Cdd:cd20483 84 SE--AADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 212 -GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKL-GERHPVLELPTDH-PRPVVPSYRGSRYEFSIEPALAEALRGT 288
Cdd:cd20483 162 aTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLeGIPDASKLLPFAKaERPPVKDYERSTVEATLDKELLARMKRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 289 ARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGA 368
Cdd:cd20483 242 CAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 369 QAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQplvadiealdsVAGlSFGQLDWKSRT----------TQFDLSLDTY 438
Cdd:cd20483 322 YEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-----------VHG-KFPEYDTGDFKftdydhydipTACDIALEAE 389
|
410 420 430
....*....|....*....|....*....|....
gi 2310915810 439 EKG-GRLYAALTYATDLFEARTVERMARHWQNLL 471
Cdd:cd20483 390 EDPdGGLDLRLEFSTTLYDSADMERFLDNFVTFL 423
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
4087-4504 |
6.09e-77 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 263.54 E-value: 6.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQLPF 4165
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSFIEDG-LGQPVQVVHRQAQVPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHH-LIYTHHHILLDGWSNAQLLSEVLESYAGRS- 4243
Cdd:cd19536 80 TELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFlLVISDHHSILDGWSLYLLVKEILAVYNQLLe 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4244 -------PEQPrdgrYSDYIAWLQRQ-DAAATEAFWREQMAALDEPTrlvealAQPGLTSANGVGEHLRE--VDATATAR 4313
Cdd:cd19536 160 ykplslpPAQP----YRDFVAHERASiQQAASERYWREYLAGATLAT------LPALSEAVGGGPEQDSEllVSVPLPVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4314 LRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLaPQMTLDELLQGLQ 4393
Cdd:cd19536 230 SRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4394 RQNLALREQEHTPLFELQRWAgfGGEAVFDNLLVFENYPVDEVL-ERSSAGGVRFGAVAMHEQTNYPLALALG-GGDSLS 4471
Cdd:cd19536 309 EQELESLSHEQVPLADIQRCS--EGEPLFDSIVNFRHFDLDFGLpEWGSDEGMRRGLLFSEFKSNYDVNLSVLpKQDRLE 386
|
410 420 430
....*....|....*....|....*....|...
gi 2310915810 4472 LQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19536 387 LKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1549-1975 |
1.08e-76 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 264.20 E-value: 1.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1549 VRDIYPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQA 1625
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMpavLKLT-GELDPERLEKALQELINRHDALRTVFIRQEN-GEPVQVILEER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1626 TLELRLA----PPGSDPQRQAEA----EREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY 1697
Cdd:pfam00668 79 PFELEIIdisdLSESEEEEAIEAfiqrDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1698 A----GQEVAA-TVGRYRDYIGW----LQGRDAMATEFFWRDRLASLEMPTRLARQARTEQPGQ---GEHLRELDPQTTR 1765
Cdd:pfam00668 159 QqllkGEPLPLpPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSfkgDRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1766 QLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGM 1845
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1846 QALNLALREHEHTPLYDIQRWAGH----GGEALFDSILVFENFPVAEALRQAP--ADLEFS-TPSNHEQTNYPLTL-GVT 1917
Cdd:pfam00668 317 QEDLLSAEPHQGYPFGDLVNDLRLprdlSRHPLFDPMFSFQNYLGQDSQEEEFqlSELDLSvSSVIEEEAKYDLSLtASE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 1918 LGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEAL 1975
Cdd:pfam00668 397 RGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
51-478 |
6.16e-76 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 260.85 E-value: 6.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 51 RLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF-PRGADDSLAQAPLQRP-LEVAF 128
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLASSpLRLEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 129 EDCSGLPEAEQE-ARLREeaqreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAyat 207
Cdd:cd19532 83 VQISDEAEVEEEfERLKN-------HVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 208 gaePGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLEL---PTDHPRPVVPSYRGSRYEFSIEPALAEA 284
Cdd:cd19532 153 ---QPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:cd19532 230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 365 VLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALDSVAGLSfgqLDWKSRTTQFDLSLDTYEKGGRl 444
Cdd:cd19532 310 AYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEG---EEFEDARTPYDLSLDIIDNPDG- 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 2310915810 445 YAALTYAT--DLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19532 386 DCLLTLKVqsSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
2586-2827 |
5.57e-75 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 251.11 E-value: 5.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2586 LSHAQQRMWFLwklEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDC 2665
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2666 AG----ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQP 2741
Cdd:COG4908 78 SAlpepEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*.
gi 2310915810 2822 EGVTPF 2827
Cdd:COG4908 238 HGATVN 243
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
2583-3005 |
2.76e-74 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 256.64 E-value: 2.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19546 4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAgASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPT 2742
Cdd:cd19546 84 PVVP-ATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2743 LAPLKLQYADYAAWHRAWLDsGEGAR------QLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELL 2816
Cdd:cd19546 163 RAPLPLQFADYALWERELLA-GEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2817 ACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN-RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAA 2895
Cdd:cd19546 242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2896 LGAQAHQDLPFEQLVDALQPERNLSHSPLFQV---MYNHQSGERQDAQVDGLHIESFAWDGAAAQFDL--ALDTWET--- 2967
Cdd:cd19546 322 REARRHQDVPFERLAELLALPPSADRHPVFQValdVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLslALTERRNddg 401
|
410 420 430
....*....|....*....|....*....|....*....
gi 2310915810 2968 -PDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19546 402 dPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
4087-4504 |
1.02e-73 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 254.54 E-value: 1.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVD-VSGLDIPRFRAAWQSALDRHAILRSGFAWQgELQQPLQIVYRQRQLPF 4165
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLElVGGTDEDVLREAWRRVADRYEILRTGFTWR-DRAEPLQYVRDDLAPPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAA--NRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA--- 4240
Cdd:cd19547 80 ALLDWSGEDpdRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEela 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 -GRSPEQPRDGRYSDYIAWLQRQDAAATEA--FWREQMAALdEPTRLVEALA-QPGL--TSANGVGEHLREVDATAtarl 4314
Cdd:cd19547 160 hGREPQLSPCRPYRDYVRWIRARTAQSEESerFWREYLRDL-TPSPFSTAPAdREGEfdTVVHEFPEQLTRLVNEA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4315 rdfARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQR 4394
Cdd:cd19547 235 ---ARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4395 QNLALREQEHTPLFELQRWAG---FGGEAVFDNLLVFENYPVDEVLERSSAggVRFGAVAMHEQTNYPLALALGGGDSLS 4471
Cdd:cd19547 312 DLATTAAHGHVPLAQIKSWASgerLSGGRVFDNLVAFENYPEDNLPGDDLS--IQIIDLHAQEKTEYPIGLIVLPLQKLA 389
|
410 420 430
....*....|....*....|....*....|...
gi 2310915810 4472 LQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19547 390 FHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
4087-4504 |
1.18e-72 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 250.69 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLyeQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQ----- 4160
Cdd:cd19542 1 IYPCTPMQEGMLLSQL--RSPGLYFNHFVFDLDSsVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSldppi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4161 RQLPFAEEDLSQAANRDAALLalaaaerergfELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA 4240
Cdd:cd19542 79 EEVETDEDSLDALTRDLLDDP-----------TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 GRSPEQPRDgrYSDYIAWLQRQDAAATEAFWREQMAAldeptrlVEALAQPgltSANGVGEHLREVDATA--TARLRDFA 4318
Cdd:cd19542 148 GQLLPPAPP--FSDYISYLQSQSQEESLQYWRKYLQG-------ASPCAFP---SLSPKRPAERSLSSTRrsLAKLEAFC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLA 4398
Cdd:cd19542 216 ASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4399 LREQEHTPLFELQRWAGF-GGEAVFDNLLVFENYPVDEvlERSSAGGVRFGAVAMHEQTNYPLALA-LGGGDSLSLQFSY 4476
Cdd:cd19542 296 SLPHQHLSLREIQRALGLwPSGTLFNTLVSYQNFEASP--ESELSGSSVFELSAAEDPTEYPVAVEvEPSGDSLKVSLAY 373
|
410 420
....*....|....*....|....*...
gi 2310915810 4477 DRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19542 374 STSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1899-2565 |
6.82e-70 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 262.31 E-value: 6.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1899 FSTPSNhEQTNY----PLTLGVTLGE---RLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGER 1971
Cdd:TIGR03443 141 QDAPDN-QQTTYstgsTTDLTVFLTPsspELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1972 QeALRDWQAPLEALP-RGGVAAAFAHQVASAPEAIALVCGDEHL---------SYAELDMRAERLARGLRARGVVAEALV 2041
Cdd:TIGR03443 220 S-LLPDPTKDLDWSGfRGAIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2042 AIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI---------------CQETLAERLPCPA--- 2103
Cdd:TIGR03443 299 MIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIviekagtldqlvrdyIDKELELRTEIPAlal 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2104 ---------EVERLPLET-AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:TIGR03443 379 qddgslvggSLEGGETDVlAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASISFDAAAEQLFVPLLAGARVL------LGDAGQwsaqhLADEVERHAVTILDLPPAY---LQQQAEE----LRH 2240
Cdd:TIGR03443 459 FTMLSGIAHDPIQRDMFTPLFLGAQLLvptaddIGTPGR-----LAEWMAKYGATVTHLTPAMgqlLSAQATTpipsLHH 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 A---GRRIAVRTCilggeawdaslLTQQAVqAEAWF--NAYGPTE---AV----ITPlawhcRAQEGG--------APAi 2300
Cdd:TIGR03443 534 AffvGDILTKRDC-----------LRLQTL-AENVCivNMYGTTEtqrAVsyfeIPS-----RSSDSTflknlkdvMPA- 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2301 GRALgarraciLDAAL---------QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFV----ADP-------------- 2353
Cdd:TIGR03443 596 GKGM-------KNVQLlvvnrndrtQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfVDPshwidldkennkpe 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 ---FSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE-AAVVALDGVGGPLLAAYLV 2429
Cdd:TIGR03443 669 refWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEPTLVSYIV 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2430 GRD------AMRGED------------------LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP----- 2480
Cdd:TIGR03443 749 PQDksdeleEFKSEVddeessdpvvkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdta 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2481 KVDAAARRQAGEPPREGL---ERSVAAIWEALL--GVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERP 2555
Cdd:TIGR03443 829 QLAAVAKNRSASAADEEFtetEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSP 908
|
810
....*....|
gi 2310915810 2556 VLADFAASLE 2565
Cdd:TIGR03443 909 TIKGFAKEVD 918
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
4281-5122 |
2.29e-69 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 260.77 E-value: 2.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4281 PTRLVEALAQPGLTSAngvgehlrevDATATARLRDFArrhqvtlntLVQAGWALLLQRYTGQHTVVFG--ATVSGRPad 4358
Cdd:TIGR03443 23 NNRLVEATYSLQLPSA----------EVTAGGGSTPFI---------ILLAAFAALVYRLTGDEDIVLGtsSNKSGRP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4359 lpgvenqvglFIntlpVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQrwagfggeavfdnllvfENYPVDEVLE 4438
Cdd:TIGR03443 82 ----------FV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELS-----------------EHIQAAKKLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4439 RSSaGGVRFGAVAMH--EQTNYP------LALALGGGDS-LSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQrrlv 4509
Cdd:TIGR03443 131 RTP-PLFRLAFQDAPdnQQTTYStgsttdLTVFLTPSSPeLELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPD---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4510 dlqmlekaelSAIGAIWNRSDSGYPATPL-------------VHQRVAERARMAPDAVAVIFDEEKL---------TYAE 4567
Cdd:TIGR03443 206 ----------EPIGKVSLITPSQKSLLPDptkdldwsgfrgaIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4568 LDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRahlllthshller 4647
Cdd:TIGR03443 276 INEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAK------------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4648 lpiPEGLSCLS------------VDREEEW----------------AGFP---AHD---PEVALHGDNLAYVI------- 4686
Cdd:TIGR03443 343 ---PRALIVIEkagtldqlvrdyIDKELELrteipalalqddgslvGGSLeggETDvlaPYQALKDTPTGVVVgpdsnpt 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4687 --YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLI--RDDsLWLPERT 4762
Cdd:TIGR03443 420 lsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVptADD-IGTPGRL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 YAEMHRHGVTVGVFPPVYLQQLAEHAERdgNPPPVRVYCFGGDAVAQAsyD-LAWRALKPK-YLFNGYGPTET--VVTPL 4838
Cdd:TIGR03443 499 AEWMAKYGATVTHLTPAMGQLLSAQATT--PIPSLHHAFFVGDILTKR--DcLRLQTLAENvCIVNMYGTTETqrAVSYF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAA----YMPIGT-------LLGNRSGyildgQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPD 4907
Cdd:TIGR03443 575 EIPSRSSDSTFLKnlkdVMPAGKgmknvqlLVVNRND-----RTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNN 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4908 PFGAPGS---------------------RLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4966
Cdd:TIGR03443 650 WFVDPSHwidldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4967 VVVAQPGAVGQQ-LVGYVVAQ------EPAVADSPEAQA------------ECRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:TIGR03443 730 VTLVRRDKDEEPtLVSYIVPQdksdelEEFKSEVDDEESsdpvvkglikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKL 809
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5028 PLTPNGKLDRKGLPQPDASLLQQVYVAPRSD--------LEQQVAGIWAEVL--QLQQVGLDDNFFELGGHSLLAIQVTA 5097
Cdd:TIGR03443 810 PLNPNGKVDKPALPFPDTAQLAAVAKNRSASaadeefteTEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIF 889
|
970 980
....*....|....*....|....*
gi 2310915810 5098 RMQSEVGVELPLAALFQTESLQAYA 5122
Cdd:TIGR03443 890 ELRKKLNVELPLGLIFKSPTIKGFA 914
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
2131-2475 |
5.30e-69 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 237.57 E-value: 5.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQ 2210
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL--LPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVITPLAW 2288
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERfEEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2289 HCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgsGERLYRTGDLA 2368
Cdd:cd04433 159 PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWL 2447
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpDPEWGERVVAVVVLRPG--ADLDAEELRAHV 308
|
330 340
....*....|....*....|....*...
gi 2310915810 2448 AGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd04433 309 RERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1096-1529 |
1.09e-68 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 241.08 E-value: 1.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1096 GEVALAPVQ--RWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRF-REERGAWHQAYAEQAGEPL 1172
Cdd:pfam00668 3 DEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILEERPFEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 W----RRQAGS--EEALLALCEE-AQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLD 1245
Cdd:pfam00668 83 EiidiSDLSESeeEEAIEAFIQRdLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1246 AdlG-----PRSSSYQTWSRHLHEQAG--ARLDELDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAErTRQL 1316
Cdd:pfam00668 163 K--GeplplPPKTPYKDYAEWLQQYLQseDYQKDAAYWLEQLegELPVLQLPKDYARPADRSFKGDRLSFTLDED-TEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1317 LQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLgeaiDLSRTVGWFTSLFPVRLTPAA--DLGESLKA 1394
Cdd:pfam00668 240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP----DIERMVGMFVNTLPLRIDPKGgkTFSELIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1395 IKEQLRGV-PDKGVGYGLLRYLAGEEAATRLAALPQPRITF-NYLGRFD----RQFDGaalLVPATESAGAAQDPCApla 1468
Cdd:pfam00668 316 VQEDLLSAePHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQDSqeeeFQLSE---LDLSVSSVIEEEAKYD--- 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 1469 nwLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHCLDPRHRGVTPSDF 1529
Cdd:pfam00668 390 --LSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDA 448
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
3621-4051 |
1.47e-68 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 240.70 E-value: 1.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3621 VSGETVLLPFQ--RLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRF-HETDGT---WHAEHAEA 3694
Cdd:pfam00668 1 VQDEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEpvqVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3695 TLGGALLWRAEAVD--RQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQ 3772
Cdd:pfam00668 81 ELEIIDISDLSESEeeEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3773 SLRGEAPRLPGKTsPFKAWAGRVSEHARGESMKAQLQFWRELLEG--APAELPCEHPQGALEQRFATSVQSRFDRSLTER 3850
Cdd:pfam00668 161 LLKGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGelPVLQLPKDYARPADRSFKGDRLSFTLDEDTEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3851 LLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELfadiDLSRTVGWFTSLFPVRL--SPVADLGESLK 3928
Cdd:pfam00668 240 LRKLA-KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP----DIERMVGMFVNTLPLRIdpKGGKTFSELIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3929 AIKEQLR-AIPDKGLGYGLLRYLAGEESARVLAGLPQARITF-NYLGQFD-AQFDEMALLDPAGESAGAEMDPGApldnw 4005
Cdd:pfam00668 315 RVQEDLLsAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQDSqEEEFQLSELDLSVSSVIEEEAKYD----- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2310915810 4006 LSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFC 4051
Cdd:pfam00668 390 LSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHP 435
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1552-1956 |
2.01e-68 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 239.14 E-value: 2.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTEGD-YVNQLRMD-IGGLDPDRFRAAWQATLDAHEILRSGFLWKDgWPQPLQVVFEQatlel 1629
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSDaYFNQNVLElVGGTDEDVLREAWRRVADRYEILRTGFTWRD-RAEPLQYVRDD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 rLAPP-------GSDPQRQAEA-------EREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQ 1695
Cdd:cd19547 75 -LAPPwalldwsGEDPDRRAELlerlladDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1696 RYA----GQEVAATVGR-YRDYIGWLQGRDAMA--TEFFWRDRLASLEmPTRLArQARTEQPGQGEHL-RELDPQTTRQL 1767
Cdd:cd19547 154 VYEelahGREPQLSPCRpYRDYVRWIRARTAQSeeSERFWREYLRDLT-PSPFS-TAPADREGEFDTVvHEFPEQLTRLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1768 ASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQA 1847
Cdd:cd19547 232 NEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1848 LNLALREHEHTPLYDIQRWAGH---GGEALFDSILVFENFPvAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGERLSL 1924
Cdd:cd19547 312 DLATTAAHGHVPLAQIKSWASGerlSGGRVFDNLVAFENYP-EDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAF 390
|
410 420 430
....*....|....*....|....*....|..
gi 2310915810 1925 QYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19547 391 HFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
4087-4504 |
1.57e-67 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 235.66 E-value: 1.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLfhSLYEQASSDYINQMRVDVS-GLDIPRFRAAWQSALDRHAILRSGFAwQGELQQPLQIVYRQRQLPF 4165
Cdd:cd19545 1 IYPCTPLQEGLM--ALTARQPGAYVGQRVFELPpDIDLARLQAAWEQVVQANPILRTRIV-QSDSGGLLQVVVKESPISW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAANRDAALLALAAAerergfelqrAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPE 4245
Cdd:cd19545 78 TESTSLDEYLEEDRAAPMGLG----------GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4246 QPRDgrYSDYIAWLQRQDAAATEAFWREQMAALDEP--TRLVEALAQPgltsangvgehlrEVDATATARLR-DFARRHQ 4322
Cdd:cd19545 148 QPPP--FSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfPPLPSSRYQP-------------RPDATLEHSISlPSSASSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4323 VTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQ 4402
Cdd:cd19545 213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4403 EHTPlfeLQRWAGFGGEAV----FDNLLVFEnYPVDEVLERSSAGGVRFGAVAMHEQTNYPLALALG-GGDSLSLQFSYD 4477
Cdd:cd19545 293 EHTG---LQNIRRLGPDARaacnFQTLLVVQ-PALPSSTSESLELGIEEESEDLEDFSSYGLTLECQlSGSGLRVRARYD 368
|
410 420
....*....|....*....|....*..
gi 2310915810 4478 RGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19545 369 SSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
4087-4502 |
9.61e-67 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 233.87 E-value: 9.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG---LDipRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQL 4163
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSrarLD--AFLAALQQVIDRHDILRTAILWEG-LSEPVQVVWRQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4164 PFAEEDLSQAANRDAALLALAAAERERgFELQRAPLLRLLLVK-TAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGR 4242
Cdd:cd19544 78 PVEELTLDPGDDALAQLRARFDPRRYR-LDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4243 SPEQPRDGRYSDYIAWLQRQ-DAAATEAFWREQMAALDEPT---RLVEALAqpgltSANGVGEHLREVDATATARLRDFA 4318
Cdd:cd19544 157 AAALPPPVPYRNFVAQARLGaSQAEHEAFFREMLGDVDEPTapfGLLDVQG-----DGSDITEARLALDAELAQRLRAQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLApQMTLDELLQGLQRQNLA 4398
Cdd:cd19544 232 RRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4399 LREQEHTPLFELQRWAGFGGEA-VFDNLLvfeNY----PVDEVLERSSAGGVRFgaVAMHEQTNYPLALA---LGGGDSL 4470
Cdd:cd19544 311 LLRHEHASLALAQRCSGVPAPTpLFSALL---NYrhsaAAAAAAALAAWEGIEL--LGGEERTNYPLTLSvddLGDGFSL 385
|
410 420 430
....*....|....*....|....*....|..
gi 2310915810 4471 SLQfsYDRGLFPaatiERLGRHLTTLLEAFAE 4502
Cdd:cd19544 386 TAQ--VVAPIDA----ERVCAYMETALEQLVD 411
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
4541-5040 |
1.29e-66 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 236.72 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAHLL-LTHSHLLERLPIPEglscLSVDR-EEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:PRK04813 86 SPAERIEMIIEVAKPSLIiATEELPLEILGIPV----ITLDElKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHI------VATGERYEMtpedceLHFMSFAFDGSHEGWMHPLINGArvlirddSLWL--------PERTYA 4764
Cdd:PRK04813 162 QISHDNLVSFTnwmledFALPEGPQF------LNQAPYSFDLSVMDLYPTLASGG-------TLVAlpkdmtanFKQLFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVFPPVYLQQL-------AEHAerdgnpPPVRVYCFGGDA--VAQAsydlawRALKPKY----LFNGYGPT 4831
Cdd:PRK04813 229 TLPQLPINVWVSTPSFADMClldpsfnEEHL------PNLTHFLFCGEElpHKTA------KKLLERFpsatIYNTYGPT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4832 E-TV------VTP-LLwkaragdacgAAY--MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTA 4901
Cdd:PRK04813 297 EaTVavtsieITDeML----------DQYkrLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4902 ERFvpdpFGAPGSRLYRSGDLtrGRA-DGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVaqP----GAVg 4976
Cdd:PRK04813 367 EAF----FTFDGQPAYHTGDA--GYLeDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PynkdHKV- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4977 QQLVGYVVAQEPAVadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK04813 438 QYLIAYVVPKEEDF----EREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1552-1956 |
1.14e-65 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 230.80 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTEGD-YVNQLRMDIGG-LDPDRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQATLEL 1629
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSvYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSFIE-DGLGQPVQVVHRQAQVPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RL--APPGSDP----QRQAEAEREAGFDPARAPLQRLVLVPLA-NGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ-- 1700
Cdd:cd19536 80 TEldLTPLEEQldplRAYKEETKIRRFDLGRAPLVRAALVRKDeRERFLLVISDHHSILDGWSLYLLVKEILAVYNQLle 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1701 ---EVAATVGRYRDYIGWLQG-RDAMATEFFWRDRLASLEMPT----RLARQARTEQPGQgehLRELDPQTTRQlASFAQ 1772
Cdd:cd19536 160 ykpLSLPPAQPYRDFVAHERAsIQQAASERYWREYLAGATLATlpalSEAVGGGPEQDSE---LLVSVPLPVRS-RSLAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1773 GQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPViAAPQPQQSVADYLQGMQALNLAL 1852
Cdd:cd19536 236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPL-RVTLSEETVEDLLKRAQEQELES 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1853 REHEHTPLYDIQRWAghGGEALFDSILVFENFPVAEALRQAPADLEFSTPSNHEQ--TNYPLTLGVT-LGERLSLQYVYA 1929
Cdd:cd19536 315 LSHEQVPLADIQRCS--EGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSEfkSNYDVNLSVLpKQDRLELKLAYN 392
|
410 420
....*....|....*....|....*..
gi 2310915810 1930 RRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19536 393 SQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
2584-3005 |
1.18e-65 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 230.94 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFE-EVDGQARQTILANMPLRIVL 2662
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEATLRQRV----AEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19543 82 LDLSHLSEAEQEAELealaEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2739 EQPTLAPLKlQYADYAawhrAWLDSGEGARQLDYWRERL-GAEQPVlELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19543 162 QPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLaGFEEPT-PLPKELPADADGSYEPGEVSFELSAELTARLQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNrAE---VERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREA 2894
Cdd:cd19543 236 LARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AElpgIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2895 ALGAQAHQDLPfeqLVDaLQpERNLSHSPLFQVM-----YNHQSGERQDAQVDGLHIESFAWDGaAAQFDLALDTweTP- 2968
Cdd:cd19543 315 QLELREHEYVP---LYE-IQ-AWSEGKQALFDHLlvfenYPVDESLEEEQDEDGLRITDVSAEE-QTNYPLTVVA--IPg 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 2310915810 2969 DGLGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19543 387 EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
52-478 |
1.54e-64 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 228.52 E-value: 1.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADD---SLAQAPLQRP-LEVa 127
Cdd:cd19546 7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDvhqRILDADAARPeLPV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 128 fedcsgLPEAEQE--ARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAY 205
Cdd:cd19546 86 ------VPATEEElpALLADRAAH----LFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 206 ATGAEPGLPALPIQYADYALWQRSWLeAGEQER------QLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEP 279
Cdd:cd19546 156 REGRAPERAPLPLQFADYALWERELL-AGEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 280 ALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRN-RAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:cd19546 235 EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSL--- 435
Cdd:cd19546 315 GRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLSLalt 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2310915810 436 DTYEKGGR---LYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19546 395 ERRNDDGDpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
1387-1542 |
3.38e-64 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 216.37 E-value: 3.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1387 DLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAAtrLAALPQPRITFNYLGRFDRQfDGAALLVPATESAGAAQDPCAP 1466
Cdd:TIGR01720 1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEK--LAASPQPEISFNYLGQFDAD-SNDELFQPSSYSPGEAISPESP 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 1467 LANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHCLDPRHRGVTPSDFPLAGLSQTQLDEL 1542
Cdd:TIGR01720 78 RPYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
4541-5042 |
6.02e-64 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 228.87 E-value: 6.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERArmaPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:TIGR01734 7 QAFAETY---PQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLlYMMQDSrahLLLTHSHLLERLPIP-EGLSCLSVDREE--EWAGFPaHDPEVALHGDNLAYVIYTSGSTGMPKG 4697
Cdd:TIGR01734 84 IPSERI-EMIIEA---AGPELVIHTAELSIDaVGTQIITLSALEqaETSGGP-VSFDHAVKGDDNYYIIYTSGSTGNPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4698 VAVSHGPLIAHIVATGERYeMTPEdcELHFMS---FAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTV 4773
Cdd:TIGR01734 159 VQISHDNLVSFTNWMLADF-PLSE--GKQFLNqapFSFDLSVMDLYPCLASGGTlHCLDKDITNNFKLLFEELPKTGLNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4774 GVFPPVYLQQ--LAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTplLWKARAGDACGAA 4851
Cdd:TIGR01734 236 WVSTPSFVDMclLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKAT-IYNTYGPTEATVA--VTSVKITQEILDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4852 Y--MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpFGAPGSRLYRSGDLTRgRADG 4929
Cdd:TIGR01734 313 YprLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHEGQPAYRTGDAGT-ITDG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4930 VVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVA--QPGAVGQQLVGYVVAQEpavaDSPEAQAECRAQLKTA 5007
Cdd:TIGR01734 388 QLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPkyNKDHKVEYLIAAIVPET----EDFEKEFQLTKAIKKE 463
|
490 500 510
....*....|....*....|....*....|....*
gi 2310915810 5008 LRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:TIGR01734 464 LKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAE 498
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
4543-5037 |
1.02e-63 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 225.95 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAhlllthshllerlpipeglsclsvdreeewagfpahdpEVALhgDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:cd17631 81 PPEVAYILADSGA--------------------------------------KVLF--DDLALLMYTSGTTGRPKGAMLTH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:cd17631 121 RNLLWNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRK--FDPETVLDLIERHRVTSFFLVPTMI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAEHAERDG-NPPPVRVYCFGGDAVAQASYdLAWRALKPKYLfNGYGPTET--VVTPLLWK---ARAGdACGAAYMPI 4855
Cdd:cd17631 199 QALLQHPRFATtDLSSLRAVIYGGAPMPERLL-RALQARGVKFV-QGYGMTETspGVTFLSPEdhrRKLG-SAGRPVFFV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLG 4935
Cdd:cd17631 276 EV-------RIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPE 5014
Cdd:cd17631 341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEAVVAVVVPRPGAELDEDELIAHC--------RERLAR 412
|
490 500
....*....|....*....|...
gi 2310915810 5015 YMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17631 413 YKIPKSVEFVDALPRNATGKILK 435
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
2002-2481 |
1.73e-63 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 227.74 E-value: 1.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:TIGR03098 14 PDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIcqeTLAERL---------------------PCPAEVERLPLETAAWP---ASADTRPLPEVAGETLAYVIY 2137
Cdd:TIGR03098 94 ADCNVRLLV---TSSERLdllhpalpgchdlrtliivgdPAHASEGHPGEEPASWPkllALGDADPPHPVIDSDMAAILY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVE 2217
Cdd:TIGR03098 171 TSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD--YLLPRDVLKALE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2218 RHAVT-ILDLPPAYLQ----QQAEELRHAGRRIAVRtcilGGEAWDASL--LTQQAVQAEAwFNAYGPTEAV----ITPl 2286
Cdd:TIGR03098 249 KHGITgLAAVPPLWAQlaqlDWPESAAPSLRYLTNS----GGAMPRATLsrLRSFLPNARL-FLMYGLTEAFrstyLPP- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 awhcrAQEGGAP-AIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRT- 2364
Cdd:TIGR03098 323 -----EEVDRRPdSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHLPELa 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 ---GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLV------GRDAMR 2435
Cdd:TIGR03098 398 vwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAF---GVPDPTLGQAIVlvvtppGGEELD 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 2436 GEDLLAELRTwlagRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:TIGR03098 475 RAALLAECRA----RLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1993-2479 |
3.23e-63 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 228.46 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1993 AFAHQVASAPEAIALVCGDE-----HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLICQ----------------ETLAERLPCPAEV-------ERLPLETAAW-----PASA 2119
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITAdgglrggkvidlkekvDEALEELPSLEHVivvgrtgADVPMEGDLDwdellAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2120 DTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGDCQLQFASISF-----DAaaeqLFVPL 2193
Cdd:COG0365 174 AEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGWatghsYI----VYGPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2194 LAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDASLLtqqavq 2268
Cdd:COG0365 250 LNGATVVLyeGRPDFPDPGRLWELIEKYGVTVFFTAPTAiraLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVW------ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2269 aEAWFNA--------YGPTE---AVITPLawhcraqeGGAP----AIGRALGARRACILDAALQPCAPGMIGELYIGGQC 2333
Cdd:COG0365 324 -EWWYEAvgvpivdgWGQTEtggIFISNL--------PGLPvkpgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2334 --LARGYLGRPGQTAERFVaDPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:COG0365 395 pgMFRGYWNDPERYRETYF-GRFPG----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2412 AVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:COG0365 470 AVVGVpDEIRGQVVKAFVVLKPgVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1552-1954 |
4.17e-63 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 223.47 E-value: 4.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTEGD-YV--NQLRMDigglDP---DRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQA 1625
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDpYLlrSLLAFD----SRarlDAFLAALQQVIDRHDILRTAILW-EGLSEPVQVVWRQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1626 TL---ELRLaPPGSDPQRQAEAEREAG---FDPARAPLQRLVLVP-LANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA 1698
Cdd:cd19544 76 ELpveELTL-DPGDDALAQLRARFDPRryrLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1699 GQEVA-ATVGRYRDYIG--WLQGRDAMATEFFwRDRLASLEMPT---RLArQARTEQPGQGEHLRELDPQTTRQLASFAQ 1772
Cdd:cd19544 155 GRAAAlPPPVPYRNFVAqaRLGASQAEHEAFF-REMLGDVDEPTapfGLL-DVQGDGSDITEARLALDAELAQRLRAQAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1773 GQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQpQQSVADYLQGMQALNLAL 1852
Cdd:cd19544 233 RLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1853 REHEHTPLYDIQRWAG-HGGEALFDSILVFENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVT-LGERLSLQyVYAR 1930
Cdd:cd19544 312 LRHEHASLALAQRCSGvPAPTPLFSALLNYRHSAAAAAAAALAAWEGIELLGGEERTNYPLTLSVDdLGDGFSLT-AQVV 390
|
410 420
....*....|....*....|....
gi 2310915810 1931 RDFDAADIAELdrhLLHLLQRMAE 1954
Cdd:cd19544 391 APIDAERVCAY---METALEQLVD 411
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
655-994 |
7.05e-63 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 219.85 E-value: 7.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 655 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPA 734
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 735 KLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTH 812
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKapESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 813 WTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLA 892
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAA 968
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdpewGERVVAVVVLRPGADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 2310915810 969 SLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
3182-3521 |
1.52e-62 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 219.08 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3182 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPA 3261
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3262 KLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKapESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLA 3419
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAA 3495
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdpewGERVVAVVVLRPGADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 2310915810 3496 SLPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
4547-5038 |
1.47e-61 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 223.45 E-value: 1.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEE-----KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:COG0365 19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 PRERLLYMMQDSRA----------------HLLLTHSHLLERLPIPEglSCLSVDREEE---------WAGFPAHDPE-- 4674
Cdd:COG0365 99 GAEALADRIEDAEAkvlitadgglrggkviDLKEKVDEALEELPSLE--HVIVVGRTGAdvpmegdldWDELLAAASAef 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 --VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGER-YEMTPEDCelhFMSFAfDgshEGWMH--------PL 4743
Cdd:COG0365 177 epEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDV---FWCTA-D---IGWATghsyivygPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDSLWLP--ERTYAEMHRHGVTV-GVFPPVY--LQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRA 4818
Cdd:COG0365 250 LNGATVVLYEGRPDFPdpGRLWELIEKYGVTVfFTAPTAIraLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4819 LKpKYLFNGYGPTET---VVTPL-LWKARAGdACGAAyMPigtllgnrsGY---ILDGQLNLLPVGVAGELYLGGE--GV 4889
Cdd:COG0365 330 VG-VPIVDGWGQTETggiFISNLpGLPVKPG-SMGKP-VP---------GYdvaVVDEDGNPVPPGEEGELVIKGPwpGM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4890 ARGYLERPALTAERFVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVV 4969
Cdd:COG0365 398 FRGYWNDPERYRETYFGRFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4970 AQPGAV-GQQLVGYVVAQEPAVADspeaqAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:COG0365 473 GVPDEIrGQVVKAFVVLKPGVEPS-----DELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRR 537
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
4088-4504 |
1.50e-61 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 219.15 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqQPLQIVYRQRQLPFA 4166
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGpLDVAALERALNELVARHEALRTTFVEVDG--EPVQVILPPLPLPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4167 EEDLSQAANRDAALLALAAAERERG--FELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSP 4244
Cdd:cd19531 80 VVDLSGLPEAEREAEAQRLAREEARrpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4245 EQPRD-----GRYSDYIAWlQRQDAAATE-----AFWREQMAalDEPTRLveAL----AQPGLTSANGvGEHLREVDATA 4310
Cdd:cd19531 160 GRPSPlpplpIQYADYAVW-QREWLQGEVlerqlAYWREQLA--GAPPVL--ELptdrPRPAVQSFRG-ARVRFTLPAEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4311 TARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpaDLPGVENQVGLFINTLPVVVTLAPQMTLDELLQ 4390
Cdd:cd19531 234 TAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGR--NRAELEGLIGFFVNTLVLRTDLSGDPTFRELLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4391 --------GLQRQNL-------AL---REQEHTPLfelqrwagfggeavFDNLLVFENYPVDEVLerssAGGVRFGAVAM 4452
Cdd:cd19531 312 rvretaleAYAHQDLpfeklveALqpeRDLSRSPL--------------FQVMFVLQNAPAAALE----LPGLTVEPLEV 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4453 HEQT-NYPLALALG-GGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19531 374 DSGTaKFDLTLSLTeTDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
4682-5036 |
2.01e-61 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 215.61 E-value: 2.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDslWLPER 4761
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK--FDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4762 TYAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTPLLW 4840
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGyDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 KARAGDAcgaAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPdpfgapgsRLYRSG 4920
Cdd:cd04433 159 PPDDDAR---KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED--------GWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqae 4999
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEwGERVVAVVVLRPGADLD------- 300
|
330 340 350
....*....|....*....|....*....|....*..
gi 2310915810 5000 cRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd04433 301 -AEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
4544-5040 |
4.34e-61 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 219.36 E-value: 4.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:cd05936 6 EEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLpipeglsclsvdreeewAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd05936 86 RELEHILNDSGAKALIVAVSFTDLL-----------------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERYEMTPEDCELH------FMSFAFDgshEGWMHPLINGARVLI--RDDslwlPERTYAEMHRHGVTV-- 4773
Cdd:cd05936 149 NLVANALQIKAWLEDLLEGDDVVlaalplFHVFGLT---VALLLPLALGATIVLipRFR----PIGVLKEIRKHRVTIfp 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4774 GVfPPVYLqQLAEHAERDG-NPPPVRVYCFGGDAVAQAsYDLAWRALKPKYLFNGYGPTET--VVT--PLLWKARAGDac 4848
Cdd:cd05936 222 GV-PTMYI-ALLNAPEFKKrDFSSLRLCISGGAPLPVE-VAERFEELTGVPIVEGYGLTETspVVAvnPLDGPRKPGS-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4849 gaaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRAD 4928
Cdd:cd05936 297 ------IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4929 G---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraql 5004
Cdd:cd05936 363 GyffIVD---RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYsGEAVKAFVVLKEGASLTEEEIIAFC---- 435
|
490 500 510
....*....|....*....|....*....|....*.
gi 2310915810 5005 ktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05936 436 ----REQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
539-1001 |
1.06e-60 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 219.70 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQaymledsgvqlllsqsHL 618
Cdd:cd17647 23 YRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQ----------------NI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 KLPLAQGVQRIDLDQADAWLenHAENNPGIElngenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:cd17647 87 YLGVAKPRGLIVIRAAGVVV--GPDSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 699 QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQaFLQDEDVASCTSLKRIVCSGE 778
Cdd:cd17647 155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQ-LLTAQATTPFPKLHHAFFVGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 779 ALPAD--AQQQVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDTVPIGRPIGNLGCYILDGN--LEPVP 845
Cdd:cd17647 234 ILTKRdcLRLQTLA--ENVRIVNMYGTTETQRAVSYFevpsrssdpTFLKNLKDVMPAGRGMLNVQLLVVNRNdrTQICG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 846 VGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE----------------------RMYRTGDLARYRADGVIEYA 903
Cdd:cd17647 312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 904 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEG-GDWREALAAHLAASL-------- 970
Cdd:cd17647 392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrrdKDEEPTLVSYIVPRFDKpDDESFAQEDVPKEVStdpivkgl 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 971 ------------------PEYMVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:cd17647 472 igyrklikdireflkkrlASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1552-1956 |
1.11e-60 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 216.02 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLhGTEGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPQPLQVVFEQATLELR 1630
Cdd:cd19542 1 IYPCTPMQEGMLLSQL-RSPGLYFNHFVFDLdSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSLDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1631 LAPPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGrYR 1710
Cdd:cd19542 80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPP-FS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1711 DYIGWLQGRDAMATEFFWRDRLASLEmptrlarqaRTEQP---GQGEHLRELDpQTTRQLA---SFAQGQKVTLNTLVQA 1784
Cdd:cd19542 159 DYISYLQSQSQEESLQYWRKYLQGAS---------PCAFPslsPKRPAERSLS-STRRSLAkleAFCASLGVTLASLFQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1785 AWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQ 1864
Cdd:cd19542 229 AWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1865 RWAG-HGGEALFDSILVFENFPvAEALRQAPADLEFSTPSNHEQTNYPLTLGVT-LGERLSLQYVYARRDFDAADIAELD 1942
Cdd:cd19542 309 RALGlWPSGTLFNTLVSYQNFE-ASPESELSGSSVFELSAAEDPTEYPVAVEVEpSGDSLKVSLAYSTSVLSEEQAEELL 387
|
410
....*....|....
gi 2310915810 1943 RHLLHLLQRMAETP 1956
Cdd:cd19542 388 EQFDDILEALLANP 401
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
2002-2479 |
2.25e-60 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 218.23 E-value: 2.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK04813 16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIC-QETLAERLPCP----AEVERLPLETAAWPASAdtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK04813 96 EVAKPSLIIAtEELPLEILGIPvitlDELKDIFATGNPYDFDH------AVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAgqwsaqhlaDEVERHAV---TILDLP------ 2227
Cdd:PRK04813 170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPK---------DMTANFKQlfeTLPQLPinvwvs 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2228 -----------PAYLQQQAEELRH---AGRRIAVRTcilggeawdASLLTQQAVQAEAwFNAYGPTEAV-------ITP- 2285
Cdd:PRK04813 241 tpsfadmclldPSFNEEHLPNLTHflfCGEELPHKT---------AKKLLERFPSATI-YNTYGPTEATvavtsieITDe 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2286 -LAWHCRAqeggaPaIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpFSGSGERLYRT 2364
Cdd:PRK04813 311 mLDQYKRL-----P-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdgvggPL--------LAAYLVGRDAMRG 2436
Cdd:PRK04813 381 GDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-------PYnkdhkvqyLIAYVVPKEEDFE 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2310915810 2437 ED--LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK04813 453 REfeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1552-1956 |
6.39e-60 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 213.31 E-value: 6.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTeGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQATLELR 1630
Cdd:cd19545 1 IYPCTPLQEGLMALTARQP-GAYVGQRVFELpPDIDLARLQAAWEQVVQANPILRTRIVQSDS-GGLLQVVVKESPISWT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1631 LAppgSDPQRQAEAEREAGFDPArAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGrYR 1710
Cdd:cd19545 79 ES---TSLDEYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPP-FS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1711 DYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQARTEQPGQGEHLReldpqTTRQLASFAQGQkVTLNTLVQAAWALLL 1790
Cdd:cd19545 154 RFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLE-----HSISLPSSASSG-VTLATVLRAAWALVL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1791 QRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHG 1870
Cdd:cd19545 228 SRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1871 GEAL-FDSILVFENfpvaEALRQAPADLEFSTPSNHEQ----TNYPLTLGVTL-GERLSLQYVYARRDFDAADIAELDRH 1944
Cdd:cd19545 308 RAACnFQTLLVVQP----ALPSSTSESLELGIEEESEDledfSSYGLTLECQLsGSGLRVRARYDSSVISEEQVERLLDQ 383
|
410
....*....|..
gi 2310915810 1945 LLHLLQRMAETP 1956
Cdd:cd19545 384 FEHVLQQLASAP 395
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
3066-3528 |
1.37e-59 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 216.62 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLsqshl 3145
Cdd:cd17647 23 YRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 klplaqGVQRIDLDRGApwfedysEANPDIHldgenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:cd17647 98 ------VIRAAGVVVGP-------DSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3226 QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQaFLQDEDVASCTSLKRIVCSGE 3305
Cdd:cd17647 155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQ-LLTAQATTPFPKLHHAFFVGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3306 ALPAD--AQQQVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDAVPIGRPIANLACYILDGN--LEPVP 3372
Cdd:cd17647 234 ILTKRdcLRLQTLA--ENVRIVNMYGTTETQRAVSYFevpsrssdpTFLKNLKDVMPAGRGMLNVQLLVVNRNdrTQICG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3373 VGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE----------------------RMYRTGDLARYRADGVIEYA 3430
Cdd:cd17647 312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3431 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESES-GDWREALAAHLAASL-------- 3497
Cdd:cd17647 392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrrdKDEEPTLVSYIVPRFDKpDDESFAQEDVPKEVStdpivkgl 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 3498 ------------------PEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:cd17647 472 igyrklikdireflkkrlASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
4088-4504 |
4.45e-59 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 212.27 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGF-AWQGELQQ-PLQIVYRQRqlp 4164
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGsLDLARLKQALDAVMERHDVLRTRFcEEAGRYEQvVLDKTVRFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4165 FAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSP 4244
Cdd:cd19066 79 IEIIDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4245 EQPRD----GRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRLvEALAQPGLTSANGVGEHLREVDATATARLRD 4316
Cdd:cd19066 159 QKPTLpppvGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPL-PKAKRPSQVASYEVLTLEFFLRSEETKRLRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4317 FARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQN 4396
Cdd:cd19066 238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4397 LALREQEHTPLFELQRWAGFGGEA----VFDNLLVFENYPvdevLERSSAGGVRFGAVAMH--EQTNYPLALAL--GGGD 4468
Cdd:cd19066 316 REAIEHQRVPFIELVRHLGVVPEApkhpLFEPVFTFKNNQ----QQLGKTGGFIFTTPVYTssEGTVFDLDLEAseDPDG 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 2310915810 4469 SLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19066 392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1990-2479 |
2.96e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 212.74 E-value: 2.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETL-------AERLP---------------CPAEVERLpleTAAWPASADTRPLPEV 2127
Cdd:PRK06187 88 IRLKPEEIAYILNDAEDRVVLVDSEFvpllaaiLPQLPtvrtvivegdgpaapLAPEVGEY---EELLAAASDTFDFPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2128 AGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGARVLLgdAGQ 2206
Cdd:PRK06187 165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVI--PRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2207 WSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-------QAVQaeawfnAYGP 2278
Cdd:PRK06187 242 FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSsLRLVIYGGAALPPALLREfkekfgiDLVQ------GYGM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 TE----AVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAP--GMIGELYIGGQCLARGYLGRPGQTAERFVAD 2352
Cdd:PRK06187 316 TEtspvVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETIDGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2353 pfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK06187 396 --------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDEKWGERPVAVVVLK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 2432 DamrGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06187 468 P---GATLDAkELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
3052-3525 |
5.46e-58 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 209.64 E-value: 5.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLD----YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3127
Cdd:cd17654 1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3128 AYMLEDSGVELLLSQSHLklplaqgvqridldRGAPWFEDYSEANPDIHLDgENLAYVIYTSGSTGKPKGAGNRHSALSN 3207
Cdd:cd17654 81 LTVMKKCHVSYLLQNKEL--------------DNAPLSFTPEHRHFNIRTD-ECLAYVIHTSGTTGTPKIVAVPHKCILP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLV-ALINREGVDTLHFVPSMLQAF- 3285
Cdd:cd17654 146 NIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLAdILFKRHRITVLQATPTLFRRFg 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3286 ---LQDEDVASCTSLKRIVCSGEALPADAQQQVFA-KLPQAGLYNLYGPTEaaidVTHWTC---VEEGKDAVPIGRPIAN 3358
Cdd:cd17654 226 sqsIKSTVLSATSSLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITE----VSCWALaykVPEEDSPVQLGSPLLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 LACYILDGNLEPVPvgvlGELYLAGQ---GLARGYHQRPGLTaerfvaspfvagerMYRTGDLARyRADGVIEYAGRIDH 3435
Cdd:cd17654 302 TVIEVRDQNGSEGT----GQVFLGGLnrvCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3436 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESgdwREALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd17654 363 QIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSS---SRIHKELQLTLLSSHAIPDTFVQIDKLPLT 439
|
490
....*....|
gi 2310915810 3516 PNGKLDRKAL 3525
Cdd:cd17654 440 SHGKVDKSEL 449
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1996-2476 |
6.14e-57 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 206.31 E-value: 6.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1996 HQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE 2075
Cdd:cd17631 3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2076 RLAYMLRDSGARWLIcqetlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:cd17631 83 EVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2156 VAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:cd17631 124 LWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVI--LRKFDPETVLDLIERHRVTSFFLVPTMIQAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 AEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF-NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILD 2313
Cdd:cd17631 202 LQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFvQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2314 AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRI 2393
Cdd:cd17631 282 PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVDRKKDMIISGGENV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2394 EIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNAN 2471
Cdd:cd17631 354 YPAEVEDVLYEHPAVAEVAVIGVpDEKWGEAVVAVVVPRP---GAELDEdELIAHCRERLARYKIPKSVEFVDALPRNAT 430
|
....*
gi 2310915810 2472 GKLDR 2476
Cdd:cd17631 431 GKILK 435
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
512-1000 |
9.41e-57 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 208.10 E-value: 9.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 512 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 591
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 592 DPEYPEERQAYMLEDSGVQLLLSQS------HLKLP-------------LAQGVQRIDLDQADAW--LENHAENNPGIEL 650
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSerldllHPALPgchdlrtliivgdPAHASEGHPGEEPASWpkLLALGDADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 651 NGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVvaaPGDH 730
Cdd:TIGR03098 161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV---LHDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 731 RDPAKLVELINREGVDTLHFVPSM-LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaAID 809
Cdd:TIGR03098 238 LLPRDVLKALEKHGITGLAAVPPLwAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-AFR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 810 VTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP-----FVAGER 884
Cdd:TIGR03098 317 STYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfpgeLHLPEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVgYVVLESEGGDW-R 959
Cdd:TIGR03098 397 AVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIV-LVVTPPGGEELdR 475
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2310915810 960 EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:TIGR03098 476 AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
4538-5040 |
9.87e-57 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 208.10 E-value: 9.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4538 LVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL 4617
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 DIEYPRERLLYMMQDSRAHLLLTHSHLLERL--------------------PIPEGLSCLSVDREEEWAGFPAHDPEVAL 4677
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLhpalpgchdlrtliivgdpaHASEGHPGEEPASWPKLLALGDADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4678 HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDdsLW 4757
Cdd:TIGR03098 161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD--YL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 LPERTYAEMHRHGVT-VGVFPPVYLqQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVT 4836
Cdd:TIGR03098 239 LPRDVLKALEKHGITgLAAVPPLWA-QLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFRS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRL 4916
Cdd:TIGR03098 318 TYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YR----SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVAQEPAVA 4991
Cdd:TIGR03098 394 PElavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDpTLGQAIVLVVTPPGGEEL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 4992 DSPEAQAECRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:TIGR03098 474 DRAALLAECRA--------RLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
3044-3522 |
3.70e-56 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 204.00 E-value: 3.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLlsqshlklplaqgvqridldrgapwFEDyseanpdihldgenLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:cd17631 80 TPPEVAYILADSGAKVL-------------------------FDD--------------LALLMYTSGTTGRPKGAMLTH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SALSnrlcWMQQ----AYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVALINREGVDTLHF 3277
Cdd:cd17631 121 RNLL----WNAVnalaALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVILR---KFDPETVLDLIERHRVTSFFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 VPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQagLYNLYGPTEAAIDVThwtcVEEGKDA----VP 3351
Cdd:cd17631 194 VPTMIQALLQHPRFATTdlSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVT----FLSPEDHrrklGS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 3431
Cdd:cd17631 268 AGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3432 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWL 3507
Cdd:cd17631 341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVE 420
|
490
....*....|....*
gi 2310915810 3508 ALERMPLSPNGKLDR 3522
Cdd:cd17631 421 FVDALPRNATGKILK 435
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
525-998 |
4.04e-56 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 204.24 E-value: 4.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLD----YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:cd17654 1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 601 AYMLEDSGVQLLLSQSHlklplaqgvqridldQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSN 680
Cdd:cd17654 81 LTVMKKCHVSYLLQNKE---------------LDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 681 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVE-LINREGVDTLHFVPSMLQAF- 758
Cdd:cd17654 146 NIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFg 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 759 ---LQDEDVASCTSLKRIVCSGEALPADAQQQVFA-KLPQAGLYNLYGPTEaaidVTHWTC---VEEGKDTVPIGRPIGN 831
Cdd:cd17654 226 sqsIKSTVLSATSSLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITE----VSCWALaykVPEEDSPVQLGSPLLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 832 LGCYILDGNLEPVPVGVLGELyLAGRGLARGYHQRPGLTaerfvaspfvagerMYRTGDLARyRADGVIEYAGRIDHQVK 911
Cdd:cd17654 302 TVIEVRDQNGSEGTGQVFLGG-LNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQIK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 912 LRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVleSEGGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNG 991
Cdd:cd17654 366 RRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIV--GESSSSRI-HKELQLTLLSSHAIPDTFVQIDKLPLTSHG 442
|
....*..
gi 2310915810 992 KLDRKAL 998
Cdd:cd17654 443 KVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3049-4073 |
4.50e-56 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 219.27 E-value: 4.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAF----GEER--LDYAELNRRANRLAHALIERGVGADRLVgVAMERSIEMVVALMAILKAGGAYVPVDP-- 3120
Cdd:PRK05691 20 AQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 ---EYPEERQAYMLEDSGVELLLSQSHLKLPLaQGVQRIDLDRGAPWF----------EDYSEANpdihLDGENLAYVIY 3187
Cdd:PRK05691 99 sarRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLcvdtldpalaEAWQEPA----LQPDDIAFLQY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKL 3263
Cdd:PRK05691 174 TSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLErPLRW 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGvDTLHFVPSMlqAFLQDEDVASCTSLKRIVCSG--------EALPADAQQQVFAKLPQAGL-----YNLYGP 3330
Cdd:PRK05691 254 LEAISEYG-GTISGGPDF--AYRLCSERVSESALERLDLSRwrvaysgsEPIRQDSLERFAEKFAACGFdpdsfFASYGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAIDVTHWT------------------CVEEGKDAVPI--GRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK05691 331 AEATLFVSGGRrgqgipaleldaealarnRAEPGTGSVLMscGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3390 YHQRPGLTAERFVAspfVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH--PWVREA--AVL 3465
Cdd:PRK05691 411 YWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-KTVERevEVVRKGrvAAF 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3466 AV--DGRQLVGYVVlesesgdwrEALAAHLAASLPEYMV--------------PAQWLALE--RMPLSPNGKLDRKA--- 3524
Cdd:PRK05691 486 AVnhQGEEGIGIAA---------EISRSVQKILPPQALIksirqavaeacqeaPSVVLLLNpgALPKTSSGKLQRSAcrl 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3525 ------------LPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAA-GIQFT 3591
Cdd:PRK05691 557 rladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDElGIDLN 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3592 PKDLFQQQTVQGLArvARVgAAVQMEQGPVSGETVLLPFQ----------RLFFE-QPIPNRQHWNQSLLLKPREALNAK 3660
Cdd:PRK05691 637 LRQLFEAPTLAAFS--AAV-ARQLAGGGAAQAAIARLPRGqalpqslaqnRLWLLwQLDPQSAAYNIPGGLHLRGELDEA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3661 ALEAALQALVEHHDALRLRFHETDGTWHA---EHAEATLGGALLWRAEAVDRQALESLC--EESQRSLDLTDGPLLRSLL 3735
Cdd:PRK05691 714 ALRASFQRLVERHESLRTRFYERDGVALQridAQGEFALQRIDLSDLPEAEREARAAQIreEEARQPFDLEKGPLLRVTL 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3736 VDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELL 3815
Cdd:PRK05691 794 VRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQL 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3816 --EGAPAELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGR 3893
Cdd:PRK05691 874 gdEQPVLELATDHPRSARQAHSAARYSLRVDASLSEA-LRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3894 EELfadiDLSRTVGWF--TSLFPVRLSPVADLGESLKAIKEQ-LRAIPDKGLGYgllrylageesARVLAGLPQARITFN 3970
Cdd:PRK05691 953 PRL----ETQGLVGFFinTQVLRAQLDGRLPFTALLAQVRQAtLGAQAHQDLPF-----------EQLVEALPQAREQGL 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3971 YLGQFDAQFDEMALLDPAGESAGAEMDpgapldnWLSLNGRvFD----------GELSIDWSFSSQMFGEDQVRRLADDY 4040
Cdd:PRK05691 1018 FQVMFNHQQRDLSALRRLPGLLAEELP-------WHSREAK-FDlqlhseedrnGRLTLSFDYAAELFDAATIERLAEHF 1089
|
1130 1140 1150
....*....|....*....|....*....|...
gi 2310915810 4041 VAELTALvdfcCDSPRHGAtpSDFPLAGLDQAR 4073
Cdd:PRK05691 1090 LALLEQV----CEDPQRAL--GDVQLLDAAERA 1116
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
3627-3864 |
4.61e-56 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 196.80 E-value: 4.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3627 LLPFQRLFFEQpIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEAtlgGALLWR--- 3703
Cdd:COG4908 1 LSPAQKRFLFL-EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPD---ADLPLEvvd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3704 -----AEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEA 3778
Cdd:COG4908 77 lsalpEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3779 PRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAp 3856
Cdd:COG4908 157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPvlELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA- 235
|
....*...
gi 2310915810 3857 AAYRTQVN 3864
Cdd:COG4908 236 KAHGATVN 243
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2011-2480 |
7.15e-56 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 202.52 E-value: 7.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CqetlaerlpcpaeverlpletaawpasadtrplpevageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP 2170
Cdd:cd05934 81 V---------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 GD-CQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTI---LDLPPAYLQQQAEELRHAGRRIA 2246
Cdd:cd05934 122 DDvYLTVLPLFHINAQAVSVLAALSVGATLVLLP--RFSASRFWSDVRRYGATVtnyLGAMLSYLLAQPPSPDDRAHRLR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2247 VRTCILGGEAWDASLLTQQAVQaeaWFNAYGPTEAVITPLAwhCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGE 2326
Cdd:cd05934 200 AAYGAPNPPELHEEFEERFGVR---LLEGYGMTETIVGVIG--PRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2327 LYI---GGQCLARGYLGRPGQTAERFvadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:cd05934 275 LVIrglRGWGFFKGYYNMPEATAEAM--------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLL-AELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:cd05934 347 RHPAVREAAVVAVpDEVGEDEVKAVVVLRP---GETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
3031-3534 |
1.71e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 204.65 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3031 AAEYPLQrgVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILK 3110
Cdd:PRK06187 1 MQDYPLT--IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3111 AGGAYVPVDPEYPEERQAYMLEDSGVELLL-SQSHLKL-----PLAQGVQRI----DLDRGAP---------WFEDYSEA 3171
Cdd:PRK06187 79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLvDSEFVPLlaailPQLPTVRTVivegDGPAAPLapevgeyeeLLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 NPDIHLDGENLAYVIYTSGSTGKPKGAGNRH-SALSNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEFFW-PLMSGARL 3249
Cdd:PRK06187 159 FDFPDIDENDAAAMLYTSGTTGHPKGVVLSHrNLFLHSLA-VCAWLKLSRDDVYLVIVPM-FHVHAWGLPYlALMAGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNL 3327
Cdd:PRK06187 237 VIP---RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLRE-FKEKFGIDLVQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3328 YGPTEAA--IDVTHWTCVEEGKDAVPI--GRPIANLACYILDGNLEPVPV--GVLGELYLAGQGLARGYHQRPGLTAERF 3401
Cdd:PRK06187 313 YGMTETSpvVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3402 VASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-D---GRQLVGYVV 3477
Cdd:PRK06187 393 DGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDekwGERPVAVVV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3478 L-ESESGDWREALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKALpRPQAAAGQ 3534
Cdd:PRK06187 466 LkPGATLDAKELRAFLRGRLAK-FKLPKRIAFVDELPRTSVGKILKRVL-REQYAEGK 521
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
3042-3525 |
2.56e-55 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 202.41 E-value: 2.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLlsqshlklplaqgvqrIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd05936 82 LYTPRELEHILNDSGAKAL----------------IVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSAL-SNRL-CWMQQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVVAapgdHR-DPAKLVALINREGVD 3273
Cdd:cd05936 146 THRNLvANALqIKAWLEDLLEGDDVVLAALPlfhvFGLTVAL---LLPLALGATIVLI----PRfRPIGVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3274 TLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDAVP 3351
Cdd:cd05936 219 IFPGVPTMYIALLNAPEFKKRdfSSLRLCISGGAPLPVEVAER-FEELTGVPIVEGYGLTETS-PVVAVNPLDGPRKPGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 3431
Cdd:cd05936 297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3432 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWL 3507
Cdd:cd05936 370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdpySGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVE 449
|
490
....*....|....*...
gi 2310915810 3508 ALERMPLSPNGKLDRKAL 3525
Cdd:cd05936 450 FRDELPKSAVGKILRREL 467
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
3039-3525 |
3.11e-55 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 203.86 E-value: 3.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3039 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 3118
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3119 DPEYPEERQAYMLEDSGVELLLSQSH----LKLPLAQGVQRIDLDR-GAP--------------WFEDYSEANPDIHLDG 3179
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSErldlLHPALPGCHDLRTLIIvGDPahaseghpgeepasWPKLLALGDADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 --ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVvaaPGDH 3257
Cdd:TIGR03098 161 idSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV---LHDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSM-LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaAID 3336
Cdd:TIGR03098 238 LLPRDVLKALEKHGITGLAAVPPLwAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-AFR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3337 VTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP-----FVAGER 3411
Cdd:TIGR03098 317 STYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfpgeLHLPEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWRE 3487
Cdd:TIGR03098 397 AVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIVLVVTPPGGEELDRA 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:TIGR03098 477 ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1990-2479 |
3.25e-55 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 202.02 E-value: 3.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETLAERLpcpaeverlpletaawPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVA 2149
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVSFTDLL----------------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2150 VSQAALVAHC-QAAARTYGVGPGD----CQLQ-FASISFDAAaeqLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTI 2223
Cdd:cd05936 145 LTHRNLVANAlQIKAWLEDLLEGDdvvlAALPlFHVFGLTVA---LLLPLALGATIVL--IPRFRPIGVLKEIRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2224 L-DLPPAY--LQQQAEELRHAGRRIavRTCILGGeawdASLltQQAVqAEAW---FNA-----YGPTEA--VIT--PLAW 2288
Cdd:cd05936 220 FpGVPTMYiaLLNAPEFKKRDFSSL--RLCISGG----APL--PVEV-AERFeelTGVpivegYGLTETspVVAvnPLDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2289 HCRAqeGgapAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLA 2368
Cdd:cd05936 291 PRKP--G---SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTW 2446
Cdd:cd05936 358 YMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpDPYSGEAVKAFVVLKE---GASLtEEEIIAF 434
|
490 500 510
....*....|....*....|....*....|...
gi 2310915810 2447 LAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05936 435 CREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
504-998 |
1.46e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 201.95 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 504 AAEYPLQrgVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILK 583
Cdd:PRK06187 1 MQDYPLT--IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 584 AGGAYVPVDPEYPEERQAYMLEDSGVQLLL-SQSHLKL-----PLAQGVQRI----DLDQA---------DAWLENHAEN 644
Cdd:PRK06187 79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLvDSEFVPLlaailPQLPTVRTVivegDGPAAplapevgeyEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 645 NPGIELnGENLAYV-IYTSGSTGKPKGAGNRH-SALSNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEFFW-PLMSGAR 721
Cdd:PRK06187 159 FDFPDI-DENDAAAmLYTSGTTGHPKGVVLSHrNLFLHSLA-VCAWLKLSRDDVYLVIVPM-FHVHAWGLPYlALMAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 722 LVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQvFAKLPQAGLYN 799
Cdd:PRK06187 236 QVIP---RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLRE-FKEKFGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 800 LYGPTEAA--IDVTHWTCVEEGKDTVPI--GRPIGNLGCYILDGNLEPVPV--GVLGELYLAGRGLARGYHQRPGLTAER 873
Cdd:PRK06187 312 GYGMTETSpvVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 874 FVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-D---GRQLVGYV 949
Cdd:PRK06187 392 IDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDekwGERPVAVV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 950 VLEsEGGDWREALAAH-LAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06187 465 VLK-PGATLDAKELRAfLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
515-998 |
1.86e-54 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 200.10 E-value: 1.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 EYPEERQAYMLEDSGVQLLLsqshlklplaQGVQRIDLDQADAWLEnhaennPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd05936 82 LYTPRELEHILNDSGAKALI----------VAVSFTDLLAAGAPLG------ERVALTPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 674 RHSAL-SNRL-CWMQQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVVAapgdHR-DPAKLVELINREGVD 746
Cdd:cd05936 146 THRNLvANALqIKAWLEDLLEGDDVVLAALPlfhvFGLTVAL---LLPLALGATIVLI----PRfRPIGVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 747 TLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDTVP 824
Cdd:cd05936 219 IFPGVPTMYIALLNAPEFKKRdfSSLRLCISGGAPLPVEVAER-FEELTGVPIVEGYGLTETS-PVVAVNPLDGPRKPGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 825 IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 904
Cdd:cd05936 297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 905 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWL 980
Cdd:cd05936 370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdpySGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVE 449
|
490
....*....|....*...
gi 2310915810 981 ALERMPLSPNGKLDRKAL 998
Cdd:cd05936 450 FRDELPKSAVGKILRREL 467
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
522-1519 |
4.95e-54 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 212.34 E-value: 4.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 522 ERTPTAPALAF----GEER--LDYAELNRRANRLAHALIERGIGADRLVgVAMERSIEMVVALMAILKAGGAYVPVDP-- 593
Cdd:PRK05691 20 AQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 ---EYPEERQAYMLEDSGVQLLLSQSHLKLPLaQGVQRIDLDQADAWL------ENHAENNPGIELNGENLAYVIYTSGS 664
Cdd:PRK05691 99 sarRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLcvdtldPALAEAWQEPALQPDDIAFLQYTSGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 665 TGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKLVELI 740
Cdd:PRK05691 178 TALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLErPLRWLEAI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 741 NREGvDTLHFVPSMlqAFLQDEDVASCTSLKRIVCSG--------EALPADAQQQVFAKLPQAGL-----YNLYGPTEAA 807
Cdd:PRK05691 258 SEYG-GTISGGPDF--AYRLCSERVSESALERLDLSRwrvaysgsEPIRQDSLERFAEKFAACGFdpdsfFASYGLAEAT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 808 IDVTHWT------------------CVEEGKDTVPI--GRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQR 866
Cdd:PRK05691 335 LFVSGGRrgqgipaleldaealarnRAEPGTGSVLMscGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRN 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 867 PGLTAERFVAspfVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH--PWVREA--AVLAV-- 940
Cdd:PRK05691 415 PEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-KTVERevEVVRKGrvAAFAVnh 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 941 DGRQLVGYVVleseggdwrEALAAHLAASLPEYMV--------------PAQWLALE--RMPLSPNGKLDRKA------- 997
Cdd:PRK05691 490 QGEEGIGIAA---------EISRSVQKILPPQALIksirqavaeacqeaPSVVLLLNpgALPKTSSGKLQRSAcrlrlad 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 998 --------LPAPEVSVAQAGYSAPRNAVERtLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRD 1068
Cdd:PRK05691 561 gsldsyalFPALQAVEAAQTAASGDELQAR-IAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQ 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1069 LFQHQNIRSLalAAKAGAATAEQGPASGEVALAPVQR-----------WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGR 1137
Cdd:PRK05691 640 LFEAPTLAAF--SAAVARQLAGGGAAQAAIARLPRGQalpqslaqnrlWLLWQLDPQSAAYNIPGGLHLRGELDEAALRA 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1138 ALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR----RQAGSEEALLALC---EEAQRSLDLEQGPLLRALLVDMA 1210
Cdd:PRK05691 718 SFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRidlsDLPEAEREARAAQireEEARQPFDLEKGPLLRVTLVRLD 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1211 DGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAD----LDADLGP---RSSSYQTWSRH-LHEQAGARldELDYWQAQLHD 1282
Cdd:PRK05691 798 DEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAacqgQTAELAPlplGYADYGAWQRQwLAQGEAAR--QLAYWKAQLGD 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1283 A--PHALPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGRED 1360
Cdd:PRK05691 876 EqpVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLA-QAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1361 LGeaidLSRTVGWF--TSLFPVRLTPAADLGESLKAIKEQ-LRGVPDKGVGYGLLrylageeaatrLAALPQPR------ 1431
Cdd:PRK05691 955 LE----TQGLVGFFinTQVLRAQLDGRLPFTALLAQVRQAtLGAQAHQDLPFEQL-----------VEALPQAReqglfq 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1432 ITFNYlgrfdRQFDGAALLvpATESAGAAQDPcaplanWLSIEGQV---------YGGELSLHWSFSREMFAEATVQRLv 1502
Cdd:PRK05691 1020 VMFNH-----QQRDLSALR--RLPGLLAEELP------WHSREAKFdlqlhseedRNGRLTLSFDYAAELFDAATIERL- 1085
|
1130
....*....|....*...
gi 2310915810 1503 ddyARELHALIEH-CLDP 1519
Cdd:PRK05691 1086 ---AEHFLALLEQvCEDP 1100
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
3041-3525 |
9.03e-54 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 200.72 E-value: 9.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAF----GEER-LDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGA 3114
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 YVPVDPEYPEERQAYMLEDSGVELLLSQSHL-----------KLPLAQG----------VQRIDLDRGAPWFEDYSEA-- 3171
Cdd:COG0365 91 HSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkeKVDEALEelpslehvivVGRTGADVPMEGDLDWDELla 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 -----NPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLM 3244
Cdd:COG0365 171 aasaeFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3245 SGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFA- 3317
Cdd:COG0365 251 NGATVVLyeGRP-DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkkyDLSSLRLLGSAGEPLNPEVWEWWYEa 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 -KLPqagLYNLYGPTEAaidVTHWTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ--GLARGYHQ 3392
Cdd:COG0365 330 vGVP---IVDGWGQTET---GGIFISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3393 RPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---- 3468
Cdd:COG0365 404 DP----ERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPdeir 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3469 GRQLVGYVVLE---SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:COG0365 480 GQVVKAFVVLKpgvEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
517-995 |
9.19e-54 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 197.06 E-value: 9.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 596 PEERQAYMLEDSGVQLLLsqshlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRH 675
Cdd:cd17631 80 TPPEVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 676 SALSnrlcWMQQ----AYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVELINREGVDTLHF 750
Cdd:cd17631 121 RNLL----WNAVnalaALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVILR---KFDPETVLDLIERHRVTSFFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 751 VPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQagLYNLYGPTEAAIDVThwTCVEEGKDTVP--IG 826
Cdd:cd17631 194 VPTMIQALLQHPRFATTdlSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVT--FLSPEDHRRKLgsAG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 827 RPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRI 906
Cdd:cd17631 270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 907 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLEsEGGDWREALAAHLAASL-PEYMVPAQWLA 981
Cdd:cd17631 343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAVVVPR-PGAELDEDELIAHCRERlARYKIPKSVEF 421
|
490
....*....|....
gi 2310915810 982 LERMPLSPNGKLDR 995
Cdd:cd17631 422 VDALPRNATGKILK 435
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
514-998 |
4.91e-53 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 198.41 E-value: 4.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 514 HRLFEEQVERTPTAPALAF----GEER-LDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGA 587
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 588 YVPVDPEYPEERQAYMLEDSGVQLLLSQSHL-----------KLPLAQG----------VQRIDLDQA-------DAWLE 639
Cdd:COG0365 91 HSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkeKVDEALEelpslehvivVGRTGADVPmegdldwDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 640 NHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLM 717
Cdd:COG0365 171 AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 718 SGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFA- 790
Cdd:COG0365 251 NGATVVLyeGRP-DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkkyDLSSLRLLGSAGEPLNPEVWEWWYEa 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 791 -KLPqagLYNLYGPTEAaidVTHWTCVEEGKDTVP--IGRPIgnLGCY--ILDGNLEPVPVGVLGELYLAGR--GLARGY 863
Cdd:COG0365 330 vGVP---IVDGWGQTET---GGIFISNLPGLPVKPgsMGKPV--PGYDvaVVDEDGNPVPPGEEGELVIKGPwpGMFRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 864 HQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD-- 941
Cdd:COG0365 402 WNDP----ERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPde 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 942 --GRQLVGYVVLES--EGGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:COG0365 478 irGQVVKAFVVLKPgvEPSDeLAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2002-2479 |
5.70e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 197.05 E-value: 5.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETL-------AERLP-------CP-AEVERLPLETAAWP---ASADTR-PLPEVAGETLAYVIYTSGST 2142
Cdd:PRK07656 99 ARGDAKALFVLGLFlgvdysaTTRLPalehvviCEtEEDDPHTEKMKTFTdflAAGDPAeRAPEVDPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLLgdAGQWSAQHLADEVER 2218
Cdd:PRK07656 179 GRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAG---VNAPLMRGATILP--LPVFDPDEVFRLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2219 HAVTILDLPPA---YLqqqaeeLRHAGRRI----AVRTCILGGEAWDASLLtqQAVQAEAWFN----AYGPTEAviTPLA 2287
Cdd:PRK07656 254 ERITVLPGPPTmynSL------LQHPDRSAedlsSLRLAVTGAASMPVALL--ERFESELGVDivltGYGLSEA--SGVT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRA---QEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerLYrT 2364
Cdd:PRK07656 324 TFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW------LH-T 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLA----AYLVGRD--AMRGED 2438
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI---GVPDERLGevgkAYVVLKPgaELTEEE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2310915810 2439 LLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07656 474 LIAYCREHLAK----YKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
2015-2480 |
1.02e-52 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 196.20 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICqet 2094
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 laerlpcpaeverlpLETAAWPASADTRPlpevageTLAYviyTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:cd17647 99 ---------------IRAAGVVVGPDSNP-------TLSF---TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASISFDAAAEQLFVPLLAGARVLL---GDAGQwsAQHLADEVERHAVTILDLPPAY---LQQQAEE----LRHA--- 2241
Cdd:cd17647 154 TMLSGIAHDPIQRDMFTPLFLGAQLLVptqDDIGT--PGRLAEWMAKYGATVTHLTPAMgqlLTAQATTpfpkLHHAffv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2242 GRRIAVRTCilggeawdasLLTQQAVQAEAWFNAYGPTE---AVITPLAWHCRAQEGGAPAIGRALGARRAcILDAAL-- 2316
Cdd:cd17647 232 GDILTKRDC----------LRLQTLAENVRIVNMYGTTEtqrAVSYFEVPSRSSDPTFLKNLKDVMPAGRG-MLNVQLlv 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 -------QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFV----ADP-----------------FSGSGERLYRTGDLA 2368
Cdd:cd17647 301 vnrndrtQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldkdnnepwrqfWLGPRDRLYRTGDLG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE-AAVVALDGVGGPLLAAYLVGRDA-------------- 2433
Cdd:cd17647 381 RYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnITLVRRDKDEEPTLVSYIVPRFDkpddesfaqedvpk 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2434 -----------MRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:cd17647 461 evstdpivkglIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
4564-5043 |
1.10e-52 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 196.20 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRahlllthsh 4643
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAK--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4644 llerlpiPEGLSCLsvdreeEWAGfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDC 4723
Cdd:cd17647 93 -------PRGLIVI------RAAG-------VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4724 ELHFMSFAFDGSHEGWMHPLINGARVLI--RDDsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAehAERDGNPPPVRVYC 4801
Cdd:cd17647 153 FTMLSGIAHDPIQRDMFTPLFLGAQLLVptQDD-IGTPGRLAEWMAKYGATVTHLTPAMGQLLT--AQATTPFPKLHHAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4802 FGGDAVAQASYdLAWRALKPKY-LFNGYGPTET--VVTPLLWKARAGDAC----GAAYMPIGTLLGNRSGYILD--GQLN 4872
Cdd:cd17647 230 FVGDILTKRDC-LRLQTLAENVrIVNMYGTTETqrAVSYFEVPSRSSDPTflknLKDVMPAGRGMLNVQLLVVNrnDRTQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFV------PDPFG---------------APGSRLYRSGDLTRGRADGVV 4931
Cdd:cd17647 309 ICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvePDHWNyldkdnnepwrqfwlGPRDRLYRTGDLGRYLPNGDC 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4932 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAVADSPEAQA------------ 4998
Cdd:cd17647 389 ECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPtLVSYIVPRFDKPDDESFAQEdvpkevstdpiv 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4999 -------ECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQP 5043
Cdd:cd17647 469 kgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2014-2479 |
1.60e-52 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 192.94 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05972 81 ------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASISFDAAA-EQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCIL 2252
Cdd:cd05972 125 HWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2253 GGE--------AWDASLltqqavqAEAWFNAYGPTEAVITpLAwHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMI 2324
Cdd:cd05972 205 AGEplnpevieWWRAAT-------GLPIRDGYGQTETGLT-VG-NFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYI--GGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:cd05972 276 GDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2403 LAHPYVAEAAVVAL-DGVGGPLLAAYLVGR-DAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05972 348 LEHPAVAEAAVVGSpDPVRGEVVKAFVVLTsGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
4552-5040 |
1.62e-52 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 193.28 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4552 DAVAVIFDEEKLTYAELDSRANRLAHALIARG-VGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSrahlllthshllerlpipeglsclsvdreeewagfpahDPEVALhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd05941 81 TDS--------------------------------------EPSLVL---DPALILYTSGTTGRPKGVVLTHANLAANVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV--LIRDDslwlPERTYAEMHRHGVTV--GVfPPVYLQQLA 4785
Cdd:cd05941 120 ALVDAWRWTEDDVLLHVLPlHHVHGLVNALLCPLFAGASVefLPKFD----PKEVAISRLMPSITVfmGV-PTIYTRLLQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4786 EHAERDGNPPPVRVYCFG-------GDAVAQASYDLAWRALKPKYLFNGYGPTETVVT---PLLWKARAGDacgaaympI 4855
Cdd:cd05941 195 YYEAHFTDPQFARAAAAErlrlmvsGSAALPVPTLEEWEAITGHTLLERYGMTEIGMAlsnPLDGERRPGT--------V 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYL 4934
Cdd:cd05941 267 GMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaecraQLKTALRER 5011
Cdd:cd05941 340 GRssVD-IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGERVVAVVVLRAGAAALSLE-------ELKEWAKQR 411
|
490 500
....*....|....*....|....*....
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05941 412 LAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
4541-5040 |
4.87e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 193.97 E-value: 4.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRA-------HLLLTHSHLLERLP-------IPEGLSCLSVDREEEWAGFPAH----DPEVALHGDNL 4682
Cdd:PRK07656 89 YTADEAAYILARGDAkalfvlgLFLGVDYSATTRLPalehvviCETEEDDPHTEKMKTFTDFLAAgdpaERAPEVDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CELHFmsFAFDGSHEGWMHPLINGARVLIRddSLWLP 4759
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylAANPF--FHVFGYKAGVNAPLMRGATILPL--PVFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4760 ERTYAEMHRHGVTVGVFPPVYLQQLAEHAER-DGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETvvTPL 4838
Cdd:PRK07656 245 DEVFRLIETERITVLPGPPTMYNSLLQHPDRsAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEA--SGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDacGAAYMP--IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrL 4916
Cdd:PRK07656 323 TTFNRLDD--DRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW------L 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGQqlvGYVVAQEPAVAD 4992
Cdd:PRK07656 395 H-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPderlGEVGK---AYVVLKPGAELT 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2310915810 4993 SPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK07656 471 EEELIAYC--------REHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
2584-3005 |
1.28e-51 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 190.27 E-value: 1.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTI--LANMPLRIV 2661
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIdpYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2662 LEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQP 2741
Cdd:cd19533 82 DLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPLkLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELpADRvrPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:cd19533 162 PPAPF-GSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSL-ARR--APGRSLAFLRRTAELPPELTRTLLEAAEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2822 EGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANR-NRAEVERLiGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQA 2900
Cdd:cd19533 238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2901 HQDLPFEQLVDALQPERNLshSPLFQVMYNHQSGERQ--DAQVDGLHIESFAwdGAAAqfDLALDTWETPDGLGAA--LT 2976
Cdd:cd19533 317 HQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFDYGldFGGVVGLTHNLSS--GPTN--DLSIFVYDRDDESGLRidFD 390
|
410 420
....*....|....*....|....*....
gi 2310915810 2977 YATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19533 391 ANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
4547-5040 |
1.76e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 192.71 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06187 16 ARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHL-------LLTHSHLLERLPI----------PEGLSCLSVDREEEW-AGFPAHDPEVALHGDNLAYVIYT 4688
Cdd:PRK06187 96 AYILNDAEDRVvlvdsefVPLLAAILPQLPTvrtvivegdgPAAPLAPEVGEYEELlAAASDTFDFPDIDENDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFdgsheGWMH-PLINGARVLIRDDslWLPERTY 4763
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVpmfhVHAW-----GLPYlALMAGAKQVIPRR--FDPENLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVTV--GVfpPVYLQQLAEHAErdgnPPPV-----RVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETvvT 4836
Cdd:PRK06187 249 DLIETERVTFffAV--PTIWQMLLKAPR----AYFVdfsslRLVIYGGAALPPALLR-EFKEKFGIDLVQGYGMTET--S 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKAR--AGDACGAAYMpigtllgnRS------GY---ILDGQLNLLPV--GVAGELYLGGEGVARGYLERPALTAER 4903
Cdd:PRK06187 320 PVVSVLPpeDQLPGQWTKR--------RSagrplpGVearIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4904 FVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGY 4982
Cdd:PRK06187 392 IDGG--------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPVAV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4983 VVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06187 464 VVLKPGATLD--------AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
3922-4077 |
1.82e-51 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 179.78 E-value: 1.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3922 DLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESArvLAGLPQARITFNYLGQFDAQfDEMALLDPAGESAGAEMDPGAP 4001
Cdd:TIGR01720 1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEK--LAASPQPEISFNYLGQFDAD-SNDELFQPSSYSPGEAISPESP 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4002 LDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARLDAL 4077
Cdd:TIGR01720 78 RPYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1553-1956 |
1.93e-51 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 189.87 E-value: 1.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1553 YPLSPMQQGMLF-HSLHGTEGDYvNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLE 1628
Cdd:cd19531 2 LPLSFAQQRLWFlDQLEPGSAAY-NIpgaLRLR-GPLDVAALERALNELVARHEALRTTFVEVDG--EPVQVILPPLPLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1629 LRL--APPGSDPQRQAEAER----EAG--FDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAgq 1700
Cdd:cd19531 78 LPVvdLSGLPEAEREAEAQRlareEARrpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1701 evAATVGR----------YRDYI----GWLQGrDAMATEF-FWRDRLAS----LEMPTRLARQARteQPGQGEHLR-ELD 1760
Cdd:cd19531 156 --AFLAGRpsplpplpiqYADYAvwqrEWLQG-EVLERQLaYWREQLAGappvLELPTDRPRPAV--QSFRGARVRfTLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1761 PQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPaeLPGIEAQIGLFINTLPVIAAPQPQQSVAD 1840
Cdd:cd19531 231 AELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRN--RAELEGLIGFFVNTLVLRTDLSGDPTFRE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1841 YLQGMQALNLALREHEHTP-------LyDIQRWAGHGgeALFDSILVFENFPvAEALRQAPADLEFsTPSNHEQTNYPLT 1913
Cdd:cd19531 309 LLARVRETALEAYAHQDLPfeklveaL-QPERDLSRS--PLFQVMFVLQNAP-AAALELPGLTVEP-LEVDSGTAKFDLT 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2310915810 1914 LGVT-LGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19531 384 LSLTeTDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
3627-4048 |
3.28e-51 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 189.16 E-value: 3.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3627 LLPFQR--LFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT---WHAEHAEATLGGALL 3701
Cdd:cd19066 4 LSPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRyeqVVLDKTVRFRIEIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3702 WRAEAVDRQALESLCEE-SQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEaPR 3780
Cdd:cd19066 84 LRNLADPEARLLELIDQiQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK-PT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3781 LPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAP--AELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAA 3858
Cdd:cd19066 163 LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPppLPLPKAKRPSQVASYEVLTLEFFLRSEETKR-LREVARE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3859 YRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREelfaDIDLSRTVGWFTSLFPVRL--SPVADLGESLKAIKEQLRA 3936
Cdd:cd19066 242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP----DEAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQSRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3937 IPDKGLGYGLLRYL-AGEESARVLAGLPQARITFnylgqfdAQFDEMALLDPAGESAGAEMDP--GAPLDNWLSLNGRVf 4013
Cdd:cd19066 318 AIEHQRVPFIELVRhLGVVPEAPKHPLFEPVFTF-------KNNQQQLGKTGGFIFTTPVYTSseGTVFDLDLEASEDP- 389
|
410 420 430
....*....|....*....|....*....|....*
gi 2310915810 4014 DGELSIDWSFSSQMFGEDQVRRLADDYVAELTALV 4048
Cdd:cd19066 390 DGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLI 424
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
2005-2479 |
1.82e-50 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 189.50 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2005 IALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDS 2084
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2085 GARWLICQETLAERL----------------PCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGSTGQPKG 2147
Cdd:cd05959 101 RARVVVVSGELAPVLaaaltksehtlvvlivSGGAGPEAGALLLAElVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAHCQAAAR-TYGVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTIL- 2224
Cdd:cd05959 181 VVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFFAyGLGNSLTFPLSVGATTVL-MPERPTPAAVFKRIRRYRPTVFf 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLltqqavqAEAWFNAY--------GPTEAVITPLAWHCRAQEGG 2296
Cdd:cd05959 260 GVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEV-------GERWKARFgldildgiGSTEMLHIFLSNRPGRVRYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsGErLYRTGDLARYRVDGQV 2376
Cdd:cd05959 333 TT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GE-WTRTGDKYVRDDDGFY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2377 EYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAY 2454
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVeDEDGLTKPKAFVVLRPGYEDSEALEeELKEFVKDRLAPY 482
|
490 500
....*....|....*....|....*
gi 2310915810 2455 MQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05959 483 KYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1100-1329 |
2.14e-50 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 180.23 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQRWFFEqSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR----- 1174
Cdd:COG4908 1 LSPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVvdlsa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1175 -RQAGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD----L 1248
Cdd:COG4908 80 lPEPEREAELEELVaEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGepppL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1249 GPRSSSYQTWSRHLHEQA-GARLD-ELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAY 1324
Cdd:COG4908 160 PELPIQYADYAAWQRAWLqSEALEkQLEYWRQQLAGAPPVleLPTDRPRPAVQTFRGATLSFTLPAELTEALKALA-KAH 238
|
....*
gi 2310915810 1325 RTQVN 1329
Cdd:COG4908 239 GATVN 243
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
4563-5035 |
2.24e-50 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 187.20 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLllths 4642
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 hllerLPIPeglsclsvdreEEWAGF-PAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPE 4721
Cdd:cd05903 77 -----FVVP-----------ERFRQFdPAAMP------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4722 DCEL------HFMSFAFdgsheGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP- 4794
Cdd:cd05903 135 DVFLvaspmaHQTGFVY-----GFTLPLLLGAPVVLQDI--WDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPl 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGDAVAQASYDLAWRALKPkYLFNGYGPTE-----TVVTPLLWKARAG-DACGAAYMPIgtllgnrsgYILD 4868
Cdd:cd05903 208 SRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTEcpgavTSITPAPEDRRLYtDGRPLPGVEI---------KVVD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAeRFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVdHQVKIR-GFR 4947
Cdd:cd05903 278 DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTA-DAAPEGW-------FRTGDLARLDEDGYLRITGRS-KDIIIRgGEN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4948 IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSpeaqAECRAQLKtalRERLPEYMVPSHLLFLAR 5026
Cdd:cd05903 349 IPVLEVEDLLLGHPGVIEAAVVALPDErLGERACAVVVTKSGALLTF----DELVAYLD---RQGVAKQYWPERLVHVDD 421
|
....*....
gi 2310915810 5027 MPLTPNGKL 5035
Cdd:cd05903 422 LPRTPSGKV 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
516-998 |
3.41e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 188.57 E-value: 3.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:PRK07656 10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 595 YPEERQAYMLEDSGVQLLLSQSHL---------KLPLAQGVQRIDLDQADA----------WLENHAENNPGIELNGENL 655
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLFlgvdysattRLPALEHVVICETEEDDPhtekmktftdFLAAGDPAERAPEVDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 656 AYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPFsFDVSVWEFFW--PLMSGARLVVAApgdHRD 732
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMLTHrQLLSNAADWAEYL-GLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLP---VFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 733 PAKLVELINREGVDTLHFVPSMLQAFLQ-----DEDVASCtslkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEA 806
Cdd:PRK07656 244 PDEVFRLIETERITVLPGPPTMYNSLLQhpdrsAEDLSSL----RLAVTGAAsMPVALLERFESELGVDIVLTGYGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 807 AiDVTHWTCVEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAGER 884
Cdd:PRK07656 320 S-GVTTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA------IDADG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESEGGDWRE 960
Cdd:PRK07656 393 WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLgeVGkaYVVLKPGAELTEE 472
|
490 500 510
....*....|....*....|....*....|....*...
gi 2310915810 961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07656 473 ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2584-3005 |
3.05e-49 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 183.03 E-value: 3.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTILANMPLRIVL 2662
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEAT--LRQRVAEEIRQPFDLARGPLLRVRLLALAGQEH-VLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19536 82 LDLTPLEEQLdpLRAYKEETKIRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKlQYADYAAWHRAWLDSGEGARqldYWRERL-GAEQPVLELPADrvrpAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19536 162 PLSLPPAQ-PYRDFVAHERASIQQAASER---YWREYLaGATLATLPALSE----AVGGGPEQDSELLVSVPLPVRSRSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNR--AEVERLIGFFVNTQVLRCQVdAGLAFRDLLGRVREAAL 2896
Cdd:cd19536 234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2897 GAQAHQDLPfeqLVDAlqpERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALT 2976
Cdd:cd19536 313 ESLSHEQVP---LADI---QRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKQDRLE 386
|
410 420 430
....*....|....*....|....*....|...
gi 2310915810 2977 ----YATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19536 387 lklaYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
52-478 |
3.16e-49 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 183.34 E-value: 3.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF------PRGADDSLAQAPLQrple 125
Cdd:cd19533 4 LTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFteeegePYQWIDPYTPVPIR---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 126 vaFEDCSGLPEAEQEAR--LREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
Cdd:cd19533 80 --HIDLSGDPDPEGAAQqwMQEDLR----KPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 204 AYATGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYefsIEPALAE 283
Cdd:cd19533 154 ALLKGRPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAE---LPPELTR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 284 ALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANR-NRAEVEGLiGLFVNTQVLRSVFDGRTSVATLLAGLK 362
Cdd:cd19533 230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTLPLRLTVDPQQTFAELVAQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 363 DTVLGAQAHQDLPFERLVEAFKVERSLshSPLFQVMYNHQPLVADIeALDSVAG----LSFGQLDwksrttqfDLSLDTY 438
Cdd:cd19533 309 RELRSLLRHQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFDYGL-DFGGVVGlthnLSSGPTN--------DLSIFVY 377
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2310915810 439 EK--GGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19533 378 DRddESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
4551-5040 |
6.52e-49 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 183.06 E-value: 6.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEK----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:cd17654 1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSrahlllthshllerlpipeGLSCLSVDREEEWAGFPAHDPEV---ALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd17654 81 LTVMKKC-------------------HVSYLLQNKELDNAPLSFTPEHRhfnIRTDECLAYVIHTSGTTGTPKIVAVPHK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERYEMTPEDCeLHFMSFA-FDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEM--HRHGVTVGVFPPVY 4780
Cdd:cd17654 142 CILPNIQHFRSLFNITSEDI-LFLTSPLtFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITVLQATPTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 LQQLAEHAERDGN---PPPVRVYCFGGDAVAQASYDLAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACgaayMPIG 4856
Cdd:cd17654 221 FRRFGSQSIKSTVlsaTSSLRVLALGGEPFPSLVILSSWRGKGNRtRIFNIYGITEVSCWALAYKVPEEDSP----VQLG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 TLLGNRSGYILDGQLNllpvGVAGELYLGgeGVARGYlerpaltaerFVPDPFGAPGSRLYRSGDLTRgRADGVVDYLGR 4936
Cdd:cd17654 297 SPLLGTVIEVRDQNGS----EGTGQVFLG--GLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4937 VDHQVKIRGFRIELGEIEARLREHPAVrEAVVVAQPGAvgQQLVGYVVAQEpavADSPEaqaECRAQLKTALRERLPEYM 5016
Cdd:cd17654 360 KDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ--QRLIAFIVGES---SSSRI---HKELQLTLLSSHAIPDTF 430
|
490 500
....*....|....*....|....
gi 2310915810 5017 VpshllFLARMPLTPNGKLDRKGL 5040
Cdd:cd17654 431 V-----QIDKLPLTSHGKVDKSEL 449
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2003-2479 |
1.64e-48 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 181.72 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2003 EAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGdRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGarwlicqetlaerlpcPAEVERLpletaawpasadtrplpevagetlAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd05941 81 TDSE----------------PSLVLDP------------------------ALILYTSGTTGRPKGVVLTHANLAANVRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASIS-----FDAaaeqLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPP-------A 2229
Cdd:cd05941 121 LVDAWRWTEDDVLLHVLPLHhvhglVNA----LLCPLFAGASVEF--LPKFDPKEVAISRLMPSITVFMGVPtiytrllQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2230 YLQQQAEELRHAGRRIA--VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVIT---PLAWHCRAQeggapAIGRA 2303
Cdd:cd05941 195 YYEAHFTDPQFARAAAAerLRLMVSGSAALPVPTLEEwEAITGHTLLERYGMTEIGMAlsnPLDGERRPG-----TVGMP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2304 LGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGR- 2381
Cdd:cd05941 270 LPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRs 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2382 ADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRLPAYMQPTAW 2460
Cdd:cd05941 343 SVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVpDPDWGERVVAVVVLRAGAAALS-LEELKEWAKQRLAPYKRPRRL 421
|
490
....*....|....*....
gi 2310915810 2461 QVLSSLPLNANGKLDRKAL 2479
Cdd:cd05941 422 ILVDELPRNAMGKVNKKEL 440
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2006-2474 |
2.67e-48 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 182.41 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDE--HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:cd05911 1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQE--------------------TLAERLPCPAEVERLPLETAAWPASADTRPLPEvAGETLAYVIYTSGSTG 2143
Cdd:cd05911 81 SKPKVIFTDPdglekvkeaakelgpkdkiiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD-GKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2144 QPKGVAVSQAALVAHC-QAAARTYG-VGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAV 2221
Cdd:cd05911 160 LPKGVCLSHRNLIANLsQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP--KFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2222 TILDLPPAYLQQ-------QAEELRHagrriaVRTCILGGeawdASLltQQAVQAE-------AWFN-AYGPTEAviTPL 2286
Cdd:cd05911 238 TFLYLVPPIAAAlakspllDKYDLSS------LRVILSGG----APL--SKELQELlakrfpnATIKqGYGMTET--GGI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 AWHCRAQEGGAPAIGRALGARRACILDAAL-QPCAPGMIGELYI-GGQCLaRGYLGRPGQTAERFVADPFsgsgerlYRT 2364
Cdd:cd05911 304 LTVNPDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVrGPQVM-KGYYNNPEATKETFDEDGW-------LHT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLA-E 2442
Cdd:cd05911 376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIpDEVSGELPRAYVVRKP---GEKLTEkE 452
|
490 500 510
....*....|....*....|....*....|...
gi 2310915810 2443 LRTWLAGRLPAYMQPTA-WQVLSSLPLNANGKL 2474
Cdd:cd05911 453 VKDYVAKKVASYKQLRGgVVFVDEIPKSASGKI 485
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
3043-3525 |
8.09e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 181.64 E-value: 8.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK07656 10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHL---------KLPLAQGVQRIDLDRGAP-------WFEDYSEANPDIH---LDGENL 3182
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLFlgvdysattRLPALEHVVICETEEDDPhtekmktFTDFLAAGDPAERapeVDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3183 AYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPFsFDVSVWEFFW--PLMSGARLVVAApgdHRD 3259
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMLTHrQLLSNAADWAEYL-GLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLP---VFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ-----DEDVASCtslkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEA 3333
Cdd:PRK07656 244 PDEVFRLIETERITVLPGPPTMYNSLLQhpdrsAEDLSSL----RLAVTGAAsMPVALLERFESELGVDIVLTGYGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3334 AiDVTHWTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGER 3411
Cdd:PRK07656 320 S-GVTTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA------IDADG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESESGDWRE 3487
Cdd:PRK07656 393 WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLgeVGkaYVVLKPGAELTEE 472
|
490 500 510
....*....|....*....|....*....|....*...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK07656 473 ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
4531-5037 |
8.21e-48 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 181.41 E-value: 8.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPLVHQRVAErarMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:cd05959 1 EKYNAATLVDLNLNE---GRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPI----------------PEGLSCLSVDREEEWAGFPAHDPE 4674
Cdd:cd05959 78 GIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAaltksehtlvvlivsgGAGPEAGALLLAELVAAEAEQLKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDcELHF----MSFAFdGSHEGWMHPLINGARVL 4750
Cdd:cd05959 158 AATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIRED-DVCFsaakLFFAY-GLGNSLTFPLSVGATTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IrddslwLPER-------TYAEMHRHGVTVGVfPPVYLQQLAEHAERDGNPPPVRvYCFGGDAVAQASYDLAWRALKPKY 4823
Cdd:cd05959 236 L------MPERptpaavfKRIRRYRPTVFFGV-PTLYAAMLAAPNLPSRDLSSLR-LCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4824 LFNGYGPTEtvVTPLLWKARAGDA-CGAAYMPIgtllgnrSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPAL 4899
Cdd:cd05959 308 ILDGIGSTE--MLHIFLSNRPGRVrYGTTGKPV-------PGYeveLRDEDGGDVADGEPGELYVRGPSSATMYWNNRDK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFVpdpfgapGSrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQ 4978
Cdd:cd05959 379 TRDTFQ-------GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGlTK 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 4979 LVGYVVaqepaVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd05959 451 PKAFVV-----LRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
2015-2479 |
9.21e-48 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 179.57 E-value: 9.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 LAERLPCPAEVERLPLetaawPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:TIGR01923 81 LEEKDFQADSLDRIEA-----AGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASISFDAAAEQLFVPLLAGARVLLGDAgqwSAQhLADEVERHAVTILDLPPAYLQQQAEELrhaGRRIAVRTCILGG 2254
Cdd:TIGR01923 156 LLSLPLYHISGLSILFRWLIEGATLRIVDK---FNQ-LLEMIANERVTHISLVPTQLNRLLDEG---GHNENLRKILLGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 EAWDASLLTQQAVQAEAWFNAYGPTEA-----VITPLAWHCRaqeggaPAIGRALGARRACILDAALQPcapgmIGELYI 2329
Cdd:TIGR01923 229 SAIPAPLIEEAQQYGLPIYLSYGMTETcsqvtTATPEMLHAR------PDVGRPLAGREIKIKVDNKEG-----HGEIMV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2330 GGQCLARGYLgRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVA 2409
Cdd:TIGR01923 298 KGANLMKGYL-YQGELTPAFEQQGW-------FNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2410 EAAVVAL-DGVGGPLLAAYLVGRDamrgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:TIGR01923 370 EAVVVPKpDAEWGQVPVAYIVSES----DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
4562-5035 |
1.14e-47 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 180.49 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTH 4641
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4642 SHLLERL--------PIP-------EGLSCLSVDREEEW-AGFPAHD--PEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd05911 90 PDGLEKVkeaakelgPKDkiivlddKPDGVLSIEDLLSPtLGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHI--VATGERYEMTPEDCELHFMSFAfdgshegWM-------HPLINGARVLI--RDDS-LWLperTYAEMHRhgV 4771
Cdd:cd05911 170 NLIANLsqVQTFLYGNDGSNDVILGFLPLY-------HIyglfttlASLLNGATVIImpKFDSeLFL---DLIEKYK--I 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4772 TVGVFPPVYLQQLAEHAERD-GNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVvtpllwkaragdaCGA 4850
Cdd:cd05911 238 TFLYLVPPIAAALAKSPLLDkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETG-------------GIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4851 AYMPIGTLLGNRSGYIL----------DGQLNLLPvGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSG 4920
Cdd:cd05911 305 TVNPDGDDKPGSVGRLLpnveakivddDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQL-VGYVVAQEPAVADSpea 4996
Cdd:cd05911 377 DIGYFDEDGylyIVD---RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELpRAYVVRKPGEKLTE--- 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 4997 qaecrAQLKTALRERLPEYmvpSHL----LFLARMPLTPNGKL 5035
Cdd:cd05911 451 -----KEVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKI 485
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
539-998 |
2.30e-47 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 178.41 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 KlplAQGVQRIDLDQAdaWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:TIGR01923 82 E---EKDFQADSLDRI--EAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 699 QKTPFsFDVSVWEFFWP-LMSGARLVVaapgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEdvASCTSLKRIVCSG 777
Cdd:TIGR01923 157 LSLPL-YHISGLSILFRwLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLDEG--GHNENLRKILLGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 778 EALPA----DAQQQvfaKLPqagLYNLYGPTEAAIDVTHWTcVEEGKDTVPIGRPIGNLGCYILDGNLEPVpvgvlGELY 853
Cdd:TIGR01923 229 SAIPAplieEAQQY---GLP---IYLSYGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 854 LAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 933
Cdd:TIGR01923 297 VKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 934 EAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:TIGR01923 370 EAVVVPKPdaewGQVPVAYIVSESDISQ--AKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
3066-3525 |
2.56e-47 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 178.03 E-value: 2.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 KlplAQGVQRIDLDRgaPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:TIGR01923 82 E---EKDFQADSLDR--IEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3226 QKTPFsFDVSVWEFFWP-LMSGARLVVaapgdHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEdvASCTSLKRIVCSG 3304
Cdd:TIGR01923 157 LSLPL-YHISGLSILFRwLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLDEG--GHNENLRKILLGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3305 EALPA----DAQQQvfaKLPqagLYNLYGPTEAAIDVTHWTcVEEGKDAVPIGRPIANLACYILDGNLEPVpvgvlGELY 3380
Cdd:TIGR01923 229 SAIPAplieEAQQY---GLP---IYLSYGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3381 LAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 3460
Cdd:TIGR01923 297 VKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3461 EAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:TIGR01923 370 EAVVVPKPdaewGQVPVAYIVSESDISQ--AKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4560-5041 |
2.58e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 177.48 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLll 4639
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 thshllerlpipeglscLSVDreeewagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT 4719
Cdd:cd05934 79 -----------------VVVD---------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4720 PEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTV----GVFPPVYLQQLAEHAERDGnp 4794
Cdd:cd05934 121 EDDVYLTVLPlFHINAQAVSVLAALSVGATLVLLPR--FSASRFWSDVRRYGATVtnylGAMLSYLLAQPPSPDDRAH-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 pPVRVyCFGGDAVAQAsydlaWRALKPKY---LFNGYGPTETVVTplLWKARAGDAcgaAYMPIGTLlgnRSGY---ILD 4868
Cdd:cd05934 197 -RLRA-AYGAPNPPEL-----HEEFEERFgvrLLEGYGMTETIVG--VIGPRDEPR---RPGSIGRP---APGYevrIVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGE---GVARGYLERPALTAERFvPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05934 262 DDGQELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM-RNGW-------FHTGDLGYRDADGFFYFVDRKKDMIRRRG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMVPSHLLFLA 5025
Cdd:cd05934 334 ENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEE-------LFAFCEGQLAYFKVPRYIRFVD 406
|
490
....*....|....*.
gi 2310915810 5026 RMPLTPNGKLDRKGLP 5041
Cdd:cd05934 407 DLPKTPTEKVAKAQLR 422
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1097-1516 |
4.46e-47 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 177.22 E-value: 4.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL-- 1172
Cdd:cd19066 1 KIPLSPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRie 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 ---WRRQAGSEEALLALCEEAQRS-LDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD- 1247
Cdd:cd19066 81 iidLRNLADPEARLLELIDQIQQTiYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1248 --LGPRSSSYQTWSRHLHEQAG--ARLDELDYWQAQLHDAPH--ALPCENPHGALENRHERKLVLTLDAERTRQLLQEAp 1321
Cdd:cd19066 161 ptLPPPVGSYADYAAWLEKQLEseAAQADLAYWTSYLHGLPPplPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1322 AAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDlgeaIDLSRTVGWFTSLFPVRL--TPAADLGESLKAIKEQL 1399
Cdd:cd19066 240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD----EAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1400 RGVPDKGVGYG--LLRYLAGEEAATRlAALPQPRITF-NYLGRFDRQFDGAALLVPATESAGAAQDpcapLANWLSIEGQ 1476
Cdd:cd19066 316 REAIEHQRVPFieLVRHLGVVPEAPK-HPLFEPVFTFkNNQQQLGKTGGFIFTTPVYTSSEGTVFD----LDLEASEDPD 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2310915810 1477 vygGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:cd19066 391 ---GDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
2006-2479 |
6.78e-47 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 176.88 E-value: 6.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSG 2085
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2086 ARWLIcqetlaerlpcpaeverlpletaawpasadtrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAART 2165
Cdd:cd05919 83 ARLVV------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMARE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2166 Y-GVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTILDLPP---AYLQQQAEELRH 2240
Cdd:cd05919 127 AlGLTPGDRVFSSAKMFFGyGLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVLYGVPtfyANLLDSCAGSPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRriAVRTCILGGEAWDASLltqqavqAEAWFNAY--------GPTEAVITPLAwhCRAQEGGAPAIGRALGARRACIL 2312
Cdd:cd05919 206 ALR--SLRLCVSAGEALPRGL-------GERWMEHFggpildgiGATEVGHIFLS--NRPGAWRLGSTGRPVPGYEIRLV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:cd05919 275 DEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2393 IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:cd05919 347 VSPVEVESLIIQHPAVAEAAVVAVpESTGLSRLTAFVVLKSPAAPQESLARdIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
....*....
gi 2310915810 2471 NGKLDRKAL 2479
Cdd:cd05919 427 TGKLQRFKL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2012-2479 |
7.92e-47 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 176.85 E-value: 7.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 QETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP- 2170
Cdd:cd05971 85 DGS-----------------------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPr 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 -GDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ---QQAEELRHAGRRI 2245
Cdd:cd05971 130 dGDLYWTPADWAWIGGLLDVLLPsLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKmmrQQGEQLKHAQVKL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2246 avRTCILGGEAWDASLLTQQAVQAEAWFN-AYGPTEA--VITPLAWHCRAQEGgapAIGRALGARRACILDAALQPCAPG 2322
Cdd:cd05971 210 --RAIATGGESLGEELLGWAREQFGVEVNeFYGQTECnlVIGNCSALFPIKPG---SMGKPIPGHRVAIVDDNGTPLPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2323 MIGELYIGGQCLAR--GYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIES 2400
Cdd:cd05971 285 EVGEIAVELPDPVAflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2401 QLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKA 2478
Cdd:cd05971 357 CLLKHPAVLMAAVVGIpDPIRGEIVKAFVVLNPGETPSDALArEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRE 436
|
.
gi 2310915810 2479 L 2479
Cdd:cd05971 437 L 437
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
2014-2479 |
9.21e-47 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 176.89 E-value: 9.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGArwlicQE 2093
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHV-----SY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAERLPCPAEVERLPletaawpasaDTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd17654 92 LLQNKELDNAPLSFTP----------EHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 qLQFASI-SFDAAAEQLFVPLLAGARVLLG-DAGQWSAQHLADEV-ERHAVTILDLPPAYLQQ---QAEELRHAGRRIAV 2247
Cdd:cd17654 162 -LFLTSPlTFDPSVVEIFLSLSSGATLLIVpTSVKVLPSKLADILfKRHRITVLQATPTLFRRfgsQSIKSTVLSATSSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2248 RTCILGGEAWDASLLTQQAVQAE---AWFNAYGPTEAVITPLAWHCRAQEGGAPaIGRALGARRACILDAalqpCAPGMI 2324
Cdd:cd17654 241 RVLALGGEPFPSLVILSSWRGKGnrtRIFNIYGITEVSCWALAYKVPEEDSPVQ-LGSPLLGTVIEVRDQ----NGSEGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQ---CLARGYLGRPGQTaerfvadpfsgsgerLYRTGDLARyRVDGQVEYLGRADQQIKIRGFRIEIGEIESQ 2401
Cdd:cd17654 316 GQVFLGGLnrvCILDDEVTVPKGT---------------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2402 LLAHPYVAEAAVVALDgvgGPLLAAYLVGR--DAMRGEDLLAELrtwlagrLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd17654 380 IESCLGVESCAVTLSD---QQRLIAFIVGEssSSRIHKELQLTL-------LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
4555-5040 |
1.85e-46 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 175.73 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4555 AVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSR 4634
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4635 AhlllthshlleRLpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHG--PLIAHIVAT 4712
Cdd:cd05919 83 A-----------RL--------------------------VVTSADDIAYLLYSSGTTGPPKGVMHAHRdpLLFADAMAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4713 gERYEMTPEDCELHF--MSFAFdGSHEGWMHPLINGARVLIrDDSLWLPERTYAEMHRHGVTV--GVfPPVYLQQLAEHA 4788
Cdd:cd05919 126 -EALGLTPGDRVFSSakMFFGY-GLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVlyGV-PTFYANLLDSCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 ERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPLlwKARAGDAcgaaymPIGTLLGNRSGY--- 4865
Cdd:cd05919 202 GSPDALRSLRLCVSAGEALPRGLGE-RWMEHFGGPILDGIGATEVGHIFL--SNRPGAW------RLGSTGRPVPGYeir 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05919 273 LVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPavADSPEAQAEcraQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd05919 345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGlSRLTAFVVLKSP--AAPQESLAR---DIHRHLLERLSAHKVPRRIAFV 419
|
490
....*....|....*.
gi 2310915810 5025 ARMPLTPNGKLDRKGL 5040
Cdd:cd05919 420 DELPRTATGKLQRFKL 435
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2022-2479 |
3.49e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 175.32 E-value: 3.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2022 RAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAG----YLPLDPNYPAERLAYMLRDSGARWLICQETLAE 2097
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2098 RLPCPAEVERLP---LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:cd05922 82 RLRDALPASPDPgtvLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSaQHLADEVERHAVTILD-LPPAYlqqqaEELRHAGRRIA----VRT 2249
Cdd:cd05922 162 LTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLD-DAFWEDLREHGATGLAgVPSTY-----AMLTRLGFDPAklpsLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2250 CILGGEAWDASLLTQQAVQAEAW--FNAYGPTEA--VITPLAWHcraQEGGAP-AIGRALGARRACILDAALQPCAPGMI 2324
Cdd:cd05922 236 LTQAGGRLPQETIARLRELLPGAqvYVMYGQTEAtrRMTYLPPE---RILEKPgSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQCLARGYLGRPGQTAERfvadpfSGSGERLYrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05922 313 GEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2405 HPYVAEAAVVALDGVGGPLLAAYLVGRDamrgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05922 386 IGLIIEAAAVGLPDPLGEKLALFVTAPD----KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
4090-4326 |
1.41e-45 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 166.37 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4090 LSPMQQGMLFHslyEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqQPLQIVYRQRQLPFAEE 4168
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGpLDVEALERALRELVRRHPALRTRFVEEDG--EPVQRIDPDADLPLEVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4169 DLSQAANRDAALLALAAAE--RERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA----GR 4242
Cdd:COG4908 76 DLSALPEPEREAELEELVAeeASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAalleGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4243 SPEQP-RDGRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATATARLRDF 4317
Cdd:COG4908 156 PPPLPeLPIQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRG-ATLSFTLPAELTEALKAL 234
|
....*....
gi 2310915810 4318 ARRHQVTLN 4326
Cdd:COG4908 235 AKAHGATVN 243
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
2002-2479 |
1.93e-45 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 174.04 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVC--GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAY 2079
Cdd:cd05926 1 PDAPALVVpgSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2080 MLRDSGARWLICQEtlAERLPC--PAEVERLPLETAAW------------------PASADTRPLPEVAGETLAYVIYTS 2139
Cdd:cd05926 81 YLADLGSKLVLTPK--GELGPAsrAASKLGLAILELALdvgvlirapsaeslsnllADKKNAKSEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2140 GSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQL----------QFASisfdaaaeqLFVPLLAGARVLLgdAGQWSA 2209
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfhvhgLVAS---------LLSTLAAGGSVVL--PPRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVT-----------ILDLPPAYLQQQAEELRHagrriaVRTCilggeawDASLLTQQAVQAEAWFN---- 2274
Cdd:cd05926 228 STFWPDVRDYNATwytavptihqiLLNRPEPNPESPPPKLRF------IRSC-------SASLPPAVLEALEATFGapvl 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 -AYGPTEAV--IT--PLAWHCRAqeggAPAIGRALGArRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERF 2349
Cdd:cd05926 295 eAYGMTEAAhqMTsnPLPPGPRK----PGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2350 VADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL 2428
Cdd:cd05926 370 FKDGW-------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpDEKYGEEVAAAV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2429 VGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05926 443 VLREGASVTE--EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1553-1956 |
3.18e-45 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 171.82 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1553 YPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQAT--- 1626
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVaieMFLT-GSLDLARLKQALDAVMERHDVLRTRFCEEAG--RYEQVVLDKTVrfr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1627 ---LELR-LAPPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG--- 1699
Cdd:cd19066 79 ieiIDLRnLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaer 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1700 --QEVAATVGRYRDYIGWLQ---GRDAMATEF-FWRDRLASLEMPTRLARQARTEQPGQGEHLR---ELDPQTTRQLASF 1770
Cdd:cd19066 159 qkPTLPPPVGSYADYAAWLEkqlESEAAQADLaYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTlefFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1771 AQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNL 1850
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1851 ALREHEHTPLYDIQRWAGHGGEA----LFDSILVFENFPVAEALrqaPADLEFSTPSNH--EQTNYPLTLGVTLGER--L 1922
Cdd:cd19066 317 EAIEHQRVPFIELVRHLGVVPEApkhpLFEPVFTFKNNQQQLGK---TGGFIFTTPVYTssEGTVFDLDLEASEDPDgdL 393
|
410 420 430
....*....|....*....|....*....|....
gi 2310915810 1923 SLQYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19066 394 LLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
4551-5040 |
1.05e-44 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 172.11 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLY 4628
Cdd:cd05926 1 PDAPALVVPGstPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4629 MMQDSRAH--------------LLLTHSHLLERLPIPEGLSCLSVDREE---EWAGFPAHDPEVALHGDNLAYVIYTSGS 4691
Cdd:cd05926 81 YLADLGSKlvltpkgelgpasrAASKLGLAILELALDVGVLIRAPSAESlsnLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIA--HIVATGerYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVlirddslWLPERTYA---- 4764
Cdd:cd05926 161 TGRPKGVPLTHRNLAAsaTNITNT--YKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSV-------VLPPRFSAstfw 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 -EMHRHGVTVGVFPPVYLQQLAEHAERD--GNPPPVRVycfggdaVAQASYDLA---WRALKPKY---LFNGYGPTETV- 4834
Cdd:cd05926 232 pDVRDYNATWYTAVPTIHQILLNRPEPNpeSPPPKLRF-------IRSCSASLPpavLEALEATFgapVLEAYGMTEAAh 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 -VT--PLLWKARAgdaCGAAYMPIGTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFga 4911
Cdd:cd05926 305 qMTsnPLPPGPRK---PGSVGKPVGVEVR-----ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4912 pgsrlYRSGDLTRGRADGvvdYL---GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQE 4987
Cdd:cd05926 375 -----FRTGDLGYLDADG---YLfltGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEEVAAAVVLRE 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4988 PAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05926 447 GASVT--------EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
3066-3479 |
4.31e-44 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 170.09 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd05911 13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 ---------KLP----------LAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAgnrhsALS 3206
Cdd:cd05911 93 lekvkeaakELGpkdkiivlddKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGV-----CLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3207 NR--LCWMQQAYG-----LGVGDTVLQKTPfsfdvsvweFFWplMSGARLVVAAP--GDHR------DPAKLVALINREG 3271
Cdd:cd05911 168 HRnlIANLSQVQTflygnDGSNDVILGFLP---------LYH--IYGLFTTLASLlnGATViimpkfDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3272 VDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA 3349
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLdkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3350 VpiGRPIANLACYILD--GNlEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVI 3427
Cdd:cd05911 317 V--GRLLPNVEAKIVDddGK-DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGYFDEDGYL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3428 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV----LAVDGRQLVGYVVLE 3479
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigipDEVSGELPRAYVVRK 443
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
3063-3520 |
7.03e-44 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 167.94 E-value: 7.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHLKlplaqgvqridldrgapwfedyseaNPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 3222
Cdd:cd05903 81 ERFR-------------------------QFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3223 TVLQKTPFS-FDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTL----HFVPSMLQAFLQDEDVASctSL 3297
Cdd:cd05903 136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLS--RL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3298 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:cd05903 211 RTFVCGGATVPRSLARRA-AELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3458 WVREAAVLAVDGRQL----VGYVVLES-ESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd05903 363 GVIEAAVVALPDERLgeraCAVVVTKSgALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
539-952 |
7.29e-44 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 169.32 E-value: 7.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:cd05911 13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 K------LPLAQGVQRI-----------DLDQADAWLENHAENNPGIELN--GENLAYVIYTSGSTGKPKGAgnrhsALS 679
Cdd:cd05911 93 LekvkeaAKELGPKDKIivlddkpdgvlSIEDLLSPTLGEEDEDLPPPLKdgKDDTAAILYSSGTTGLPKGV-----CLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 680 NR--LCWMQQAYG-----LGVGDTVLQKTPfsfdvsvweFFWplMSGARLVVAAP--GDHR------DPAKLVELINREG 744
Cdd:cd05911 168 HRnlIANLSQVQTflygnDGSNDVILGFLP---------LYH--IYGLFTTLASLlnGATViimpkfDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 745 VDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtCVEEGKDT 822
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLdkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV--NPDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 823 VPIGRPIGNLGCYILD--GNlEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVI 900
Cdd:cd05911 315 GSVGRLLPNVEAKIVDddGK-DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGYFDEDGYL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 901 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV----LAVDGRQLVGYVVLE 952
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigipDEVSGELPRAYVVRK 443
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
2014-2474 |
3.84e-43 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 166.02 E-value: 3.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIcqe 2093
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpCPAEVERlpletaawpasadTRPLPEvaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05903 79 -------VPERFRQ-------------FDPAAM--PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASIS-FDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCI 2251
Cdd:cd05903 137 FLVASPMAhQTGFVYGFTLPLLLGAPVVLQD--IWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSrLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LGGEAWDASLLTQQAVQAEAW-FNAYGPTE-----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIG 2325
Cdd:cd05903 215 CGGATVPRSLARRAAELLGAKvCSAYGSTEcpgavTSITPAPEDRRLYTDGRPLPGVEIK-----VVDDTGATLAPGVEG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2326 ELYIGGQCLARGYLGRPGQTAErfvADPfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAH 2405
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTAD---AAP-----EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGH 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2406 PYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAG-RLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:cd05903 362 PGVIEAAVVALpDERLGERACAVVVTKSGALLT--FDELVAYLDRqGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2002-2474 |
4.40e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 167.80 E-value: 4.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK08316 25 PDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLpcPAEVERLPLETAAWPASADTR--------------------PLPEVAGETLAYVIYTSGS 2141
Cdd:PRK08316 105 DHSGARAFLVDPALAPTA--EAALALLPVDTLILSLVLGGReapggwldfadwaeagsvaePDVELADDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2142 TGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQwsAQHLADEVERHA 2220
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPyLYVGATNVILDAPD--PELILRTIEAER 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2221 VTILDLPPAY---LqqqaeeLRH---AGRRI-AVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEavITPLAWHCR 2291
Cdd:PRK08316 261 ITSFFAPPTVwisL------LRHpdfDTRDLsSLRKGYYGASIMPVEVLKelRERLPGLRFYNCYGQTE--IAPLATVLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEggapAIGRALGARRAC------ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTG 2365
Cdd:PRK08316 333 PEE----HLRRPGSAGRPVlnvetrVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF--------HSG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR--GEDLLAE 2442
Cdd:PRK08316 401 DLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLpDPKWIEAVTAVVVPKAGATvtEDELIAH 480
|
490 500 510
....*....|....*....|....*....|..
gi 2310915810 2443 LRtwlaGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK08316 481 CR----ARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
536-993 |
9.05e-43 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 164.86 E-value: 9.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQ 615
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 616 SHLKlplaqgvQRIDLDQADAwlenhaennpgielngenLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05903 81 ERFR-------QFDPAAMPDA------------------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 696 TVLQKTPFS-FDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTL----HFVPSMLQAFLQDEDVASctSL 770
Cdd:cd05903 136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLS--RL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 771 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:cd05903 211 RTFVCGGATVPRSLARRA-AELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 851 ELYLAGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 931 WVREAAVLAVDGRQL----VGYVVLESEGG-DWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd05903 363 GVIEAAVVALPDERLgeraCAVVVTKSGALlTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
516-994 |
9.51e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 166.98 E-value: 9.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 596 PEERQAYMLEDSGVQLLLSQSHL---------KLPLAQGVQRID-----------LDQADAwLENHAENNPGIELNGENL 655
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFaprvaevlpRLPKLRTLVVVEdgsgndllpgaVDYEDA-LAAGSPERDFGERSPDDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 656 aYVIYTSGSTGKPKGAGNRHSALsnrlcWMQQAYGL--------------------GVGDTVLQKTPFSFDVSVWEFFWP 715
Cdd:PRK07798 167 -YLLYTGGTTGMPKGVMWRQEDI-----FRVLLGGRdfatgepiedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 716 LMSGARlVVAAPGDHRDPAKLVELINREGVDTLHFV------PsMLQAFLQDEDvASCTSLKRIVCSGEALPADAQQQVF 789
Cdd:PRK07798 241 LFSGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGP-YDLSSLFAIASGGALFSPSVKEALL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 790 AKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRpignlGCYILDGNLEPVPVGVLGELYLAGRG-LARGYHQ 865
Cdd:PRK07798 318 ELLPNVVLTDSIGSSETGFGGSGTVAkgaVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 866 RPGLTAERFvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-DGR- 943
Cdd:PRK07798 393 DPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVpDERw 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 944 -QLVGYVVLESEGGDWREALAAHLAASL-PEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK07798 470 gQEVVAVVQLREGARPDLAELRAHCRSSlAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
4563-5037 |
1.17e-42 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 164.05 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllths 4642
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 hllerlpipeglSCLSVDREEewagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05972 74 ------------KAIVTDAED------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 ceLHFMSfafdgSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP 4794
Cdd:cd05972 124 --IHWNI-----ADPGWakgawssfFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTPLLWKAragdacgaayMPI--GTLLGNRSGY---ILDG 4869
Cdd:cd05972 197 SHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFPD----------MPVkpGSMGRPTPGYdvaIIDD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4870 QLNLLPVGVAGEL--YLGGEGVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFR 4947
Cdd:cd05972 266 DGRELPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4948 IELGEIEARLREHPAVREAVVVAQPGAVGQQLV-GYVVAQEPAvadspEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVLTSGY-----EPSEELAEELQGHVKKVLAPYKYPREIEFVEE 412
|
490
....*....|.
gi 2310915810 5027 MPLTPNGKLDR 5037
Cdd:cd05972 413 LPKTISGKIRR 423
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3061-3526 |
1.29e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 164.00 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 sqshlklplaqgvqrIDLdrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05934 81 ---------------VDP------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFL-QDEDVASCTSLK 3298
Cdd:cd05934 122 DDVYLTVLPlFHINAQAVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPDDRAHRL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVthWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:cd05934 199 RAAYGAPNPPELHEE--FEERFGVRLLEGYGMTETIVGV--IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYL---AGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:cd05934 275 LVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3456 HPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 3526
Cdd:cd05934 348 HPAVREAAVVAVPdevgEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
4547-5036 |
2.26e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 165.83 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07798 13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHL-------LLTHSHLLERLP-------IPEG----LSCLSVDREEEWAGFPAHDPEVALHGDNLaYVIYT 4688
Cdd:PRK07798 93 RYLLDDSDAVAlvyerefAPRVAEVLPRLPklrtlvvVEDGsgndLLPGAVDYEDALAAGSPERDFGERSPDDL-YLLYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGplIAHIVATGERYEMT---PEDCELHfMSFAFDGSHEGWM--HPLINGA-------------RVL 4750
Cdd:PRK07798 172 GGTTGMPKGVMWRQE--DIFRVLLGGRDFATgepIEDEEEL-AKRAAAGPGMRRFpaPPLMHGAgqwaafaalfsgqTVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IRDDSLWLPERTYAEMHRHGVTVGVFP-PVYLQQLAEHAERDGNP--PPVRVYCFGGdAVAQASYDLAWRALKPKYLF-N 4826
Cdd:PRK07798 249 LLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPYdlSSLFAIASGG-ALFSPSVKEALLELLPNVVLtD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4827 GYGPTETVVTPLLWKARAGDACGAAYMPIGtllgnRSGYILDGQLNLLPVGVAGELYLGGEG-VARGYLERPALTAERFv 4905
Cdd:PRK07798 328 SIGSSETGFGGSGTVAKGAVHTGGPRFTIG-----PRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEKTAETF- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4906 pdpFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYVV 4984
Cdd:PRK07798 402 ---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPdERWGQEVVAVVQ 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4985 AQEPAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK07798 479 LREGARPDL--------AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
2014-2479 |
2.77e-42 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 163.03 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05935 82 EL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASIsFDAAAEQ--LFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCI 2251
Cdd:cd05935 128 ILACLPL-FHVTGFVgsLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LGGEAWDASLLTQQAVQAEAWF--NAYGPTEAV----ITPLAwHCRAQEGGAPAIGralgaRRACILDA-ALQPCAPGMI 2324
Cdd:cd05935 205 TGGGAPMPPAVAEKLLKLTGLRfvEGYGLTETMsqthTNPPL-RPKLQCLGIP*FG-----VDARVIDIeTGRELPPNEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQCLARGYLGRPGQTAERFVADpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2405 HPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05935 355 HPAI*EVCVISVpDERVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
534-999 |
4.71e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 162.08 E-value: 4.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 614 sqshlklplaqgvqrIDLdqadawlenhaennpgielngenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05934 81 ---------------VDP------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 694 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFL-QDEDVASCTSLK 771
Cdd:cd05934 122 DDVYLTVLPlFHINAQAVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPDDRAHRL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 772 RIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVthWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGE 851
Cdd:cd05934 199 RAAYGAPNPPELHEE--FEERFGVRLLEGYGMTETIVGV--IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 852 LYL---AGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:cd05934 275 LVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 929 HPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 999
Cdd:cd05934 348 HPAVREAAVVAVPdevgEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
4544-5042 |
7.01e-42 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 164.92 E-value: 7.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDE-EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK06087 30 QQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSC----------LSVDREEEWA-----------GFPAHDPeVALHGDN 4681
Cdd:PRK06087 110 EAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLqnqlpqlqqiVGVDKLAPATsslslsqiiadYEPLTTA-ITTHGDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDceLHFMSFAFD---GSHEGWMHPLINGARVLIRDDslWL 4758
Cdd:PRK06087 189 LAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD--VFMMPAPLGhatGFLHGVTAPFLIGARSVLLDI--FT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4759 PERTYAEMHRHGVT--VGVFPPVYlqQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRA-LKpkyLFNGYGPTETv 4834
Cdd:PRK06087 265 PDACLALLEQQRCTcmLGATPFIY--DLLNLLEKQPaDLSALRFFLCGGTTIPKKVARECQQRgIK---LLSVYGSTES- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 vtpllwkaragdaCGAAYMPIGTLL---GNRSGY--------ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAER 4903
Cdd:PRK06087 339 -------------SPHAVVNLDDPLsrfMHTDGYaaagveikVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4904 FVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRvDHQVKIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVG 4981
Cdd:PRK06087 406 LDEEGW-------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDErLGERSCA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4982 YVVAQEPavADSPEAqAECRAQLKtalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK06087 478 YVVLKAP--HHSLTL-EEVVAFFS---RKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
3048-3467 |
1.51e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 163.18 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYPEER 3126
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALG-HNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3127 QAYMLEDSGVELLLSQSHLkLPLAQ------GVQRIDLDRGAP-------------WFEDYSEANPDIHLDGENLAYVIY 3187
Cdd:PRK08316 100 LAYILDHSGARAFLVDPAL-APTAEaalallPVDTLILSLVLGgreapggwldfadWAEAGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSALsnrlcwMQQ------AYGLGVGDTVLQKTPF----SFDVsvweFFWP-LMSGAR-LVVAAPg 3255
Cdd:PRK08316 179 TSGTESLPKGAMLTHRAL------IAEyvscivAGDMSADDIPLHALPLyhcaQLDV----FLGPyLYVGATnVILDAP- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3256 dhrDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEA 3333
Cdd:PRK08316 248 ---DPELILRTIEAERITSFFAPPTVWISLLRhpDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3334 AIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermy 3413
Cdd:PRK08316 325 APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF------- 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3414 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK08316 398 HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
3054-3525 |
2.18e-41 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 160.92 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIERGVG--ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKDlrGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLsqshlklplaqgvqridldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd05941 81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhrdpAKLVALINREGVDTLHF-VPSM----LQA 3284
Cdd:cd05941 121 LVDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKFD----PKEVAISRLMPSITVFMgVPTIytrlLQY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3285 F------LQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVthwTCVEEGkDAVP--IGRPI 3356
Cdd:cd05941 196 YeahftdPQFARAAAAERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTEIGMAL---SNPLDG-ERRPgtVGMPL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRI-D 3434
Cdd:cd05941 271 PGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWR-EALAAHLAASLPEYMVPAQWLAL 3509
Cdd:cd05941 345 DIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPdpdwGERVVAVVVLRAGAAALSlEELKEWAKQRLAPYKRPRRLILV 424
|
490
....*....|....*.
gi 2310915810 3510 ERMPLSPNGKLDRKAL 3525
Cdd:cd05941 425 DELPRNAMGKVNKKEL 440
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1998-2494 |
2.58e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 162.99 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 AYMLRDSGARWLICQET-----LAERLPCPAEVERLPLETAA----------------WPASADTRPLPEVAG------- 2129
Cdd:PRK06164 100 AHILGRGRARWLVVWPGfkgidFAAILAAVPPDALPPLRAIAvvddaadatpapapgaRVQLFALPDPAPPAAageraad 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 -ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAgqWS 2208
Cdd:PRK06164 180 pDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPV--FD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2209 AQHLADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEA----WFNAYGPTEAV-- 2282
Cdd:PRK06164 258 AARTARALRRHRVTHTFGNDEMLRRI---LDTAGERADFPSARLFGFASFAPALGELAALARArgvpLTGLYGSSEVQal 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2283 --ITPLA--WHCRAQEGGAPAIGRAlGARRACILDAALqpCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsg 2358
Cdd:PRK06164 335 vaLQPATdpVSVRIEGGGRPASPEA-RVRARDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY---- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2359 erlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGED 2438
Cdd:PRK06164 408 ---FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGASPDE 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2439 llAELRTWLAGRLPAYMQPTAWQVLSSLP--LNANGKLDRKALPKvDAAARRQAGEPP 2494
Cdd:PRK06164 485 --AGLMAACREALAGFKVPARVQVVEAFPvtESANGAKIQKHRLR-EMAQARLAAERA 539
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3043-3533 |
5.04e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 161.98 E-value: 5.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHL---------KLPLAQGVQRI------DLDRGAPWFEDYSEANPDIHLDGENLA---Y 3184
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFaprvaevlpRLPKLRTLVVVedgsgnDLLPGAVDYEDALAAGSPERDFGERSPddlY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALsnrlcWMQQAYGL--------------------GVGDTVLQKTPFSFDVSVWEFFWPLM 3244
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDI-----FRVLLGGRdfatgepiedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAALF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3245 SGARlVVAAPGDHRDPAKLVALINREGVDTLHFV------PsMLQAFLQDEDvASCTSLKRIVCSGEALPADAQQQVFAK 3318
Cdd:PRK07798 243 SGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGP-YDLSSLFAIASGGALFSPSVKEALLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3319 LPQAGLYNLYGPTEAAIDVTHWTcveeGKDAVPIGRPIANLA--CYILDGNLEPVPVGVLGELYLAGQG-LARGYHQRPG 3395
Cdd:PRK07798 320 LPNVVLTDSIGSSETGFGGSGTV----AKGAVHTGGPRFTIGprTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3396 LTAERFvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQ 3471
Cdd:PRK07798 396 KTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPderwGQE 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3472 LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD-RKAlpRPQAAAG 3533
Cdd:PRK07798 473 VVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADyRWA--KEQAAER 533
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
4563-5040 |
5.70e-41 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 159.59 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLpipeglsclsvdreeewagfpahDPEvalhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05969 81 ELYERT-----------------------DPE------DPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFMSFAF-DGSHEGWMHPLINGARVLIrDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQL----AEHAER-DGNPpp 4796
Cdd:cd05969 132 IYWCTADPGWvTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmkegDELARKyDLSS-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4797 VRVYCFGGDAVAQASYDLAWRALKpKYLFNGYGPTET----VVTPLLWKARAGDacgaaympIGTLLGNRSGYILDGQLN 4872
Cdd:cd05969 209 LRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTETgsimIANYPCMPIKPGS--------MGKPLPGVKAAVVDENGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYL--GGEGVARGYLERPALTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIEL 4950
Cdd:cd05969 280 ELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4951 GEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEpavadSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPL 5029
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLrGEIIKAFISLKE-----GFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|.
gi 2310915810 5030 TPNGKLDRKGL 5040
Cdd:cd05969 427 TRSGKIMRRVL 437
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
2014-2479 |
6.38e-41 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 159.59 E-value: 6.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAERlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD- 2172
Cdd:cd05969 81 ELYER----------------------TDP------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDi 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2173 --CQLQFASISFDAAAeqLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAV 2247
Cdd:cd05969 133 ywCTADPGWVTGTVYG--IWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLSSL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2248 RTCILGGEAWDAslltqqavQAEAW----FN-----AYGPTEAVITPLAwHCRAQEGGAPAIGRALGARRACILDAALQP 2318
Cdd:cd05969 210 RFIHSVGEPLNP--------EAIRWgmevFGvpihdTWWQTETGSIMIA-NYPCMPIKPGSMGKPLPGVKAAVVDENGNE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CAPGMIGELYI--GGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIG 2396
Cdd:cd05969 281 LPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:cd05969 353 EVESALMEHPAVAEAGVIGKpDPLRGEIIKAFISLKEGFEpSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
|
....*
gi 2310915810 2475 DRKAL 2479
Cdd:cd05969 433 MRRVL 437
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
544-998 |
8.48e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 159.53 E-value: 8.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 544 RRANRLAHALIERG-IGADRLVGVAMERSiEMVVALMAILKAGGA----YVPVDPEYPEERQAYMLEDSGVQLLLSQ--- 615
Cdd:cd05922 1 LGVSAAASALLEAGgVRGERVVLILPNRF-TYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADaga 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 616 -SHLKLPLAQGVQRIDLDQADAWleNHAENN-PGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05922 80 aDRLRDALPASPDPGTVLDADGI--RAARASaPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 694 GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKR 772
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRlGFDPAKLPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 773 IVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGEL 852
Cdd:cd05922 236 LTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 853 YLAGRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:cd05922 316 VHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 933 REAAVLAVD---GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05922 390 IEAAAVGLPdplGEKLALFVTAPDKIDP--KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
527-998 |
9.36e-41 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 158.99 E-value: 9.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 527 APALAFGEERLDYAELNRRANRLAHALIERG--IGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGkdLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLsqshlklplaqgvqridldqadawlenhaennpgielngeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd05941 81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhrdpAKLVELINREGVDTLHF-VPSM----LQA 757
Cdd:cd05941 121 LVDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKFD----PKEVAISRLMPSITVFMgVPTIytrlLQY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 758 F------LQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVthwTCVEEGkDTVP--IGRPI 829
Cdd:cd05941 196 YeahftdPQFARAAAAERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTEIGMAL---SNPLDG-ERRPgtVGMPL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 830 GNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRI-D 907
Cdd:cd05941 271 PGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWR-EALAAHLAASLPEYMVPAQWLAL 982
Cdd:cd05941 345 DIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPdpdwGERVVAVVVLRAGAAALSlEELKEWAKQRLAPYKRPRRLILV 424
|
490
....*....|....*.
gi 2310915810 983 ERMPLSPNGKLDRKAL 998
Cdd:cd05941 425 DELPRNAMGKVNKKEL 440
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
2132-2479 |
1.08e-40 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 155.18 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2132 LAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagqwSAQH 2211
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLE----RNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWhcR 2291
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATK--R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEGGAPAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQtaerfvaDPFSGSGerLYRTGDLARYR 2371
Cdd:cd17630 156 PDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV-------PEFNEDG--WFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2372 VDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRL 2451
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV---GVPDEELGQRPVAVIVGRGPADPAELRAWLKDKL 293
|
330 340
....*....|....*....|....*...
gi 2310915810 2452 PAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd17630 294 ARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2014-2481 |
1.48e-40 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 158.07 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQe 2093
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletAAWPASADTRPLPEvagetlayvIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDc 2173
Cdd:cd05973 80 -------------------AANRHKLDSDPFVM---------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 qlQFASISFDAAAEQLFV----PLLAGARVLLGDAGqWSAQHLADEVERHAVTILD-LPPAYlqqqaEELRHAGRRIAVR 2248
Cdd:cd05973 131 --SFWNAADPGWAYGLYYaitgPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAgSPTAY-----RLLMAAGAEVPAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 tciLGGEAWDASL----LTQQAVQaeaWFNA---------YGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAA 2315
Cdd:cd05973 203 ---PKGRLRRVSSagepLTPEVIR---WFDAalgvpihdhYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQ----CLARGYLGRPGQTaerfvadpFSGsgeRLYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:cd05973 277 GDELGPGEPGRLAIDIAnsplMWFRGYQLPDTPA--------IDG---GYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRG-EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLN 2469
Cdd:cd05973 346 RIGPFDVESALIEHPAVAEAAVIGVpDPERTEVVKAFVVLRGGHEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
|
490
....*....|..
gi 2310915810 2470 ANGKLDRKALPK 2481
Cdd:cd05973 426 PSGKIQRFLLRR 437
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1996-2444 |
1.67e-40 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 160.87 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1996 HQVASAPEAIALV------CGDEHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPL- 2068
Cdd:cd05931 1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 --DPNYPAERLAYMLRDSGARWLICQETLAERLP----CPAEVERLPLETAAWPA--SADTRPLPEVAGETLAYVIYTSG 2140
Cdd:cd05931 80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRafaaSRPAAGTPRLLVVDLLPdtSAADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2141 STGQPKGVAVSQAALVAHCQAAARTYGVGPG-----------DCQLQFAsisfdaaaeqLFVPLLAGARVLL-------G 2202
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGdvvvswlplyhDMGLIGG----------LLTPLYSGGPSVLmspaaflR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2203 DAGQWsaqhlADEVERHAVTILDLPP-AYlqqqaeelRHAGRRI-----------AVRTCILGGEAWDASLLTQQA---- 2266
Cdd:cd05931 230 RPLRW-----LRLISRYRATISAAPNfAY--------DLCVRRVrdedlegldlsSWRVALNGAEPVRPATLRRFAeafa 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2267 ---VQAEAWFNAYGPTEAV----------------ITPLAWHCRAQEGGAPA--------IGRALGARRACILDAA-LQP 2318
Cdd:cd05931 297 pfgFRPEAFRPSYGLAEATlfvsggppgtgpvvlrVDRDALAGRAVAVAADDpaarelvsCGRPLPDQEVRIVDPEtGRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfSGSGERLYRTGDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2399 ESQL-LAHPYVAEAAVVAL---DGVGGPLLAAYLVGRDAMRGED--LLAELR 2444
Cdd:cd05931 455 EATAeEAHPALRPGCVAAFsvpDDGEERLVVVAEVERGADPADLaaIAAAIR 506
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
4561-5040 |
1.82e-40 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 157.98 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllt 4640
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4641 hshllerlpipeglSCLSVDReeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05971 80 --------------SALVTDG-----------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDCELHFMSfafdgSHEGWMHPLIN--------GARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDg 4792
Cdd:cd05971 129 RDGDLYWTP-----ADWAWIGGLLDvllpslyfGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQL- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4793 NPPPVRVYCF--GGDAVAQASydLAW--RALKPKyLFNGYGPTET--VVT--PLLWKARAGdACGAAYmPigtllGNRSG 4864
Cdd:cd05971 203 KHAQVKLRAIatGGESLGEEL--LGWarEQFGVE-VNEFYGQTECnlVIGncSALFPIKPG-SMGKPI-P-----GHRVA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4865 yILDGQLNLLPVGVAGELylggeGVAR-------GYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRV 4937
Cdd:cd05971 273 -IVDDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4938 DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQePAVADSPEAQAECRAQLKTalreRLPEYM 5016
Cdd:cd05971 339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIrGEIVKAFVVLN-PGETPSDALAREIQELVKT----RLAAHE 413
|
490 500
....*....|....*....|....
gi 2310915810 5017 VPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05971 414 YPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1952-2479 |
2.41e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 160.59 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1952 MAEtpQAALGEL-ALLDAGERQEALRDWQAPLEALPrggVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGL 2030
Cdd:PRK06178 1 MAE--EAYLAELrALQQAAWPAGIPREPEYPHGERP---LTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2031 RARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAE------------- 2097
Cdd:PRK06178 76 RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPvveqvraetslrh 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2098 --------------RLPCPAEVERLPLETAAW----PASADTR---PLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK06178 156 vivtsladvlpaepTLPLPDSLRAPRLAAAGAidllPALRACTapvPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAA-ARTYGVGPGDCQLQFASIsFDAAAEQ--LFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLP------ 2227
Cdd:PRK06178 236 YTAAAAyAVAVVGGEDSVFLSFLPE-FWIAGENfgLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTRTVMLvdnave 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2228 ----PAYLQQQAEELRHAG---------RRIAVRTCILGGeawdaslltqqAVQAEAwfnAYGPTEAViTPLAWHCRAQE 2294
Cdd:PRK06178 313 lmdhPRFAEYDLSSLRQVRvvsfvkklnPDYRQRWRALTG-----------SVLAEA---AWGMTETH-TCDTFTAGFQD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2295 G-----GAPA-IGRALGARRACILD---AALQPCapGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTG 2365
Cdd:PRK06178 378 DdfdllSQPVfVGLPVPGTEFKICDfetGELLPL--GAEGEIVVRTPSLLKGYWNKPEATAEALR--------DGWLHTG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVG-GPLLAAYLVGRDamrGEDLLAE-L 2443
Cdd:PRK06178 448 DIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDkGQVPVAFVQLKP---GADLTAAaL 524
|
570 580 590
....*....|....*....|....*....|....*.
gi 2310915810 2444 RTWLAGRLPAYMQPTAwQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06178 525 QAWCRENMAVYKVPEI-RIVDALPMTATGKVRKQDL 559
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1990-2475 |
4.52e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 159.28 E-value: 4.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETLAERL-PCPAEVERL-------------------PLETAAWPASADtRPLPEVAG 2129
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALVYEREFAPRVaEVLPRLPKLrtlvvvedgsgndllpgavDYEDALAAGSPE-RDFGERSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLaYVIYTSGSTGQPKGVAVSQAALVaHCQAAARTYGVGP---------GDCQLQFASISFDA-----AAEQL--FVPL 2193
Cdd:PRK07798 164 DDL-YLLYTGGTTGMPKGVMWRQEDIF-RVLLGGRDFATGEpiedeeelaKRAAAGPGMRRFPApplmhGAGQWaaFAAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2194 LAGARVLLGDAGQWSAQHLADEVERHAVTIL----DlppAYLQQQAEELRHAGRriavrtcilggeaWDAS--------- 2260
Cdd:PRK07798 242 FSGQTVVLLPDVRFDADEVWRTIEREKVNVItivgD---AMARPLLDALEARGP-------------YDLSslfaiasgg 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2261 LLTQQAVQAE--AWF------NAYGPTEaviTPLAWHCRAQEGGAPAIGRALGAR-RACILDAALQPCAPG--MIGELYI 2329
Cdd:PRK07798 306 ALFSPSVKEAllELLpnvvltDSIGSSE---TGFGGSGTVAKGAVHTGGPRFTIGpRTVVLDEDGNPVEPGsgEIGWIAR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2330 GGQcLARGYLGRPGQTAERF-VADpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV 2408
Cdd:PRK07798 383 RGH-IPLGYYKDPEKTAETFpTID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2409 AEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:PRK07798 457 ADALVVGVpDERWGQEVVAVVQLREGARPD--LAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
521-940 |
5.88e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 158.56 E-value: 5.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALG-HNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 600 QAYMLEDSGVQLLLSQSHLkLPLAQGVQRID-------------------LDQADAWLENHAENNPGIELNGENLAYVIY 660
Cdd:PRK08316 100 LAYILDHSGARAFLVDPAL-APTAEAALALLpvdtlilslvlggreapggWLDFADWAEAGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 661 TSGSTGKPKGAGNRHSALsnrlcwMQQ------AYGLGVGDTVLQKTPF----SFDVsvweFFWP-LMSGAR-LVVAAPg 728
Cdd:PRK08316 179 TSGTESLPKGAMLTHRAL------IAEyvscivAGDMSADDIPLHALPLyhcaQLDV----FLGPyLYVGATnVILDAP- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 729 dhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEA 806
Cdd:PRK08316 248 ---DPELILRTIEAERITSFFAPPTVWISLLRhpDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 807 AIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGElyLAGRG--LARGYHQRPGLTAERFVASPFvager 884
Cdd:PRK08316 325 APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGE--IVHRSpqLMLGYWDDPEKTAEAFRGGWF----- 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 885 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK08316 398 --HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1971-2474 |
6.09e-40 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 159.66 E-value: 6.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1971 RQEALRDWQAPLEALPRGG----VAAAFAHQVASAPEAIALVC-GDE-----HLSYAELDMRAERLARGLRARGVVAEAL 2040
Cdd:cd17634 32 VKNTSFAPGAPSIKWFEDAtlnlAANALDRHLRENGDRTAIIYeGDDtsqsrTISYRELHREVCRFAGTLLDLGVKKGDR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2041 VAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAER------LPCPAEVERL---PLE 2111
Cdd:cd17634 112 VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAgrsvplKKNVDDALNPnvtSVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2112 T---------------AAW--------PASADTRPLPeVAGETLAYVIYTSGSTGQPKGVA-VSQAALVAHCQAAARTYG 2167
Cdd:cd17634 192 HvivlkrtgsdidwqeGRDlwwrdliaKASPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLhTTGGYLVYAATTMKYVFD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2168 VGPGDCQLQFASISFDAAAEQL-FVPLLAGARVLLGD-AGQW-SAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGR- 2243
Cdd:cd17634 271 YGPGDIYWCTADVGWVTGHSYLlYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRA----LMAAGDd 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2244 ------RIAVRTCILGGEAWDAslltqqavQAEAWF------------NAYGPTE---AVITPLAWhcrAQEGGAPAIGR 2302
Cdd:cd17634 347 aiegtdRSSLRILGSVGEPINP--------EAYEWYwkkigkekcpvvDTWWQTEtggFMITPLPG---AIELKAGSATR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2303 ALGARRACILDAALQPCAPGMIGELYIG----GQclARGYLGRPgqtaERFVADPFSgSGERLYRTGDLARYRVDGQVEY 2378
Cdd:cd17634 416 PVFGVQPAVVDNEGHPQPGGTEGNLVITdpwpGQ--TRTLFGDH----ERFEQTYFS-TFKGMYFSGDGARRDEDGYYWI 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2379 LGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQ 2456
Cdd:cd17634 489 TGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIpHAIKGQAPYAYVVLNHGVEpSPELYAELRNWVRKEIGPLAT 568
|
570
....*....|....*...
gi 2310915810 2457 PTAWQVLSSLPLNANGKL 2474
Cdd:cd17634 569 PDVVHWVDSLPKTRSGKI 586
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
3013-3534 |
8.17e-40 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 158.68 E-value: 8.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3013 PMLDAEERGQllegwnATAAEYPLQRGVHRLFEEQVERTPTAPALA------FGEERLDYAELNRRANRLAHALIERGVG 3086
Cdd:PRK13295 5 AVLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3087 ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLK--------------LPLAQG 3152
Cdd:PRK13295 79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpeLPALRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3153 VQRIDLDrGAPWFEDY-----SEANPDIH-------LDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:PRK13295 159 VVVVGGD-GADSFEALlitpaWEQEPDAPailarlrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVD-TLHFVPsmlqaFLQD------EDVA 3292
Cdd:PRK13295 238 DDVILMASPMAHQTGfMYGLMMPVMLGATAVLQ---DIWDPARAAELIRTEGVTfTMASTP-----FLTDltravkESGR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3293 SCTSLKRIVCSGEALPA----DAQQQVFAKLPQAglynlYGPTE-AAIDVTHWTCVEEgKDAVPIGRPIANLACYILDGN 3367
Cdd:PRK13295 310 PVSSLRTFLCAGAPIPGalveRARAALGAKIVSA-----WGMTEnGAVTLTKLDDPDE-RASTTDGCPLPGVEVRVVDAD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3368 LEPVPVGVLGELYLAGQGLARGYHQRPGLTAerfvaspfVAGERMYRTGDLARYRADGVIEYAGRiDHQVKLRG-LRIEL 3446
Cdd:PRK13295 384 GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3447 GEIEARLLEHPWVREAAVLAVDGRQL----VGYVVLE-SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK13295 455 VEIEALLYRHPAIAQVAIVAYPDERLgeraCAFVVPRpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQ 534
|
570
....*....|...
gi 2310915810 3522 RKALpRPQAAAGQ 3534
Cdd:PRK13295 535 KFRL-REMLRGED 546
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3071-3525 |
9.51e-40 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 156.45 E-value: 9.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3071 RRANRLAHALIERG-VGADRLVGVAMERSiEMVVALMAILKAGGA----YVPVDPEYPEERQAYMLEDSGVELLLSQ--- 3142
Cdd:cd05922 1 LGVSAAASALLEAGgVRGERVVLILPNRF-TYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADaga 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 -SHLKLPLAQ--------GVQRIDLDR-GAPWFEdyseanpdihLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWM 3212
Cdd:cd05922 80 aDRLRDALPAspdpgtvlDADGIRAARaSAPAHE----------VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3213 QQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDV 3291
Cdd:cd05922 150 AEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRlGFDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPV 3371
Cdd:cd05922 228 AKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3372 PVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 3451
Cdd:cd05922 308 PPGEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3452 RLLEHPWVREAAVLAVD---GRQLVgyVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05922 382 AARSIGLIIEAAAVGLPdplGEKLA--LFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
3055-3525 |
1.29e-39 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 155.31 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3055 PALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3134
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3135 GVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRH--SALSNRLcWM 3212
Cdd:cd05919 82 EARLVVT------------------------------------SADDIAYLLYSSGTTGPPKGVMHAHrdPLLFADA-MA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3213 QQAYGLGVGDTVL--QKTPFSFDV--SVWeffWPLMSGARLVVAApgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD 3288
Cdd:cd05919 125 REALGLTPGDRVFssAKMFFGYGLgnSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDV--ASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEaaidVTHwTCVEEGKDAVPI---GRPIANLACYI 3363
Cdd:cd05919 200 CAGspDALRSLRLCVSAGEALPRGLGER-WMEHFGGPILDGIGATE----VGH-IFLSNRPGAWRLgstGRPVPGYEIRL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd05919 274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESE---SGDWREALAAHLAASLPEYMVPAQWLALERMPLSP 3516
Cdd:cd05919 347 VSPVEVESLIIQHPAVAEAAVVAVpestGLSRLTAFVVLKSPaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
....*....
gi 2310915810 3517 NGKLDRKAL 3525
Cdd:cd05919 427 TGKLQRFKL 435
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1999-2479 |
1.80e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 155.92 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1999 ASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGvvaeaLVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLA 2078
Cdd:PRK07787 11 AAADIADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2079 YMLRDSGArwlicQETLAERLPCPAEVERLPLETAAWPASAdtrpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAH 2158
Cdd:PRK07787 86 HILADSGA-----QAWLGPAPDDPAGLPHVPVRLHARSWHR----YPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2159 CQAAARTYGVGPGDCqLQFASISFDAAAEQLFV--PLLAGARVLlgDAGQWSAQHLADEVERHAVTILDLPPAYlQQQAE 2236
Cdd:PRK07787 157 LDALAEAWQWTADDV-LVHGLPLFHVHGLVLGVlgPLRIGNRFV--HTGRPTPEAYAQALSEGGTLYFGVPTVW-SRIAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2237 ELRHAGRRIAVRTCILGGEAWDA------SLLTQQAVqaeawFNAYGPTEAVITPLAwhcraqeggapaigRALGARRAC 2310
Cdd:PRK07787 233 DPEAARALRGARLLVSGSAALPVpvfdrlAALTGHRP-----VERYGMTETLITLST--------------RADGERRPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2311 ILDAALQ--------------PCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQV 2376
Cdd:PRK07787 294 WVGLPLAgvetrlvdedggpvPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2377 EYLGR-ADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrgEDLLAELRTWLAGRLPAY 2454
Cdd:PRK07787 367 RIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVpDDDLGQRIVAYVVGAD----DVAADELIDFVAQQLSVH 442
|
490 500
....*....|....*....|....*
gi 2310915810 2455 MQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07787 443 KRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
3052-3525 |
3.57e-39 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 155.55 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLD--YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:cd05926 1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEDSGVELLLSQ-----SHLKLPLAQGVQRIDLDRGAPWFEDYSEAN-------------PDIHLDGENLAYVIYTSGS 3191
Cdd:cd05926 81 YLADLGSKLVLTPkgelgPASRAASKLGLAILELALDVGVLIRAPSAEslsnlladkknakSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3192 TGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAApgdhR-DPAKLVALIN 3268
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLPP----RfSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3269 REGVDTLHFVPSMLQAFLQDEDVASCT---SLKRIVCSGEALPAD---AQQQVFAklpqAGLYNLYGPTEAAIDVTHWTC 3342
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNRPEPNPESpppKLRFIRSCSASLPPAvleALEATFG----APVLEAYGMTEAAHQMTSNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAVPIGRPIANLACyILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYR 3422
Cdd:cd05926 312 PPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3423 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLP 3498
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPdekyGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*..
gi 2310915810 3499 EYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
3060-3525 |
3.80e-39 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 155.87 E-value: 3.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQSHLkLPLAQGVQ----------------RIDLDRGAPW--FEDYSEANPDIH----LDgENLAYVI-YTSGSTGKPK 3196
Cdd:cd12119 102 FVDRDF-LPLLEAIAprlptvehvvvmtddaAMPEPAGVGVlaYEELLAAESPEYdwpdFD-ENTAAAIcYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3197 GAGNRHSAL---SNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVaaPGDHRDPAKLVALINREGV 3272
Cdd:cd12119 180 GVVYSHRSLvlhAMAAL-LTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIEREGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3273 DTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSGEALPadaqQQVFAKLPQAGL--YNLYGPTE-------AAIDVTHWT 3341
Cdd:cd12119 256 TFAAGVPTVWQGLLDHLEANGRDlsSLRRVVIGGSAVP----RSLIEAFEERGVrvIHAWGMTEtsplgtvARPPSEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3342 CVEEGKDAVPI--GRPIANLACYILDGNLEPVPV--GVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGD 3417
Cdd:cd12119 332 LSEDEQLALRAkqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHL 3493
Cdd:cd12119 405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPhpkwGERPLAVVVLKEGATVTAEELLEFL 484
|
490 500 510
....*....|....*....|....*....|..
gi 2310915810 3494 AASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd12119 485 ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
68-478 |
4.89e-39 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 152.85 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 68 QSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF-PRGADDSLAQAPLQRPlEVAFEDCSGLPEAEQEARlREE 146
Cdd:cd19542 18 SPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSL-DPPIEEVETDEDSLDALT-RDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 147 AQRESLQpfdlcEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSayatgAEPGLPALPiqYADYAlw 226
Cdd:cd19542 96 LDDPTLF-----GQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN-----GQLLPPAPP--FSDYI-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 227 qrSWLEAGEQERQLEYWRGKLGERHPVLElptdhprPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNI 306
Cdd:cd19542 162 --SYLQSQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQAAWAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 307 LLQRYSGQTDLRVGVPIANRN--RAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFK 384
Cdd:cd19542 233 VLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 385 VERSlshSPLFQVMYNHQPLvADIEALDSVAGLSFGQLDWKSRtTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMA 464
Cdd:cd19542 313 LWPS---GTLFNTLVSYQNF-EASPESELSGSSVFELSAAEDP-TEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELL 387
|
410
....*....|....
gi 2310915810 465 RHWQNLLRGMLENP 478
Cdd:cd19542 388 EQFDDILEALLANP 401
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1555-1779 |
7.05e-39 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 147.11 E-value: 7.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1555 LSPMQQGMLFhsLHGTEGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRLAP 1633
Cdd:COG4908 1 LSPAQKRFLF--LEPGSNAYNIPAVLRLeGPLDVEALERALRELVRRHPALRTRFVEEDG--EPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1634 PGS--DPQRQAEAEREA------GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAAT 1705
Cdd:COG4908 77 LSAlpEPEREAELEELVaeeasrPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1706 V------GRYRDYIGW----LQGRDAMATEFFWRDRLASLEMPTRL--ARQARTEQPGQGEHLR-ELDPQTTRQLASFAQ 1772
Cdd:COG4908 157 PplpelpIQYADYAAWqrawLQSEALEKQLEYWRQQLAGAPPVLELptDRPRPAVQTFRGATLSfTLPAELTEALKALAK 236
|
....*..
gi 2310915810 1773 GQKVTLN 1779
Cdd:COG4908 237 AHGATVN 243
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
525-998 |
1.04e-38 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 154.01 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLD--YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:cd05926 1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLE------------------NHAENNPGIELNGENLAYVIYTSGS 664
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELALDvgvlirapsaeslsnllaDKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 665 TGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAApgdhR-DPAKLVELIN 741
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLPP----RfSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 742 REGVDTLHFVPSMLQAFLQDEDVASCT---SLKRIVCSGEALPAD---AQQQVFAklpqAGLYNLYGPTEAAIDVTHWTC 815
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNRPEPNPESpppKLRFIRSCSASLPPAvleALEATFG----APVLEAYGMTEAAHQMTSNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 816 VEEGKDTVPIGRPIGNLGCyILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYR 895
Cdd:cd05926 312 PPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 896 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLP 971
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPdekyGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*..
gi 2310915810 972 EYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
2584-3005 |
1.92e-38 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 150.92 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLpsVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQAR--QTILANMPLRIV 2661
Cdd:cd19542 2 YPCTPMQEGMLLSQLRSPGLYFNHF--VFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTflQVVLKSLDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2662 LEDCAGASEATLRQRVAEEIrqpfDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYaaarRGEQP 2741
Cdd:cd19542 80 EVETDEDSLDALTRDLLDDP----TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY----NGQLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPlklQYADYAAWHRawldSGEGARQLDYWRERLGAEQPVLElpadrvrPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:cd19542 152 PPAP---PFSDYISYLQ----SQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCAS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2822 EGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN--RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQ 2899
Cdd:cd19542 218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2900 AHQDLPFEQLVDALqpeRNLSHSPLFQVMYNHQ-SGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYA 2978
Cdd:cd19542 298 PHQHLSLREIQRAL---GLWPSGTLFNTLVSYQnFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYS 374
|
410 420
....*....|....*....|....*..
gi 2310915810 2979 TDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19542 375 TSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
486-998 |
2.25e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 154.44 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 486 PMLDAEERGQllegwnATAAEYPLQRGVHRLFEEQVERTPTAPALA------FGEERLDYAELNRRANRLAHALIERGIG 559
Cdd:PRK13295 5 AVLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 560 ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLK--------------LPLAQG 625
Cdd:PRK13295 79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpeLPALRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 626 VQRIDLDQADAW----LENHAENNPGI-------ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:PRK13295 159 VVVVGGDGADSFeallITPAWEQEPDApailarlRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 695 DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVD-TLHFVPsmlqaFLQD------EDVAS 766
Cdd:PRK13295 239 DVILMASPMAHQTGfMYGLMMPVMLGATAVLQ---DIWDPARAAELIRTEGVTfTMASTP-----FLTDltravkESGRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 767 CTSLKRIVCSGEALPA----DAQQQVFAKLPQAglynlYGPTE-AAIDVTHWTCVEEGKDTVPiGRPIGNLGCYILDGNL 841
Cdd:PRK13295 311 VSSLRTFLCAGAPIPGalveRARAALGAKIVSA-----WGMTEnGAVTLTKLDDPDERASTTD-GCPLPGVEVRVVDADG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 842 EPVPVGVLGELYLAGRGLARGYHQRPGLTAerfvaspfVAGERMYRTGDLARYRADGVIEYAGRiDHQVKLRG-LRIELG 920
Cdd:PRK13295 385 APLPAGQIGRLQVRGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 921 EIEARLLEHPWVREAAVLAVDGRQL----VGYVVLE-SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:PRK13295 456 EIEALLYRHPAIAQVAIVAYPDERLgeraCAFVVPRpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQK 535
|
...
gi 2310915810 996 KAL 998
Cdd:PRK13295 536 FRL 538
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1991-2479 |
2.57e-38 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 153.76 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAgyLPLdp 2070
Cdd:COG1021 28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 N-YPAER---LAYMLRDSGARWLICQ------------ETLAERLPCPAEV-------ERLPLetAAWPASADTRPLPEV 2127
Cdd:COG1021 104 FaLPAHRraeISHFAEQSEAVAYIIPdrhrgfdyralaRELQAEVPSLRHVlvvgdagEFTSL--DALLAAPADLSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2128 AGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASiSFDAAAEQLFVPLLAGARVLLGDA 2204
Cdd:COG1021 182 DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTvylAALPAAH-NFPLSSPGVLGVLYAGGTVVLAPD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GqwSAQHLADEVERHAVTILDL-PPAYLQ--QQAEELRHAGRriAVRTCILGGeawdASLLTQQAVQAEAwfnaygptea 2281
Cdd:COG1021 261 P--SPDTAFPLIERERVTVTALvPPLALLwlDAAERSRYDLS--SLRVLQVGG----AKLSPELARRVRP---------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 vitplAWHCRAQ------EG-------GAPA------IGRALGA----RracILDAALQPCAPGMIGELYIGGQCLARGY 2338
Cdd:COG1021 323 -----ALGCTLQqvfgmaEGlvnytrlDDPEevilttQGRPISPddevR---IVDEDGNPVPPGEVGELLTRGPYTIRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2339 LGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIkIR-GFRIEIGEIESQLLAHPYVAEAAVVAL- 2416
Cdd:COG1021 395 YRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMp 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2417 DGVGGPLLAAYLVgrdaMRGEDL-LAELRTWLAGR-LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:COG1021 467 DEYLGERSCAFVV----PRGEPLtLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
4517-5035 |
2.73e-38 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 154.15 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4517 AELSAIGAiWNRSDSGYPatplVHQRV-----AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVA 4591
Cdd:PRK06155 1 GEPLGAGL-AARAVDPLP----PSERTlpamlARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4592 IAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCL------------S 4658
Cdd:PRK06155 76 LMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeAADPGDLPLpavwlldapasvS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4659 VDREEEWAGFPAHD---PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGS 4735
Cdd:PRK06155 156 VPAGWSTAPLPPLDapaPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4736 HEGWMHPLINGARVLIrdDSLWLPERTYAEMHRHGVTV----GVFPPVYLQQLAEHAERDGnppPVRVYCFGGDAVAQAS 4811
Cdd:PRK06155 236 LNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVtyllGAMVSILLSQPARESDRAH---RVRVALGPGVPAALHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 ydlAWRALKPKYLFNGYGPTET--VVTPLLWKARAGdacgaaYMpiGTLlgnRSGY---ILDGQLNLLPVGVAGELYLGG 4886
Cdd:PRK06155 311 ---AFRERFGVDLLDGYGSTETnfVIAVTHGSQRPG------SM--GRL---APGFearVVDEHDQELPDGEPGELLLRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4887 E---GVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PRK06155 377 DepfAFATGYFGMPEKTVE--------AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4964 REAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAE-CRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK06155 449 AAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRhCEP--------RLAYFAVPRYVEFVAALPKTENGKV 513
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
3066-3478 |
4.61e-38 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 154.27 E-value: 4.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 -----KLPLAQGVQR------------IDLDR-GAP---------WFEDYSEANPDIH----LDGENLAYVIYTSGSTGK 3194
Cdd:cd17634 167 vragrSVPLKKNVDDalnpnvtsvehvIVLKRtGSDidwqegrdlWWRDLIAKASPEHqpeaMNAEDPLFILYTSGTTGK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVV--AAPgDHRDPAKLVALINRE 3270
Cdd:cd17634 247 PKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVP-NWPTPARMWQVVDKH 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAG--LYNLYGPTEaaidvTHWTCVE 3344
Cdd:cd17634 326 GVNILYTAPTAIRALMAAGDDAiegtDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTE-----TGGFMIT 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3345 EGKDAVPIG-----RPIANLACYILDGNLEPVPVGVLGELYLAGQ--GLARGYHQRPgltaERFVASPFVAGERMYRTGD 3417
Cdd:cd17634 401 PLPGAIELKagsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGD 476
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL 3478
Cdd:cd17634 477 GARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgiphAIKGQAPYAYVVL 541
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
4547-5035 |
6.83e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 152.39 E-value: 6.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLERLP--------IPEGLSCLSVDRE--EEWAGF-------PAHDPEVALHGDNLAYVIYTS 4689
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAEaalallpvDTLILSLVLGGREapGGWLDFadwaeagSVAEPDVELADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFafdgSHEGWMHPLIN-----GARVLIRD--DslwlPERT 4762
Cdd:PRK08316 181 GTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL----YHCAQLDVFLGpylyvGATNVILDapD----PELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 YAEMHRHGVTVGVFPPVYLQQLAEHAERDgnpppvrvycfggdavaqaSYDLawRALKPKY------------------- 4823
Cdd:PRK08316 253 LRTIEAERITSFFAPPTVWISLLRHPDFD-------------------TRDL--SSLRKGYygasimpvevlkelrerlp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4824 ---LFNGYGPTE-----TVVTPLLWKARAGdACGAAYMPIGTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLE 4895
Cdd:PRK08316 312 glrFYNCYGQTEiaplaTVLGPEEHLRRPG-SAGRPVLNVET-------RVVDDDGNDVAPGEVGEIVHRSPQLMLGYWD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4896 RPALTAERFVPDPFgapgsrlyRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP 4972
Cdd:PRK08316 384 DPEKTAEAFRGGWF--------HSGDLGVMDEEGyitVVD---RKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4973 GAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK08316 453 DPKwIEAVTAVVVPKAGATVTEDELIAHC--------RARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
4530-5040 |
9.25e-38 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 150.94 E-value: 9.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4530 DSGYPATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLK 4609
Cdd:cd05920 8 AAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4610 AGGAYVPLDIEYPRERLLYMMQDSRAhlllthshllerlpipeglSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTS 4689
Cdd:cd05920 88 LGAVPVLALPSHRRSELSAFCAHAEA-------------------VAYIVPDRHAGFDHRALARELAESIPEVALFLLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA--FDGSHEGWMHPLINGARVLIRDDSLwlPERTYAEMH 4767
Cdd:cd05920 149 GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDPS--PDAAFPLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4768 RHGVTV-GVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTpllwKARAGD 4846
Cdd:cd05920 227 REGVTVtALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT-LQQVFGMAEGLLN----YTRLDD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4847 AcgaaympiGTLLGNRSGY---------ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:cd05920 302 P--------DEVIIHTQGRpmspddeirVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------Y 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVAdspea 4996
Cdd:cd05920 367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERSCAFVVLRDPPPS----- 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2310915810 4997 qaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05920 442 ----AAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4571-5040 |
1.02e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 150.28 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4571 RANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA----YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLE 4646
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4647 RLPIpeGLSCLSVD----REEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05922 82 RLRD--ALPASPDPgtvlDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLwLPERTYAEMHRHGVT--VGVfPPVYlQQLAEHAERDGNPPPVRVY 4800
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV-LDDAFWEDLREHGATglAGV-PSTY-AMLTRLGFDPAKLPSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGDAVAQASYDlAWRALKPKY-LFNGYGPTE-TVVTPLLWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGV 4878
Cdd:cd05922 237 TQAGGRLPQETIA-RLRELLPGAqVYVMYGQTEaTRRMTYLPPERILEKPGS----IGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4879 AGELYLGGEGVARGYLERPAltaerFVPDPfGAPGSRLYrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLR 4958
Cdd:cd05922 312 PGEIVHRGPNVMKGYWNDPP-----YRRKE-GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAAR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4959 EHPAVREAVVVAQPGAVGQQLVGYVVAqepavadspEAQAECRAQLKtALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:cd05922 385 SIGLIIEAAAVGLPDPLGEKLALFVTA---------PDKIDPKDVLR-SLAERLPPYKVPATVRVVDELPLTASGKVDYA 454
|
..
gi 2310915810 5039 GL 5040
Cdd:cd05922 455 AL 456
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
514-998 |
1.10e-37 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 151.84 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVgVAMERSIEMVVALMAILKAGGayVPVD 592
Cdd:COG1021 28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQLPNVAEFVIVFFALFRAGA--IPVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PeYPEERQA---YMLEDSG-VQLLLSQSHLK---LPLAQGVQR--------IDLDQADAW-----LENHAENNPGIELNG 652
Cdd:COG1021 105 A-LPAHRRAeisHFAEQSEaVAYIIPDRHRGfdyRALARELQAevpslrhvLVVGDAGEFtsldaLLAAPADLSEPRPDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 653 ENLAYVIYTSGSTGKPKGAGNRH------SALSNRLCwmqqayGLGVGDTVLQKTP--FSFDVSVWEFFWPLMSGARLVV 724
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHddylysVRASAEIC------GLDADTVYLAALPaaHNFPLSSPGVLGVLYAGGTVVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 725 AAPGdhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqAGLYNLYG 802
Cdd:COG1021 258 APDP---SPDTAFPLIERERVTVTALVPPLALLWLDaaERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-CTLQQVFG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 803 PTEAAIDVTHwtcVEEGKDTV--PIGRPIgnlgCY-----ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFV 875
Cdd:COG1021 334 MAEGLVNYTR---LDDPEEVIltTQGRPI----SPddevrIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 876 ASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL----VGYVVL 951
Cdd:COG1021 407 PDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgersCAFVVP 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2310915810 952 ESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:COG1021 481 RGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
4547-5048 |
1.33e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 152.50 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLE---------------------------RLPIPEGLSCLSVdREEEWAGF---------PA 4670
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLAPvveqvraetslrhvivtsladvlpaepTLPLPDSLRAPRL-AAAGAIDLlpalractaPV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLI-----AHIVATgeryEMTPEDCELHFMS-FAFDGSHEGWMHPLI 4744
Cdd:PRK06178 202 PLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMVytaaaAYAVAV----VGGEDSVFLSFLPeFWIAGENFGLLFPLF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4745 NGARV--LIRddslWLPERTYAEMHRHGVTVGVFPPVYLQQLAEH---AERD-GNPPPVRVYCFggdaVAQASYDL--AW 4816
Cdd:PRK06178 276 SGATLvlLAR----WDAVAFMAAVERYRVTRTVMLVDNAVELMDHprfAEYDlSSLRQVRVVSF----VKKLNPDYrqRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKYLFNG-YGPTETVVTPLLWKARAGDACGAAYMPI-------GTLLgnrsgYILDGQLN-LLPVGVAGELYLGGE 4887
Cdd:PRK06178 348 RALTGSVLAEAaWGMTETHTCDTFTAGFQDDDFDLLSQPVfvglpvpGTEF-----KICDFETGeLLPLGAEGEIVVRTP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4888 GVARGYLERPALTAERFVpDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PRK06178 423 SLLKGYWNKPEATAEALR-DGW-------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSA 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4968 VVAQPGA-VGQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPShLLFLARMPLTPNGKLdRKGLPQPDAS 5046
Cdd:PRK06178 495 VVGRPDPdKGQVPVAFVQLKPGADLTAAALQAWC--------RENMAVYKVPE-IRIVDALPMTATGKV-RKQDLQALAE 564
|
..
gi 2310915810 5047 LL 5048
Cdd:PRK06178 565 EL 566
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
4563-5040 |
1.90e-37 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 148.78 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSrahlllths 4642
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 hllerlpipeGLSCLSVDREEewagfpahdpevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05935 73 ----------GAKVAVVGSEL----------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFMSF----AFDGShegWMHPLINGARVLIRddSLWLPERTYAEMHRHGVTVGV-FPPVYLQQLAEHAERDGNPPPV 4797
Cdd:cd05935 127 VILACLPLfhvtGFVGS---LNTAVYVGGTYVLM--ARWDRETALELIEKYKVTFWTnIPTMLVDLLATPEFKTRDLSSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4798 RVYCFGGDAVAQAsydLAWRALKPKYLF--NGYGPTETVV-TPLLWKARAGDACgaaympIGTLLGNRSGYILDGQ-LNL 4873
Cdd:cd05935 202 KVLTGGGAPMPPA---VAEKLLKLTGLRfvEGYGLTETMSqTHTNPPLRPKLQC------LGIP*FGVDARVIDIEtGRE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4874 LPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEI 4953
Cdd:cd05935 273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4954 EARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadsPEAQAECRAQ-LKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:cd05935 349 EAKLYKHPAI*EVCVISVPDErVGEEVKAFIVLR-------PEYRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 2310915810 5032 NGKLDRKGL 5040
Cdd:cd05935 422 SGKILWRLL 430
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
3054-3477 |
1.99e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 149.75 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAhaliERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3133
Cdd:PRK07787 16 ADAVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3134 SGVELLLSQSHlklPLAQGVQRIDLDRGAPWFEDYSEANPDihldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQ 3213
Cdd:PRK07787 91 SGAQAWLGPAP---DDPAGLPHVPVRLHARSWHRYPEPDPD------APALIVYTSGTTGPPKGVVLSRRAIAADLDALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3214 QAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLV-VAAPgdhrDPAKLVALINREGvdTLHF-VPSMLQAFLQDE 3289
Cdd:PRK07787 162 EAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQALSEGG--TLYFgVPTVWSRIAADP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLKRIVCSGEA-LPAdaqqQVFAKLpqAGLYNL-----YGPTEAAIDVThwTCVEEGKDAVPIGRPIANLACYI 3363
Cdd:PRK07787 235 EAARALRGARLLVSGSAaLPV----PVFDRL--AALTGHrpverYGMTETLITLS--TRADGERRPGWVGLPLAGVETRL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGV--LGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGR--IDhQVKL 3439
Cdd:PRK07787 307 VDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIKS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV 3477
Cdd:PRK07787 380 GGYRIGAGEIETALLGHPGVREAAVVGVPdddlGQRIVAYVV 421
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
3055-3525 |
2.59e-37 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 150.21 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3055 PALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3134
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3135 GVELLLSQSHLKLPLAQGVQRIDLD-------------RGAPWFEDY----SEANPDIHLDGENLAYVIYTSGSTGKPKG 3197
Cdd:cd05959 101 RARVVVVSGELAPVLAAALTKSEHTlvvlivsggagpeAGALLLAELvaaeAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3198 AGNRHSALSnrlcWMQQAYGLGV-----GDTVLQ--KTPFSFDVSVWEFFwPLMSGARLVVAApgDHRDPAKLVALINRE 3270
Cdd:cd05959 181 VVHLHADIY----WTAELYARNVlgireDDVCFSaaKLFFAYGLGNSLTF-PLSVGATTVLMP--ERPTPAAVFKRIRRY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVDTLHFVPSMLQAFLQDEDvASCTSLKRI---VCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAidvtHWTCVEEGK 3347
Cdd:cd05959 254 RPTVFFGVPTLYAAMLAAPN-LPSRDLSSLrlcVSAGEALPAEVGER-WKARFGLDILDGIGSTEML----HIFLSNRPG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3348 DAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvaGErMYRTGDLARYRADG 3425
Cdd:cd05959 328 RVRYgtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR-QLVGYVVLESESGDW---REALAAHLAASLP 3498
Cdd:cd05959 401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVedeDGLtKPKAFVVLRPGYEDSealEEELKEFVKDRLA 480
|
490 500
....*....|....*....|....*..
gi 2310915810 3499 EYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05959 481 PYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
533-998 |
2.86e-37 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 150.47 E-value: 2.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 613 LSQSHLkLPLAQGVQ-RIDLDQA---------------------DAWLENHA--ENNPGIElngENLAYVI-YTSGSTGK 667
Cdd:cd12119 102 FVDRDF-LPLLEAIApRLPTVEHvvvmtddaampepagvgvlayEELLAAESpeYDWPDFD---ENTAAAIcYTSGTTGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 668 PKGAGNRHSAL---SNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVaaPGDHRDPAKLVELINRE 743
Cdd:cd12119 178 PKGVVYSHRSLvlhAMAAL-LTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 744 GVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSGEALPadaqQQVFAKLPQAGL--YNLYGPTE-------AAIDVTH 812
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGRDlsSLRRVVIGGSAVP----RSLIEAFEERGVrvIHAWGMTEtsplgtvARPPSEH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 813 WTCVEEGKDTVPI--GRPIGNLGCYILDGNLEPVPV--GVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRT 888
Cdd:cd12119 330 SNLSEDEQLALRAkqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 889 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAA 964
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPhpkwGERPLAVVVLKEGATVTAEELLE 482
|
490 500 510
....*....|....*....|....*....|....
gi 2310915810 965 HLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd12119 483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3062-3525 |
3.13e-37 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 148.35 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS 3141
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 qshlklplaqgvqridldrgapwfedyseanpdihlDGEN-LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05971 85 ------------------------------------DGSDdPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTPFS-------FDVSV--WEFFWPLMSgarlvvaapgdHR----DPAKLVALINREGVDTLHFVPSMLQAFLQ 3287
Cdd:cd05971 129 RDGDLYWTPADwawigglLDVLLpsLYFGVPVLA-----------HRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3288 DEDVASCT--SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAvPIGRPIANLACYILD 3365
Cdd:cd05971 198 QGEQLKHAqvKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3366 GNLEPVPVGVLGELYL----AGQGLarGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd05971 276 DNGTPLPPGEVGEIAVelpdPVAFL--GYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3442 LRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL-ESESGD---WREALAAHLAASLPeYMVPAQWLALERMP 3513
Cdd:cd05971 347 YRIGPAEIEECLLKHPAVLMAAVVgipdPIRGEIVKAFVVLnPGETPSdalAREIQELVKTRLAA-HEYPREIEFVNELP 425
|
490
....*....|..
gi 2310915810 3514 LSPNGKLDRKAL 3525
Cdd:cd05971 426 RTATGKIRRREL 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
3048-3525 |
3.21e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 150.52 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALieRGVGADRLVGVAMERS--IEMVVALMAILKAGGAYVPVDPEYPEE 3125
Cdd:PRK06188 22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAF--EALGLGTGDAVALLSLnrPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3126 RQAYMLEDSGVELLL------------------SQSHLkLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDgenLAYVIY 3187
Cdd:PRK06188 100 DHAYVLEDAGISTLIvdpapfveralallarvpSLKHV-LTLGPVPDGVDLLAAAAKFGPAPLVAAALPPD---IAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweFFWP-LMSGARLVVAapgDHRDPAKLVAL 3266
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVL---AKFDPAEVLRA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3267 INREGVDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEAL-PADAQQ------QVFAKLpqaglynlYGPTEAAIDV 3337
Cdd:PRK06188 251 IEEQRITATFLVPTMIYALLDHPDLrtRDLSSLETVYYGASPMsPVRLAEaierfgPIFAQY--------YGQTEAPMVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPI----GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMy 3413
Cdd:PRK06188 323 TYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDGWL- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3414 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESG-DWREA 3488
Cdd:PRK06188 396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPdekwGEAVTAVVVLRPGAAvDAAEL 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 2310915810 3489 LAAHLAASLPEYmVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06188 476 QAHVKERKGSVH-APKQVDFVDSLPLTALGKPDKKAL 511
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
4089-4504 |
3.69e-37 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 147.95 E-value: 3.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqqplqiVYRQRQLPFAE 4167
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGaLDVDALRAALADVVARHESLRTVFPEDDG-------GPYQVVLPAAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4168 E--DLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AG 4241
Cdd:cd19540 76 ArpDLTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4242 RSPE-QPRDGRYSDYIAWlQRQ----------DAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATA 4310
Cdd:cd19540 156 RAPDwAPLPVQYADYALW-QREllgdeddpdsLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRG-GTVEFTIDAEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4311 TARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQ 4390
Cdd:cd19540 234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGD--EALDDLVGMFVNTLVLRTDVSGDPTFAELLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4391 GLQRQNLA------------------LREQEHTPLFELqrwagfggeavfdnLLVFENYPVDEV-LERSSAGGVRFGAva 4451
Cdd:cd19540 312 RVRETDLAafahqdvpferlvealnpPRSTARHPLFQV--------------MLAFQNTAAATLeLPGLTVEPVPVDT-- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4452 mhEQTNYPLALAL-------GGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19540 376 --GVAKFDLSFTLterrdadGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
536-998 |
4.49e-37 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 147.63 E-value: 4.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQ 615
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 616 SHLklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05935 81 SEL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 696 TVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhRDPAKlvELINREGVDTLHFVPSMLQAFLQD-EDVASCTSLKR 772
Cdd:cd05935 127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWD-RETAL--ELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSSLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 773 IVCSGEALPADAQQQVFAKLpqAGLYNL--YGPTEAaIDVTHWTCVEEGKDTVpIGRPIGNLGCYILD-GNLEPVPVGVL 849
Cdd:cd05935 203 VLTGGGAPMPPAVAEKLLKL--TGLRFVegYGLTET-MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 850 GELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 930 PWVREAAVLAVD----GRQLVGYVVLESE--GGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05935 356 PAI*EVCVISVPdervGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
3041-3532 |
5.69e-37 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 149.91 E-value: 5.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVgVAMERSIEMVVALMAILKAGGayVPVD 3119
Cdd:COG1021 28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQLPNVAEFVIVFFALFRAGA--IPVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PeYPEERQA---YMLEDSG-VELLLSQSHLK---LPLAQGVQR-----------------IDLD--RGAPwfEDYSEANP 3173
Cdd:COG1021 105 A-LPAHRRAeisHFAEQSEaVAYIIPDRHRGfdyRALARELQAevpslrhvlvvgdagefTSLDalLAAP--ADLSEPRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3174 DIhldgENLAYVIYTSGSTGKPKGAGNRH------SALSNRLCwmqqayGLGVGDTVLQKTP--FSFDVSVWEFFWPLMS 3245
Cdd:COG1021 182 DP----DDVAFFQLSGGTTGLPKLIPRTHddylysVRASAEIC------GLDADTVYLAALPaaHNFPLSSPGVLGVLYA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVVAAPGDhrdPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQ----------- 3312
Cdd:COG1021 252 GGTVVLAPDPS---PDTAFPLIERERVTVTALVPPLALLWLDaaERSRYDLSSLRVLQVGGAKLSPELArrvrpalgctl 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3313 QQVF--AKlpqaGLYNlYGPTEAAIDVTHWTCveegkdavpiGRPIanlaCY-----ILDGNLEPVPVGVLGELYLAGQG 3385
Cdd:COG1021 329 QQVFgmAE----GLVN-YTRLDDPEEVILTTQ----------GRPI----SPddevrIVDEDGNPVPPGEVGELLTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3386 LARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:COG1021 390 TIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVV 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3466 AVDGRQL----VGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALpRPQAAA 3532
Cdd:COG1021 464 AMPDEYLgersCAFVVPRGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL-RAALAA 533
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
528-998 |
5.78e-37 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 147.61 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 528 PALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 607
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 608 GVQLLLSqshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRH--SALSNRLcWM 685
Cdd:cd05919 82 EARLVVT------------------------------------SADDIAYLLYSSGTTGPPKGVMHAHrdPLLFADA-MA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 686 QQAYGLGVGDTVL--QKTPFSFDV--SVWeffWPLMSGARLVVAApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD 761
Cdd:cd05919 125 REALGLTPGDRVFssAKMFFGYGLgnSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 762 EDV--ASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEaaidVTHwTCVEEGKDTVPI---GRPIGNLGCYI 836
Cdd:cd05919 200 CAGspDALRSLRLCVSAGEALPRGLGER-WMEHFGGPILDGIGATE----VGH-IFLSNRPGAWRLgstGRPVPGYEIRL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd05919 274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 917 IELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESE---GGDWREALAAHLAASLPEYMVPAQWLALERMPLSP 989
Cdd:cd05919 347 VSPVEVESLIIQHPAVAEAAVVAVpestGLSRLTAFVVLKSPaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
....*....
gi 2310915810 990 NGKLDRKAL 998
Cdd:cd05919 427 TGKLQRFKL 435
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
539-951 |
7.92e-37 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 150.42 E-value: 7.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS-- 616
Cdd:cd17634 87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADgg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 617 -----------------HLKLPLAQGVQRIDLDQAD------AWLENH---AENNPGIE---LNGENLAYVIYTSGSTGK 667
Cdd:cd17634 167 vragrsvplkknvddalNPNVTSVEHVIVLKRTGSDidwqegRDLWWRdliAKASPEHQpeaMNAEDPLFILYTSGTTGK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 668 PKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVV--AAPgDHRDPAKLVELINRE 743
Cdd:cd17634 247 PKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVP-NWPTPARMWQVVDKH 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 744 GVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAG--LYNLYGPTEaaidvTHWTCVE 817
Cdd:cd17634 326 GVNILYTAPTAIRALMAAGDDAiegtDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTE-----TGGFMIT 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 818 --EGKDTVPIG---RPIGNLGCYILDGNLEPVPVGVLGELYLAGR--GLARGYHQRPgltaERFVASPFVAGERMYRTGD 890
Cdd:cd17634 401 plPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGD 476
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL 951
Cdd:cd17634 477 GARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgiphAIKGQAPYAYVVL 541
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
535-998 |
8.59e-37 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 147.19 E-value: 8.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLS 614
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 615 qshlklplaqgvqridlDQADawlenhaennpgielngeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:cd05971 85 -----------------DGSD------------------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 695 DTVLQKTPFS-------FDVSV--WEFFWPLMSgarlvvaapgdHR----DPAKLVELINREGVDTLHFVPSMLQAFLQD 761
Cdd:cd05971 130 DGDLYWTPADwawigglLDVLLpsLYFGVPVLA-----------HRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 762 EDVASCT--SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDTvPIGRPIGNLGCYILDG 839
Cdd:cd05971 199 GEQLKHAqvKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 840 NLEPVPVGVLGELylagrGLAR-------GYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd05971 277 NGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 913 RGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL-ESEGGD---WREALAAHLAASLPeYMVPAQWLALER 984
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVgipdPIRGEIVKAFVVLnPGETPSdalAREIQELVKTRLAA-HEYPREIEFVNE 423
|
490
....*....|....
gi 2310915810 985 MPLSPNGKLDRKAL 998
Cdd:cd05971 424 LPRTATGKIRRREL 437
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
4540-5040 |
1.04e-36 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 149.14 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGayVPL-- 4617
Cdd:COG1021 28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVfa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 -------DIEY------------PRERLLYmmqDSRAHLLLTHshllERLPIPEglSCLSVDREEEWAGF------PAHD 4672
Cdd:COG1021 106 lpahrraEISHfaeqseavayiiPDRHRGF---DYRALARELQ----AEVPSLR--HVLVVGDAGEFTSLdallaaPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA--FDGSHEGWMHPLINGAR-V 4749
Cdd:COG1021 177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTvV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4750 LIRDDSlwlPERTYAEMHRHGVTV-GVFPPVYLQQLAEHAERDGNPPPVRVYCFGGdavAQASYDLAwRALKPKY---LF 4825
Cdd:COG1021 257 LAPDPS---PDTAFPLIERERVTVtALVPPLALLWLDAAERSRYDLSSLRVLQVGG---AKLSPELA-RRVRPALgctLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYG-------------PTETVVTpllwkaragdACGaayMPIgtllgnrSGY----ILDGQLNLLPVGVAGELYLGGEG 4888
Cdd:COG1021 330 QVFGmaeglvnytrlddPEEVILT----------TQG---RPI-------SPDdevrIVDEDGNPVPPGEVGELLTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4889 VARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVkIR-GFRIELGEIEARLREHPAVREAV 4967
Cdd:COG1021 390 TIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4968 VVAQPGAV-GQQLVGYVVAQEPAVAdspeaqaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:COG1021 462 VVAMPDEYlGERSCAFVVPRGEPLT---------LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1971-2497 |
1.09e-36 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 149.14 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1971 RQEALRDWQAPLEALPRGG--VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERS 2048
Cdd:PRK06155 2 EPLGAGLAARAVDPLPPSErtLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2049 FDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLE---------TAAWPASA 2119
Cdd:PRK06155 82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALE-AADPGDLPLPavwlldapaSVSVPAGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2120 DTRPLPEVA----------GETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQL 2189
Cdd:PRK06155 161 STAPLPPLDapapaaavqpGDTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2190 FVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQA 2266
Cdd:PRK06155 240 FQALLAGATYVLEP--RFSASGFWPAVRRHGATVTYLLGAMvsiLLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2267 VQAeawFNAYGPTEAVItPLAWHCRAQEGGapAIGRALGARRACILDAALQPCAPGMIGELYIGGQ---CLARGYLGRPG 2343
Cdd:PRK06155 318 VDL---LDGYGSTETNF-VIAVTHGSQRPG--SMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2344 QTAERFvadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDG-VGGP 2422
Cdd:PRK06155 392 KTVEAW--------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSeLGED 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2423 LLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAA----RRQAG-EPPREG 2497
Cdd:PRK06155 464 EVMAAVVLRDGTALE--PVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTAdtwdREAAGvQLPRSG 541
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1981-2479 |
1.15e-36 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 148.88 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRggVAAAFAHQVASAPEAIALVCGDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK05852 11 ASDFGPR--IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGAR-------------------WLICQETLAERLPCPAEVErLPLETAAWPASA 2119
Cdd:PRK05852 89 SRADLVVVPLDPALPIAEQRVRSQAAGARvvlidadgphdraepttrwWPLTVNVGGDSGPSGGTLS-VHLDAATEPTPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2120 DTrpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLA 2195
Cdd:PRK05852 168 TS--TPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAvmplYHGHGLIAA---LLATLAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ---QQAEELRHAGRRIA---VRTCilggeawdASLLTQQAVQA 2269
Cdd:PRK05852 243 GGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQillERAATEPSGRKPAAlrfIRSC--------SAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2270 -EAWFN-----AYGPTEAV----ITPLAWHCRAQEGGAPA--IGRALGARRAcILDAALQPCAPGMIGELYIGGQCLARG 2337
Cdd:PRK05852 315 lQTEFAapvvcAFGMTEAThqvtTTQIEGIGQTENPVVSTglVGRSTGAQIR-IVGSDGLPLPAGAVGEVWLRGTTVVRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2338 YLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL- 2416
Cdd:PRK05852 394 YLGDPTITAANFT--------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVp 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2417 DGVGGPLLAAYLVGRDAMR--GEDLLAELRTwlagRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK05852 466 DQLYGEAVAAVIVPRESAPptAEELVQFCRE----RLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1998-2479 |
1.68e-36 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 147.47 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:cd05920 25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 AYMLRDSGARWLICQETLAERLPCPAEVERLpletaawpasadtRPLPEVAgetlaYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05920 105 SAFCAHAEAVAYIVPDRHAGFDHRALARELA-------------ESIPEVA-----LFLLSGGTTGTPKLIPRTHNDYAY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2158 HCQAAARTYGVGPGDCQLQF--ASISFDAAAEQLFVPLLAGARVLLGDAGqwSAQHLADEVERHAVTILDLPPAYLQQQA 2235
Cdd:cd05920 167 NVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDP--SPDAAFPLIEREGVTVTALVPALVSLWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2236 EELRHAGRRI-AVRTCILGGEAWDASLltqqAVQAEAWFNA-----YGPTEAVITplawHCRAQEGGAPAI---GRALGA 2306
Cdd:cd05920 245 DAAASRRADLsSLRLLQVGGARLSPAL----ARRVPPVLGCtlqqvFGMAEGLLN----YTRLDDPDEVIIhtqGRPMSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 R-RACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:cd05920 317 DdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRIKDQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedlLAELRTWLAGR-LPAYMQPTAWQVL 2463
Cdd:cd05920 390 INRGGEKIAAEEVENLLLRHPAVHDAAVVAMpDELLGERSCAFVVLRDPPPS---AAQLRRFLRERgLAAYKLPDRIEFV 466
|
490
....*....|....*.
gi 2310915810 2464 SSLPLNANGKLDRKAL 2479
Cdd:cd05920 467 DSLPLTAVGKIDKKAL 482
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
528-998 |
1.80e-36 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 147.90 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 528 PALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 607
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 608 GVQLLLSQS------------------HLKLPLAQGVQRIDLDQADAWLEnHAENNPGIELNGENLAYVIYTSGSTGKPK 669
Cdd:cd05959 101 RARVVVVSGelapvlaaaltksehtlvVLIVSGGAGPEAGALLLAELVAA-EAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 670 GAGNRHSALSnrlcWMQQAYGLGV-----GDTVLQ--KTPFSFDVSVWEFFwPLMSGARLVVAApgDHRDPAKLVELINR 742
Cdd:cd05959 180 GVVHLHADIY----WTAELYARNVlgireDDVCFSaaKLFFAYGLGNSLTF-PLSVGATTVLMP--ERPTPAAVFKRIRR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 743 EGVDTLHFVPSMLQAFLQDEDvASCTSLKRI---VCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAidvtHWTCVEEG 819
Cdd:cd05959 253 YRPTVFFGVPTLYAAMLAAPN-LPSRDLSSLrlcVSAGEALPAEVGER-WKARFGLDILDGIGSTEML----HIFLSNRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 820 KDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvaGErMYRTGDLARYRAD 897
Cdd:cd05959 327 GRVRYgtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 898 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR-QLVGYVVLESEGGDW---REALAAHLAASL 970
Cdd:cd05959 400 GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVedeDGLtKPKAFVVLRPGYEDSealEEELKEFVKDRL 479
|
490 500
....*....|....*....|....*...
gi 2310915810 971 PEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05959 480 APYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
4547-5035 |
2.12e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 148.28 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVI------FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK13295 34 VASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YpRER-LLYMMQDSRAHL------------LLTHSHLLERLPIPEGLSCLSVDREEEWAGF---PAHDPEVALHG----- 4679
Cdd:PRK13295 114 F-REReLSFMLKHAESKVlvvpktfrgfdhAAMARRLRPELPALRHVVVVGGDGADSFEALlitPAWEQEPDAPAilarl 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 ----DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------HFMSFAFdgsheGWMHPLINGARV 4749
Cdd:PRK13295 193 rpgpDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILmaspmaHQTGFMY-----GLMMPVMLGATA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4750 LIRDdsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGY 4828
Cdd:PRK13295 268 VLQD--IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPvSSLRTFLCAGAPIPGALVERARAALGAK-IVSAW 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GPTE----TVVTP--LLWKARAGDACGAAYMPIgtllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAE 4902
Cdd:PRK13295 345 GMTEngavTLTKLddPDERASTTDGCPLPGVEV---------RVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4903 rfvpdpfGAPGsrLYRSGDLTRGRADGVVDYLGRvDHQVKIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLV 4980
Cdd:PRK13295 416 -------DADG--WFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQVAIVAYPDErLGERAC 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4981 GYVVAQEPAVADSPEAQAECRAQlKTALrerlpEYMvPSHLLFLARMPLTPNGKL 5035
Cdd:PRK13295 486 AFVVPRPGQSLDFEEMVEFLKAQ-KVAK-----QYI-PERLVVRDALPRTPSGKI 533
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1991-2479 |
3.61e-36 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 146.50 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:cd05923 6 MLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLICQEtlaERLPCPA------EVERLPLE------TAAWPASADTRPLPEVAgetlAYVIYT 2138
Cdd:cd05923 86 RLKAAELAELIERGEMTAAVIAV---DAQVMDAifqsgvRVLALSDLvglgepESAGPLIEDPPREPEQP----AFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2139 SGSTGQPKGVAVSQ------AALVAHcQAAAR------TYGVGPgdcqlQFASISFDAaaeqLFVPLLA--GARVLLGDa 2204
Cdd:cd05923 159 SGTTGLPKGAVIPQraaesrVLFMST-QAGLRhgrhnvVLGLMP-----LYHVIGFFA----VLVAALAldGTYVVVEE- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 gqWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLL--TQQAVQAEAwFNAYGPTEA 2281
Cdd:cd05923 228 --FDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLerVNQHLPGEK-VNIYGTTEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VITPLAWHCRAQEGGAPaiGRALGARRACILDAALQPCAPGMIGELYI--GGQCLARGYLGRPGQTAERFVadpfsgsgE 2359
Cdd:cd05923 305 MNSLYMRDARTGTEMRP--GFFSEVRIVRIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ--------D 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2360 RLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGED 2438
Cdd:cd05923 375 GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVaDERWGQSVTACVVPREGTLSAD 454
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2310915810 2439 LLAELrtWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05923 455 ELDQF--CRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
2583-3004 |
7.23e-36 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 143.09 E-value: 7.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19537 1 DTALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCagaseatlrqRVAEEIRQPFDLARgpllrvrllalagqEHV---------LVITQHHIVSDGWSMQVMVDELLQAYA 2733
Cdd:cd19537 81 DTL----------DVWKEINRPFDLER--------------EDPirvfispdtLLVVMSHIICDLTTLQLLLREVSAAYN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2734 aarrgeQPTLAPLKLQYADYAAWHRAWLDSgegarQLDYWRERLgAEQPVLELPAdrvRPAQASGRGQRLDMALPVPLSE 2813
Cdd:cd19537 137 ------GKLLPPVRREYLDSTAWSRPASPE-----DLDFWSEYL-SGLPLLNLPR---RTSSKSYRGTSRVFQLPGSLYR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2814 ELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVD--AGLAFRDLLGRV 2891
Cdd:cd19537 202 SLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPssSDASAADFLRAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2892 REAALGAQAHQdLPFEQLVDALQPERNLSHSPLFQVM--YNHQSGERQDAQVDGLHIEsFAW-DGaaAQFDL-----ALD 2963
Cdd:cd19537 282 RRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEPL-YTWaEG--AKFPLmfeftALS 357
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2310915810 2964 twetPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLEN 3004
Cdd:cd19537 358 ----DDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
3030-3525 |
9.52e-36 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 145.16 E-value: 9.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3030 TAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMAI 3108
Cdd:cd05920 7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRpGDRVV-VQLPNVAEFVVLFFAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLsqshlklplaqGVQRIDLDRGAPWFEDYSEANPDIhldgenlAYVIYT 3188
Cdd:cd05920 86 LRLGAVPVLALPSHRRSELSAFCAHAEAVAYI-----------VPDRHAGFDHRALARELAESIPEV-------ALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3189 SGSTGKPKGAGNRHSAL------SNRLCWMQQayglgvgDTVL---QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrd 3259
Cdd:cd05920 148 GGTTGTPKLIPRTHNDYaynvraSAEVCGLDQ-------DTVYlavLPAAHNFPLACPGVLGTLLAGGRVVLAPDPS--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV 3337
Cdd:cd05920 218 PDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPiGRPIANL-ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTG 3416
Cdd:cd05920 297 TRLDDPDEVIIHTQ-GRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAH 3492
Cdd:cd05920 370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdellGERSCAFVVLRDPPPSAAQLRRFL 449
|
490 500 510
....*....|....*....|....*....|...
gi 2310915810 3493 LAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05920 450 RERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
527-950 |
1.04e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 144.75 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 527 APALAFGEERLDYAELNRRANRLAhaliERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 606
Cdd:PRK07787 16 ADAVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 607 SGVQLLLSQSHlklPLAQGVQRIDLD-QADAWlENHAENNPgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWM 685
Cdd:PRK07787 91 SGAQAWLGPAP---DDPAGLPHVPVRlHARSW-HRYPEPDP------DAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 686 QQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLV-VAAPgdhrDPAKLVELINREGvdTLHF-VPSMLQAFLQD 761
Cdd:PRK07787 161 AEAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQALSEGG--TLYFgVPTVWSRIAAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 762 EDVASCTSLKRIVCSGEA-LPAdaqqQVFAKLpqAGLYNL-----YGPTEAAIDVTHWTCVEEGKDTVpiGRPIGNLGCY 835
Cdd:PRK07787 234 PEAARALRGARLLVSGSAaLPV----PVFDRL--AALTGHrpverYGMTETLITLSTRADGERRPGWV--GLPLAGVETR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 836 ILDGNLEPVPVGV--LGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGR--IDhQVK 911
Cdd:PRK07787 306 LVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIK 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2310915810 912 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV 950
Cdd:PRK07787 379 SGGYRIGAGEIETALLGHPGVREAAVVGVPdddlGQRIVAYVV 421
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
3063-3525 |
1.96e-35 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 143.00 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHLklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 3222
Cdd:cd05935 81 SEL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3223 TVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhRDPAKlvALINREGVDTLHFVPSMLQAFLQD-EDVASCTSLKR 3299
Cdd:cd05935 127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWD-RETAL--ELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSSLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3300 IVCSGEALPADAQQQVFAKLpqAGLYNL--YGPTEAaIDVTHWTCVEEGKDAVpIGRPIANLACYILD-GNLEPVPVGVL 3376
Cdd:cd05935 203 VLTGGGAPMPPAVAEKLLKL--TGLRFVegYGLTET-MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3377 GELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 3456
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3457 PWVREAAVLAVD----GRQLVGYVVLESEsgdWR-----EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05935 356 PAI*EVCVISVPdervGEEVKAFIVLRPE---YRgkvteEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
3047-3465 |
2.62e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 144.92 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVER----TPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVGVAMERSiEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK07786 22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKlPLAQGVQRID------------LDRGAPWFED-YSEANPD---IHLDGENLAYV 3185
Cdd:PRK07786 101 LTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVpllstvvvaggsSDDSVLGYEDlLAEAGPAhapVDIPNDSPALI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrDPAKLV 3264
Cdd:PRK07786 180 MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAF-DPGQLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 ALINREGVDTLHFVPSMLQAFLQDEDVAScTSLKRIVCSGEALPADAQ--QQVFAKLPQAGLYNLYGPTEaaidVTHWTC 3342
Cdd:PRK07786 259 DVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTllRQMAATFPEAQILAAFGQTE----MSPVTC 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAV----PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDL 3418
Cdd:PRK07786 334 MLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGDL 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2310915810 3419 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:PRK07786 407 VRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI 453
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
84-478 |
2.83e-35 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 142.24 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 84 LDRQALERAFASLVQRHETLRTVFprgADDS----LAQAPLQRpLEVafEDCSGLPEAEQEARLREEAQRESLQPFDLCE 159
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVF---LDDGtqqiLPEVPWYG-ITV--HDLRGLSEEEAEAALEELRERLSHRVLDVER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 160 GPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYsayaTGAEPGLPALPIQYADYALWQRSwLEAGEQERQ 239
Cdd:cd19535 111 GPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALY----EDPGEPLPPLELSFRDYLLAEQA-LRETAYERA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 240 LEYWRGKLGE-----RHPVLELPTDHPRPVVpsyrgSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQ 314
Cdd:cd19535 186 RAYWQERLPTlppapQLPLAKDPEEIKEPRF-----TRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 315 TDLRVGVPIANRNR--AEVEGLIGLFvntqvlrsvfdgrTSVatLLaglkdtvLGAQAHQDLPFERLVEAF--KVERSLS 390
Cdd:cd19535 261 PRFLLNLTLFNRLPlhPDVNDVVGDF-------------TSL--LL-------LEVDGSEGQSFLERARRLqqQLWEDLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 391 HSPLFQV--------MYNHQPLVA--------DIEALDSVAGLSFGQLDWK-SRTTQFDLSLDTYEKGGRLYAALTYATD 453
Cdd:cd19535 319 HSSYSGVvvvrrllrRRGGQPVLApvvftsnlGLPLLDEEVREVLGELVYMiSQTPQVWLDHQVYEEDGGLLLNWDAVDE 398
|
410 420
....*....|....*....|....*
gi 2310915810 454 LFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19535 399 LFPEGMLDDMFDAYVRLLERLADDD 423
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4541-5128 |
5.75e-35 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 149.55 E-value: 5.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEK------LTYAELDSRANRLAHALIARGvGPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:PRK05691 13 QALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPldiEYP--------RERLLYMMQDSRAHLLLTHSHLLERLpipEGLSCLSVDREEEWAGFPAHDPEVA-------LHG 4679
Cdd:PRK05691 92 VP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDTLDPALAeawqepaLQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAH--IVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVLIRDDSL 4756
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGIDLNPDDVIVSWLPLYHDmGLIGGLLQPIFSGVPCVLMSPAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 WL--PERTYAEMHRHGVTVGVFPPVYLQ----QLAEHAERDGNPPPVRVYCFGGDAVAQASYDL-----AWRALKPKYLF 4825
Cdd:PRK05691 246 FLerPLRWLEAISEYGGTISGGPDFAYRlcseRVSESALERLDLSRWRVAYSGSEPIRQDSLERfaekfAACGFDPDSFF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYGPTETV-----------VTPL------LWKARAGDACGAAYMPIGTLLGNRSGYILDGQ-LNLLPVGVAGELYLGGE 4887
Cdd:PRK05691 326 ASYGLAEATlfvsggrrgqgIPALeldaeaLARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4888 GVARGYLERPALTAERFVPdpfgAPGSRLYRSGDLTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA 4966
Cdd:PRK05691 406 SIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVRKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4967 VVVAQpgAV---GQQLVGYVVAQEPAVADSPEAQAecraqLKTALRERLPE--YMVPSHLLFL--ARMPLTPNGKLDRKG 5039
Cdd:PRK05691 481 RVAAF--AVnhqGEEGIGIAAEISRSVQKILPPQA-----LIKSIRQAVAEacQEAPSVVLLLnpGALPKTSSGKLQRSA 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5040 --LPQPDASL------------LQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGV 5105
Cdd:PRK05691 554 crLRLADGSLdsyalfpalqavEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGI 633
|
650 660
....*....|....*....|...
gi 2310915810 5106 ELPLAALFQTESLQAYAELAAAQ 5128
Cdd:PRK05691 634 DLNLRQLFEAPTLAAFSAAVARQ 656
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
521-1001 |
7.13e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 143.20 E-value: 7.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:PRK06188 22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 601 AYMLEDSGVQLLL------------------SQSHLkLPLAQGVQRIDL-DQADAW----LENHAEnnpgielnGENLAY 657
Cdd:PRK06188 102 AYVLEDAGISTLIvdpapfveralallarvpSLKHV-LTLGPVPDGVDLlAAAAKFgpapLVAAAL--------PPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweFFWP-LMSGARLVVAapgDHRDPAKL 736
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVL---AKFDPAEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 737 VELINREGVDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEAL-PADAQQ------QVFAKLpqaglynlYGPTEAA 807
Cdd:PRK06188 248 LRAIEEQRITATFLVPTMIYALLDHPDLrtRDLSSLETVYYGASPMsPVRLAEaierfgPIFAQY--------YGQTEAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 808 IDVTHWTCVEEGKDTVPI----GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGE 883
Cdd:PRK06188 320 MVITYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 884 RMyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGG-DW 958
Cdd:PRK06188 394 WL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPdekwGEAVTAVVVLRPGAAvDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 959 REALAAHLAASLPEYmVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:PRK06188 473 AELQAHVKERKGSVH-APKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
2010-2479 |
1.01e-34 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 142.77 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL 2089
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETL-------AERLP-----------CPAEVERLPLETA--AWPASADTR-PLPEVAGETLAYVIYTSGSTGQPKGV 2148
Cdd:cd12119 102 FVDRDFlplleaiAPRLPtvehvvvmtddAAMPEPAGVGVLAyeELLAAESPEyDWPDFDENTAAAICYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2149 AVSQAALVAHCQAAART--YGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGAR-VLLGDAGQwsAQHLADEVERHAVTIL 2224
Cdd:cd12119 182 VYSHRSLVLHAMAALLTdgLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKlVLPGPYLD--PASLAELIEREGVTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLltqqavqAEAW-------FNAYGPTE-----AVITPLAWHCR 2291
Cdd:cd12119 259 AGVPTVWQGLLDHLEANGRDLsSLRRVVIGGSAVPRSL-------IEAFeergvrvIHAWGMTEtsplgTVARPPSEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEGGAPAI----GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvADPFsgsgerlYRTG 2365
Cdd:cd12119 332 LSEDEQLALrakqGRPVPGVELRIVDDDgrELPWDGKAVGELQVRGPWVTKSYYKNDEESEALT-EDGW-------LRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGG--PLlaAYLVGRDamrGEDLLA- 2441
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVpHPKWGerPL--AVVVLKE---GATVTAe 478
|
490 500 510
....*....|....*....|....*....|....*...
gi 2310915810 2442 ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
2004-2479 |
1.01e-34 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 141.08 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2004 AIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLR 2082
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGnRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2083 DsgarwliCQETLAerlpcpaeverlpLETAAWPASADTrplpevagetlAYVIYTSGSTGQPKGVAVSQAALVAHCQAA 2162
Cdd:cd05958 81 K-------ARITVA-------------LCAHALTASDDI-----------CILAFTSGTTGAPKATMHFHRDPLASADRY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2163 AR-TYGVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd05958 130 AVnVLRLREDDRFVGSPPLAFTfGLGGVLLFPFGVGASGVLLE--EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRIA-VRTCILGGEAWDASLltqqavqAEAWFNAYG--------PTEAV---ITPLAWHCRAQEGGAPAIGRalgarR 2308
Cdd:cd05958 208 AGPDLSsLRKCVSAGEALPAAL-------HRAWKEATGipiidgigSTEMFhifISARPGDARPGATGKPVPGY-----E 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARgYLGRPGQtaerfvADPFSGsgERLYrTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd05958 276 AKVVDDEGNPVPDGTIGRLAVRGPTGCR-YLADKRQ------RTYVQG--GWNI-TGDTYSRDPDGYFRHQGRSDDMIVS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGR-DAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSL 2466
Cdd:cd05958 346 GGYNIAPPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVVLRpGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTEL 425
|
490
....*....|...
gi 2310915810 2467 PLNANGKLDRKAL 2479
Cdd:cd05958 426 PRTATGKLQRFAL 438
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
503-998 |
1.48e-34 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 141.31 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 503 TAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVAMERSIEMVVALMAI 581
Cdd:cd05920 7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRpGDRVV-VQLPNVAEFVVLFFAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 582 LKAGGayVPVDPeYPEERQAymlEDSGvqlLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPgielngenlAYVIYT 661
Cdd:cd05920 86 LRLGA--VPVLA-LPSHRRS---ELSA---FCAHAEAVAYIVPDRHAGFDHRALARELAESIPEV---------ALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 662 SGSTGKPKGAGNRHSAL------SNRLCWMQQayglgvgDTVL---QKTPFSFDVSVWEFFWPLMSGARLVVAAPGdhrD 732
Cdd:cd05920 148 GGTTGTPKLIPRTHNDYaynvraSAEVCGLDQ-------DTVYlavLPAAHNFPLACPGVLGTLLAGGRVVLAPDP---S 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 733 PAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV 810
Cdd:cd05920 218 PDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 811 THWTCVEEGKDTVPiGRPIGNLG-CYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTG 889
Cdd:cd05920 297 TRLDDPDEVIIHTQ-GRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAH 965
Cdd:cd05920 370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdellGERSCAFVVLRDPPPSAAQLRRFL 449
|
490 500 510
....*....|....*....|....*....|...
gi 2310915810 966 LAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05920 450 RERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
4119-4504 |
2.56e-34 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 139.76 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4119 SGLDIPRFRAAWQSALDRHAILRSGFawQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERErgFELQRAP 4198
Cdd:cd20484 34 SKLDVEKFKQACQFVLEQHPILKSVI--EEEDGVPFQKIEPSKPLSFQEEDISSLKESEIIAYLREKAKEP--FVLENGP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4199 LLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA----GRSPE-QPRDGRYSDYIAWLQR----QDAAATEA 4269
Cdd:cd20484 110 LMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqGKQPTlASSPASYYDFVAWEQDmlagAEGEEHRA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4270 FWREQMAA----LDEPTRLVEALAQpgltSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHT 4345
Cdd:cd20484 190 YWKQQLSGtlpiLELPADRPRSSAP----SFEG-QTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4346 VVFGATVSGRPADlpGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQR-----------------QNLAL-REQEHTPL 4407
Cdd:cd20484 265 IIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLtvldgldhaaypfpamvRDLNIpRSQANSPV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4408 FE-------------LQRWAgfggeAVFDNLLVFENypVDEVlerssaggvrfgavamHEQTNYPLALAL-GGGDSLSLQ 4473
Cdd:cd20484 343 FQvaffyqnflqstsLQQFL-----AEYQDVLSIEF--VEGI----------------HQEGEYELVLEVyEQEDRFTLN 399
|
410 420 430
....*....|....*....|....*....|.
gi 2310915810 4474 FSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd20484 400 IKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1554-1956 |
3.18e-34 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 139.44 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLFhsLHGTEG-------DYVNQLRmdiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPqPLQVVF--EQ 1624
Cdd:cd19539 3 PLSFAQERLWF--IDQGEDggpayniPGAWRLT---GPLDVEALREALRDVVARHEALRTLLVRDDGGV-PRQEILppGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1625 ATLELR-LAPPGSDPQRQAEA---EREA-GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG 1699
Cdd:cd19539 77 APLEVRdLSDPDSDRERRLEEllrERESrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1700 --QEVAATV----GRYRDYIGWLQ---GRDAMATEF-FWRDRLASLE---MPTRLARQARTEQPGqGEHLRELDPQTTRQ 1766
Cdd:cd19539 157 rrKGPAAPLpelrQQYKEYAAWQRealAAPRAAELLdFWRRRLRGAEptaLPTDRPRPAGFPYPG-ADLRFELDAELVAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1767 LASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQ 1846
Cdd:cd19539 236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1847 ALNLALREHEHTPLYDIQRWAG----HGGEALFDSILVFENFPVAE----ALRQAPADLEFSTpsnheQTNYPLTLGVTL 1918
Cdd:cd19539 314 KALVDAQRHQELPFQQLVAELPvdrdAGRHPLVQIVFQVTNAPAGElelaGGLSYTEGSDIPD-----GAKFDLNLTVTE 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2310915810 1919 ---GERLSLQYVYARrdFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19539 389 egtGLRGSLGYATSL--FDEETIQGFLADYLQVLRQLLANP 427
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2002-2474 |
3.27e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 141.64 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGL-RARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETLAER---------------------LPCPAEV-------ERLPLETAAWPA--------SADTRPL 2124
Cdd:PRK08314 104 VTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdyLPAEPEIavpawlrAEPPLQALAPGGvvawkealAAGLAPP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 PEVAG-ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQ--LFVPLLAGARVLL 2201
Cdd:PRK08314 184 PHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTGMVhsMNAPIYAGATVVL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 gdAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGG-----EAWDASLLTQQAVQaeaWFNAY 2276
Cdd:PRK08314 263 --MPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGgaampEAVAERLKELTGLD---YVEGY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2277 GPTEAV----ITPLAwHCRAQEGGAPAIGraLGARracILDAA-LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVa 2351
Cdd:PRK08314 338 GLTETMaqthSNPPD-RPKLQCLGIPTFG--VDAR---VIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVG 2430
Cdd:PRK08314 411 ---EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATpDPRRGETVKAVVVL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2310915810 2431 RDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK08314 488 RPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1990-2414 |
4.45e-34 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 142.16 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGD----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGY 2065
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2066 LPLDPNYPAERLAYMLRDSGARWLIC--QETLAERLPCPAEVERLPL-------------------------ETAAWPAS 2118
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVedQEQLDKLLEVRDELPSLRHivvldprglrddprllsldellalgREVADPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2119 ADTRpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQF-------------------AS 2179
Cdd:COG1022 173 LEAR-RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplahvfertvsyyalaagAT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2180 ISFDAAAEQL-------------FVP-----LLAGARVLLGDAG-------QWsAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:COG1022 252 VAFAESPDTLaedlrevkptfmlAVPrvwekVYAGIQAKAEEAGglkrklfRW-ALAVGRRYARARLAGKSPSLLLRLKH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 A-------EELRHA-GRRIavRTCILGGEAWDASLLTqqavqaeaWFNA--------YGPTE--AVITplawhcrAQEGG 2296
Cdd:COG1022 331 AladklvfSKLREAlGGRL--RFAVSGGAALGPELAR--------FFRAlgipvlegYGLTEtsPVIT-------VNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APAI---GRALgarracildaalqpcaPGM---I---GELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDL 2367
Cdd:COG1022 394 DNRIgtvGPPL----------------PGVevkIaedGEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDI 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2310915810 2368 ARYRVDGQVEYLGRADQQIKIR-GFRIEIGEIESQLLAHPYVAEAAVV 2414
Cdd:COG1022 451 GELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
52-478 |
8.79e-34 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 137.58 E-value: 8.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFprgaDDSLAQAPLQ-----RPLEV 126
Cdd:cd19536 4 LSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSF----IEDGLGQPVQvvhrqAQVPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 127 AFEDCSGLpeAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLL-LTLHHIVSDGWSMNVLIEEFSRFY--- 202
Cdd:cd19536 80 TELDLTPL--EEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYnql 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 203 SAYATGAEPglPALPiqYADYALWQRSwleAGEQERQLEYWRGKLGErhpvLELPTDHP-RPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19536 158 LEYKPLSLP--PAQP--YRDFVAHERA---SIQQAASERYWREYLAG----ATLATLPAlSEAVGGGPEQDSELLVSVPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNR--AEVEGLIGLFVNTQVLRSVFDGRTsVATLLA 359
Cdd:cd19536 227 PVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTLSEET-VEDLLK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 360 GLKDTVLGAQAHQDLPferLVEAFKVERSLshsPLFQVMYN--HQPLVADIEALDSVAGLSFGQLDWKSRTTqFDLSLDT 437
Cdd:cd19536 306 RAQEQELESLSHEQVP---LADIQRCSEGE---PLFDSIVNfrHFDLDFGLPEWGSDEGMRRGLLFSEFKSN-YDVNLSV 378
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2310915810 438 YEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19536 379 LPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
4545-5037 |
9.32e-34 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 140.45 E-value: 9.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4545 ERARMAPDAVAVIF------DEEKLTYAELDSRANRLAHALIARGvGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPR---ERLLYMMQDSRAH-------LLLTHSHLLERLPIPEGLSCLSVDREEewAGFPAHDPEVALHGDNLAYVIYT 4688
Cdd:cd05931 80 PPTPGrhaERLAAILADAGPRvvlttaaALAAVRAFAASRPAAGTPRLLVVDLLP--DTSAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVL-------IRDDSLWLpe 4760
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGPSVlmspaafLRRPLRWL-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4761 rtyAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPP--------------PVRVycfggDAVAQ-----ASYDLAWRALKP 4821
Cdd:cd05931 236 ---RLISRYRATISAAPNFAYDLCVRRVRDEDLEGldlsswrvalngaePVRP-----ATLRRfaeafAPFGFRPEAFRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4822 KY------LFNGYGPTETVVTpLLWKARAGDACGAAYMPIGTLLGNR---SGYILDGQ---------LNLLPVGVAGELY 4883
Cdd:cd05931 308 SYglaeatLFVSGGPPGTGPV-VLRVDRDALAGRAVAVAADDPAARElvsCGRPLPDQevrivdpetGRELPDGEVGEIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4884 LGGEGVARGYLERPALTAERFVPDPfGAPGSRLYRSGDLtrG-RADGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HP 4961
Cdd:cd05931 387 VRGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDL--GfLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4962 AVREAVVVA--QPGAVGQQLVgyVVAQEPAVADSPEAqaecrAQLKTALRERLP-EYMVPSHLLFLAR---MPLTPNGKL 5035
Cdd:cd05931 464 ALRPGCVAAfsVPDDGEERLV--VVAEVERGADPADL-----AAIAAAIRAAVArEHGVAPADVVLVRpgsIPRTSSGKI 536
|
..
gi 2310915810 5036 DR 5037
Cdd:cd05931 537 QR 538
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
520-1013 |
1.38e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 139.91 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 520 QVER----TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAMERSiEMVVALMAILKAGGAYVPVDPE 594
Cdd:PRK07786 22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 595 YPEERQAYMLEDSGVQLLLSQSHLKlPLAQGVQRID-----------------LDQADAWLENHAENNPgIELNGENLAY 657
Cdd:PRK07786 101 LTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVpllstvvvaggssddsvLGYEDLLAEAGPAHAP-VDIPNDSPAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrDPAKL 736
Cdd:PRK07786 179 IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAF-DPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 737 VELINREGVDTLHFVPSMLQAFLQDEDVAScTSLKRIVCSGEALPADAQ--QQVFAKLPQAGLYNLYGPTEaaidVTHWT 814
Cdd:PRK07786 258 LDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTllRQMAATFPEAQILAAFGQTE----MSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 815 CVEEGKDTV----PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGD 890
Cdd:PRK07786 333 CMLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWR-EALAAH 965
Cdd:PRK07786 406 LVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAdekwGEVPVAVAAVRNDDAALTlEDLAEF 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 966 LAASLPEYMVPAQWLALERMPLSPNGKLD----RKALPAPEVSVAQAGYSAP 1013
Cdd:PRK07786 486 LTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGF 537
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
3066-3525 |
1.76e-33 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 137.25 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 KlplaqgvqridlDRGAPwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRlcWMQQAYGLG-VGDTV 3224
Cdd:cd05969 83 Y------------ERTDP----------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKYVLDlHPDDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3225 LQKT--PFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVAS--CTSLK 3298
Cdd:cd05969 133 YWCTadPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKegDELARKydLSSLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDVTHWTCVeegkDAVP--IGRPIANLACYILDGNLEPVP 3372
Cdd:cd05969 211 FIHSVGEPLNPEAirwGMEVF-GVP---IHDTWWQTEtGSIMIANYPCM----PIKPgsMGKPLPGVKAAVVDENGNELP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3373 VGVLGELYLAGQ--GLARGYHQRPgltaERFVASpFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd05969 283 PGTKGILALKPGwpSMFRGIWNDE----ERYKNS-FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3451 ARLLEHPWVREAAVLAVD----GRQLVGYVVLES--ESGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRK 3523
Cdd:cd05969 356 SALMEHPAVAEAGVIGKPdplrGEIIKAFISLKEgfEPSDeLKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435
|
..
gi 2310915810 3524 AL 3525
Cdd:cd05969 436 VL 437
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
4534-5030 |
1.85e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 139.49 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:PRK06164 7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 YVPLDIEYPRERLLYMMQDSRAH-------------LLLTHSHLLERLPIPEGLSCLSVDREE--------EWAGFPAHD 4672
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAADAtpapapgaRVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 P-------EVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLIN 4745
Cdd:PRK06164 167 PappaaagERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4746 GARVLIRDdsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGgdAVAQASYDLAWRALKPKYLF 4825
Cdd:PRK06164 247 GAPLVCEP--VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFA--SFAPALGELAALARARGVPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NG-YGPTETVVTPLLWkaRAGDACGAAYMPIGTLLGN----RSGYILDGQLnlLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:PRK06164 323 TGlYGSSEVQALVALQ--PATDPVSVRIEGGGRPASPearvRARDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLV 4980
Cdd:PRK06164 399 ARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4981 GYVVAQEPAVADSPEaqaecraqLKTALRERLPEYMVPSHLLFLARMPLT 5030
Cdd:PRK06164 472 AFVIPTDGASPDEAG--------LMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
516-995 |
2.38e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 139.14 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:PRK12583 23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 EYPEERQAYMLEDSGVQ-----------------------LLLSQ----SHLKLPLAQGVQRIDLDQADAWLENHAENNP 646
Cdd:PRK12583 103 AYRASELEYALGQSGVRwvicadafktsdyhamlqellpgLAEGQpgalACERLPELRGVVSLAPAPPPGFLAWHELQAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 647 GIELNGENLAY------------VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvWEFFW 714
Cdd:PRK12583 183 GETVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL------YHCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 715 PLMS-------GARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQ 785
Cdd:PRK12583 257 MVLAnlgcmtvGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNfdLSSLRTGIMAGAPCPIEVM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 786 QQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEG--KDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGY 863
Cdd:PRK12583 335 RRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDleRRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 864 HQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD-- 941
Cdd:PRK12583 414 WNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPde 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 942 --GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:PRK12583 488 kyGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
3039-3527 |
2.65e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 138.07 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3039 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:PRK06839 3 GIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRgAPWFEDYSE---ANPDIHLD-GENLAYVI-YTSGST 3192
Cdd:PRK06839 83 LNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQR-VISITSLKEiedRKIDNFVEkNESASFIIcYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3193 GKPKGA-----GNRHSALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAapgDHRDPAKLVAL 3266
Cdd:PRK06839 162 GKPKGAvltqeNMFWNALNNTF-----AIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVP---RKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3267 INREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGlyNLYGPTEAAIDVTHWTCVE 3344
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFEttNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3345 EGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRAD 3424
Cdd:PRK06839 312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3425 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEY 3500
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY 464
|
490 500
....*....|....*....|....*..
gi 2310915810 3501 MVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PRK06839 465 KIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
3038-3525 |
2.97e-33 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 137.64 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAF--GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAY 3115
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3116 VPVDPEYPEERQAYMLEDSGVELLLSQshlklPLAQGVQ----------RIDLDRGAPWFEDYSEANPDIHLDGENLAYV 3185
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIA-----VDAQVMDaifqsgvrvlALSDLVGLGEPESAGPLIEDPPREPEQPAFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL--GVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKL 3263
Cdd:cd05923 156 FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPqaGLY-NLYGPTEA-----AI 3335
Cdd:cd05923 234 LKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLP--GEKvNIYGTTEAmnslyMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTCVEEG-KDAVPIGRpianlacyILDGNLEPVPVGVLGELYLAGQGLA--RGYHQRPGLTAERFVaspfvagERM 3412
Cdd:cd05923 312 DARTGTEMRPGfFSEVRIVR--------IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DGW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREA 3488
Cdd:cd05923 377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVTACVVPREGTLSADEL 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 2310915810 3489 LAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05923 457 DQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
539-1003 |
3.87e-33 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 136.48 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 KlplaqgvQRIDLdqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRlcWMQQAYGLG-VGDTV 697
Cdd:cd05969 83 Y-------ERTDP---------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKYVLDlHPDDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 698 LQKT--PFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVAS--CTSLK 771
Cdd:cd05969 133 YWCTadPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKegDELARKydLSSLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 772 RIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDVTHWTCVeegkDTVP--IGRPIGNLGCYILDGNLEPVP 845
Cdd:cd05969 211 FIHSVGEPLNPEAirwGMEVF-GVP---IHDTWWQTEtGSIMIANYPCM----PIKPgsMGKPLPGVKAAVVDENGNELP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 846 VGVLGELYLAGR--GLARGYHQRPgltaERFVASpFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:cd05969 283 PGTKGILALKPGwpSMFRGIWNDE----ERYKNS-FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 924 ARLLEHPWVREAAVLAVD----GRQLVGYVVLES--EGGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRK 996
Cdd:cd05969 356 SALMEHPAVAEAGVIGKPdplrGEIIKAFISLKEgfEPSDeLKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435
|
....*..
gi 2310915810 997 ALPAPEV 1003
Cdd:cd05969 436 VLKAKEL 442
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
4537-5040 |
4.34e-33 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 137.26 E-value: 4.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4537 PLVHQRVAERARMAPDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPLDieyPRERLLYMMQDSRAHLLLTHSHLLERLPIPE---------GLSCLSVDREEEWAG----FPAHDPEVAlhgdn 4681
Cdd:cd05923 81 ALIN---PRLKAAELAELIERGEMTAAVIAVDAQVMDAifqsgvrvlALSDLVGLGEPESAGplieDPPREPEQP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 lAYVIYTSGSTGMPKGVAVSHGpliahivATGERYEMTPEDCELHFmsfafdGSHE---GWMhPL--------------- 4743
Cdd:cd05923 153 -AFVFYTSGTTGLPKGAVIPQR-------AAESRVLFMSTQAGLRH------GRHNvvlGLM-PLyhvigffavlvaala 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALkPK 4822
Cdd:cd05923 218 LDGTYVVVEEFD---PADALKLIEQERVTSLFATPTHLDALAAAAEFAGlKLSSLRHVTFAGATMPDAVLERVNQHL-PG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 YLFNGYGPTETVVTPLLWKARAGDAcgaayMPIGTLLGNRSGYILDGQLNLLPVGVAGELY--LGGEGVARGYLERPALT 4900
Cdd:cd05923 294 EKVNIYGTTEAMNSLYMRDARTGTE-----MRPGFFSEVRIVRIGGSPDEALANGEEGELIvaAAADAAFTGYLNQPEAT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQL 4979
Cdd:cd05923 369 AKKLQ--------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSV 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4980 VGYVVAQEPAVADSpEAQAECRAQlktalreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05923 441 TACVVPREGTLSAD-ELDQFCRAS-------ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
4089-4504 |
4.44e-33 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 135.86 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELqqPLQIVYRQRQlpfAE 4167
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGkLDVQALQQALYDVVERHESLRTVFPEEDGV--PYQLILEEDE---AT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4168 EDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPEQ- 4246
Cdd:cd19538 78 PKLEIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4247 ----PRDGRYSDYIAWLQRQDAAATE---------AFWREQMAALDEPTRLVEALAQPGLTSANgvGEHLR-EVDATATA 4312
Cdd:cd19538 158 pelaPLPVQYADYALWQQELLGDESDpdsliarqlAYWKKQLAGLPDEIELPTDYPRPAESSYE--GGTLTfEIDSELHQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4313 RLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADlpGVENQVGLFINTLPVVVTLAPQMTLDELLQGL 4392
Cdd:cd19538 236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDTSGNPSFRELLERV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4393 QRQNLALREQEHTPlFEL-------QRWAGFggEAVFDNLLVFENYP--------VDEVLERSSAGGVRFG-AVAMHEQT 4456
Cdd:cd19538 314 KETNLEAYEHQDIP-FERlvealnpTRSRSR--HPLFQIMLALQNTPqpsldlpgLEAKLELRTVGSAKFDlTFELREQY 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2310915810 4457 NYplalalGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19538 391 ND------GTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
3631-3851 |
4.57e-33 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 135.95 E-value: 4.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRL-FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATL------GGAL 3700
Cdd:cd19531 9 QRLwFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVqviLPPLPLPLpvvdlsGLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3701 LWRAEAVDRQALEslceESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR 3780
Cdd:cd19531 89 AEREAEAQRLARE----EARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3781 LPgktsP-------FKAWAgRvsEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGAlEQRFATSVQS-RFDRSLTER 3850
Cdd:cd19531 165 LP----PlpiqyadYAVWQ-R--EWLQGEVLERQLAYWREQLAGAPPvlELPTDRPRPA-VQSFRGARVRfTLPAELTAA 236
|
.
gi 2310915810 3851 L 3851
Cdd:cd19531 237 L 237
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
4546-5037 |
4.87e-33 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 137.28 E-value: 4.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRER 4625
Cdd:TIGR02262 14 VVEGRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4626 LLYMMQDSRAHLLLTHShllERLPIPEGLSCLSVDREEEWAGFPAHDPEVAL----------------HGDNLAYVIYTS 4689
Cdd:TIGR02262 94 YAYMLEDSRARVVFVSG---ALLPVIKAALGKSPHLEHRVVVGRPEAGEVQLaellateseqfkpaatQADDPAFWLYSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIaHIVATGERYEMTPEDCELHFMS----FAFdGSHEGWMHPLINGARVLIRDDSLwLPERTYAE 4765
Cdd:TIGR02262 171 GSTGMPKGVVHTHSNPY-WTAELYARNTLGIREDDVCFSAaklfFAY-GLGNALTFPMSVGATTVLMGERP-TPDAVFDR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4766 MHRHGVTV--GVfPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAqASYDLAWRALKPKYLFNGYGPTEtvVTPLLWKAR 4843
Cdd:TIGR02262 248 LRRHQPTIfyGV-PTLYAAMLADPNLPSEDQVRLRLCTSAGEALP-AEVGQRWQARFGVDIVDGIGSTE--MLHIFLSNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4844 AGDA-CGAAYMPIG----TLLGNRSGYILDgqlnllpvGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapgSRLYR 4918
Cdd:TIGR02262 324 PGDVrYGTSGKPVPgyrlRLVGDGGQDVAD--------GEPGELLISGPSSATMYWNNRAKSRDTFQ--------GEWTR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4919 SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVaqPGAVGQQLV---GYVVAQEPAVAdspe 4995
Cdd:TIGR02262 388 SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVV--GVADEDGLIkpkAFVVLRPGQTA---- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2310915810 4996 aqaeCRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:TIGR02262 462 ----LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
4533-5035 |
6.06e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 137.78 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4533 YPATPLVHQrVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:PRK08314 7 LPETSLFHN-LEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRAN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------------------LPIPEGL------SCLS 4658
Cdd:PRK08314 86 AVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdylpaepeIAVPAWLraepplQALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4659 VDREEEW-----AGFPAhdPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAF 4732
Cdd:PRK08314 166 PGGVVAWkealaAGLAP--PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPlFHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4733 DGSHEGWMHPLINGARVLI-----RDDSLWLPERtyaemhrHGVTVGVFPPVYLQQLAehaerdgNPPPVRVYCF----- 4802
Cdd:PRK08314 244 TGMVHSMNAPIYAGATVVLmprwdREAAARLIER-------YRVTHWTNIPTMVVDFL-------ASPGLAERDLsslry 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4803 ---GGDAVAQASYDLAWRALKPKYLfNGYGPTETV----VTPllwKARAGDACgaaympIGTLLGNRSGYILDGQ-LNLL 4874
Cdd:PRK08314 310 iggGGAAMPEAVAERLKELTGLDYV-EGYGLTETMaqthSNP---PDRPKLQC------LGIPTFGVDARVIDPEtLEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4875 PVGVAGELYLGGEGVARGYLERPALTAERFVPdpfgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqVKIRGFRIELG 4951
Cdd:PRK08314 380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE----IDGKRFFRTGDLGRMDEEGyffITDRLKRM---INASGFKVWPA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4952 EIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQaecraQLKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:PRK08314 453 EVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEE-----EIIAWAREHMAAYKYPRIVEFVDSLPKSG 527
|
....
gi 2310915810 5032 NGKL 5035
Cdd:PRK08314 528 SGKI 531
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
50-398 |
6.17e-33 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 134.62 E-value: 6.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 50 DRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF---PRGADDSLAQAPLQRplev 126
Cdd:cd19537 2 TALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYvprDGGLRRSYSSSPPRV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 127 afedcsglpeaeQEAR---LREEAQReslqPFDLCEGPLLRVRLirlgeERHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
Cdd:cd19537 78 ------------QRVDtldVWKEINR----PFDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLREVSAAYN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 204 AyatgaePGLPALPIQYADYALWQRSwleagEQERQLEYWRGKLgERHPVLELPtdhPRPVVPSYRGSRYEFSIEPALAE 283
Cdd:cd19537 137 G------KLLPPVRREYLDSTAWSRP-----ASPEDLDFWSEYL-SGLPLLNLP---RRTSSKSYRGTSRVFQLPGSLYR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 284 ALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFD--GRTSVATLLAGL 361
Cdd:cd19537 202 SLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPssSDASAADFLRAV 281
|
330 340 350
....*....|....*....|....*....|....*..
gi 2310915810 362 KDTVLGAQAHQdLPFERLVEAFKVERSLSHSPLFQVM 398
Cdd:cd19537 282 RRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVM 317
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
3050-3525 |
8.42e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 137.09 E-value: 8.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07470 19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRkGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQS--------------HLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:PRK07470 98 YLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSAL----SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVWEffwpLMSGARLV--VAAPGDHRDPAKLVALIN 3268
Cdd:PRK07470 178 PKAAVLTHGQMafviTNHLADLMP--GTTEQDASLVVAPLSHGAGIHQ----LCQVARGAatVLLPSERFDPAEVWALVE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3269 REGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT----HWTC 3342
Cdd:PRK07470 252 RHRVTNLFTVPTILKMLVEHPAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTGNITvlppALHD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAV--PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLAR 3420
Cdd:PRK07470 331 AEDGPDARigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLGH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGY-VVLESESGDWREALAAH-LAAS 3496
Cdd:PRK07470 404 LDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWgeVGVaVCVARDGAPVDEAELLAwLDGK 483
|
490 500
....*....|....*....|....*....
gi 2310915810 3497 LPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK07470 484 VARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1990-2479 |
1.13e-32 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 136.21 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPeaiALVCGD--EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:cd05904 10 VSFLFASAHPSRP---ALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLICQETLAERLP--------CP-AEVERLPLETAAWPASADTRPLPEVAGETLAYVIYT 2138
Cdd:cd05904 87 ANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAslalpvvlLDsAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2139 SGSTGQPKGVAVSQAALVAHCQA--AARTYGVGPGDCQLQFA------SISFDAAAeqlfvPLLAGARVLLgdAGQWSAQ 2210
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSEDVFLCVLpmfhiyGLSSFALG-----LLRLGATVVV--MPRFDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDL-PPAYLQQQAEELRHAGRRIAVRTCILGG--------EAWDASLLTQQAVQaeawfnAYGPTEA 2281
Cdd:cd05904 240 ELLAAIERYKVTHLPVvPPIVLALVKSPIVDKYDLSSLRQIMSGAaplgkeliEAFRAKFPNVDLGQ------GYGMTES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 viTPLAWHCRAQEGGAP---AIGRALGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfvadpfSGS 2357
Cdd:cd05904 314 --TGVVAMCFAPEKDRAkygSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA-------TID 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR-DAMR 2435
Cdd:cd05904 385 KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpDEEAGEVPMAFVVRKpGSSL 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2310915810 2436 GEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05904 465 TED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
4543-5040 |
2.69e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 134.99 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 PRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLS-VDREEEWAGFPAHDPEVALH-GDNLAYVI-YTSGSTGMPKGV 4698
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEkNESASFIIcYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHP-LINGARVLIRDDslWLPERTYAEMHRHGVTVGVFP 4777
Cdd:PRK06839 168 VLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVPRK--FEPTKALSMIEKHKVTVVMGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEHAERDG-NPPPVRVYCFGGdavAQASYDLAWRALKPKYLF-NGYGPTETVVTP-LLWKARAGDACGAAYMP 4854
Cdd:PRK06839 246 PTIHQALINCSKFETtNLQSVRWFYNGG---APCPEELMREFIDRGFLFgQGFGMTETSPTVfMLSEEDARRKVGSIGKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IgtlLGNRSGYIlDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYL 4934
Cdd:PRK06839 323 V---LFCDYELI-DENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------TIQDGWLCTGDLARVDEDGFVYIV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECRAqlktalreRLP 5013
Cdd:PRK06839 391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKKSSSVLIEKDVIEHCRL--------FLA 462
|
490 500
....*....|....*....|....*..
gi 2310915810 5014 EYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
2002-2479 |
2.80e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 134.70 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERL--PCPAEVERLPLETAAWPASADTRPLPEVAGetlayVIYTSGSTGQPKGV----------A 2149
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLipGISVKFAELMNGPKEEAEIQEEFDLDEVAT-----IMYTSGTTGKPKGViqtygnhwwsA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2150 VSqaalvahcqaAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPA 2229
Cdd:PRK03640 171 VG----------SALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVE--KFDAEKINKLLQTGGVTIISVVST 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2230 YLQQQAEELRHAGRRIAVRTCILGGEAWDASLLtQQAVQAE-AWFNAYGPTEA---VITPLAWHCRAQEGGApaiGRALG 2305
Cdd:PRK03640 239 MLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLL-EQCKEKGiPVYQSYGMTETasqIVTLSPEDALTKLGSA---GKPLF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAaLQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK03640 315 PCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRSDL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVgrdamRGEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:PRK03640 386 IISGGENIYPAEIEEVLLSHPGVAEAGVVGVpDDKWGQVPVAFVV-----KSGEVtEEELRHFCEEKLAKYKVPKRFYFV 460
|
490
....*....|....*.
gi 2310915810 2464 SSLPLNANGKLDRKAL 2479
Cdd:PRK03640 461 EELPRNASGKLLRHEL 476
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
4562-5042 |
3.00e-32 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 132.86 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSrahlllth 4641
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4642 shllerlpipeglsclsvdreeewagfpahdpEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPE 4721
Cdd:cd05912 73 --------------------------------DVKL--DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4722 DCELHFMSFAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYLQQLaehAERDGNPPPVRVYC 4801
Cdd:cd05912 119 DNWLCALPLFHISGLSILMRSVIYGMTVYLVDK--FDAEQVLHLINSGKVTIISVVPTMLQRL---LEILGEGYPNNLRC 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4802 F--GGDAVAQASydLAWRALKPKYLFNGYGPTET---VVTplLWKARAGDACGAAYMPigtllgnrsgyILDGQL----N 4872
Cdd:cd05912 194 IllGGGPAPKPL--LEQCKEKGIPVYQSYGMTETcsqIVT--LSPEDALNKIGSAGKP-----------LFPVELkiedD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGE 4952
Cdd:cd05912 259 GQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAE 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4953 IEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVAdspeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:cd05912 331 IEEVLLSHPAIKEAGVVGIPDDKwGQVPVAFVVSERPISE----------EELIAYCSEKLAKYKVPKKIYFVDELPRTA 400
|
490
....*....|.
gi 2310915810 5032 NGKLDRKGLPQ 5042
Cdd:cd05912 401 SGKLLRHELKQ 411
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
539-998 |
4.07e-32 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 132.85 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQShl 618
Cdd:cd05972 3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 klplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:cd05972 81 ----------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 699 QKTPFSFDVSVW-EFFWPLMSGARLVVAApGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQdEDVAS--CTSLKRIVC 775
Cdd:cd05972 127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSykFSHLRLVVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 776 SGEALPADAQQQVFAKLpQAGLYNLYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGNLEPVPVGVLGEL- 852
Cdd:cd05972 205 AGEPLNPEVIEWWRAAT-GLPIRDGYGQTEtgLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGDIa 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 853 -YLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:cd05972 280 iKLPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 932 VREAAVLA----VDGRQLVGYVVLESEGGDW----REALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05972 353 VAEAAVVGspdpVRGEVVKAFVVLTSGYEPSeelaEELQGHVKKVLAP-YKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
3043-3522 |
4.43e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 135.29 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:PRK12583 23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGV-----------------------ELLLSQ----SHLKLPLAQGVQRIDLDRgAPWFEDYSE--A 3171
Cdd:PRK12583 103 AYRASELEYALGQSGVrwvicadafktsdyhamlqellpGLAEGQpgalACERLPELRGVVSLAPAP-PPGFLAWHElqA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 NPDI-----------HLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvWEFF 3240
Cdd:PRK12583 182 RGETvsrealaerqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL------YHCF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3241 WPLMS-------GARLVVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADA 3311
Cdd:PRK12583 256 GMVLAnlgcmtvGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNfdLSSLRTGIMAGAPCPIEV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3312 QQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEG--KDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK12583 334 MRRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDleRRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3390 YHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD- 3468
Cdd:PRK12583 413 YWNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPd 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3469 ---GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:PRK12583 487 ekyGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1553-1956 |
4.61e-32 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 132.49 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1553 YPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLEL 1629
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLaeyLEIT-GPVDLAVLERALRQVIAEAETLRLRFTEEEG--EPYQWIDPYTPVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSnAQLLaevlqryaGQEVA 1703
Cdd:cd19533 79 RHidlsgdPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFS-FALF--------GQRVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1704 ATvgryrdYIGWLQGRDAMATEF------------------------FWRDRLASLEMPTRLARQARTEQPGQGEHLREL 1759
Cdd:cd19533 150 EI------YTALLKGRPAPPAPFgsfldlveeeqayrqserferdraFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1760 DPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGR--PAELpgieAQIGLFINTLPVIAAPQPQQS 1837
Cdd:cd19533 224 PPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAAR----QTPGMVANTLPLRLTVDPQQT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1838 VADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEA--LFD---SILVFEnFPVAEALRQAPADLEFSTPSNheqtnypl 1912
Cdd:cd19533 300 FAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELhpLFGptvNYMPFD-YGLDFGGVVGLTHNLSSGPTN-------- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2310915810 1913 TLGVTLGER-----LSLQYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19533 371 DLSIFVYDRddesgLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
4526-5038 |
7.15e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 135.13 E-value: 7.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4526 WNRSDSGYPATPLVHQrVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PRK05605 22 WTPHDLDYGDTTLVDL-YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4606 AVLKAGGAYV---PLdieYPRERLLYMMQDSRA------------HLLLTHSHLLE-------------------RLPIP 4651
Cdd:PRK05605 101 AVLRLGAVVVehnPL---YTAHELEHPFEDHGArvaivwdkvaptVERLRRTTPLEtivsvnmiaampllqrlalRLPIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4652 ------EGLSCLS---------VDREEEWAGFPAHDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHiVATGERY 4716
Cdd:PRK05605 178 alrkarAALTGPApgtvpwetlVDAAIGGDGSDVSHPRPTP--DDVALILYTSGTTGKPKGAQLTHRNLFAN-AAQGKAW 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4717 -EMTPEDCELHF----MSFAFDGSHEGWMHPLINGARVLI-RDDslwlPERTYAEMHRHGVTV--GVfPPVYlQQLAEHA 4788
Cdd:PRK05605 255 vPGLGDGPERVLaalpMFHAYGLTLCLTLAVSIGGELVLLpAPD----IDLILDAMKKHPPTWlpGV-PPLY-EKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 ERDGNP-PPVRvYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETvvTPLLwkarAGDacgaaymPIGTllGNRSGYI- 4866
Cdd:PRK05605 329 EERGVDlSGVR-NAFSGAMALPVSTVELWEKLTGGLLVEGYGLTET--SPII----VGN-------PMSD--DRRPGYVg 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 ---------LDGQLNL---LPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYL 4934
Cdd:PRK05605 393 vpfpdtevrIVDPEDPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPE 5014
Cdd:PRK05605 465 DRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEG-------LRAYCREHLTR 537
|
570 580
....*....|....*....|....
gi 2310915810 5015 YMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:PRK05605 538 YKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
3066-3525 |
8.26e-32 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 132.08 E-value: 8.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSqshl 3145
Cdd:cd05972 3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 klplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:cd05972 79 --------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3226 QKTPFSFDVSVW-EFFWPLMSGARLVVAApGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQdEDVAS--CTSLKRIVC 3302
Cdd:cd05972 127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSykFSHLRLVVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3303 SGEALPADAQQQVFAKLpQAGLYNLYGPTE--AAIDVTHWTCVEEGKdavpIGRPIANLACYILDGNLEPVPVGVLGEL- 3379
Cdd:cd05972 205 AGEPLNPEVIEWWRAAT-GLPIRDGYGQTEtgLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGDIa 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3380 -YLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:cd05972 280 iKLPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3459 VREAAVLA----VDGRQLVGYVVLESESGDW----REALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05972 353 VAEAAVVGspdpVRGEVVKAFVVLTSGYEPSeelaEELQGHVKKVLAP-YKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
4547-5038 |
8.48e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 134.01 E-value: 8.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRA------------HLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVA-LHGDNLAYVIYTSGSTG 4693
Cdd:PRK07470 97 AYLAEASGAramichadfpehAAAVRAASPDLTHVVAIGGARAGLDYEALVARHLGARVANAaVDHDDPCWFFFTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIahIVATGERYEMTP----EDCELHFMSFafdgSHEGWMHPLINGAR----VLIRDDSLwLPERTYAE 4765
Cdd:PRK07470 177 RPKAAVLTHGQMA--FVITNHLADLMPgtteQDASLVVAPL----SHGAGIHQLCQVARgaatVLLPSERF-DPAEVWAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4766 MHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTE-----TVVTPLL 4839
Cdd:PRK07470 250 VERHRVTNLFTVPTILKMLVEHPAVDRyDHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEvtgniTVLPPAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4840 WKARAGDACGaaympIGTLLGNRSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrl 4916
Cdd:PRK07470 329 HDAEDGPDAR-----IGTCGFERTGMevqIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 yRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGqqlVGYVVAQEPAVAD 4992
Cdd:PRK07470 397 -RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPdpvwGEVG---VAVCVARDGAPVD 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 4993 SpeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:PRK07470 473 E--------AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1992-2479 |
8.96e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 134.01 E-value: 8.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1992 AAFAHQVASA-PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPldP 2070
Cdd:PRK07470 10 AHFLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP--T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NY---PAErLAYMLRDSGARWLICQETLAE-----RLPCPAEVERLPLETAAWPASADT-------RPLPEVAGE--TLA 2133
Cdd:PRK07470 88 NFrqtPDE-VAYLAEASGARAMICHADFPEhaaavRAASPDLTHVVAIGGARAGLDYEAlvarhlgARVANAAVDhdDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVS--QAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLfVPLLAGARVLLGDAGQWSAQH 2211
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLThgQMAFVITNHLADLMPGTTEQDASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERHAVTILDLPPAYLQQQAEE----------LRH---AG-------RRIAVRTciLGgeawdaSLLTQqavqaea 2271
Cdd:PRK07470 246 VWALVERHRVTNLFTVPTILKMLVEHpavdrydhssLRYviyAGapmyradQKRALAK--LG------KVLVQ------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 wFNAYGPTEAVIT--PLAWHcRAQEGGAPAIGRALGAR---RACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTA 2346
Cdd:PRK07470 311 -YFGLGEVTGNITvlPPALH-DAEDGPDARIGTCGFERtgmEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2347 ERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLA 2425
Cdd:PRK07470 389 KAFRDGWF--------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVpDPVWGEVGV 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2426 AYLVGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07470 461 AVCVARDGAPVDE--AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
4088-4504 |
1.09e-31 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 131.72 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFawQGELQQPLQIVYRQRQLPFA 4166
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGpVDLAVLERALRQVIAEAETLRLRF--TEEEGEPYQWIDPYTPVPIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4167 EEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY-AGRSPE 4245
Cdd:cd19533 80 HIDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtALLKGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4246 QPRDGRYSDYIAWLQRQDAAAT-------EAFWREQMAALDEPTrlveALAQPGLTSANGVGEHLREVDATATARLRDFA 4318
Cdd:cd19533 160 PAPPAPFGSFLDLVEEEQAYRQserferdRAFWTEQFEDLPEPV----SLARRAPGRSLAFLRRTAELPPELTRTLLEAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpadLPGVENQV-GLFINTLPVVVTLAPQMTLDELLQGLQRQNL 4397
Cdd:cd19533 236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR---LGAAARQTpGMVANTLPLRLTVDPQQTFAELVAQVSRELR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4398 ALREQEHTPLFELQRWAGFGGE-----AVFDNLLVFEnYPVDEvlerssaGGVRfgAVAMHEQTNYPLALAL-----GGG 4467
Cdd:cd19533 313 SLLRHQRYRYEDLRRDLGLTGElhplfGPTVNYMPFD-YGLDF-------GGVV--GLTHNLSSGPTNDLSIfvydrDDE 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 2310915810 4468 DSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19533 383 SGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
4538-5035 |
1.10e-31 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 134.63 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4538 LVHQRVAERARMAPDAVAVIFDEEK------LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------LPIPEGLSCLSVDREE---EWAG------ 4667
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAgrsvplkknvddalnPNVTSVEHVIVLKRTGsdiDWQEgrdlww 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4668 -------FPAHDPEvALHGDNLAYVIYTSGSTGMPKGVAVSHGpliAHIVATGER----YEMTPEDCelhFMSFafdgSH 4736
Cdd:cd17634 214 rdliakaSPEHQPE-AMNAEDPLFILYTSGTTGKPKGVLHTTG---GYLVYAATTmkyvFDYGPGDI---YWCT----AD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4737 EGWMH--------PLINGARVLIRDDS-LW-LPERTYAEMHRHGVTVGVFPPVYLQQLA---EHAERDGNPPPVRVYCFG 4803
Cdd:cd17634 283 VGWVTghsyllygPLACGATTLLYEGVpNWpTPARMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4804 GDAVAQASYDLAWRALKPKY--LFNGYGPTET---VVTPLLWKARAGDACgaaymPIGTLLGNRSGyILDGQLNLLPVGV 4878
Cdd:cd17634 363 GEPINPEAYEWYWKKIGKEKcpVVDTWWQTETggfMITPLPGAIELKAGS-----ATRPVFGVQPA-VVDNEGHPQPGGT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4879 AGELYLGGE--GVARGYLERPaltaERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:cd17634 437 EGNLVITDPwpGQTRTLFGDH----ERFEQTYF-STFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESV 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAQePAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:cd17634 512 LVAHPKVAEAAVVGIPHAIkGQAPYAYVVLN-HGVEPSPELYAELRNW----VRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
2002-2496 |
1.10e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 134.13 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAerlPCPAEV------------------------ERLPLETAAWPASADtrpLPEvagETLAYVIY 2137
Cdd:PRK07786 111 SDCGAHVVVTEAALA---PVATAVrdivpllstvvvaggssddsvlgyEDLLAEAGPAHAPVD---IPN---DSPALIMY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQWSAQHLADEV 2216
Cdd:PRK07786 182 TSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGAFDPGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFN--AYGPTEavITPLAwhCRAQe 2294
Cdd:PRK07786 262 EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQIlaAFGQTE--MSPVT--CMLL- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2295 gGAPAI------GRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLA 2368
Cdd:PRK07786 337 -GEDAIrklgsvGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF--------HSGDLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAmrGEDL-LAELRTW 2446
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGrADEKWGEVPVAVAAVRND--DAALtLEDLAEF 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2447 LAGRLPAYMQPTAWQVLSSLPLNANGKLD----RKALPKVDAAARRQAGEPPRE 2496
Cdd:PRK07786 486 LTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGFTE 539
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
512-998 |
1.13e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 133.06 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 512 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVP 590
Cdd:PRK06839 3 GIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 591 VDPEYPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLdQADAWLENHAE----NNPGIELNGENLAYVI-YTSGST 665
Cdd:PRK06839 83 LNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYV-QRVISITSLKEiedrKIDNFVEKNESASFIIcYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 666 GKPKGA-----GNRHSALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAapgDHRDPAKLVEL 739
Cdd:PRK06839 162 GKPKGAvltqeNMFWNALNNTF-----AIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVP---RKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 740 INREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGlyNLYGPTEAAIDVTHWTCVE 817
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFEttNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 818 EGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRAD 897
Cdd:PRK06839 312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 898 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEY 973
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY 464
|
490 500
....*....|....*....|....*
gi 2310915810 974 MVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06839 465 KIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
3066-3525 |
1.52e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 133.72 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 K--------LPLAQGVQRID----LDRGAP---------WFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHsa 3204
Cdd:PRK06087 132 KqtrpvdliLPLQNQLPQLQqivgVDKLAPatsslslsqIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTH-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 lsNRLCWMQQAYGLGVG----DTVLQKTPFSFDVSvweFFW----PLMSGARLVVAapgDHRDPAKLVALINREGVDTLH 3276
Cdd:PRK06087 210 --NNILASERAYCARLNltwqDVFMMPAPLGHATG---FLHgvtaPFLIGARSVLL---DIFTPDACLALLEQQRCTCML 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3277 ----FVPSMLQAFlqDEDVASCTSLKRIVCSGEALPADAQQQVFaklpQAG--LYNLYGPTEAAI-------DVTHWTCV 3343
Cdd:PRK06087 282 gatpFIYDLLNLL--EKQPADLSALRFFLCGGTTIPKKVARECQ----QRGikLLSVYGSTESSPhavvnldDPLSRFMH 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3344 EEgkdavpiGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRA 3423
Cdd:PRK06087 356 TD-------GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------EGWYYSGDLCRMDE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3424 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESE--SGDWREALAAHLAASL 3497
Cdd:PRK06087 423 AGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPderlGERSCAYVVLKAPhhSLTLEEVVAFFSRKRV 502
|
490 500
....*....|....*....|....*...
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06087 503 AKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1979-2503 |
1.53e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 133.19 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1979 QAPLEALPRGGVAAAfaHQVASA----PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAI-AAERSFDLVV 2053
Cdd:PRK06188 1 QATMADLLHSGATYG--HLLVSAlkryPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlSLNRPEVLMA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2054 GLLGILkAGAGYLPLDPNYPAERLAYMLRDSGARWLICQ--------ETLAERLPCPAEVERL-PLETA----AWPASAD 2120
Cdd:PRK06188 79 IGAAQL-AGLRRTALHPLGSLDDHAYVLEDAGISTLIVDpapfveraLALLARVPSLKHVLTLgPVPDGvdllAAAAKFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2121 TRPL-PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAeqLFVPLLA--GA 2197
Cdd:PRK06188 158 PAPLvAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLrgGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2198 RVLLG--DAGQWsaqhlADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIA----VRTCILGGEAWDASLLtqqavqAEA 2271
Cdd:PRK06188 236 VIVLAkfDPAEV-----LRAIEEQRITATFLVPTMIYAL---LDHPDLRTRdlssLETVYYGASPMSPVRL------AEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 -------WFNAYGPTEA--VITPL--AWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLG 2340
Cdd:PRK06188 302 ierfgpiFAQYYGQTEApmVITYLrkRDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGV 2419
Cdd:PRK06188 382 RPEETAEAFRDG--------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVpDEK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2420 GGPLLAAYLVGR-DAMRGEdllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALpkvdaaaRrqagEPPREGL 2498
Cdd:PRK06188 454 WGEAVTAVVVLRpGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL-------R----ARYWEGR 519
|
....*
gi 2310915810 2499 ERSVA 2503
Cdd:PRK06188 520 GRAVG 524
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
523-998 |
1.89e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 132.86 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07470 19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRkGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 602 YMLEDSGVQLLLSQS--------------HLKLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGK 667
Cdd:PRK07470 98 YLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 668 PKGAGNRHSAL----SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVWEffwpLMSGARLV--VAAPGDHRDPAKLVELIN 741
Cdd:PRK07470 178 PKAAVLTHGQMafviTNHLADLMP--GTTEQDASLVVAPLSHGAGIHQ----LCQVARGAatVLLPSERFDPAEVWALVE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 742 REGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT----HWTC 815
Cdd:PRK07470 252 RHRVTNLFTVPTILKMLVEHPAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTGNITvlppALHD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 816 VEEGKDTV--PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLAR 893
Cdd:PRK07470 331 AEDGPDARigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLGH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGY-VVLESEGGDWREALAAH-LAAS 969
Cdd:PRK07470 404 LDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWgeVGVaVCVARDGAPVDEAELLAwLDGK 483
|
490 500
....*....|....*....|....*....
gi 2310915810 970 LPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07470 484 VARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
523-998 |
2.94e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.93 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:PRK06145 14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLD---QADAWL--ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:PRK06145 94 ILGDAGAKLLLVDEEFDAIVALETPKIVIDaaaQADSRRlaQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 678 LSNRLCWMQQAYGLGVGDTVLQKTPF----SFDVSVWEFFWplmSGARLVVaapgdHR--DPAKLVELINREGVDTLHFV 751
Cdd:PRK06145 174 LHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIERHRLTCAWMA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 752 PSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLY-NLYGPTEAaidVTHWTCVEEGKDTVPI--- 825
Cdd:PRK06145 246 PVMLSRVLTvpDRDRFDLDSLAWCIGGGEKTP-ESRIRDFTRVFTRARYiDAYGLTET---CSGDTLMEAGREIEKIgst 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 826 GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGR 905
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 906 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLA 981
Cdd:PRK06145 395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHddrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKV 474
|
490
....*....|....*..
gi 2310915810 982 LERMPLSPNGKLDRKAL 998
Cdd:PRK06145 475 RDELPRNPSGKVLKRVL 491
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
4089-4504 |
2.96e-31 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 130.58 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElQQPLQIVYRQRQLPFAE 4167
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGpLDVEALREALRDVVARHEALRTLLVRDDG-GVPRQEILPPGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4168 EDLSQAANRDAALLALAA-AERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGR---- 4242
Cdd:cd19539 82 RDLSDPDSDRERRLEELLrERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARrkgp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4243 -SPEQPRDGRYSDYIAWLQRQDA----AATEAFWREQMAALdEPTRLVEALAQPGLTSANGvGEHLREVDATATARLRDF 4317
Cdd:cd19539 162 aAPLPELRQQYKEYAAWQREALAapraAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPG-ADLRFELDAELVAALREL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4318 ARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNL 4397
Cdd:cd19539 240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4398 -ALREQEhTPLFELQRWAG----FGGEAVFDNLLVFENYPvDEVLERSSAGGVRFGAVAMhEQTNYPLAL-ALGGGDSLS 4471
Cdd:cd19539 318 dAQRHQE-LPFQQLVAELPvdrdAGRHPLVQIVFQVTNAP-AGELELAGGLSYTEGSDIP-DGAKFDLNLtVTEEGTGLR 394
|
410 420 430
....*....|....*....|....*....|...
gi 2310915810 4472 LQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19539 395 GSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1990-2479 |
3.18e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 131.92 E-value: 3.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAhqvasAPEAIALVCGD-EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PRK07514 9 LRAAFA-----DRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 DPNYPAERLAYMLRDSGARWLICQ-------ETLAERLPCPaEVERL------PLETAAWPASADTRPLPeVAGETLAYV 2135
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDpanfawlSKIAAAAGAP-HVETLdadgtgSLLEAAAAAPDDFETVP-RGADDLAAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2136 IYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAeqLFVP----LLAGARVLlgdagqWSAQH 2211
Cdd:PRK07514 162 LYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPI-FHTHG--LFVAtnvaLLAGASMI------FLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERH---AVTILDLPPAY--LQQQAEELRHAGRRIavRTCILGgeawDASLL--TQQAVQA---EAWFNAYGPTEA 2281
Cdd:PRK07514 233 DPDAVLALmprATVMMGVPTFYtrLLQEPRLTREAAAHM--RLFISG----SAPLLaeTHREFQErtgHAILERYGMTET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VI---TPLAWHCRAQEGGAPAIGRALgarRACILDAAlQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsg 2358
Cdd:PRK07514 307 NMntsNPYDGERRAGTVGFPLPGVSL---RVTDPETG-AELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2359 erlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLL----AAYLVGRD-- 2432
Cdd:PRK07514 379 ---FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI---GVPHPDFgegvTAVVVPKPga 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2310915810 2433 AMRGEDLLAELRtwlaGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07514 453 ALDEAAILAALK----GRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
511-998 |
3.54e-31 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 131.48 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 511 RGVHRLFEEQVERTPTAPALAF--GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAY 588
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 589 VPVDPEYPEERQAYMLEDSGVQLLLSQshlklPLAQGVQ----------RIDLDQADAWLENHAENNPGIELNGENLAYV 658
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIA-----VDAQVMDaifqsgvrvlALSDLVGLGEPESAGPLIEDPPREPEQPAFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 659 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL--GVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKL 736
Cdd:cd05923 156 FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 737 VELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPqaGLY-NLYGPTEA-----AI 808
Cdd:cd05923 234 LKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLP--GEKvNIYGTTEAmnslyMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 809 DVTHWTCVEEGKDT-VPIGRpignlgcyILDGNLEPVPVGVLGELYLAGRGLA--RGYHQRPGLTAERFVaspfvagERM 885
Cdd:cd05923 312 DARTGTEMRPGFFSeVRIVR--------IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DGW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREA 961
Cdd:cd05923 377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVTACVVPREGTLSADEL 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 2310915810 962 LAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05923 457 DQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
4089-4504 |
5.87e-31 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 129.50 E-value: 5.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQRQLPF-- 4165
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGpLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLRLeh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 ----AEEDLSQAANRDAALLalaaaerergFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAG 4241
Cdd:cd19532 83 vqisDEAEVEEEFERLKNHV----------YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4242 RsPEQPRDGRYSDYIAwLQRQDAAATE-----AFWREQMAALDEP----------TRlvEALAQPGLTSANgvgehlREV 4306
Cdd:cd19532 153 Q-PLLPPPLQYLDFAA-RQRQDYESGAldedlAYWKSEFSTLPEPlpllpfakvkSR--PPLTRYDTHTAE------RRL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4307 DATATARLRDFARRHQVT-----LntlvqAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAP 4381
Cdd:cd19532 223 DAALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRRDP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4382 QMTLDELLQ--------GLQRQNLAL----------REQEHTPLFelQrwagfggeavfdnllVFENYPVdEVLERSSAG 4443
Cdd:cd19532 296 SQTFADVLKetrdkayaALAHSRVPFdvlldelgvpRSATHSPLF--Q---------------VFINYRQ-GVAESRPFG 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4444 GVRFGAVAMHE-QTNYPLAL---ALGGGDSLsLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19532 358 DCELEGEEFEDaRTPYDLSLdiiDNPDGDCL-LTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1952-2480 |
7.72e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 130.89 E-value: 7.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1952 MAETPQAALGELALLDAGERQEALRdwqaPLEALPRGGVAAAFAHQVASA--PEAIALVCGDEHLSYAELDMRAERLARG 2029
Cdd:PRK13383 1 VAPTAARALVRSGLLNPPSPRAVLR----LLREASRGGTNPYTLLAVTAArwPGRTAIIDDDGALSYRELQRATESLARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2030 LRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLP 2109
Cdd:PRK13383 77 LTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2110 LETAAWPASADTRPLPEVAGETlayVIYTSGSTGQPKGV----AVSQAALVAHCQAAARTYGVGPgdcQLQFASISFDAA 2185
Cdd:PRK13383 157 DPATAGAEESGGRPAVAAPGRI---VLLTSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGS---RISVAMPMFHGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2186 AEQLFVPLLA-GARVLLG---DAGQWSAQ---HLADEVERHAVT---ILDLPPaylqqqaeELRHAGRRIAVRTCILGGE 2255
Cdd:PRK13383 231 GLGMLMLTIAlGGTVLTHrhfDAEAALAQaslHRADAFTAVPVVlarILELPP--------RVRARNPLPQLRVVMSSGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2256 AWDASLlTQQAVQA--EAWFNAYGPTEAVITPLAwhCRAQEGGAP-AIGRALGARRACILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK13383 303 RLDPTL-GQRFMDTygDILYNGYGSTEVGIGALA--TPADLRDAPeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYLGRPGQTaerfVADPFSGsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAA 2412
Cdd:PRK13383 380 LAGTRYTDGGGKA----VVDGMTS-------TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2413 VVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PRK13383 449 VIGVpDERFGHRLAAFVVLHP---GSGVdAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
3050-3525 |
9.00e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 130.39 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:PRK06145 14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfEDYS------EANPDIHLDGE-NLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK06145 94 ILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQ--ADSRrlaqggLEIPPQAAVAPtDLVRLMYTSGTTDRPKGVMHSY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SALSNRLCWMQQAYGLGVGDTVLQKTPF----SFDVSVWEFFWplmSGARLVVaapgdHR--DPAKLVALINREGVDTLH 3276
Cdd:PRK06145 172 GNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3277 FVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLY-NLYGPTEAaidVTHWTCVEEGKDAVPI- 3352
Cdd:PRK06145 244 MAPVMLSRVLTvpDRDRFDLDSLAWCIGGGEKTP-ESRIRDFTRVFTRARYiDAYGLTET---CSGDTLMEAGREIEKIg 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 --GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYA 3430
Cdd:PRK06145 320 stGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3431 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQW 3506
Cdd:PRK06145 393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHddrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQL 472
|
490
....*....|....*....
gi 2310915810 3507 LALERMPLSPNGKLDRKAL 3525
Cdd:PRK06145 473 KVRDELPRNPSGKVLKRVL 491
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
522-954 |
1.30e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 130.85 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 522 ERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGigaDRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK08314 21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLqqecgVRKG---DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 597 EERQAYMLEDSGVQLLLSQSHL---------KLPLAQGV--------------------------QRIDLDQADAWLENH 641
Cdd:PRK08314 97 EEELAHYVTDSGARVAIVGSELapkvapavgNLRLRHVIvaqysdylpaepeiavpawlraepplQALAPGGVVAWKEAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 642 AENNPGIELNG--ENLAYVIYTSGSTGKPKGAGNRH-SALSNRLC---WmqqaYGLGVGDTVLQKTPFsFDVS--VWEFF 713
Cdd:PRK08314 177 AAGLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHrTVMANAVGsvlW----SNSTPESVVLAVLPL-FHVTgmVHSMN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 714 WPLMSGARLVVAAPGDhRDPAKlvELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPadaqQQVFAK 791
Cdd:PRK08314 252 APIYAGATVVLMPRWD-REAAA--RLIERYRVTHWTNIPTMVVDFLASPGLAErdLSSLRYIGGGGAAMP----EAVAER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 792 LPQagLYNL-----YGPTEAaIDVTHwtcveegkdTVPIGRPigNLGCY----------ILD-GNLEPVPVGVLGELYLA 855
Cdd:PRK08314 325 LKE--LTGLdyvegYGLTET-MAQTH---------SNPPDRP--KLQCLgiptfgvdarVIDpETLEELPPGEVGEIVVH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 856 GRGLARGYHQRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 935
Cdd:PRK08314 391 GPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500
....*....|....*....|...
gi 2310915810 936 AVLAVD----GRQLVGYVVLESE 954
Cdd:PRK08314 468 CVIATPdprrGETVKAVVVLRPE 490
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
4543-5040 |
1.40e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 129.54 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAV--IFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK09088 1 IAFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCL--SVDREEEwagfpahDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:PRK09088 81 LSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFiaSADALEP-------ADTPSIPPERVSLILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPED---CE---LHFMSFAFDgshegwMHP-LINGARVLIRDDslWLPERTYAEMHRH-- 4769
Cdd:PRK09088 154 MLSERNLQQTAHNFGVLGRVDAHSsflCDapmFHIIGLITS------VRPvLAVGGSILVSNG--FEPKRTLGRLGDPal 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4770 GVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTE--TV----VTPLLWKAR 4843
Cdd:PRK09088 226 GITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIP-MVDGFGMSEagTVfgmsVDCDVIRAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4844 AGDAcGAAYMPIGTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLT 4923
Cdd:PRK09088 305 AGAA-GIPTPTVQT-------RVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4924 RGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQlVGYVVAQePAVADSPEAqaecrAQ 5003
Cdd:PRK09088 370 RRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE-VGYLAIV-PADGAPLDL-----ER 442
|
490 500 510
....*....|....*....|....*....|....*..
gi 2310915810 5004 LKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
4534-4986 |
1.50e-30 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 130.05 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:cd05904 2 PTDLPLDSVSFLFASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLP---IP---------EGLSCLSVDREEEWAGFPAhdpeVALHG 4679
Cdd:cd05904 82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAslaLPvvlldsaefDSLSFSDLLFEADEAEPPV----VVIKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT--GERYEMTPEDCEL------HFMSFAFDGshegwMHPLINGARVLI 4751
Cdd:cd05904 158 DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLcvlpmfHIYGLSSFA-----LGLLRLGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 rddslwLPERTYAEM----HRHGVTVG-VFPPVYLqQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLF- 4825
Cdd:cd05904 233 ------MPRFDLEELlaaiERYKVTHLpVVPPIVL-ALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLg 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYGPTETvvTPLLwkARAGDACG--AAYMPIGTLLGNRSGYILD---GQlnLLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:cd05904 306 QGYGMTES--TGVV--AMCFAPEKdrAKYGSVGRLVPNVEAKIVDpetGE--SLPPNQTGELWIRGPSIMKGYLNNPEAT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVPDPFgapgsrlYRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VG 4976
Cdd:cd05904 380 AATIDKEGW-------LHTGDLCYIDEDGylfIVD---RLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEeAG 449
|
490
....*....|
gi 2310915810 4977 QQLVGYVVAQ 4986
Cdd:cd05904 450 EVPMAFVVRK 459
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
3048-3482 |
1.56e-30 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 129.66 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 3125
Cdd:cd05904 15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3126 RQAYMLEDSGVELLLSQSHL--KLP-LAQGVQRIDLDRGAPWFED--------YSEANPDIHLDgeNLAYVIYTSGSTGK 3194
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELaeKLAsLALPVVLLDSAEFDSLSFSdllfeadeAEPPVVVIKQD--DVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAgnrhsALSNR-LCWMQQAYGLGVG------DTVLQKTPFSfdvSVWEFFWPLMSGARL---VVAAPGdhRDPAKLV 3264
Cdd:cd05904 173 SKGV-----MLTHRnLIAMVAQFVAGEGsnsdseDVFLCVLPMF---HIYGLSSFALGLLRLgatVVVMPR--FDLEELL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 ALINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 3342
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST-GVVAMCF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAVP--IGRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvaGERMYRTGDLA 3419
Cdd:cd05904 322 APEKDRAKYgsVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGDLC 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQL-VGYVVLESES 3482
Cdd:cd05904 396 YIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpdeEAGEVpMAFVVRKPGS 462
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
2014-2479 |
2.34e-30 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 127.46 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSgarwlicqe 2093
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletaawpasadtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05912 73 --------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASISFDAAAEQLFVPLLAGARVLLGDAgqWSAQHLADEVERHAVTILDLPPAYLQQQAEELrHAGRRIAVRTCILG 2253
Cdd:cd05912 121 WLCALPLFHISGLSILMRSVIYGMTVYLVDK--FDAEQVLHLINSGKVTIISVVPTMLQRLLEIL-GEGYPNNLRCILLG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2254 GEAWDASLLTQQAVQAEAWFNAYGPTE-----AVITPLAWHCRAQEGGAPAIGralgarraCILDAALQPCAPGMIGELY 2328
Cdd:cd05912 198 GGPAPKPLLEQCKEKGIPVYQSYGMTEtcsqiVTLSPEDALNKIGSAGKPLFP--------VELKIEDDGQPPYEVGEIL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 IGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV 2408
Cdd:cd05912 270 LKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2409 AEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05912 342 KEAGVVGIpDDKWGQVPVAFVVSERPISEEELIAYCSEKLAK----YKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1998-2479 |
2.34e-30 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 129.79 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVC------GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:PRK13295 34 VASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2072 YPAERLAYMLRDSGARWLICQ------------ETLAERLPCPAEV-----------ERLpLETAAWPASADT------- 2121
Cdd:PRK13295 114 FRERELSFMLKHAESKVLVVPktfrgfdhaamaRRLRPELPALRHVvvvggdgadsfEAL-LITPAWEQEPDApailarl 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2122 RPLPEvageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLqFASisfdAAAEQ------LFVPLLA 2195
Cdd:PRK13295 193 RPGPD----DVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIL-MAS----PMAHQtgfmygLMMPVML 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWF 2273
Cdd:PRK13295 264 GATAVLQD--IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSsLRTFLCAGAPIPGALVERaRAALGAKIV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2274 NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfvadp 2353
Cdd:PRK13295 342 SAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT------ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 fsgSGERLYRTGDLARYRVDGQVEYLGRADQQIkIRGFR-IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK13295 416 ---DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGEnIPVVEIEALLYRHPAIAQVAIVAYpDERLGERACAFVVPR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2432 DamrGEDL-LAELRTWL-AGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK13295 492 P---GQSLdFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
4546-5042 |
2.61e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 128.93 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRER 4625
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4626 LLYMMQDSRAHLLLTHSHLLERLPIpeglscLSVDREEEWAGFPAHDPEV--ALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIP------GISVKFAELMNGPKEEAEIqeEFDLDEVATIMYTSGTTGKPKGVIQTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRD--DslwlPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:PRK03640 165 NHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEkfD----AEKINKLLQTGGVTIISVVSTML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAEHAERDGNPPPVRVYCFGGDAVAQASydLAWRALKPKYLFNGYGPTET---VVTplLWKARAGDACGAAympiGTL 4858
Cdd:PRK03640 241 QRLLERLGEGTYPSSFRCMLLGGGPAPKPL--LEQCKEKGIPVYQSYGMTETasqIVT--LSPEDALTKLGSA----GKP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDgQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRVD 4938
Cdd:PRK03640 313 LFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecraQLKTALRERLPEYMV 5017
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwGQVPVAFVVKSGEVTEE----------ELRHFCEEKLAKYKV 453
|
490 500
....*....|....*....|....*
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK03640 454 PKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
4543-5040 |
2.80e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 128.85 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK06145 8 IAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHshllERLPIPEGLSCLSV--------DREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGM 4694
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLVD----EEFDAIVALETPKIvidaaaqaDSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4695 PKGVAVSHGPL----IAHIVATGeryeMTPEDCEL------HFMSFAFDGSHEGWmhplINGARVLIRDdslWLPERTYA 4764
Cdd:PRK06145 164 PKGVMHSYGNLhwksIDHVIALG----LTASERLLvvgplyHVGAFDLPGIAVLW----VGGTLRIHRE---FDPEAVLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGdavAQASYDLAWRALKPKY----LFNGYGPTETVVTPLLW 4840
Cdd:PRK06145 233 AIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGG---GEKTPESRIRDFTRVFtrarYIDAYGLTETCSGDTLM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 KA-RAGDACGAAympiGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRS 4919
Cdd:PRK06145 310 EAgREIEKIGST----GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQA 4998
Cdd:PRK06145 378 GDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPGATLTLEALDR 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2310915810 4999 ECRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06145 458 HCRQ--------RLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2010-2479 |
4.35e-30 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 127.33 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEH-LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARW 2088
Cdd:cd05907 1 GVWQpITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LICQETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGV 2168
Cdd:cd05907 81 LFVEDP-----------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2169 GPGDCQLQFASISFdaAAEQ---LFVPLLAGARVLLGDAGQWSAQHLAdEV------------ERH--AVTILDLPPayL 2231
Cdd:cd05907 126 TEGDRHLSFLPLAH--VFERragLYVPLLAGARIYFASSAETLLDDLS-EVrptvflavprvwEKVyaAIKVKAVPG--L 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2232 QQQAEELRHAGRriaVRTCILGGEAWDASLLTqqavqaeaWFNA--------YGPTE--AVITplAWHCRAQEGGApaIG 2301
Cdd:cd05907 201 KRKLFDLAVGGR---LRFAASGGAPLPAELLH--------FFRAlgipvyegYGLTEtsAVVT--LNPPGDNRIGT--VG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2302 RALgarracildaalqpcaPGMI------GELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQ 2375
Cdd:cd05907 266 KPL----------------PGVEvriaddGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2376 VEYLGRA-DQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLV-------------------GRDAMR 2435
Cdd:cd05907 323 LHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI---GDGRPFLVALIVpdpealeawaeehgiaytdVAELAA 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2436 GEDLLAELRTWLA---GRLPAYMQ-------PTAWQVLSSLpLNANGKLDRKAL 2479
Cdd:cd05907 400 NPAVRAEIEAAVEaanARLSRYEQikkflllPEPFTIENGE-LTPTLKLKRPVI 452
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
3064-3487 |
4.47e-30 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 127.33 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQs 3143
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3144 hlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRlCWMQQAYGL----- 3218
Cdd:cd05907 85 ----------------------------------DPDDLATIIYTSGTTGRPKGV-----MLSHR-NILSNALALaerlp 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3219 -GVGDTVLQKTPFS--FDVSVWEFFwPLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCT 3295
Cdd:cd05907 125 aTEGDRHLSFLPLAhvFERRAGLYV-PLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3296 SLKR-------------IVCSGEALPADaqqqVFAKLPQAGL--YNLYGPTE--AAIDVTHWTCVEEGKdavpIGRPIAN 3358
Cdd:cd05907 199 GLKRklfdlavggrlrfAASGGAPLPAE----LLHFFRALGIpvYEGYGLTEtsAVVTLNPPGDNRIGT----VGKPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 LACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:cd05907 271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKKDLII 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3439 LR-GLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESES-GDWRE 3487
Cdd:cd05907 335 TSgGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEAlEAWAE 385
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
2004-2474 |
4.59e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 128.48 E-value: 4.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2004 AIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQETLAE-------RLPCPAEVERLPLET-------AAWPASADTRPLP-EVAGETLAyviYTSGSTGQPKGV 2148
Cdd:PRK08276 82 SGAKVLIVSAALADtaaelaaELPAGVPLLLVVAGPvpgfrsyEEALAAQPDTPIAdETAGADML---YSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2149 -------AVSQAALVAHCQAAARTYGvGPGDCQL------QFASISFDAAAEQLfvpllaGARVLLGDagQWSAQHLADE 2215
Cdd:PRK08276 159 krplpglDPDEAPGMMLALLGFGMYG-GPDSVYLspaplyHTAPLRFGMSALAL------GGTVVVME--KFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVTILDLPPAY---LQQQAEELRhagrriavrtcilggEAWDASLLtQQAVQAEA------------WFNA----- 2275
Cdd:PRK08276 230 IERYRVTHSQLVPTMfvrMLKLPEEVR---------------ARYDVSSL-RVAIHAAApcpvevkramidWWGPiihey 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTEA----VITPLAWHCRAQEGGAPAIGRALgarracILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfva 2351
Cdd:PRK08276 294 YASSEGggvtVITSEDWLAHPGSVGKAVLGEVR------ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA---- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpfSGSGERLYRTGDLARYRVDGqveYL---GRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAA 2426
Cdd:PRK08276 364 ---ARNPHGWVTVGDVGYLDEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpdEEMGERVKAV 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2310915810 2427 YLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK08276 438 VQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1994-2479 |
5.15e-30 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 128.77 E-value: 5.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASA-----PEAIALVCGDEH-----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:cd05970 18 FAYDVVDAmakeyPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPAERLAYMLRDSGARWLIC------QETLAERLP-CPAEVERL---PLETAAW--------PASAD-TRPL 2124
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAiaedniPEEIEKAAPeCPSKPKLVwvgDPVPEGWidfrklikNASPDfERPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 PEVA--GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAA-EQLFVPLLAGARVLL 2201
Cdd:cd05970 178 ANSYpcGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 GDAGQWSAQHLADEVERHAVTILDLPPA-YLQQQAEELRHAGRRiAVRTCILGGEAWDASLL-TQQAVQAEAWFNAYGPT 2279
Cdd:cd05970 258 YDYDKFDPKALLEKLSKYGVTTFCAPPTiYRFLIREDLSRYDLS-SLRYCTTAGEALNPEVFnTFKEKTGIKLMEGFGQT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EAVITPLAWHCRAQEGGApaIGRALGARRACILDAALQPCAPGMIGELYI--------GgqcLARGYLGRPGQTAERFva 2351
Cdd:cd05970 337 ETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgkpvG---LFGGYYKDAEKTAEVW-- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV- 2429
Cdd:cd05970 410 --HDG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVpDPIRGQVVKATIVl 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2430 GRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05970 484 AKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1583-1843 |
1.20e-29 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 125.65 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPQPLQVVFEQATLELRLAPPGSDpqrqAEAEREAG------FDPARAP 1656
Cdd:cd19532 34 GPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLRLEHVQISDE----AEVEEEFErlknhvYDLESGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1657 LQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIgwLQGRDA-----MATEF-FWRD 1730
Cdd:cd19532 110 TMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQYLDFA--ARQRQDyesgaLDEDLaYWKS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1731 RLAS-------LEMPTRLARQARTeQPGQGEHLRELDPQTTRQLASFAQGQKVT-----LntlvqAAWALLLQRHCGQET 1798
Cdd:cd19532 188 EFSTlpeplplLPFAKVKSRPPLT-RYDTHTAERRLDAALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDD 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2310915810 1799 VAFGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADYLQ 1843
Cdd:cd19532 262 ICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADVLK 304
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1104-1316 |
1.42e-29 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 125.55 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1104 QR-WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRR------Q 1176
Cdd:cd19531 9 QRlWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVdlsglpE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAdldADLGPRSSS- 1254
Cdd:cd19531 89 AEREAEAQRLArEEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA---AFLAGRPSPl 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 1255 ---------YQTWSRHLheQAGARLDE-LDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQL 1316
Cdd:cd19531 166 pplpiqyadYAVWQREW--LQGEVLERqLAYWREQLAGAPPVleLPTDRPRPAVQSFRGARVRFTLPAELTAAL 237
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
537-954 |
1.54e-29 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 125.79 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQs 616
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 617 hlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAgnrhsALSNRlCWMQQAYGL----- 691
Cdd:cd05907 85 ----------------------------------DPDDLATIIYTSGTTGRPKGV-----MLSHR-NILSNALALaerlp 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 692 -GVGDTVLQKTPFS--FDVSVWEFFwPLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT 768
Cdd:cd05907 125 aTEGDRHLSFLPLAhvFERRAGLYV-PLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 769 SLKR-------------IVCSGEALPADaqqqVFAKLPQAGL--YNLYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGN 831
Cdd:cd05907 199 GLKRklfdlavggrlrfAASGGAPLPAE----LLHFFRALGIpvYEGYGLTEtsAVVTLNPPGDNRIGT----VGKPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 832 LGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd05907 271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKKDLII 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2310915810 912 LR-GLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESE 954
Cdd:cd05907 335 TSgGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPE 378
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
4546-5034 |
1.71e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.53 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMA-PDAVAV-IFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK07514 10 RAAFAdRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCLSV-----DRE----EEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:PRK07514 90 AELDYFIGDAEPALVVCDPANFAWLsKIAAAAGAPHVetldaDGTgsllEAAAAAPDDFETVPRGADDLAAILYTSGTTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSF-----AFDGSHEGwmhpLINGARVlirddsLWLP----ERTYA 4764
Cdd:PRK07514 170 RSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIfhthgLFVATNVA----LLAGASM------IFLPkfdpDAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVfPPVYLQQLAEHAerdgnpppvrvycFGGDAVAQ------------ASYDLAWRALKPKYLFNGYGPTE 4832
Cdd:PRK07514 240 LMPRATVMMGV-PTFYTRLLQEPR-------------LTREAAAHmrlfisgsapllAETHREFQERTGHAILERYGMTE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4833 TVV---TPLLWKARAGdACGAAyMPiGTLLgnRSGYILDGQlnLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF 4909
Cdd:PRK07514 306 TNMntsNPYDGERRAG-TVGFP-LP-GVSL--RVTDPETGA--ELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4910 gapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEP 4988
Cdd:PRK07514 379 -------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPdFGEGVTAVVVPKPG 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 4989 AVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGK 5034
Cdd:PRK07514 452 AALDE--------AAILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
3049-3481 |
2.50e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 126.61 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGvgaDRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK08314 21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLqqecgVRKG---DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGV-------ELL--LSQSHLKLPLAQGV--------------------------QRIDLDRGAPWfEDY 3168
Cdd:PRK08314 97 EEELAHYVTDSGArvaivgsELApkVAPAVGNLRLRHVIvaqysdylpaepeiavpawlraepplQALAPGGVVAW-KEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3169 SEAN--PDIHLDG-ENLAYVIYTSGSTGKPKGAGNRH-SALSNRLC---WmqqaYGLGVGDTVLQKTPFsFDVS--VWEF 3239
Cdd:PRK08314 176 LAAGlaPPPHTAGpDDLAVLPYTSGTTGVPKGCMHTHrTVMANAVGsvlW----SNSTPESVVLAVLPL-FHVTgmVHSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3240 FWPLMSGARLVVAAPGDhRDPAKLvaLINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPadaqQQVFA 3317
Cdd:PRK08314 251 NAPIYAGATVVLMPRWD-REAAAR--LIERYRVTHWTNIPTMVVDFLASPGLAErdLSSLRYIGGGGAAMP----EAVAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 KLPQagLYNL-----YGPTEAaIDVTHWTCVEEGKDAVpIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYH 3391
Cdd:PRK08314 324 RLKE--LTGLdyvegYGLTET-MAQTHSNPPDRPKLQC-LGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3392 QRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--- 3468
Cdd:PRK08314 400 NRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPdpr 476
|
490
....*....|....
gi 2310915810 3469 -GRQLVGYVVLESE 3481
Cdd:PRK08314 477 rGETVKAVVVLRPE 490
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
4536-4992 |
3.12e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 125.10 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4536 TPLVHQRVAERARMAPdavAVIFDEEKLTYAELDSRANRLAHALiaRGVGpevRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK07787 2 ASLNPAAVAAAADIAD---AVRIGGRVLSRSDLAGAATAVAERV--AGAR---RVAVLATPTLATVLAVVGALIAGVPVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PL--DIEyPRERLlYMMQDSRAHLLLThshllERLPIPEGLSCLSVDREEE-WAGFPAHDPEVAlhgdnlAYVIYTSGST 4692
Cdd:PRK07787 74 PVppDSG-VAERR-HILADSGAQAWLG-----PAPDDPAGLPHVPVRLHARsWHRYPEPDPDAP------ALIVYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4693 GMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV--LIRDDslwlPERtYAEMHRH 4769
Cdd:PRK07787 141 GPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPlFHVHGLVLGVLGPLRIGNRFvhTGRPT----PEA-YAQALSE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4770 GVTV--GVfPPVYlQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPllwKARAGDA 4847
Cdd:PRK07787 216 GGTLyfGV-PTVW-SRIAADPEAARALRGARLLVSGSAALPVPVFD-RLAALTGHRPVERYGMTETLITL---STRADGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4848 CGAAYmpIGTLLGNRSGYILDGQLNLLPVGVA--GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRG 4925
Cdd:PRK07787 290 RRPGW--VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVV 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4926 RADGVVDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVAD 4992
Cdd:PRK07787 361 DPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdLGQRIVAYVVGADDVAAD 429
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
522-1000 |
3.96e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 126.20 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 602 YMLEDSGVQLLLSQSHLkLPLAQGVQRiDLDQADAWLEnHAENNPGIELNGENLA-------------------YVIYTS 662
Cdd:PRK07788 140 EVAAREGVKALVYDDEF-TDLLSALPP-DLGRLRAWGG-NPDDDEPSGSTDETLDdliagsstaplpkppkpggIVILTS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 663 GSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFWPLmsGARLVVaapgdHR--DPAKLVE 738
Cdd:PRK07788 217 GTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrfDPEATLE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 739 LINREGVDTLHFVPSMLQAFL-QDEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEAAIdVTH 812
Cdd:PRK07788 290 DIAKHKATALVVVPVMLSRILdLGPEVLAkydTSSLKIIFVSGSALSPELATRALEAF---GpvLYNLYGSTEVAF-ATI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 813 WTCVEEGKDTVPIGRPIgnLGCY--ILDGNLEPVPVGVLGELYLAGRGLARGYhqrpglTAERfvASPFVAGerMYRTGD 890
Cdd:PRK07788 366 ATPEDLAEAPGTVGRPP--KGVTvkILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--DKQIIDG--LLSSGD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHL 966
Cdd:PRK07788 434 VGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeefGQRLRAFVVKAPGAALDEDAIKDYV 513
|
490 500 510
....*....|....*....|....*....|....
gi 2310915810 967 AASLPEYMVPAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:PRK07788 514 RDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
4547-5044 |
4.56e-29 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 125.69 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIF-----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL---- 4617
Cdd:cd05970 27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAthql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 ---DIEYPRER--LLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGF------------PAHDPEVALhGD 4680
Cdd:cd05970 107 takDIVYRIESadIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFrkliknaspdfeRPTANSYPC-GE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVaTGERYEMTPEDcELHFMSfafdgSHEGWMHPL--------INGARVLIR 4752
Cdd:cd05970 186 DILLVYFSSGTTGMPKMVEHDFTYPLGHIV-TAKYWQNVREG-GLHLTV-----ADTGWGKAVwgkiygqwIAGAAVFVY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4753 DDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTE 4832
Cdd:cd05970 259 DYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFN-TFKEKTGIKLMEGFGQTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4833 TVVTpllwkaragdacgAAYMPI-----GTLLGNRSGY---ILDGQLNLLPVGVAGELYLGGE-----GVARGYLERPAL 4899
Cdd:cd05970 338 TTLT-------------IATFPWmepkpGSMGKPAPGYeidLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFvpdpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQ 4978
Cdd:cd05970 405 TAEVW--------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrGQV 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4979 LVGYVVaqepaVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPD 5044
Cdd:cd05970 477 VKATIV-----LAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
521-937 |
5.35e-29 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 125.04 E-value: 5.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 521 VERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:cd05904 15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 599 RQAYMLEDSGVQLLLSQSHL--KLP-LAQGVQRIDLDQADAWL------ENHAENNPGIELNGENLAYVIYTSGSTGKPK 669
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELaeKLAsLALPVVLLDSAEFDSLSfsdllfEADEAEPPVVVIKQDDVAALLYSSGTTGRSK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 670 GAgnrhsALSNR-LCWMQQAYGLGVG------DTVLQKTPFSfdvSVWEFFWPLMSGARL---VVAAPGdhRDPAKLVEL 739
Cdd:cd05904 175 GV-----MLTHRnLIAMVAQFVAGEGsnsdseDVFLCVLPMF---HIYGLSSFALGLLRLgatVVVMPR--FDLEELLAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 740 INREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVE 817
Cdd:cd05904 245 IERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST-GVVAMCFAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 818 EGKDTVP--IGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvaGERMYRTGDLARY 894
Cdd:cd05904 324 EKDRAKYgsVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGDLCYI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2310915810 895 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 937
Cdd:cd05904 398 DEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
3049-3527 |
5.38e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 125.81 E-value: 5.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQSHLkLPLAQGVQRiDLDRGAPWFEDYSEANPDI-----------HLDGENL-------AYVIYTSG 3190
Cdd:PRK07788 140 EVAAREGVKALVYDDEF-TDLLSALPP-DLGRLRAWGGNPDDDEPSGstdetlddliaGSSTAPLpkppkpgGIVILTSG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3191 STGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFWPLmsGARLVVaapgdHR--DPAKLVAL 3266
Cdd:PRK07788 218 TTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrfDPEATLED 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3267 INREGVDTLHFVPSMLQAFL-QDEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEAAIdVTHW 3340
Cdd:PRK07788 291 IAKHKATALVVVPVMLSRILdLGPEVLAkydTSSLKIIFVSGSALSPELATRALEAF---GpvLYNLYGSTEVAF-ATIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3341 TCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqrpglTAERfvASPFVAGerMYRTGDLAR 3420
Cdd:PRK07788 367 TPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--DKQIIDG--LLSSGDVGY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAAS 3496
Cdd:PRK07788 437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeefGQRLRAFVVKAPGAALDEDAIKDYVRDN 516
|
490 500 510
....*....|....*....|....*....|.
gi 2310915810 3497 LPEYMVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PRK07788 517 LARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1982-2483 |
5.68e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 125.81 E-value: 5.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1982 LEALPRGGVAAAFAHQVA-SAPEAIALVcgDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK07788 42 AADIRRYGPFAGLVAHAArRAPDRAALI--DERgtLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-PCPAEVERLPletaAWPASADTRPLPEVAGETLA---- 2133
Cdd:PRK07788 120 GKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLsALPPDLGRLR----AWGGNPDDDEPSGSTDETLDdlia 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 ---------------YVIYTSGSTGQPKGVA-------VSQAALVAHC---------QAAARTYGVGPGDCQLQFAsisf 2182
Cdd:PRK07788 196 gsstaplpkppkpggIVILTSGTTGTPKGAPrpepsplAPLAGLLSRVpfragettlLPAPMFHATGWAHLTLAMA---- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2183 daaaeqlfvpllAGARVLLG---DAgqwsAQHLADeVERHAVTILDLPPAYLQQQAEELRHAGRRI---AVRTCILGGEA 2256
Cdd:PRK07788 272 ------------LGSTVVLRrrfDP----EATLED-IAKHKATALVVVPVMLSRILDLGPEVLAKYdtsSLKIIFVSGSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2257 WDASLLTQ-QAVQAEAWFNAYGPTE----AVITP--LAwhcraqegGAPAI-GRA-LGARRAcILDAALQPCAPGMIGEL 2327
Cdd:PRK07788 335 LSPELATRaLEAFGPVLYNLYGSTEvafaTIATPedLA--------EAPGTvGRPpKGVTVK-ILDENGNEVPRGVVGRI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2328 YIGGQCLARGYL-GRPGQTAERFVAdpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:PRK07788 406 FVGNGFPFEGYTdGRDKQIIDGLLS------------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2407 YVAEAAVVALDGVG-GPLLAAYLV-GRDAMRGEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVD 2483
Cdd:PRK07788 474 DVVEAAVIGVDDEEfGQRLRAFVVkAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
3040-3525 |
6.20e-29 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 126.45 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEER-----LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA 3114
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 YVPVDPEYPEERQAYMLEDSGVELLLSQ-------------SHLKLPLAQ--GVQRIDLDRGAP-----------WFEDY 3168
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQcpTVEKVVVVRHLGndftpakgrdlSYDEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3169 SEANPD--IHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 3245
Cdd:cd05968 223 KETAGDgaERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFL--QDEDVA--SCTSLKRIVCSGEALPADAQQQVF--- 3316
Cdd:cd05968 303 GATMVLydGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNahDLSSLRVLGSTGEPWNPEPWNWLFetv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3317 --AKLPqagLYNLYGPTEAAIDVTHWTCVEEGKdAVPIGRPIANLACYILDGNLEPVPvGVLGELYLAGQ--GLARGYHQ 3392
Cdd:cd05968 382 gkGRNP---IINYSGGTEISGGILGNVLIKPIK-PSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWR 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3393 RPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----D 3468
Cdd:cd05968 457 DE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVphpvK 532
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3469 GRQLVGYVVLE---SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05968 533 GEAIVCFVVLKpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
4563-5037 |
8.09e-29 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 123.40 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLpipeglsclsvdreeewagfpAHDPEVALhgdnlayviYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05973 81 ANRHKL---------------------DSDPFVMM---------FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 celhfmSFaFDGSHEGWMH--------PLINGARVLIRDDSlWLPERTYAEMHRHGVT-VGVFPPVYLQQLAEHAERD-- 4791
Cdd:cd05973 131 ------SF-WNAADPGWAYglyyaitgPLALGHPTILLEGG-FSVESTWRVIERLGVTnLAGSPTAYRLLMAAGAEVPar 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4792 -----------GNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVvtpllwkaRAGDAcGAAyMPigtllG 4860
Cdd:cd05973 203 pkgrlrrvssaGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPV--------HAGSA-GRA-MP-----G 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4861 NRSGyILDGQLNLLPVGVAGELYLGgegVARGylerPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:cd05973 268 WRVA-VLDDDGDELGPGEPGRLAID---IANS----PLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqLKTALRERLPEYMVPSH 5020
Cdd:cd05973 340 ITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADE----LQLHVKKRLSAHAYPRT 415
|
490
....*....|....*..
gi 2310915810 5021 LLFLARMPLTPNGKLDR 5037
Cdd:cd05973 416 IHFVDELPKTPSGKIQR 432
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
3030-3525 |
8.16e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 125.54 E-value: 8.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3030 TAAEYPL-QRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAI 3108
Cdd:PRK06178 24 REPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLkLPLAQGVQ---RI---------------------DLDRGA-- 3162
Cdd:PRK06178 104 LKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQVRaetSLrhvivtsladvlpaeptlplpDSLRAPrl 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3163 ---------PWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG---DTVLqktpf 3230
Cdd:PRK06178 183 aaagaidllPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVggeDSVF----- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3231 sfdVSVWEFFW----------PLMSGARLVVAApgdhR-DPAKLVALINREGVDTL-----HFVPSMLQAFLQDEDVasc 3294
Cdd:PRK06178 255 ---LSFLPEFWiagenfgllfPLFSGATLVLLA----RwDAVAFMAAVERYRVTRTvmlvdNAVELMDHPRFAEYDL--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3295 TSLKRIVCSG--EALPADAQQQvFAKLPQAGLYNL-YGPTEaaidvTH----WTCVEEGKD------AVPIGRPIANLAC 3361
Cdd:PRK06178 325 SSLRQVRVVSfvKKLNPDYRQR-WRALTGSVLAEAaWGMTE-----THtcdtFTAGFQDDDfdllsqPVFVGLPVPGTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3362 YILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLR 3440
Cdd:PRK06178 399 KICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3441 GLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPaQWLALERMPLSP 3516
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPdpdkGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTA 550
|
....*....
gi 2310915810 3517 NGKLDRKAL 3525
Cdd:PRK06178 551 TGKVRKQDL 559
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
4534-5034 |
8.33e-29 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 124.33 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHqrvAERARMA-PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:cd12118 3 PLTPLSF---LERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAhlllthshllerlpipeglSCLSVDREEEW-----AGFPAHDPEVALHGDNLAYVIY 4687
Cdd:cd12118 80 VLNALNTRLDAEEIAFILRHSEA-------------------KVLFVDREFEYedllaEGDPDFEWIPPADEWDPIALNY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDSlwlPERTYAEM 4766
Cdd:cd12118 141 TSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPmFHCNGWCFPWTVAAVGGTNVCLRKVD---AKAIYDLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4767 HRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYdLAWRALKPKYLFNGYGPTET--VVTPLLW---- 4840
Cdd:cd12118 218 EKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAV-LAKMEELGFDVTHVYGLTETygPATVCAWkpew 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 -----------KARAGdacgaayMPIGTLLGNRsgyILDGQLnLLPV---GV-AGELYLGGEGVARGYLERPALTAERFv 4905
Cdd:cd12118 297 delpteerarlKARQG-------VRYVGLEEVD---VLDPET-MKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAF- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4906 pdpfgAPGsrLYRSGDLtrgradGVVDYLGRVdhQVKIR--------GFRIELGEIEARLREHPAVREAVVVAQPGAV-G 4976
Cdd:cd12118 365 -----RGG--WFHSGDL------AVIHPDGYI--EIKDRskdiiisgGENISSVEVEGVLYKHPAVLEAAVVARPDEKwG 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4977 QQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPSHLLFLaRMPLTPNGK 5034
Cdd:cd12118 430 EVPCAFVELKEGAKVTEEEIIAFC--------REHLAGFMVPKTVVFG-ELPKTSTGK 478
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
4559-5038 |
8.78e-29 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 123.47 E-value: 8.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLL 4638
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 lthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEM 4718
Cdd:cd05907 82 ------------------------------------FVEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4719 TPEDCELHFMSFAFDGSHEGWMH-PLINGARV-------LIRDDS-------------LWlpERTYAEMHRHGVTVGvfp 4777
Cdd:cd05907 126 TEGDRHLSFLPLAHVFERRAGLYvPLLAGARIyfassaeTLLDDLsevrptvflavprVW--EKVYAAIKVKAVPGL--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 pvyLQQLAEHAERDGnpppVRVYCFGGDAVAQasyDLA--WRALK-PkyLFNGYGPTET--VVTPLLWKARAGDACGAAY 4852
Cdd:cd05907 201 ---KRKLFDLAVGGR----LRFAASGGAPLPA---ELLhfFRALGiP--VYEGYGLTETsaVVTLNPPGDNRIGTVGKPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 MPIGtllgnrsgyildgqlnlLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVD 4932
Cdd:cd05907 269 PGVE-----------------VRIADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLH 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ------------PGAVGQQLVGYVVAQEPAV--ADSPEAQ 4997
Cdd:cd05907 325 ITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVIGDgrpflvalivpdPEALEAWAEEHGIAYTDVAelAANPAVR 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2310915810 4998 AECRAQLKTALrERLPEYMVPSHLLFLARMP------LTPNGKLDRK 5038
Cdd:cd05907 405 AEIEAAVEAAN-ARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRP 450
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
2001-2487 |
9.35e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.15 E-value: 9.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGDEhLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK09088 11 RLAAVDLALGRR-WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETLAERLPCPAEVERLPLETAAwPASADTRPLPEvagETLAYVIYTSGSTGQPKGVAVSQAALvahcQ 2160
Cdd:PRK09088 90 LQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADA-LEPADTPSIPP---ERVSLILFTSGTSGQPKGVMLSERNL----Q 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2161 AAARTYGV-GPGDcqlqfASISFDAAAEQLFV--------PLLA-GARVLLGDAGQWSA--QHLADEVerHAVTILDLPP 2228
Cdd:PRK09088 162 QTAHNFGVlGRVD-----AHSSFLCDAPMFHIiglitsvrPVLAvGGSILVSNGFEPKRtlGRLGDPA--LGITHYFCVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2229 aylqQQAEELRH----AGRRIAVRTCILGGEAWDAslltqqAVQAEAWFNA-------YGPTEA-VITPLAWHCRAQEGG 2296
Cdd:PRK09088 235 ----QMAQAFRAqpgfDAAALRHLTALFTGGAPHA------AEDILGWLDDgipmvdgFGMSEAgTVFGMSVDCDVIRAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQV 2376
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2377 EYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYM 2455
Cdd:PRK09088 378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMaDAQWGEVGYLAIVPADGAPLD--LERIRSHLSTRLAKYK 455
|
490 500 510
....*....|....*....|....*....|..
gi 2310915810 2456 QPTAWQVLSSLPLNANGKLDRKALPKVDAAAR 2487
Cdd:PRK09088 456 VPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1994-2481 |
1.00e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 124.86 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVcgDEHLS---YAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:PRK06087 29 WQQTARAMPDKIAVV--DNHGAsytYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLICQETLAER------LPCPAEV---ERLPLETAAWPAS---------ADTRPL---PEVAG 2129
Cdd:PRK06087 107 SWREAELVWVLNKCQAKMFFAPTLFKQTrpvdliLPLQNQLpqlQQIVGVDKLAPATsslslsqiiADYEPLttaITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsfdAAAEQLF----VPLLAGARVLLGDag 2205
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPL---GHATGFLhgvtAPFLIGARSVLLD-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADEVERHAVT--------ILDLPPAyLQQQAEELRhagrriAVRTCILGGeAWDASLLTQQAVQAEAWF-NAY 2276
Cdd:PRK06087 262 IFTPDACLALLEQQRCTcmlgatpfIYDLLNL-LEKQPADLS------ALRFFLCGG-TTIPKKVARECQQRGIKLlSVY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2277 GPTEA---VITPLAwHCRAQEGGAPaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADP 2353
Cdd:PRK06087 334 GSTESsphAVVNLD-DPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 FsgsgerlYRTGDLARYRVDGQVEYLGRaDQQIKIRGFR-IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK06087 411 W-------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMpDERLGERSCAYVVLK 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 2432 DAMRG---EDLLAELRTwlaGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:PRK06087 483 APHHSltlEEVVAFFSR---KRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1554-1956 |
1.49e-28 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 122.53 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLF-HSLHGTEGDYvN---QLRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLEL 1629
Cdd:cd19540 3 PLSFAQQRLWFlNRLDGPSAAY-NiplALRLT-GALDVDALRAALADVVARHESLRTVFPEDDG--GPYQVVLPAAEARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RLAPPGSDPQRQAEAEREA---GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAgqevAATV 1706
Cdd:cd19540 79 DLTVVDVTEDELAARLAEAarrGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYA----ARRA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1707 GR----------YRDYIGWlQgRDAMATEF-----------FWRDRLA----SLEMPTRLARQARTEQPGqGEHLRELDP 1761
Cdd:cd19540 155 GRapdwaplpvqYADYALW-Q-RELLGDEDdpdslaarqlaYWRETLAglpeELELPTDRPRPAVASYRG-GTVEFTIDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1762 QTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADY 1841
Cdd:cd19540 232 ELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFVNTLVLRTDVSGDPTFAEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1842 LQGMQALNLALREHEHTP------LYDIQRWAGHggEALFDSILVFENFPVAE-------------ALRQAPADLEFSTP 1902
Cdd:cd19540 310 LARVRETDLAAFAHQDVPferlveALNPPRSTAR--HPLFQVMLAFQNTAAATlelpgltvepvpvDTGVAKFDLSFTLT 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 1903 SNHEQTNYPLTLGVTLgerlslqyVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19540 388 ERRDADGAPAGLTGEL--------EYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
539-998 |
3.11e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 123.32 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 K--------LPLAQGVQRID----LDQA-----DAWLENHAENNPGIE----LNGENLAYVIYTSGSTGKPKGAGNRHsa 677
Cdd:PRK06087 132 KqtrpvdliLPLQNQLPQLQqivgVDKLapatsSLSLSQIIADYEPLTtaitTHGDELAAVLFTSGTEGLPKGVMLTH-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 678 lsNRLCWMQQAYGLGVG----DTVLQKTPFSFDVSvweFFW----PLMSGARLVVAapgDHRDPAKLVELINREGVDTLH 749
Cdd:PRK06087 210 --NNILASERAYCARLNltwqDVFMMPAPLGHATG---FLHgvtaPFLIGARSVLL---DIFTPDACLALLEQQRCTCML 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 750 ----FVPSMLQAFlqDEDVASCTSLKRIVCSGEALPADAQQQVFaklpQAG--LYNLYGPTEAA--IDVTHWTCVEEGKD 821
Cdd:PRK06087 282 gatpFIYDLLNLL--EKQPADLSALRFFLCGGTTIPKKVARECQ----QRGikLLSVYGSTESSphAVVNLDDPLSRFMH 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 822 TVpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIE 901
Cdd:PRK06087 356 TD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------EGWYYSGDLCRMDEAGYIK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 902 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGG--DWREALAAHLAASLPEYMV 975
Cdd:PRK06087 428 ITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPderlGERSCAYVVLKAPHHslTLEEVVAFFSRKRVAKYKY 507
|
490 500
....*....|....*....|...
gi 2310915810 976 PAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06087 508 PEHIVVIDKLPRTASGKIQKFLL 530
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
4553-5040 |
3.27e-28 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 121.43 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4553 AVAVIFDEEKLTYAELDSRANRLAHALIARGVG-PEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQ 4631
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4632 DSRAHLLlthshllerlpipeglscLSVDREEewagfpahdpevalHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAhiva 4711
Cdd:cd05958 81 KARITVA------------------LCAHALT--------------ASDDICILAFTSGTTGAPKATMHFHRDPLA---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4712 TGERY-----EMTPED--CELH--FMSFAFDGShegWMHPLINGARVLIrddslwLPERTYAEM----HRHGVTVGVFPP 4778
Cdd:cd05958 125 SADRYavnvlRLREDDrfVGSPplAFTFGLGGV---LLFPFGVGASGVL------LEEATPDLLlsaiARYKPTVLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 VYLQQLAEH---AERDGNPppVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVvtPLLWKARAGDA-CGAAYMP 4854
Cdd:cd05958 196 TAYRAMLAHpdaAGPDLSS--LRKCVSAGEALPAALHR-AWKEATGIPIIDGIGSTEMF--HIFISARPGDArPGATGKP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IgtllgnrSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTaerFVPDPFGAPGSRLYRSgdltrgrADGVV 4931
Cdd:cd05958 271 V-------PGYeakVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRT---YVQGGWNITGDTYSRD-------PDGYF 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4932 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqLKTALRER 5011
Cdd:cd05958 334 RHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARE----LQDHAKAH 409
|
490 500
....*....|....*....|....*....
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05958 410 IAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
2002-2479 |
3.61e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 122.66 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRAR-GVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQET---LAERLPCPAEVERlPLETAAWPASADTRPLP-EVAGETLAYVI-YTSGSTGQPKGVAVSQAAL 2155
Cdd:PRK06839 96 LKDSGTTVLFVEKTfqnMALSMQKVSYVQR-VISITSLKEIEDRKIDNfVEKNESASFIIcYTSGTTGKPKGAVLTQENM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2156 VAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQLFV--PLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:PRK06839 175 FWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIV--PRKFEPTKALSMIEKHKVTVVMGVPTIHQA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 QAEELRHAGRRI-AVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACIL 2312
Cdd:PRK06839 252 LINCSKFETTNLqSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERfVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:PRK06839 332 DENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW-------LCTGDLARVDEDGFVYIVGRKKEMIISGGEN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2393 IEIGEIESQLLAHPYVAEAAVVALDGV--GGPLLAAYLVGRDAMRGEdllAELRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:PRK06839 404 IYPLEVEQVINKLSDVYEVAVVGRQHVkwGEIPIAFIVKKSSSVLIE---KDVIEHCRLFLAKYKIPKEIVFLKELPKNA 480
|
....*....
gi 2310915810 2471 NGKLDRKAL 2479
Cdd:PRK06839 481 TGKIQKAQL 489
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
4543-5041 |
3.76e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 123.11 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK07788 55 VAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCLSV------DREEEWAGFPAHDPEVALHGDNLA--------YVIY 4687
Cdd:PRK07788 135 GPQLAEVAAREGVKALVYDDEFTDLLsALPPDLGRLRAwggnpdDDEPSGSTDETLDDLIAGSSTAPLpkppkpggIVIL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAHIVA--------TGERYEMTpedcelhfmSFAFDGSheGWMHPLIN---GARVLIRDDsl 4756
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLAPLAGllsrvpfrAGETTLLP---------APMFHAT--GWAHLTLAmalGSTVVLRRR-- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 WLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVR----VYCFGgdavAQASYDLAWRALKP--KYLFNGYGP 4830
Cdd:PRK07788 282 FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSslkiIFVSG----SALSPELATRALEAfgPVLYNLYGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4831 TE----TVVTPLLWKARAGDAcGAAymPIGTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYlerpalTAERfvp 4906
Cdd:PRK07788 358 TEvafaTIATPEDLAEAPGTV-GRP--PKGVTVK-----ILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 DPFGAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVA 4985
Cdd:PRK07788 421 DKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDeEFGQRLRAFVVK 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4986 QEPAVADSPEaqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:PRK07788 499 APGAALDEDA--------IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
521-960 |
3.78e-28 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 123.12 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 521 VERTPTAPALAF------GEERLDYAELNRRANRLAHALIERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DP 593
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 EYPE--ERQAYMLEDSGVQLLLSQS-HLKLPLAQGVQRIDLDQ-----ADAWLENHAENNPGIELNGENLAYVIYTSGST 665
Cdd:cd05931 82 TPGRhaERLAAILADAGPRVVLTTAaALAAVRAFAASRPAAGTprllvVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 666 GKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARLVVAAPGDH-RDPAKLVELINRE 743
Cdd:cd05931 162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPAAFlRRPLRWLRLISRY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 744 GVdTLHFVPSMlqAF------LQDEDVAS--CTSLKRIVCSGEalPADAQQ-----QVFAK--LPQAGLYNLYGPTEAAI 808
Cdd:cd05931 242 RA-TISAAPNF--AYdlcvrrVRDEDLEGldLSSWRVALNGAE--PVRPATlrrfaEAFAPfgFRPEAFRPSYGLAEATL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 809 DVTH---WTCV---------------------EEGKDTVPIGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGY 863
Cdd:cd05931 317 FVSGgppGTGPvvlrvdrdalagravavaaddPAARELVSCGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 864 HQRPGLTAERFVASPFVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE--AAVLAV 940
Cdd:cd05931 397 WGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPgcVAAFSV 475
|
490 500
....*....|....*....|
gi 2310915810 941 DGRQLVGYVVLESEGGDWRE 960
Cdd:cd05931 476 PDDGEERLVVVAEVERGADP 495
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
4547-5042 |
6.84e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 122.30 E-value: 6.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEK--LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRE 4624
Cdd:PRK05852 26 ATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4625 RLLYMMQ--DSRAHLLLTHSHLLERLPI----PEGLSCLSVDREEEWAGFPAHDPEVALH---------GDNLAYVIYTS 4689
Cdd:PRK05852 106 EQRVRSQaaGARVVLIDADGPHDRAEPTtrwwPLTVNVGGDSGPSGGTLSVHLDAATEPTpatstpeglRPDDAMIMFTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAF-DGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR 4768
Cdd:PRK05852 186 GTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHgHGLIAALLATLASGGAVLLPARGRFSAHTFWDDIKA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 HGVTVGVFPPVYLQQLAEHA--ERDGN-PPPVR-VYCFGGDAVAQASYDLAWRALKPkyLFNGYGPTET---VVTPLLWK 4841
Cdd:PRK05852 266 VGATWYTAVPTIHQILLERAatEPSGRkPAALRfIRSCSAPLTAETAQALQTEFAAP--VVCAFGMTEAthqVTTTQIEG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 ARAGDACGAAYMPIGTLLGNRSGYI-LDGQLnlLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSG 4920
Cdd:PRK05852 344 IGQTENPVVSTGLVGRSTGAQIRIVgSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--------RTG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAE 4999
Cdd:PRK05852 414 DLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLyGEAVAAVIVPRESAPPTAEELVQF 493
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 5000 CraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK05852 494 C--------RERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
4553-5035 |
7.20e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 121.55 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4553 AVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQD 4632
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4633 SRAHLLLTHSHLLERL-----PIPEGLSCLSVDRE--------EEW-AGFPAHDPEVALHGDNLAyviYTSGSTGMPKGV 4698
Cdd:PRK08276 82 SGAKVLIVSAALADTAaelaaELPAGVPLLLVVAGpvpgfrsyEEAlAAQPDTPIADETAGADML---YSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 --AVSHGPliahivatgeryEMTPEDCELHFMSFAFDGSHE---------------GW-MHPLINGARVLIRDDslWLPE 4760
Cdd:PRK08276 159 krPLPGLD------------PDEAPGMMLALLGFGMYGGPDsvylspaplyhtaplRFgMSALALGGTVVVMEK--FDAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4761 RTYAEMHRHGVTVGVFPP---VYLQQLaehaerdgnPPPVRvycfggdavaqASYDL-----AWRALKP------KYLFN 4826
Cdd:PRK08276 225 EALALIERYRVTHSQLVPtmfVRMLKL---------PEEVR-----------ARYDVsslrvAIHAAAPcpvevkRAMID 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4827 GYGP--------TE----TVVTPLLWKARAGDACGAAympIGTLLgnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:PRK08276 285 WWGPiiheyyasSEgggvTVITSEDWLAHPGSVGKAV---LGEVR------ILDEDGNELPPGEIGTVYFEMDGYPFEYH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4895 ERPALTAERFVPDpfgapgsRLYRSGDLTRGRADGvvdYL---GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:PRK08276 356 NDPEKTAAARNPH-------GWVTVGDVGYLDEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGV 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4972 PGA-VGQQLVGYVvaqEPavADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK08276 426 PDEeMGERVKAVV---QP--ADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
4682-5038 |
1.08e-27 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 117.43 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELhfmsFAFDGSHEGWMHPLIngaRVLIRDDSLWLPER 4761
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL----LSLPLYHVGGLAILV---RSLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4762 TYA---EMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVaqaSYDLAWRALKPKY-LFNGYGPTETVVTP 4837
Cdd:cd17630 75 NQAlaeDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPI---PPELLERAADRGIpLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4838 LLWKARAGDACGaaympigtllgnrSGYILDG-QLNLLPvgvAGELYLGGEGVARGYLERPaltaerfVPDPFGAPGsrL 4916
Cdd:cd17630 152 ATKRPDGFGRGG-------------VGVLLPGrELRIVE---DGEIWVGGASLAMGYLRGQ-------LVPEFNEDG--W 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAvadspe 4995
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEeLGQRPVAVIVGRGPA------ 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2310915810 4996 aqaeCRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:cd17630 281 ----DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
3048-3487 |
1.28e-27 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 121.58 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAF------GEERLDYAELNRRANRLAHALIERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DP 3120
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPE--ERQAYMLEDSGVELLLSQS-HLKLPLAQGVQRIDLDRGAPWFEDYSEAN-----PDIHLDGENLAYVIYTSGST 3192
Cdd:cd05931 82 TPGRhaERLAAILADAGPRVVLTTAaALAAVRAFAASRPAAGTPRLLVVDLLPDTsaadwPPPSPDPDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3193 GKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARLVVAAPGDH-RDPAKLVALINRE 3270
Cdd:cd05931 162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPAAFlRRPLRWLRLISRY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVdTLHFVPSMlqAF------LQDEDVAS--CTSLKRIVCSGEalPADAQQ-----QVFAK--LPQAGLYNLYGPTEAAI 3335
Cdd:cd05931 242 RA-TISAAPNF--AYdlcvrrVRDEDLEGldLSSWRVALNGAE--PVRPATlrrfaEAFAPfgFRPEAFRPSYGLAEATL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTC---------------------VEEGKDAVPI---GRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGY 3390
Cdd:cd05931 317 FVSGGPPgtgpvvlrvdrdalagravavAADDPAARELvscGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3391 HQRPGLTAERFVASPFVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE--AAVLAV 3467
Cdd:cd05931 397 WGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPgcVAAFSV 475
|
490 500
....*....|....*....|
gi 2310915810 3468 DGRQLVGYVVLESESGDWRE 3487
Cdd:cd05931 476 PDDGEERLVVVAEVERGADP 495
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
2585-3005 |
1.33e-27 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 119.34 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTILANMPLRIVLE 2663
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2664 DCAGAS---EATLRQRVAEEIRQP-FDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19547 83 DWSGEDpdrRAELLERLLADDRAAgLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKlQYADYAAWHRAWLDSGEGARQldYWRERLG--AEQPVLELPADRvrpaqaSGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19547 163 EPQLSPCR-PYRDYVRWIRARTAQSEESER--FWREYLRdlTPSPFSTAPADR------EGEFDTVVHEFPEQLTRLVNE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANR--NRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAA 2895
Cdd:cd19547 234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2896 LGAQAHQDLPFEQLVDALQPERnLSHSPLFQVMYNHQSGERQDAQVDGLHIESfawdgaaaqFDL-ALDTWETPDG---- 2970
Cdd:cd19547 314 ATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQI---------IDLhAQEKTEYPIGlivl 383
|
410 420 430
....*....|....*....|....*....|....*....
gi 2310915810 2971 ----LGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19547 384 plqkLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
4552-5048 |
1.66e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 121.54 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4552 DAVAVIF----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL---DIEYP-R 4623
Cdd:PRK04319 59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeaFMEEAvR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLlymmQDSRAHLLLTHSHLLERLPIPEgLSCLS----VDREEE--------WAGFPAHDPE---VALHGDNLAYVIYT 4688
Cdd:PRK04319 139 DRL----EDSEAKVLITTPALLERKPADD-LPSLKhvllVGEDVEegpgtldfNALMEQASDEfdiEWTDREDGAILHYT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGPLIAHiVATGeRY--EMTPEDCelhFMSFAfD-----GSHEGWMHPLINGARVLIrDDSLWLPER 4761
Cdd:PRK04319 214 SGSTGKPKGVLHVHNAMLQH-YQTG-KYvlDLHEDDV---YWCTA-DpgwvtGTSYGIFAPWLNGATNVI-DGGRFSPER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4762 TYAEMHRHGVTVGVFPPVYLQQL----AEHAER-D----------GNPPPVRVYCFGGDAVAQASYDLAWRalkpkylfn 4826
Cdd:PRK04319 287 WYRILEDYKVTVWYTAPTAIRMLmgagDDLVKKyDlsslrhilsvGEPLNPEVVRWGMKVFGLPIHDNWWM--------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4827 gygpTETvvtpllwkaragdacGA------AYMPI-----GTLLGNRSGYILDGQLNLLPVGVAGELYL--GGEGVARGY 4893
Cdd:PRK04319 358 ----TET---------------GGimianyPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGI 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4894 LERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG 4973
Cdd:PRK04319 419 WNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4974 AVGQQLVGYVVAQEPAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKLDRK-------GLPQPDAS 5046
Cdd:PRK04319 491 PVRGEIIKAFVALRPGYEPSEELKEEIRGF----VKKGLGAHAAPREIEFKDKLPKTRSGKIMRRvlkawelGLPEGDLS 566
|
..
gi 2310915810 5047 LL 5048
Cdd:PRK04319 567 TM 568
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
2002-2479 |
2.37e-27 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 119.21 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK09029 17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICqetlAERLPCPAEVERLPLETAAWPASADTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAalvAHCQA 2161
Cdd:PRK09029 97 PSLTLDFALV----LEGENTFSALTSLHLQLVEGAHAVAWQP------QRLATMTLTSGSTGLPKAAVHTAQ---AHLAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AArtyGVgpgdCQLqfasISFDAAAEQLF-VP-------------LLAGARVLLGDagqwsAQHLADEVErhAVTILDLP 2227
Cdd:PRK09029 164 AE---GV----LSL----MPFTAQDSWLLsLPlfhvsgqgivwrwLYAGATLVVRD-----KQPLEQALA--GCTHASLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2228 PAYLQQQaeeLRHAGRRIAVRTCILGGEAWDASlLTQQAVQA--EAWFnAYGPTEAVITPlawhCRAQEGGAPAIGRALG 2305
Cdd:PRK09029 226 PTQLWRL---LDNRSEPLSLKAVLLGGAAIPVE-LTEQAEQQgiRCWC-GYGLTEMASTV----CAKRADGLAGVGSPLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDaalqpcapgmiGELYIGGQCLARGYLgRPGQTAerfvadPFSGSgERLYRTGDLARYRvDGQVEYLGRADQQ 2385
Cdd:PRK09029 297 GREVKLVD-----------GEIWLRGASLALGYW-RQGQLV------PLVND-EGWFATRDRGEWQ-NGELTILGRLDNL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVALDgvggpllaaylvgrDAMRG-----------EDLLAELRTWLAGRLPAY 2454
Cdd:PRK09029 357 FFSGGEGIQPEEIERVINQHPLVQQVFVVPVA--------------DAEFGqrpvavvesdsEAAVVNLAEWLQDKLARF 422
|
490 500
....*....|....*....|....*
gi 2310915810 2455 MQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK09029 423 QQPVAYYLLPPELKNGGIKISRQAL 447
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
503-998 |
3.38e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 120.53 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 503 TAAEYPL-QRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 581
Cdd:PRK06178 24 REPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 582 LKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLkLPLAQGVQ---------------------------------R 628
Cdd:PRK06178 104 LKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQVRaetslrhvivtsladvlpaeptlplpdslraprL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 629 IDLDQAD--AWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG---DTVLqktpf 703
Cdd:PRK06178 183 AAAGAIDllPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVggeDSVF----- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 704 sfdVSVWEFFW----------PLMSGARLVVAApgdhR-DPAKLVELINREGVDTL-----HFVPSMLQAFLQDEDVasc 767
Cdd:PRK06178 255 ---LSFLPEFWiagenfgllfPLFSGATLVLLA----RwDAVAFMAAVERYRVTRTvmlvdNAVELMDHPRFAEYDL--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 768 TSLKRIVCSG--EALPADAQQQvFAKLPQAGLYNL-YGPTEaaidvTHwTCveegkDT----------------VPIGRP 828
Cdd:PRK06178 325 SSLRQVRVVSfvKKLNPDYRQR-WRALTGSVLAEAaWGMTE-----TH-TC-----DTftagfqdddfdllsqpVFVGLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 829 IGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRID 907
Cdd:PRK06178 393 VPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPaQWLALE 983
Cdd:PRK06178 466 EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPdpdkGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVD 544
|
570
....*....|....*
gi 2310915810 984 RMPLSPNGKLDRKAL 998
Cdd:PRK06178 545 ALPMTATGKVRKQDL 559
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
513-1000 |
4.00e-27 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 120.67 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 513 VHRLFEEQVERTPTAPALAFGEER-----LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA 587
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 588 YVPVDPEYPEERQAYMLEDSGVQLLLSQ-------------SHLKLPLAQ--GVQRI--------DLDQADA----WLEN 640
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQcpTVEKVvvvrhlgnDFTPAKGrdlsYDEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 641 HAENNPGIE-LNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:cd05968 223 KETAGDGAErTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 719 GARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVA--SCTSLKRIVCSGEALPADAQQQVF--- 789
Cdd:cd05968 303 GATMVLydGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNahDLSSLRVLGSTGEPWNPEPWNWLFetv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 790 --AKLPqagLYNLYGPTEAAIDVTHWTCVEEGKdtvPIG--RPIGNLGCYILDGNLEPVPvGVLGELYLAGR--GLARGY 863
Cdd:cd05968 382 gkGRNP---IINYSGGTEISGGILGNVLIKPIK---PSSfnGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 864 HQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--- 940
Cdd:cd05968 455 WRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVphp 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 941 -DGRQLVGYVVLE---SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:cd05968 531 vKGEAIVCFVVLKpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1997-2482 |
4.43e-27 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 120.82 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1997 QVASAPEAIALVC-GDE-----HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:TIGR02188 66 HLEARPDKVAIIWeGDEpgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLIC-----------------QETLAErlpCPAEVE------RLPLETAAW------------ 2115
Cdd:TIGR02188 146 GFSAEALADRINDAGAKLVITadeglrggkviplkaivDEALEK---CPVSVEhvlvvrRTGNPVVPWvegrdvwwhdlm 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2116 -PASADTRPLPeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQlqfASI------SFda 2184
Cdd:TIGR02188 223 aKASAYCEPEP-MDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKyVFDIKDGDifwCT---ADVgwitghSY-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2185 aaeQLFVPLLAGARVLL-------GDAGQWsaqhlADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRtcILGG 2254
Cdd:TIGR02188 297 ---IVYGPLANGATTVMfegvptyPDPGRF-----WEIIEKHKVTIFYTAPTairALMRLGDEWVKKHDLSSLR--LLGS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 -------EAWDaslltqqavqaeaWFN------------AYGPTE---AVITPLAwhcraqeGGAPA----IGRALGARR 2308
Cdd:TIGR02188 367 vgepinpEAWM-------------WYYkvvgkercpivdTWWQTEtggIMITPLP-------GATPTkpgsATLPFFGIE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPC-APGMIGELYIG----GQclARGYLGRPgqtaERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLG 2380
Cdd:TIGR02188 427 PAVVDEEGNPVeGPGEGGYLVIKqpwpGM--LRTIYGDH----ERFVDtyfSPFPG----YYFTGDGARRDKDGYIWITG 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2381 RADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPT 2458
Cdd:TIGR02188 497 RVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGiPDDIKGQAIYAFVTLKDGYEpDDELRKELRKHVRKEIGPIAKPD 576
|
570 580
....*....|....*....|....
gi 2310915810 2459 AWQVLSSLPLNANGKLDRKALPKV 2482
Cdd:TIGR02188 577 KIRFVPGLPKTRSGKIMRRLLRKI 600
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2014-2479 |
5.22e-27 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 120.29 E-value: 5.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAER--------------LPCPAeVERLPLE----TAAWPASADTRPLPEV-------AGETLA----YVIYTSGSTGQ 2144
Cdd:cd05968 172 GFTRRgrevnlkeeadkacAQCPT-VEKVVVVrhlgNDFTPAKGRDLSYDEEketagdgAERTESedplMIIYTSGTTGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2145 PKG-VAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLL--GDAGQWSAQHLADEVERHAV 2221
Cdd:cd05968 251 PKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydGAPDHPKADRLWRMVEDHEI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2222 TILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDAslltqqavQAEAWF------------NAYGPTE------ 2280
Cdd:cd05968 331 THLGLSPTLiraLKPRGDAPVNAHDLSSLRVLGSTGEPWNP--------EPWNWLfetvgkgrnpiiNYSGGTEisggil 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2281 --AVITPLAwhcraqeggAPAIGRALGARRACILDAALQPcAPGMIGEL-----YIGgqcLARGYLGRPgqtaERFVADP 2353
Cdd:cd05968 403 gnVLIKPIK---------PSSFNGPVPGMKADVLDESGKP-ARPEVGELvllapWPG---MTRGFWRDE----DRYLETY 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 FSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD 2432
Cdd:cd05968 466 WS-RFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVpHPVKGEAIVCFVVLKP 544
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2310915810 2433 AMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05968 545 GVTpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
3043-3532 |
1.13e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 118.69 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLK---------------LPLAQGVQRIDLDRGA---PWFEDYSEAnPDIHL------- 3177
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVVWPGFKgidfaailaavppdaLPPLRAIAVVDDAADAtpaPAPGARVQL-FALPDpappaaa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 ----DGENLAYVIY-TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVA 3252
Cdd:PRK06164 174 geraADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3253 apgDHRDPAKLVALINREGVDtlHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGP 3330
Cdd:PRK06164 254 ---PVFDAARTARALRRHRVT--HTFGNdeMLRRILDTAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAIDVTHWTCVEEGKD-AVPIGRPIANLA----CYILDGNLepVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP 3405
Cdd:PRK06164 329 SEVQALVALQPATDPVSVrIEGGGRPASPEArvraRDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3406 FvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR-QLVGYVVLES-E 3481
Cdd:PRK06164 407 Y------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrDGKtVPVAFVIPTDgA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3482 SGDWREALAAHLAASLPeYMVPAQWLALERMP--LSPNGKLDRKALPRPQAAA 3532
Cdd:PRK06164 481 SPDEAGLMAACREALAG-FKVPARVQVVEAFPvtESANGAKIQKHRLREMAQA 532
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
3054-3534 |
1.28e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 117.70 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3133
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3134 SGVELLLSQSHLKLPLAQ-------GVQRIDLDRGA-PWFEDYSE---ANPDIHLDGENLAYV-IYTSGSTGKPKG---- 3197
Cdd:PRK08276 82 SGAKVLIVSAALADTAAElaaelpaGVPLLLVVAGPvPGFRSYEEalaAQPDTPIADETAGADmLYSSGTTGRPKGikrp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3198 -AGNRHSALSNRLCWMQQAYGLGVGDTV------LQKT-PFSFDVSVweffwpLMSGARLVVAapgDHRDPAKLVALINR 3269
Cdd:PRK08276 162 lPGLDPDEAPGMMLALLGFGMYGGPDSVylspapLYHTaPLRFGMSA------LALGGTVVVM---EKFDAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3270 EGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEaAIDVTHWTCV 3343
Cdd:PRK08276 233 YRVTHSQLVPTMFVRMLKlPEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWW---GpiIHEYYASSE-GGGVTVITSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3344 EEGKDAVPIGRP-IANLAcyILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYR 3422
Cdd:PRK08276 309 DWLAHPGSVGKAvLGEVR--ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT------VGDVGYLD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3423 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV----------VLESESGDWREA 3488
Cdd:PRK08276 381 EDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPdeemGERVKAVVqpadgadagdALAAELIAWLRG 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 3489 LAAHlaaslpeYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQ 3534
Cdd:PRK08276 461 RLAH-------YKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQ 499
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2014-2479 |
1.30e-26 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 116.51 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPldpnypaerlaymlrdsgarwlicqe 2093
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlAERLPCPAEV-ERLPLETAAWPASADTrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD 2172
Cdd:cd05974 55 --ATTLLTPDDLrDRVDRGGAVYAAVDEN-----THADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2173 CQLQFASISFDAAA-EQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEElRHAGRRIAVRTCI 2251
Cdd:cd05974 128 VHWNISSPGWAKHAwSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ-DLASFDVKLREVV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LGGEAWDASLLTQqaVQAeAW----FNAYGPTEAviTPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGeL 2327
Cdd:cd05974 207 GAGEPLNPEVIEQ--VRR-AWgltiRDGYGQTET--TALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-L 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2328 YIGGQ---CLARGYLGRPGQTAErfvadpfsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05974 281 DLGDTrpvGLMKGYAGDPDKTAH--------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIE 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2405 HPYVAEAAVV-ALDGVGGPLLAAYLVGRD-AMRGEDLLAELRTWLAGRLPAYMQPTAWQvLSSLPLNANGKLDRKAL 2479
Cdd:cd05974 353 HPAVAEAAVVpSPDPVRLSVPKAFIVLRAgYEPSPETALEIFRFSRERLAPYKRIRRLE-FAELPKTISGKIRRVEL 428
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
4541-5040 |
1.44e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 118.46 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIF----------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLlthshllerLPIPEG--------------LSCLSVDREEEWAGF-------- 4668
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAF---------IGIPKAhlarrlfgwgkpsvRRLVTVGGRLLWGGTtlatllrd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4669 -PAHDPEVA-LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELH-FMSFAFdgshegwmHPLIN 4745
Cdd:PRK09274 161 gAAAPFPMAdLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtFPLFAL--------FGPAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4746 GARVLIRD---------DslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPV--RVYCFGgdAVAQASYDL 4814
Cdd:PRK09274 233 GMTSVIPDmdptrpatvD----PAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSlrRVISAG--APVPIAVIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4815 AWRALKPKY--LFNGYGPTE----TVVT--PLLWKARAGDACGAaympiGTLLgnrsGYILDG----------------- 4869
Cdd:PRK09274 307 RFRAMLPPDaeILTPYGATEalpiSSIEsrEILFATRAATDNGA-----GICV----GRPVDGvevriiaisdapipewd 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4870 QLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfGAPGSRlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIE 4949
Cdd:PRK09274 378 DALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPD--GQGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLY 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4950 LGEIEARLREHPAV-REAVVVAQPGavGQQLVGYVVAQEPAVADSPEA-QAECRaqlktALRERLPEYMVPSHLLFLARM 5027
Cdd:PRK09274 455 TIPCERIFNTHPGVkRSALVGVGVP--GAQRPVLCVELEPGVACSKSAlYQELR-----ALAAAHPHTAGIERFLIHPSF 527
|
570
....*....|....*
gi 2310915810 5028 PLTP--NGKLDRKGL 5040
Cdd:PRK09274 528 PVDIrhNAKIFREKL 542
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
3054-3525 |
1.47e-26 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 116.81 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIERGVG--ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvpGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLsqshlklpLAQGVQRIDldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAGNRH-SALSNRLC 3210
Cdd:cd05958 80 DKARITVAL--------CAHALTASD-----------------------DICILAFTSGTTGAPKATMHFHrDPLASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3211 WMQQAYGLGVGDTVLQKTP--FSFDVSVWEFFwPLMSGARlVVAAPGdhRDPAKLVALINREGVDTLHFVPSMLQAFLQD 3288
Cdd:cd05958 129 YAVNVLRLREDDRFVGSPPlaFTFGLGGVLLF-PFGVGAS-GVLLEE--ATPDLLLSAIARYKPTVLFTAPTAYRAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVAS--CTSLKRIVCSGEALPAdaqqQVFAKLPQA---GLYNLYGPTEAaidvTHWTCVEEGKDAVP--IGRPIANLAC 3361
Cdd:cd05958 205 PDAAGpdLSSLRKCVSAGEALPA----ALHRAWKEAtgiPIIDGIGSTEM----FHIFISARPGDARPgaTGKPVPGYEA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3362 YILDGNLEPVPVGVLGELYLAGQglaRGYHqrpGLTAERfvASPFVAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd05958 277 KVVDDEGNPVPDGTIGRLAVRGP---TGCR---YLADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3442 LRIELGEIEARLLEHPWVREAAVLAV--DGRQLV--GYVVLESESGDW----REALAAHLAASLPeYMVPAQWLALERMP 3513
Cdd:cd05958 348 YNIAPPEVEDVLLQHPAVAECAVVGHpdESRGVVvkAFVVLRPGVIPGpvlaRELQDHAKAHIAP-YKYPRAIEFVTELP 426
|
490
....*....|..
gi 2310915810 3514 LSPNGKLDRKAL 3525
Cdd:cd05958 427 RTATGKLQRFAL 438
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1991-2580 |
1.47e-26 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 120.19 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:COG3319 7 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAV 2150
Cdd:COG3319 87 ALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2151 SQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAY 2230
Cdd:COG3319 167 VLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF--NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARR 2308
Cdd:COG3319 247 LLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALaaGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:COG3319 327 LLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLssLPL 2468
Cdd:COG3319 407 RRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL--LLL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2469 NANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPL 2548
Cdd:COG3319 485 LLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLL 564
|
570 580 590
....*....|....*....|....*....|..
gi 2310915810 2549 RILFERPVLADFAASLESQAASVAPVLQVLPR 2580
Cdd:COG3319 565 LALLLAPTLAALAAALAAAAAAAALSPLVPLR 596
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
516-1001 |
1.93e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 117.94 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 596 PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQ-RIDLDQADAW------------LENHAENNPgiELNGENLAYVIYTS 662
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVDRALAdCPQATRIVAWtdedhdltvevlIAAHAGQRP--EPTGRKGRVILLTS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 663 GSTGKPKGAgnRHSALSnrlcwmqqayGLGVGDTVLQKTPfsfdvsvWEFFWPLmsgarlVVAAPGDHR----------- 731
Cdd:PRK13382 206 GTTGTPKGA--RRSGPG----------GIGTLKAILDRTP-------WRAEEPT------VIVAPMFHAwgfsqlvlaas 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 732 -----------DPAKLVELINREGVDTLHFVPSMLQAFLQ--DE--DVASCTSLKRIVCSGEALPADAqqqVFAKLPQAG 796
Cdd:PRK13382 261 lactivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEvrNRYSGRSLRFAAASGSRMRPDV---VIAFMDQFG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 797 --LYNLYGPTEAA-IDVTHWTCVEEGKDTVpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYhqRPGLTAEr 873
Cdd:PRK13382 338 dvIYNNYNATEAGmIATATPADLRAAPDTA--GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 874 fvaspFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV 949
Cdd:PRK13382 413 -----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDdeqyGQRLAAFV 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 950 VLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:PRK13382 486 VLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3029-3470 |
2.48e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 118.28 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3029 ATAAEYPLQRGVHRLFEEQVERTPTAPALAF----GEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVV 3103
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDR-VAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3104 ALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL--SQSHLK--LPLAQ---GVQRI-----DLDRGAPWFEDYSE- 3170
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDklLEVRDelpSLRHIvvldpRGLRDDPRLLSLDEl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 -------ANPDI------HLDGENLAYVIYTSGSTGKPKGAgnrhsALSNR-LCWM----QQAYGLGVGDTVLQKTPFS- 3231
Cdd:COG1022 161 lalgrevADPAElearraAVKPDDLATIIYTSGTTGRPKGV-----MLTHRnLLSNaralLERLPLGPGDRTLSFLPLAh 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 -FDvSVWEFFWpLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIV------- 3301
Cdd:COG1022 236 vFE-RTVSYYA-LAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqAKAEEAGGLKRKLfrwalav 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3302 --------CSGEALP-------ADAQQQVFAKLPQA-G---------------------------LYNLYGPTE-AAIdv 3337
Cdd:COG1022 309 grryararLAGKSPSlllrlkhALADKLVFSKLREAlGgrlrfavsggaalgpelarffralgipVLEGYGLTEtSPV-- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 thwTCVEEGKDAVP--IGRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRT 3415
Cdd:COG1022 387 ---ITVNRPGDNRIgtVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA------DGWLHT 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3416 GDLARYRADGVIEYAGRIDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLAvDGR 3470
Cdd:COG1022 448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG-DGR 502
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
513-940 |
2.83e-26 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 117.21 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 513 VHRLFEEQVERTPTAPALAFGEER-LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 591
Cdd:cd05970 23 VDAMAKEYPDKLALVWCDDAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 592 DPEYPEERQAYMLEDSGVQLLLS-----------QSHLKLPLAQGVQRIDLDQADAWLENHAE--NNPGI--------EL 650
Cdd:cd05970 103 THQLTAKDIVYRIESADIKMIVAiaednipeeieKAAPECPSKPKLVWVGDPVPEGWIDFRKLikNASPDferptansYP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 651 NGENLAYVIYTSGSTGKPKGAGNRHS----ALSNRLCWMQQAYG---LGVGDTVLQKtpfsfdvSVW-EFFWPLMSGARL 722
Cdd:cd05970 183 CGEDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQNVREGglhLTVADTGWGK-------AVWgKIYGQWIAGAAV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 723 VVAapgDHR--DPAKLVELINREGVDTLHFVPSMLQaFLQDEDVA--SCTSLKRIVCSGEALPADAQQQvFAKLPQAGLY 798
Cdd:cd05970 256 FVY---DYDkfDPKALLEKLSKYGVTTFCAPPTIYR-FLIREDLSryDLSSLRYCTTAGEALNPEVFNT-FKEKTGIKLM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 799 NLYGPTEAAIDVTHWTCVEEGKDTvpIGRPIGNLGCYILDGNLEPVPVGVLGELYL---AGR--GLARGYHQRPGLTAEr 873
Cdd:cd05970 331 EGFGQTETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKpvGLFGGYYKDAEKTAE- 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 874 fvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:cd05970 408 ------VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGV 468
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2583-3003 |
3.32e-26 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 115.43 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQrmWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTI--LANMPLRI 2660
Cdd:cd19534 1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIrgDVEELFRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2661 VLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQ 2740
Cdd:cd19534 79 EVVDLSSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2741 PTLaPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGaeQPVLELPADRVRpAQASGRgqRLDMALPVPLSEELL-ACA 2819
Cdd:cd19534 159 IPL-PSKTSFQTWAELLAEYAQSPALLEELAYWRELPA--ADYWGLPKDPEQ-TYGDAR--TVSFTLDEEETEALLqEAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2820 RREGVTPFMLLLASFQVLLKRYSGQSDIRVGV------PIAnrNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVRE 2893
Cdd:cd19534 233 AAYRTEINDLLLAALALAFQDWTGRAPPAIFLeghgreEID--PGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2894 aALGAQAHQDLPFEQLVDALQPERN-LSHSPLFQVMYN----HQSGERQDAQvdglhiESFAWDGAAAQFD--------L 2960
Cdd:cd19534 311 -QLRRIPNKGIGYGILRYLTPEGTKrLAFHPQPEISFNylgqFDQGERDDAL------FVSAVGGGGSDIGpdtprfalL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2310915810 2961 ALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLE 3003
Cdd:cd19534 384 DINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3604-4049 |
3.34e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 119.96 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3604 LARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHET 3683
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3684 DGT---WHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWR 3760
Cdd:COG1020 81 RPVqviQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3761 ILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGALEQRFATS 3838
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPllELPTDRPRPAVQSYRGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3839 VQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREelfaDIDLSRTVGWFTSLFPVR-- 3916
Cdd:COG1020 241 VSFRLPAELTAALRALA-RRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP----RPELEGLVGFFVNTLPLRvd 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3917 LSPVADLGESLKAIKEQLRAipdkGLGYgllRYLAGEE------SARVLAGLP--QARITFNYLGQFDAQFDEMALLDPA 3988
Cdd:COG1020 316 LSGDPSFAELLARVRETLLA----AYAH---QDLPFERlveelqPERDLSRNPlfQVMFVLQNAPADELELPGLTLEPLE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3989 GESAGAEMDpgapldnwLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVD 4049
Cdd:COG1020 389 LDSGTAKFD--------LTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAA 441
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
3043-3528 |
4.48e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 116.78 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQGVQ-RIDLDRGAPWFEDY----SEANPDIHLD------GENLAYVIYTSGS 3191
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVDRALAdCPQATRIVAWTDEDhdltVEVLIAAHAGqrpeptGRKGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3192 TGKPKGAgnRHSALSnrlcwmqqayGLGVGDTVLQKTPfsfdvsvWEFFWPLmsgarlVVAAPGDHR------------- 3258
Cdd:PRK13382 208 TGTPKGA--RRSGPG----------GIGTLKAILDRTP-------WRAEEPT------VIVAPMFHAwgfsqlvlaasla 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 ---------DPAKLVALINREGVDTLHFVPSMLQAFLQ--DE--DVASCTSLKRIVCSGEALPADAqqqVFAKLPQAG-- 3323
Cdd:PRK13382 263 ctivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEvrNRYSGRSLRFAAASGSRMRPDV---VIAFMDQFGdv 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3324 LYNLYGPTEAAIDVThwtCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqRPGLTAErf 3401
Cdd:PRK13382 340 IYNNYNATEAGMIAT---ATPADLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3402 vaspFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV 3477
Cdd:PRK13382 413 ----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDdeqyGQRLAAFVV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3478 LESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:PRK13382 487 LKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
3047-3525 |
4.91e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 115.83 E-value: 4.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 3126
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3127 QAYMLEDSGVELLLSQSHLKlPLAQGVQRIDLDRGAPwfEDYSEANP--DIHLDgeNLAYVIYTSGSTGKPKGA----GN 3200
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFE-AKLIPGISVKFAELMN--GPKEEAEIqeEFDLD--EVATIMYTSGTTGKPKGViqtyGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 R-HSALSNRLcwmqqAYGLGVGDTVLQKTPFsFDVSVWE-FFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFV 3278
Cdd:PRK03640 166 HwWSAVGSAL-----NLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQAFLQDEDVASCTSLKRIVCSGEAlPADAQQQVFAKLPQAGLYNLYGPTEAAIDVthwtCVEEGKDAV----PIGR 3354
Cdd:PRK03640 237 STMLQRLLERLGEGTYPSSFRCMLLGGG-PAPKPLLEQCKEKGIPVYQSYGMTETASQI----VTLSPEDALtklgSAGK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLACYILDgNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRID 3434
Cdd:PRK03640 312 PLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALE 3510
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPVAFVVKSGEVTE--EELRHFCEEKLAKYKVPKRFYFVE 461
|
490
....*....|....*
gi 2310915810 3511 RMPLSPNGKLDRKAL 3525
Cdd:PRK03640 462 ELPRNASGKLLRHEL 476
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
502-943 |
5.02e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 117.12 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 502 ATAAEYPLQRGVHRLFEEQVERTPTAPALAF----GEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVV 576
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDR-VAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 577 ALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL--SQSHLK--------LP------------------------- 621
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDkllevrdeLPslrhivvldprglrddprllsldel 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 622 LAQGVQRIDLDQADAWLEnhaennpgiELNGENLAYVIYTSGSTGKPKGAgnrhsALSNR-LCWM----QQAYGLGVGDT 696
Cdd:COG1022 161 LALGREVADPAELEARRA---------AVKPDDLATIIYTSGTTGRPKGV-----MLTHRnLLSNaralLERLPLGPGDR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 697 VLQKTPFS--FDvSVWEFFWpLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKR 772
Cdd:COG1022 227 TLSFLPLAhvFE-RTVSYYA-LAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqAKAEEAGGLKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 773 IV---------------CSGEALP-------ADAQQQVFAKLPQA-G---------------------------LYNLYG 802
Cdd:COG1022 300 KLfrwalavgrryararLAGKSPSlllrlkhALADKLVFSKLREAlGgrlrfavsggaalgpelarffralgipVLEGYG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 803 PTE--AAIDVTHWTCVEEGkdTVpiGRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVAspfv 880
Cdd:COG1022 380 LTEtsPVITVNRPGDNRIG--TV--GPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA---- 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 881 agERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLAvDGR 943
Cdd:COG1022 442 --DGWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG-DGR 502
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
4537-5131 |
7.50e-26 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 117.88 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4537 PLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVP 4616
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4617 LDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPK 4696
Cdd:COG3319 81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4697 GVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVF 4776
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4777 PPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIG 4856
Cdd:COG3319 241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 TLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGR 4936
Cdd:COG3319 321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4937 VDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAecraqlktaLRERLPEYM 5016
Cdd:COG3319 401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLL---------LLLLLLPPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5017 VPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVT 5096
Cdd:COG3319 472 LPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLL 551
|
570 580 590
....*....|....*....|....*....|....*
gi 2310915810 5097 ARMQSEVGVELPLAALFQTESLQAYAELAAAQTSS 5131
Cdd:COG3319 552 LLLLALLLRLLLLLALLLAPTLAALAAALAAAAAA 586
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1977-2479 |
7.52e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 116.15 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1977 DWQAP---LEALPRGGVAAAFA----HQVASAPEAIALVCGDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAA 2045
Cdd:PRK04319 26 SWEEVekeFSWLETGKVNIAYEaidrHADGGRKDKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2046 ERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcpaeVERLP-LET------------ 2112
Cdd:PRK04319 106 PRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKP----ADDLPsLKHvllvgedveegp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2113 ------AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---Cqlqfasisfd 2183
Cdd:PRK04319 182 gtldfnALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDvywC---------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2184 aAAEQ---------LFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTI-LDLPPAY--LQQQAEELRHAGRRIAVRtCI 2251
Cdd:PRK04319 252 -TADPgwvtgtsygIFAPWLNGATNVI-DGGRFSPERWYRILEDYKVTVwYTAPTAIrmLMGAGDDLVKKYDLSSLR-HI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LG-GEAwdaslLTQQAVQaeaW-FNAYGPTeavITPLAWHcraQEGGAPAI-------------GRALGARRACILDAAL 2316
Cdd:PRK04319 329 LSvGEP-----LNPEVVR---WgMKVFGLP---IHDNWWM---TETGGIMIanypamdikpgsmGKPLPGIEAAIVDDQG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 QPCAPGMIGELYI--GGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIE 2394
Cdd:PRK04319 395 NELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2395 IGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRG-EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANG 2472
Cdd:PRK04319 467 PFEVESKLMEHPAVAEAGVIGKpDPVRGEIIKAFVALRPGYEPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSG 546
|
....*..
gi 2310915810 2473 KLDRKAL 2479
Cdd:PRK04319 547 KIMRRVL 553
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
513-1002 |
8.15e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 116.29 E-value: 8.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PEYPEERQAYMLEDSGVQLLLS-----------QSHLK------------LPLAQG-----VQR------IDLDQADA-- 636
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILCldlvfprvtnvQSATKiehvivtriadfLPFPKNllypfVQKkqsnlvVKVSESETih 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 637 -WLENHAENNPGIEL--NGEN-LAYVIYTSGSTGKPKGAGNRHSAL-SNRLCWMQQAYGLGVGD-TVLQKTPFsFDV--- 707
Cdd:PRK06710 186 lWNSVEKEVNTGVEVpcDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEeVVLGVLPF-FHVygm 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 708 -SVWEFfwPLMSGARLVVAAPGDHRdpaKLVELINREGVDTLHFVPSMLQAFL-----QDEDVASCtslkRIVCSGEA-L 780
Cdd:PRK06710 265 tAVMNL--SIMQGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnspllKEYDISSI----RACISGSApL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 781 PADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGL 859
Cdd:PRK06710 336 PVEVQEK-FETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 860 ARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PRK06710 414 MKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 940 VD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPE 1002
Cdd:PRK06710 487 VPdpyrGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
523-958 |
8.31e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 116.15 E-value: 8.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 523 RTPTAPALAFGE----------ERLDYAELNRRANRLAHALIERGIGA-DRLVgvAMER-SIEMVVALMAILKAGGAYVP 590
Cdd:PRK09274 18 ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRgMRAV--LMVTpSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 591 VDPeypeerqaymledsGV---QLL--LSQSHLK----LPLAQGV------------QRIDLDQADAW-------LENHA 642
Cdd:PRK09274 96 VDP--------------GMgikNLKqcLAEAQPDafigIPKAHLArrlfgwgkpsvrRLVTVGGRLLWggttlatLLRDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 643 ENNPGI--ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP-FSfdvsvweFFWPLMsG 719
Cdd:PRK09274 162 AAAPFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFA-------LFGPAL-G 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 720 ARLVV-----AAPGDhRDPAKLVELINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIVCSGEALPADAQQQVFAKL 792
Cdd:PRK09274 234 MTSVIpdmdpTRPAT-VDPAKLFAAIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRVISAGAPVPIAVIERFRAML 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 793 PQ-AGLYNLYGPTEA---------AIDVTHWTCVEEGKDTVpIGRPI-GNLGCYI---------LDGNLEpVPVGVLGEL 852
Cdd:PRK09274 313 PPdAEILTPYGATEAlpissiesrEILFATRAATDNGAGIC-VGRPVdGVEVRIIaisdapipeWDDALR-LATGEIGEI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 853 YLAGRGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:PRK09274 391 VVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
|
490 500
....*....|....*....|....*...
gi 2310915810 933 REAAVLAV--DGRQLVGyVVLESEGGDW 958
Cdd:PRK09274 469 KRSALVGVgvPGAQRPV-LCVELEPGVA 495
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
520-998 |
1.08e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 114.67 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 520 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 600 QAYMLEDSGVQLLLSQSHLKlPLAQGVQRIDLDQadawLENHAENNPGI--ELNGENLAYVIYTSGSTGKPKGA----GN 673
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFE-AKLIPGISVKFAE----LMNGPKEEAEIqeEFDLDEVATIMYTSGTTGKPKGViqtyGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 674 R-HSALSNRLcwmqqAYGLGVGDTVLQKTPFsFDVSVWE-FFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFV 751
Cdd:PRK03640 166 HwWSAVGSAL-----NLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 752 PSMLQAFLQDEDVASCTSLKRIVCSGEAlPADAQQQVFAKLPQAGLYNLYGPTEAAIDVthwtCVEEGKDTV----PIGR 827
Cdd:PRK03640 237 STMLQRLLERLGEGTYPSSFRCMLLGGG-PAPKPLLEQCKEKGIPVYQSYGMTETASQI----VTLSPEDALtklgSAGK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 828 PIGNLGCYILDgNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRID 907
Cdd:PRK03640 312 PLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALE 983
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPVAFVVKSGEVTE--EELRHFCEEKLAKYKVPKRFYFVE 461
|
490
....*....|....*
gi 2310915810 984 RMPLSPNGKLDRKAL 998
Cdd:PRK03640 462 ELPRNASGKLLRHEL 476
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
3047-3535 |
1.21e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 114.52 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVERTPTAPA---LAFGEeRLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK09088 4 HARLQPQRLAavdLALGR-RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSQSHLKlplAQGVQRIDLDRGAPWFeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAgnrhs 3203
Cdd:PRK09088 83 ASELDALLQDAEPRLLLGDDAVA---AGRTDVEDLAAFIASA-DALEPADTPSIPPERVSLILFTSGTSGQPKGV----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRlCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFwPLMSGARLVVAAPG-----DHRDPAKLVALINREGVDTLHF- 3277
Cdd:PRK09088 154 MLSER-NLQQTAHNFGVLGRVDAHSSFLCDAPMFHII-GLITSVRPVLAVGGsilvsNGFEPKRTLGRLGDPALGITHYf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 -VPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADaqqQVFAKLPQA-GLYNLYGPTEAAidvthwTCVEEGKDAVPI- 3352
Cdd:PRK09088 232 cVPQMAQAFRAqpGFDAAALRHLTALFTGGAPHAAE---DILGWLDDGiPMVDGFGMSEAG------TVFGMSVDCDVIr 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 ------GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGV 3426
Cdd:PRK09088 303 akagaaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3427 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGYVVLESESGDWR--EALAAHLAASLPEYMV 3502
Cdd:PRK09088 377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgeVGYLAIVPADGAPLdlERIRSHLSTRLAKYKV 456
|
490 500 510
....*....|....*....|....*....|...
gi 2310915810 3503 PAQWLALERMPLSPNGKLdRKALPRPQAAAGQT 3535
Cdd:PRK09088 457 PKHLRLVDALPRTASGKL-QKARLRDALAAGRK 488
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
522-998 |
1.36e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.49 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGiGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07638 12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 602 YMLEDSGVQLLLSQSHLKLPL--AQGvQRIDLDQADAWLENHAENnpgiELNGENLA----YVIYTSGSTGKPKGAGNRH 675
Cdd:PRK07638 91 ERLAISNADMIVTERYKLNDLpdEEG-RVIEIDEWKRMIEKYLPT----YAPIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 676 SAlsnrlcWMQqayglgvgdtvlqktpfSFDVSVWEFFwpLMSGARLVVAAPGDHR----------------------DP 733
Cdd:PRK07638 166 QS------WLH-----------------SFDCNVHDFH--MKREDSVLIAGTLVHSlflygaistlyvgqtvhlmrkfIP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 734 AKLVELINREGVDTLHFVPSMLQAFLQDEDVAScTSLKrIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHW 813
Cdd:PRK07638 221 NQVLDKLETENISVMYTVPTMLESLYKENRVIE-NKMK-IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 814 TCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYhqrpgLTAERFVASPFVAGermYRT-GDLA 892
Cdd:PRK07638 298 VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADG---WMTvRDVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVvlesEGGDWREALAAHLAA 968
Cdd:PRK07638 370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywGEKPVAII----KGSATKQQLKSFCLQ 445
|
490 500 510
....*....|....*....|....*....|
gi 2310915810 969 SLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07638 446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1990-2479 |
1.55e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 114.60 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK06145 4 LSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETLAERlpcPAEVERLPLETAAwpASADTR----------PLPEVAGETLAYVIYTS 2139
Cdd:PRK06145 84 YRLAADEVAYILGDAGAKLLLVDEEFDAI---VALETPKIVIDAA--AQADSRrlaqggleipPQAAVAPTDLVRLMYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2140 GSTGQPKGVAVSQAALvaHCQAAARTYGVGPgdcqlqfasisfdAAAEQLFV--PLL-AGARVLLGDAGQW--------- 2207
Cdd:PRK06145 159 GTTDRPKGVMHSYGNL--HWKSIDHVIALGL-------------TASERLLVvgPLYhVGAFDLPGIAVLWvggtlrihr 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2208 --SAQHLADEVERHAVTILDLPPAYLQQQ-AEELRHAGRRIAVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAV 2282
Cdd:PRK06145 224 efDPEAVLAAIERHRLTCAWMAPVMLSRVlTVPDRDRFDLDSLAWCIGGGEKTPESRIRDftRVFTRARYIDAYGLTETC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2283 ITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerly 2362
Cdd:PRK06145 304 SGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2363 RTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-L 2440
Cdd:PRK06145 376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVhDDRWGERITAVVVLNP---GATLtL 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 2310915810 2441 AELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06145 453 EALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
539-998 |
1.55e-25 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 112.83 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLllsqshl 618
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 klplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGA----GNrH--SALSNRLcwmqqAYGLG 692
Cdd:cd05912 77 ----------------------------------DDIATIMYTSGTTGKPKGVqqtfGN-HwwSAIGSAL-----NLGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 693 VGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLK 771
Cdd:cd05912 117 EDDNWLCALPL-FHISgLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 772 RIVCSGEALPADAQQQVFAK-LPqagLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGvlg 850
Cdd:cd05912 193 CILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVG--- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 851 ELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 931 WVREAAVLAVD----GRQLVGYVVLESEGGdwREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05912 340 AIKEAGVVGIPddkwGQVPVAFVVSERPIS--EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2010-2479 |
1.57e-25 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 115.07 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD--PNY--PAERLAY------ 2079
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYdePNARLRKlrhiwq 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2080 MLRDsgARWLICQETLAERLPCPAEVERLPLETAAWPASADT---RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:cd05906 116 LLGS--PVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTaadHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTYGVGPGDCQLQF------ASISF------DAAAEQLFVPllagARVLLGDAGQWsaqhlADEVERHAVTIL 2224
Cdd:cd05906 194 ARSAGKIQHNGLTPQDVFLNWvpldhvGGLVElhlravYLGCQQVHVP----TEEILADPLRW-----LDLIDRYRVTIT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPP---AYLQQQAEELRHA-GRRIAVRTCILGGEAWDA-------SLLTQQAVQAEAWFNAYGPTE--AVITpLAWHCR 2291
Cdd:cd05906 265 WAPNfafALLNDLLEEIEDGtWDLSSLRYLVNAGEAVVAktirrllRLLEPYGLPPDAIRPAFGMTEtcSGVI-YSRSFP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEGGAP----AIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDL 2367
Cdd:cd05906 344 TYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2368 ArYRVDGQVEYLGRADQQIKIRGFRIEIGEIesqllahpyvaEAAVVALDGVGGPLLAAYLVgRDAMRGEDLLAEL---R 2444
Cdd:cd05906 417 G-FLDNGNLTITGRTKDTIIVNGVNYYSHEI-----------EAAVEEVPGVEPSFTAAFAV-RDPGAETEELAIFfvpE 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2445 TWLAGRLPAYMQPTAWQVLSS--------LPLNAN-------GKLDRKAL 2479
Cdd:cd05906 484 YDLQDALSETLRAIRSVVSREvgvspaylIPLPKEeipktslGKIQRSKL 533
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
527-998 |
1.85e-25 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 113.34 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 527 APALAFGEERLDYAELNRRANRLAHALI-ERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 605
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 606 DSGVQLLLsqshlklplaqgvqridLDQAdawlENHAENnpgielngenLAYVIYTSGSTGKPKGAGNRH-SALSNRLCW 684
Cdd:cd05958 81 KARITVAL-----------------CAHA----LTASDD----------ICILAFTSGTTGAPKATMHFHrDPLASADRY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 685 MQQAYGLGVGDTVLQKTP--FSFDVSVWEFFwPLMSGARlVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDE 762
Cdd:cd05958 130 AVNVLRLREDDRFVGSPPlaFTFGLGGVLLF-PFGVGAS-GVLLEE--ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 763 DVAS--CTSLKRIVCSGEALPAdaqqQVFAKLPQA---GLYNLYGPTEAaidvTHWTCVEEGKDTVP--IGRPIGNLGCY 835
Cdd:cd05958 206 DAAGpdLSSLRKCVSAGEALPA----ALHRAWKEAtgiPIIDGIGSTEM----FHIFISARPGDARPgaTGKPVPGYEAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 836 ILDGNLEPVPVGVLGELYLAGrglARGYHqrpGLTAERfvASPFVAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd05958 278 VVDDEGNPVPDGTIGRLAVRG---PTGCR---YLADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 916 RIELGEIEARLLEHPWVREAAVLAV--DGRQLV--GYVVLESEGGDW----REALAAHLAASLPeYMVPAQWLALERMPL 987
Cdd:cd05958 349 NIAPPEVEDVLLQHPAVAECAVVGHpdESRGVVvkAFVVLRPGVIPGpvlaRELQDHAKAHIAP-YKYPRAIEFVTELPR 427
|
490
....*....|.
gi 2310915810 988 SPNGKLDRKAL 998
Cdd:cd05958 428 TATGKLQRFAL 438
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
527-993 |
1.89e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 114.23 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 527 APALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 606
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 607 SGVQLLLSQSHLK---------LPLAQGVQRIDLDQAD------AWLENHAENNPGIELNGENLAyviYTSGSTGKPKG- 670
Cdd:PRK08276 82 SGAKVLIVSAALAdtaaelaaeLPAGVPLLLVVAGPVPgfrsyeEALAAQPDTPIADETAGADML---YSSGTTGRPKGi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 671 ----AGNRHSALSNRLCWMQQAYGLGVGDTV------LQKT-PFSFDVSVweffwpLMSGARLVVAapgDHRDPAKLVEL 739
Cdd:PRK08276 159 krplPGLDPDEAPGMMLALLGFGMYGGPDSVylspapLYHTaPLRFGMSA------LALGGTVVVM---EKFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 740 INREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEaAIDVTHW 813
Cdd:PRK08276 230 IERYRVTHSQLVPTMFVRMLKlPEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWW---GpiIHEYYASSE-GGGVTVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 814 TCVE--EGKDTVpiGRP-IGNLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAgermyrTGD 890
Cdd:PRK08276 306 TSEDwlAHPGSV--GKAvLGEV--RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT------VGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGyVVLESEGGDWREALAAHL 966
Cdd:PRK08276 376 VGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPdeemGERVKA-VVQPADGADAGDALAAEL 454
|
490 500 510
....*....|....*....|....*....|.
gi 2310915810 967 AASLPE----YMVPAQWLALERMPLSPNGKL 993
Cdd:PRK08276 455 IAWLRGrlahYKCPRSIDFEDELPRTPTGKL 485
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
4541-4971 |
1.99e-25 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 115.20 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIF----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVP 4616
Cdd:COG1022 15 DLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4617 LDIEYPRERLLYMMQDSRA--------HLLLTHSHLLERLP------------IPEGLSCLSVDREEEWAGFPAHDPEV- 4675
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAkvlfvedqEQLDKLLEVRDELPslrhivvldprgLRDDPRLLSLDELLALGREVADPAELe 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4676 ----ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFDGSHegwmHPLINGA 4747
Cdd:COG1022 175 arraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLplahVFERTVSY----YALAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4748 RV-------LIRDD-------------SLWlpERTYAEMH--------------RHGVTVGvfppvylqQLAEHAERDGN 4793
Cdd:COG1022 251 TVafaespdTLAEDlrevkptfmlavpRVW--EKVYAGIQakaeeagglkrklfRWALAVG--------RRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4794 PPPVrvycfgGDAVAQASYD-LAWRALK-----------------PKYLFN-----------GYGPTET--VVT-PLLWK 4841
Cdd:COG1022 321 SPSL------LLRLKHALADkLVFSKLRealggrlrfavsggaalGPELARffralgipvleGYGLTETspVITvNRPGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 ARagdacgaaympIGTllgnrSGYILDGqlnllpVGVA----GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:COG1022 395 NR-----------IGT-----VGPPLPG------VEVKiaedGEILVRGPNVMKGYYKNPEATAEAFDADGW-------L 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4918 RSGDltrgradgvvdyLGRVDHQ--VKIRGfRI-EL-----GE------IEARLREHPAVREAVVVAQ 4971
Cdd:COG1022 446 HTGD------------IGELDEDgfLRITG-RKkDLivtsgGKnvapqpIENALKASPLIEQAVVVGD 500
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
3049-3468 |
2.21e-25 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 113.43 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEdyseanpdihLDGENLAYVIYTSGSTGKPKGAGNRHSA-LSN 3207
Cdd:PRK09029 94 ELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVA----------WQPQRLATMTLTSGSTGLPKAAVHTAQAhLAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 R---LCWMQqaygLGVGDTVLQKTPFsFDVS----VWEffWpLMSGARLVVaapgdhRDPAKLVALInrEGVDTLHFVPS 3280
Cdd:PRK09029 164 AegvLSLMP----FTAQDSWLLSLPL-FHVSgqgiVWR--W-LYAGATLVV------RDKQPLEQAL--AGCTHASLVPT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQvfakLPQAGL--YNLYGPTEAAIDVthwtCVEE--GKDAVpiGRPI 3356
Cdd:PRK09029 228 QLWRLLDNRSEP--LSLKAVLLGGAAIPVELTEQ----AEQQGIrcWCGYGLTEMASTV----CAKRadGLAGV--GSPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDgnlepvpvgvlGELYLAGQGLARGYHQRPGLTaerfvasPFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 3436
Cdd:PRK09029 296 PGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRLDNL 356
|
410 420 430
....*....|....*....|....*....|..
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD 3468
Cdd:PRK09029 357 FFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4562-5015 |
2.97e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 112.94 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGayVPLDIEyprerllymmqdsrahlllth 4641
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGA--VPVLID--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4642 shllERLPIPEGLSCLSVDREEEWAGFP-AHDPevalhgdnlAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05910 59 ----PGMGRKNLKQCLQEAEPDAFIGIPkADEP---------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDCELH-FMSFAFDGSHEGWMH--PLINGARVLIRDdslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PP 4796
Cdd:cd05910 126 GEVDLAtFPLFALFGPALGLTSviPDMDPTRPARAD-----PQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITlPS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4797 VRVYCFGGDAVAQASYDLAWRALKPKY-LFNGYGPTETV-VTPL----LWKARAGDACGAAYMPIGTLL-GNRSGYI--- 4866
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATEALpVSSIgsreLLATTTAATSGGAGTCVGRPIpGVRVRIIeid 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 -----LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgaPGSRLYRSGDLTRGRADGVVDYLGRVDHQV 4941
Cdd:cd05910 281 depiaEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAHRV 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4942 KIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGyVVAQEPAVADSpeaqaecRAQLKTALRERLPEY 5015
Cdd:cd05910 358 ITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVL-CVEPLPGTITP-------RARLEQELRALAKDY 423
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
3066-3525 |
3.77e-25 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 111.67 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELllsqshl 3145
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 klplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGA----GNrH--SALSNRLcwmqqAYGLG 3219
Cdd:cd05912 77 ----------------------------------DDIATIMYTSGTTGKPKGVqqtfGN-HwwSAIGSAL-----NLGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3220 VGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLK 3298
Cdd:cd05912 117 EDDNWLCALPL-FHISgLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEALPADAQQQVFAK-LPqagLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGvlg 3377
Cdd:cd05912 193 CILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVG--- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3458 WVREAAVLAVD----GRQLVGYVVLESESGdwREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05912 340 AIKEAGVVGIPddkwGQVPVAFVVSERPIS--EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
4681-5035 |
3.96e-25 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 109.90 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL----HFMSFafdGSHEGWMHPLINGARVLirDDSL 4756
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpFFHTF---GYKAGIVACLLTGATVV--PVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 WLPERTYAEMHRHGVTVGVFPP-VYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVV 4835
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPtLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4836 TPLlwkARAGDACgaaympigTLLGNRSGYILDG-QLNLlpvGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:cd17638 156 ATM---CRPGDDA--------ETVATTCGRACPGfEVRI---ADDGEVLVRGYNVMQGYLDDPEATAEAIDADGW----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4915 rlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGQqlvGYVVAQEPAV 4990
Cdd:cd17638 217 --LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPdermGEVGK---AFVVARPGVT 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2310915810 4991 ADSPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:cd17638 292 LTEEDVIAWC--------RERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
3050-3485 |
4.33e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 113.84 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGE----------ERLDYAELNRRANRLAHALIERGVGA-DRLVgvAMER-SIEMVVALMAILKAGGAYVP 3117
Cdd:PRK09274 18 ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRgMRAV--LMVTpSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEypeerqayMledsGVELL---LSQSHLK----LPLAQGV------------QRIDLDRGAPWF--------EDYSE 3170
Cdd:PRK09274 96 VDPG--------M----GIKNLkqcLAEAQPDafigIPKAHLArrlfgwgkpsvrRLVTVGGRLLWGgttlatllRDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 ANPDIH-LDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP-FSfdvsvweFFWPLMsGAR 3248
Cdd:PRK09274 164 APFPMAdLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFA-------LFGPAL-GMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3249 LVV-----AAPGDhRDPAKLVALINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQ 3321
Cdd:PRK09274 236 SVIpdmdpTRPAT-VDPAKLFAAIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRVISAGAPVPIAVIERFRAMLPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3322 -AGLYNLYGPTEA---------AIDVTHWTCVEEGkDAVPIGRPIANLACYILDGNLEP---------VPVGVLGELYLA 3382
Cdd:PRK09274 315 dAEILTPYGATEAlpissiesrEILFATRAATDNG-AGICVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3383 GQGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 3462
Cdd:PRK09274 394 GPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
|
490 500
....*....|....*....|....*
gi 2310915810 3463 AVLAV--DGRQLVGyVVLESESGDW 3485
Cdd:PRK09274 472 ALVGVgvPGAQRPV-LCVELEPGVA 495
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
52-379 |
5.45e-25 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 111.63 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFprgaddslAQAPLQRPLEVAFEDC 131
Cdd:cd19547 4 LAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGF--------TWRDRAEPLQYVRDDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 132 S---GLPEAEQEARLREEAQRESLQPFDLCEG------PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202
Cdd:cd19547 76 AppwALLDWSGEDPDRRAELLERLLADDRAAGlsladcPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 203 SAYATGAEPGL-PALPiqYADYALWQRSWLEAGEQERQleYWRGKLGERHPVlelptdhPRPVVPSYRGSRYEFSIE--- 278
Cdd:cd19547 156 EELAHGREPQLsPCRP--YRDYVRWIRARTAQSEESER--FWREYLRDLTPS-------PFSTAPADREGEFDTVVHefp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNrAEVEG---LIGLFVNTQVLRSVFDGRTSVA 355
Cdd:cd19547 225 EQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PELEGsehMVGIFINTIPLRIRLDPDQTVT 303
|
330 340
....*....|....*....|....
gi 2310915810 356 TLLAGLKDTVLGAQAHQDLPFERL 379
Cdd:cd19547 304 GLLETIHRDLATTAAHGHVPLAQI 327
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
3629-4049 |
1.05e-24 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 110.47 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3629 PFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGtwHAEHAEATL-GGALLWRAEAV 3707
Cdd:cd19542 6 PMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSA--EGTFLQVVLkSLDPPIEEVET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3708 DRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeapRLPGKTSP 3787
Cdd:cd19542 84 DEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------QLLPPAPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3788 FKawagRVSEHARGESMKAQLQFWRELLEGA-PAELPCEHPQGALEQRFATSVQSRFDrslterlLKQAPAAYRTQVNDL 3866
Cdd:cd19542 157 FS----DYISYLQSQSQEESLQYWRKYLQGAsPCAFPSLSPKRPAERSLSSTRRSLAK-------LEAFCASLGVTLASL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3867 LLTALARVVCRWSGAS----SSLVqlegHGREELFADIDlsRTVGWFTSLFPVRLS-----PVADLgesLKAIKEQ-LRA 3936
Cdd:cd19542 226 FQAAWALVLARYTGSRdvvfGYVV----SGRDLPVPGID--DIVGPCINTLPVRVKldpdwTVLDL---LRQLQQQyLRS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3937 IPDKGLGYGLLRYLAGEESARVLAGlpqarITFNYLGQFDAQFDEMALLDPAGESAgAEMDPGAPldnwLSLNGRVFDGE 4016
Cdd:cd19542 297 LPHQHLSLREIQRALGLWPSGTLFN-----TLVSYQNFEASPESELSGSSVFELSA-AEDPTEYP----VAVEVEPSGDS 366
|
410 420 430
....*....|....*....|....*....|...
gi 2310915810 4017 LSIDWSFSSQMFGEDQVRRLADDYVAELTALVD 4049
Cdd:cd19542 367 LKVSLAYSTSVLSEEQAEELLEQFDDILEALLA 399
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3063-3472 |
1.10e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 111.40 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEypeerqaymledsgvellLSQ 3142
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHLKLPLaqgvqridldrgapwfedySEANPDIHLdGENLA----YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL 3218
Cdd:cd05910 64 KNLKQCL-------------------QEAEPDAFI-GIPKAdepaAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3219 GVGDTVLQKTPfsfdvsVWEFFWPLMSGArlVVAAPGDHR-----DPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDV 3291
Cdd:cd05910 124 RPGEVDLATFP------LFALFGPALGLT--SVIPDMDPTrparaDPQKLVGAIRQYGVSIVFGSPALLERVARycAQHG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEA----AID----VTHWTCVEEGKDAVPIGRPIANLACY 3362
Cdd:cd05910 196 ITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvsSIGsrelLATTTAATSGGAGTCVGRPIPGVRVR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3363 ILDGNLEP---------VPVGVLGELYLAGQGLARGYHQRPglTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRI 3433
Cdd:cd05910 276 IIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRP--VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRK 353
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2310915810 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--GRQL 3472
Cdd:cd05910 354 AHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGkpGCQL 394
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
655-998 |
1.14e-24 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 108.57 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 655 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPfSFDVSVWEFFWP-LMSGARLVVAapgDHRDP 733
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLL---ERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 734 AKLVELinREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQvfAKLPQAGLYNLYGPTEAAIDVTH 812
Cdd:cd17630 78 LAEDLA--PPGVTHVSLVPTQLQRLLDsGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETASQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 813 WTCVEEGKDTVpiGRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHqrpgltaeRFVASPFVAGERMYRTGDLA 892
Cdd:cd17630 154 KRPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTTKDLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEG--GDWREalaaHL 966
Cdd:cd17630 214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGRGPAdpAELRA----WL 289
|
330 340 350
....*....|....*....|....*....|..
gi 2310915810 967 AASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
3043-3525 |
1.29e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 112.29 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEER--LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:PRK05852 21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLL----------SQSHLKLPLAQGVQRIDLDRGA---PWFEDYSEANPDIHLD---GENLAY 3184
Cdd:PRK05852 101 ALPIAEQRVRSQAAGARVVLidadgphdraEPTTRWWPLTVNVGGDSGPSGGtlsVHLDAATEPTPATSTPeglRPDDAM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGdhRDPAKL 3263
Cdd:PRK05852 181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARG--RFSAHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 V-ALINREGVDTLHFVPSMLQAFLQ---DEDVASCTSLKRIV--CSGEALPADAQ--QQVFAklpqAGLYNLYGPTEAAI 3335
Cdd:PRK05852 259 FwDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIrsCSAPLTAETAQalQTEFA----APVVCAFGMTEATH 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTCVEEGKDAVP------IGRPIAnLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvag 3409
Cdd:PRK05852 335 QVTTTQIEGIGQTENPvvstglVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3410 ermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDW 3485
Cdd:PRK05852 411 ----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdqlyGEAVAAVIVPRESAPPT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2310915810 3486 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK05852 487 AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
3181-3522 |
1.58e-24 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 107.88 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3181 NLAYVIYTSGSTGKPKG-AGNRHSALSNRLCwMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAApgdHRD 3259
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAyYRSERSWIESFVC-NEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQDEDvaSCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTh 3339
Cdd:cd17633 77 PKSWIRKINQYNATVIYLVPTMLQALARTLE--PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF-IT- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTCVEEGKDAVPIGRPIANLACYILDGNlepvpVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvagermYRTGDLA 3419
Cdd:cd17633 153 YNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:cd17633 217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdARFGEIAVALYSGDKLTYKQLKRFLKQKLS 296
|
330 340
....*....|....*....|....*
gi 2310915810 3498 pEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:cd17633 297 -RYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
3029-3535 |
1.64e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 111.77 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3029 ATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAI 3108
Cdd:PRK06155 12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLkLPLAQGVQRIDLDRGAPWFEDYSEAN---------------- 3172
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPAVWLLDAPASVsvpagwstaplpplda 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 --PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsnRLCW----MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG 3246
Cdd:PRK06155 171 paPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYN 3326
Cdd:PRK06155 247 ATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF-GVDLLD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3327 LYGPTE--AAIDVTHwtcveegKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ---GLARGYHQRPGLTAE 3399
Cdd:PRK06155 323 GYGSTEtnFVIAVTH-------GSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3400 RFVASPFVAGERMYRTgdlaryrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGY 3475
Cdd:PRK06155 396 AWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPselgEDEVMAA 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3476 VVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLdRKALPRPQAAAGQT 3535
Cdd:PRK06155 469 VVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV-QKFVLREQGVTADT 527
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
657-994 |
1.66e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 109.01 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 657 YVIYTSGSTGKPKGAGNRH-----SALSNRL---------CWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 722
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrMLMGGADfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 723 VVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS----CTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:cd05924 87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpydLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 799 NLYGPTEAAIDVTHWTcVEEGKDTVPIGRPigNLGCYILDGNLEPVPVGVLGELYLAGRGL-ARGYHQRPGLTAERFvas 877
Cdd:cd05924 165 DAFGSSETGFTGSGHS-AGSGPETGPFTRA--NPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 878 PFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES 953
Cdd:cd05924 239 PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPderwGQEVVAVVQLRE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2310915810 954 EGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd05924 319 GAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
4543-5035 |
1.94e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.79 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHL----LLTHSHLLERLPIPEGLSCLSV---DREEEWAGF--------PAHDPeVALHGDNLAYVIY 4687
Cdd:PRK07786 103 PPEIAFLVSDCGAHVvvteAALAPVATAVRDIVPLLSTVVVaggSSDDSVLGYedllaeagPAHAP-VDIPNDSPALIMY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSH----GPLIAHIVATGERYEMTPEDCELHFMSFAFDGShegwMHP-LINGARVLIRDDSLWLPERT 4762
Cdd:PRK07786 182 TSGTTGRPKGAVLTHanltGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGS----MLPgLLLGAPTVIYPLGAFDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 YAEMHRHGVTvGVF-PPVYLQQLAEHAERDGNPPPVRVYCFGG----DAVAQASYDLAWRALkpkyLFNGYGPTE-TVVT 4836
Cdd:PRK07786 258 LDVLEAEKVT-GIFlVPAQWQAVCAEQQARPRDLALRVLSWGAapasDTLLRQMAATFPEAQ----ILAAFGQTEmSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKARAGDACGAAYMPIGTLlgnrSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrL 4916
Cdd:PRK07786 333 CMLLGEDAIRKLGSVGKVIPTV----AARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG--W 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPE 4995
Cdd:PRK07786 401 FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRNDDAALTLE 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2310915810 4996 AqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK07786 481 D-------LAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
3049-3525 |
2.15e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 110.64 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGvGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07638 12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQSHLKLPL--AQGvQRIDLDRgapWFEDYSEANPDIHlDGENLA----YVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK07638 91 ERLAISNADMIVTERYKLNDLpdEEG-RVIEIDE---WKRMIEKYLPTYA-PIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SAlsnrlcWMQqayglgvgdtvlqktpfSFDVSVWEFFwpLMSGARLVVAAPGDHR----------------------DP 3260
Cdd:PRK07638 166 QS------WLH-----------------SFDCNVHDFH--MKREDSVLIAGTLVHSlflygaistlyvgqtvhlmrkfIP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALINREGVDTLHFVPSMLQAFLQDEDVAScTSLKrIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHW 3340
Cdd:PRK07638 221 NQVLDKLETENISVMYTVPTMLESLYKENRVIE-NKMK-IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3341 TCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqrpgLTAERFVASPFVAGermYRT-GDLA 3419
Cdd:PRK07638 298 VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADG---WMTvRDVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVvlesESGDWREALAAHLAA 3495
Cdd:PRK07638 370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywGEKPVAII----KGSATKQQLKSFCLQ 445
|
490 500 510
....*....|....*....|....*....|
gi 2310915810 3496 SLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK07638 446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1099-1515 |
2.28e-24 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 113.80 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1099 ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL------ 1172
Cdd:COG1020 21 SAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLpvvvll 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 -WRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADL--DADLG 1249
Cdd:COG1020 101 vDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAyaGAPLP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 PRSSSYQTWSRHL----HEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEApAA 1323
Cdd:COG1020 181 LPPLPIQYADYALwqreWLQGEELARQLAYWRQQLAGLPPLleLPTDRPRPAVQSYRGARVSFRLPAELTAALRALA-RR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1324 YRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGeaidLSRTVGWFTSLFPVR--LTPAADLGESLKAIKEQLRG 1401
Cdd:COG1020 260 HGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPE----LEGLVGFFVNTLPLRvdLSGDPSFAELLARVRETLLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1402 ------VPdkgvGYGLLRYLAGEEAATRlAALPQPRITFNYLGRFDRQFDGAAlLVPATESAGAAQDpcaplanWLSIEG 1475
Cdd:COG1020 336 ayahqdLP----FERLVEELQPERDLSR-NPLFQVMFVLQNAPADELELPGLT-LEPLELDSGTAKF-------DLTLTV 402
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2310915810 1476 QVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:COG1020 403 VETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
3048-3467 |
2.52e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 110.94 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGE--ERLDYAELNRRANRLAHALieRGVGADRL--VGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK13391 7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLF--RSLGLKRGdhVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSqSHLKLPLAQGV--------QRIDLDRGA--PWFEDYSEA---NPDIHLDGENL-AYVIYTS 3189
Cdd:PRK13391 85 PAEAAYIVDDSGARALIT-SAAKLDVARALlkqcpgvrHRLVLDGDGelEGFVGYAEAvagLPATPIADESLgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3190 GSTGKPKG--AGNRHSALSNRL---CWMQQAYGLGVGDTVLQKTPF-----SFDVSVweffwPLMSGARLVVAapgDHRD 3259
Cdd:PRK13391 164 GTTGRPKGikRPLPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPLyhsapQRAVML-----VIRLGGTVIVM---EHFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA-- 3333
Cdd:PRK13391 236 AEQYLALIEEYGVTHTQLVPTMFSRMLKlPEEVRDkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGlg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3334 --AIDVTHWTcveEGKDAVpiGRPIANLAcYILDGNLEPVPVGVLGELYLAGqGLARGYHQRPGLTAERFVASPfvageR 3411
Cdd:PRK13391 315 ftACDSEEWL---AHPGTV--GRAMFGDL-HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----T 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK13391 383 WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGV 438
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
3040-3525 |
2.60e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 111.66 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQShLKLPLAQGVQ------RIDLDRGA-----------PWFEDYS-------EANPDI 3175
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILCLD-LVFPRVTNVQsatkieHVIVTRIAdflpfpknllyPFVQKKQsnlvvkvSESETI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3176 HL----------------DGEN-LAYVIYTSGSTGKPKGAGNRHSAL-SNRLCWMQQAYGLGVGD-TVLQKTPFsFDV-- 3234
Cdd:PRK06710 185 HLwnsvekevntgvevpcDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEeVVLGVLPF-FHVyg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3235 --SVWEFfwPLMSGARLVVAAPGDHRdpaKLVALINREGVDTLHFVPSMLQAFL-----QDEDVASCtslkRIVCSGEA- 3306
Cdd:PRK06710 264 mtAVMNL--SIMQGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnspllKEYDISSI----RACISGSAp 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3307 LPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDAVPIGRPIANLACYILDGNL-EPVPVGVLGELYLAGQG 3385
Cdd:PRK06710 335 LPVEVQEK-FETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3386 LARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:PRK06710 413 IMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3466 AVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06710 486 GVPdpyrGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
654-995 |
2.97e-24 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 107.11 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 654 NLAYVIYTSGSTGKPKG-AGNRHSALSNRLCwMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAApgdHRD 732
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAyYRSERSWIESFVC-NEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 733 PAKLVELINREGVDTLHFVPSMLQAFLQDEDvaSCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTh 812
Cdd:cd17633 77 PKSWIRKINQYNATVIYLVPTMLQALARTLE--PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF-IT- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 813 WTCVEEGKDTVPIGRPIGNLGCYILDGNlepvpVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvagermYRTGDLA 892
Cdd:cd17633 153 YNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGRQLVGYVVLESEGGDWREALAAHLAASL 970
Cdd:cd17633 217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdARFGEIAVALYSGDKLTYKQLKRFLKQKLS 296
|
330 340
....*....|....*....|....*
gi 2310915810 971 pEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:cd17633 297 -RYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1981-2476 |
3.26e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 111.02 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGGVAAAFAHQVASAPEAIALVCGDEHL--SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK12583 11 GDKPLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC---------QETLAERLPCPAEVERLPLETAAWP--------ASADT 2121
Cdd:PRK12583 91 ARIGAILVNINPAYRASELEYALGQSGVRWVICadafktsdyHAMLQELLPGLAEGQPGALACERLPelrgvvslAPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2122 RPL---PEV--AGETLAY-----------------VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDcqlqfas 2179
Cdd:PRK12583 171 PGFlawHELqaRGETVSRealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2180 isfdaaaeQLFVP----------------LLAGARVLL-GDAGQWSAQHLADEVERhAVTILDLPPAYLQqqaeELRHAG 2242
Cdd:PRK12583 244 --------RLCVPvplyhcfgmvlanlgcMTVGACLVYpNEAFDPLATLQAVEEER-CTALYGVPTMFIA----ELDHPQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2243 RR----IAVRTCILGGEAWDASLLTQqaVQAEAWFN----AYGPTEAviTPLAWHCRAQ---EGGAPAIGRALGARRACI 2311
Cdd:PRK12583 311 RGnfdlSSLRTGIMAGAPCPIEVMRR--VMDEMHMAevqiAYGMTET--SPVSLQTTAAddlERRVETVGRTQPHLEVKV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2312 LDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:PRK12583 387 VDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-------MHTGDLATMDEQGYVRIVGRSKDMIIRGGE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLN 2469
Cdd:PRK12583 460 NIYPREIEEFLFTHPAVADVQVFGVpDEKYGEEIVAWVRLHP---GHAAsEEELREFCKARIAHFKVPRYFRFVDEFPMT 536
|
....*..
gi 2310915810 2470 ANGKLDR 2476
Cdd:PRK12583 537 VTGKVQK 543
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
3182-3525 |
3.55e-24 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 107.03 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3182 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPfSFDVSVWEFFWP-LMSGARLVVAapgDHRDP 3260
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLL---ERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALinREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQvfAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:cd17630 78 LAEDLA--PPGVTHVSLVPTQLQRLLDsGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETASQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTCVEEGKDAVpiGRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHqrpgltaeRFVASPFVAGERMYRTGDLA 3419
Cdd:cd17630 154 KRPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTTKDLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL--ESESGDWREalaaHL 3493
Cdd:cd17630 214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGrgPADPAELRA----WL 289
|
330 340 350
....*....|....*....|....*....|..
gi 2310915810 3494 AASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2618-2904 |
4.86e-24 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 108.73 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEvDGQarQTILANMPL-RIVLEDCAGASEATLRQRVaEEIR-----QPFDLARGP 2691
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEVPWyGITVHDLRGLSEEEAEAAL-EELRerlshRVLDVERGP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2692 LLRVRLLALAGQEHVLvitqhHI-----VSDGWSMQVMVDELLQAYAAARRgeqpTLAPLKLQYADYAAWHRAwLDSGEG 2766
Cdd:cd19535 113 LFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLLAEQA-LRETAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2767 ARQLDYWRERLGAEQPVLELPAdRVRPAQ-ASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQS 2845
Cdd:cd19535 183 ERARAYWQERLPTLPPAPQLPL-AKDPEEiKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQP 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2846 DIRVGVPIANRNR--AEVERLIGFFVNTQVLRCQVDAGLAFRDllgRVReaALGAQAHQDL 2904
Cdd:cd19535 262 RFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLE---RAR--RLQQQLWEDL 317
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
4564-5040 |
5.29e-24 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 110.03 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDS-------RAH 4636
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAedrvvfvDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4637 LLLTHSHLLERLPIPEGLSCLSVDREEEWAGFP-AHDPEVALHG-----------DNLAYVI-YTSGSTGMPKGVAVSHG 4703
Cdd:cd12119 107 FLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVgVLAYEELLAAespeydwpdfdENTAAAIcYTSGTTGNPKGVVYSHR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAH---IVATGERYeMTPEDCELHFMSFafdgSH-EGWMHP---LINGARVLIRDDSLwLPERTYAEMHRHGVTVGVF 4776
Cdd:cd12119 187 SLVLHamaALLTDGLG-LSESDVVLPVVPM----FHvNAWGLPyaaAMVGAKLVLPGPYL-DPASLAELIEREGVTFAAG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4777 PPVYLQQLAEHAERDGN--PPPVRVYCfGGDAVAQASYdlawRALKPKYL--FNGYGPTET----VVTPLLWKARAGDA- 4847
Cdd:cd12119 261 VPTVWQGLLDHLEANGRdlSSLRRVVI-GGSAVPRSLI----EAFEERGVrvIHAWGMTETsplgTVARPPSEHSNLSEd 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4848 ------CGAAYMPIGTLLgnrsgYILDGQLNLLPV-GVA-GELYLGGEGVARGYLERPAlTAERFVPDPFgapgsrlYRS 4919
Cdd:cd12119 336 eqlalrAKQGRPVPGVEL-----RIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW-------LRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqa 4998
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPLAVVVLKEGATVTAEE--- 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2310915810 4999 ecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12119 480 -----LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
502-1014 |
6.25e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 110.23 E-value: 6.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 502 ATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 581
Cdd:PRK06155 12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 582 LKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENHAENN---------------- 645
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPAVWLLDAPASVsvpagwstaplpplda 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 646 --PGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsnRLCW----MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG 719
Cdd:PRK06155 171 paPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 720 ARLVVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYN 799
Cdd:PRK06155 247 ATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF-GVDLLD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 800 LYGPTE--AAIDVTHwtcvEEGKDTVpIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR---GLARGYHQRPGLTAERF 874
Cdd:PRK06155 323 GYGSTEtnFVIAVTH----GSQRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 875 VASPFVAGERMYRTgdlaryrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVL 951
Cdd:PRK06155 398 RNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPselGEDEVMAAVV 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 952 ESEGGDWR-EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVA-----QAGYSAPR 1014
Cdd:PRK06155 471 LRDGTALEpVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADtwdreAAGVQLPR 539
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
2603-3005 |
6.39e-24 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 107.77 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2603 SAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF-EEVDGQARQTILANMPLRIvledcagASEATLRQRVAEEI 2681
Cdd:cd19545 19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISW-------TESTSLDEYLEEDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2682 RQPFDLArGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLK--LQYADYAAWhra 2759
Cdd:cd19545 92 AAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVkyLRQLDDEAA--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2760 wldsgegarqLDYWRERL-GAEQPVL-ELPADRVRPAQasgrGQRLDMALPVPLSeellacaRREGVTPFMLLLASFQVL 2837
Cdd:cd19545 168 ----------AEFWRSYLaGLDPAVFpPLPSSRYQPRP----DATLEHSISLPSS-------ASSGVTLATVLRAAWALV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2838 LKRYSGQSDIRVGVPIANRN--RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREaalgaQAHQDLPFEQLvdALQP 2915
Cdd:cd19545 227 LSRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQK-----DLLDMIPFEHT--GLQN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2916 ERNLS----HSPLFQVMYNHQS-GERQDAQVDGLHIESFAWDGAA-AQFDLALDTWETPDGLGAALTYATDLFEARTVER 2989
Cdd:cd19545 300 IRRLGpdarAACNFQTLLVVQPaLPSSTSESLELGIEEESEDLEDfSSYGLTLECQLSGSGLRVRARYDSSVISEEQVER 379
|
410
....*....|....*.
gi 2310915810 2990 MARHWQNLLRGMLENP 3005
Cdd:cd19545 380 LLDQFEHVLQQLASAP 395
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
3631-4048 |
6.69e-24 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 108.24 E-value: 6.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRL-FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVD- 3708
Cdd:cd19539 9 ERLwFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3709 ---RQALESLCEESQ-RSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGK 3784
Cdd:cd19539 89 sdrERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3785 TSPFKAWAGRVSEHARGESMKAQLQFWRELLEGA-PAELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAAYRTQV 3863
Cdd:cd19539 169 RQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAePTALPTDRPRPAGFPYPGADLRFELDAELVAA-LRELAKRARSSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3864 NDLLLTALARVVCRWSGASSSLVQLEGHGREElfadIDLSRTVGWFTSLFPVR--LSPVADLGESLKAI-KEQLRAIPDK 3940
Cdd:cd19539 248 FMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH----PRFESTVGFFVNLLPLRvdVSDCATFRDLIARVrKALVDAQRHQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3941 GLGYGLLRYLAGEEsaRVLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGaemDPGAPLDnwLSLNGRVFDGELSID 4020
Cdd:cd19539 324 ELPFQQLVAELPVD--RDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDI---PDGAKFD--LNLTVTEEGTGLRGS 396
|
410 420
....*....|....*....|....*...
gi 2310915810 4021 WSFSSQMFGEDQVRRLADDYVAELTALV 4048
Cdd:cd19539 397 LGYATSLFDEETIQGFLADYLQVLRQLL 424
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
68-478 |
7.47e-24 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 107.77 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 68 QSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQApLQRPLEVAFEDCSGLPEAEQEARLReea 147
Cdd:cd19545 18 QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQV-VVKESPISWTESTSLDEYLEEDRAA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 148 qreslqPFDLcEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRfysAYATGAEPGLPALP--IQYadyal 225
Cdd:cd19545 94 ------PMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLA---AYQGEPVPQPPPFSrfVKY----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 226 wqrswLEAGEQERQLEYWRGKLGErhpvlELPTDHPRPVVPSYR---GSRYEFSIepalaeALRGTARRqGLTLFMLLLG 302
Cdd:cd19545 159 -----LRQLDDEAAAEFWRSYLAG-----LDPAVFPPLPSSRYQprpDATLEHSI------SLPSSASS-GVTLATVLRA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 303 GFNILLQRYSGQTDLRVGVPIANRN--RAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDtvlgaQAHQDLPFE--- 377
Cdd:cd19545 222 AWALVLSRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQK-----DLLDMIPFEhtg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 378 -----RLVEAfkversLSHSPLFQVMYNHQPlvaDIEALDSvAGLSFGQLDWKSRTTQFD---LSLDTYEKGGRLYAALT 449
Cdd:cd19545 297 lqnirRLGPD------ARAACNFQTLLVVQP---ALPSSTS-ESLELGIEEESEDLEDFSsygLTLECQLSGSGLRVRAR 366
|
410 420
....*....|....*....|....*....
gi 2310915810 450 YATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19545 367 YDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
3040-3467 |
7.81e-24 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 109.89 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEER-LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 3118
Cdd:cd05970 23 VDAMAKEYPDKLALVWCDDAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3119 -------DPEY------------------PEERQAyMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDySEANp 3173
Cdd:cd05970 103 thqltakDIVYriesadikmivaiaedniPEEIEK-AAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFER-PTAN- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3174 dIHLDGENLAYVIYTSGSTGKPKGAGNRHS----ALSNRLCWMQQAYG---LGVGDTVLQKtpfsfdvSVW-EFFWPLMS 3245
Cdd:cd05970 180 -SYPCGEDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQNVREGglhLTVADTGWGK-------AVWgKIYGQWIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVVAapgDHR--DPAKLVALINREGVDTLHFVPSMLQaFLQDEDVA--SCTSLKRIVCSGEALPADAQQQvFAKLPQ 3321
Cdd:cd05970 252 GAAVFVY---DYDkfDPKALLEKLSKYGVTTFCAPPTIYR-FLIREDLSryDLSSLRYCTTAGEALNPEVFNT-FKEKTG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3322 AGLYNLYGPTEAAIDVTHWTCVEEGKDAvpIGRPIANLACYILDGNLEPVPVGVLGELYLAGQ-----GLARGYHQRPGL 3396
Cdd:cd05970 327 IKLMEGFGQTETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3397 TAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd05970 405 TAE-------VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGV 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3064-3527 |
8.62e-24 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 108.37 E-value: 8.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS 3143
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3144 hlklplaqgVQRIDLDRGapwfedyseanPDIHLdgenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDT 3223
Cdd:cd05973 81 ---------ANRHKLDSD-----------PFVMM---------FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3224 vlqktpfsfdvsvwefFW-----------------PLMSGARLVVAAPGdhRDPAKLVALINREGVDTLHFVPSMLQAFL 3286
Cdd:cd05973 132 ----------------FWnaadpgwayglyyaitgPLALGHPTILLEGG--FSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3287 QDEDVASCT---SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYI 3363
Cdd:cd05973 194 AAGAEVPARpkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYL--AGQGLA--RGYHQRPgltaerfvaSPFVAGeRMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIdiANSPLMwfRGYQLPD---------TPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---ESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:cd05973 343 SGYRIGPFDVESALIEHPAVAEAAVIGVPdperTEVVKAFVVLRGgheGTPALADELQLHVKKRLSAHAYPRTIHFVDEL 422
|
490
....*....|....*
gi 2310915810 3513 PLSPNGKLDRKALPR 3527
Cdd:cd05973 423 PKTPSGKIQRFLLRR 437
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
508-998 |
8.64e-24 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 109.68 E-value: 8.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 508 PLQR--GVHRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVA 577
Cdd:cd05906 1 PLHRpeGAPRTLLELLLRAAERGPTKGityidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 578 LMAILKAGG--AYVPVDPEYPEE-------RQAYMLEDSGVqlLLSQSHLKLPLA-----QGVQRIDLDQADAwLENHAE 643
Cdd:cd05906 81 FWACVLAGFvpAPLTVPPTYDEPnarlrklRHIWQLLGSPV--VLTDAELVAEFAgletlSGLPGIRVLSIEE-LLDTAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 644 NNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARL 722
Cdd:cd05906 158 DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 723 VVAAPGDH-RDPAKLVELINREGVdTLHFVPSMLQAFLQD--EDVASCT----SLKRIVCSGEALPADAQQQVFAKLPQA 795
Cdd:cd05906 238 VHVPTEEIlADPLRWLDLIDRYRV-TITWAPNFAFALLNDllEEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLLRLLEPY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 796 GL-------------------YNLYGPTEAAIDVTHWTCVeegkdtvpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAG 856
Cdd:cd05906 317 GLppdairpafgmtetcsgviYSRSFPTYDHSQALEFVSL---------GRPIPGVSMRIVDDEGQLLPEGEVGRLQVRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 857 RGLARGYHQRPGLTAERFVASPFvagermYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAA 936
Cdd:cd05906 388 PVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSF 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 937 VLAVDGR-------QLVGYVVLESEGGDWR-------EALAAHLAASLPEYMVPaqwLALERMPLSPNGKLDRKAL 998
Cdd:cd05906 461 TAAFAVRdpgaeteELAIFFVPEYDLQDALsetlraiRSVVSREVGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2015-2477 |
9.44e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 109.70 E-value: 9.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 LA---ERLPCPAEVE-------------------RLPLETAA---------------W--------PASADTRPLPEVAG 2129
Cdd:PRK05605 139 VAptvERLRRTTPLEtivsvnmiaampllqrlalRLPIPALRkaraaltgpapgtvpWetlvdaaiGGDGSDVSHPRPTP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAARTYGVGPGDCQLQFASISFDAAAEQL---FVPLLAGARVLLGdag 2205
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTHRNLFANAaQGKAWVPGLGDGPERVLAALPMFHAYGLTLcltLAVSIGGELVLLP--- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADEVERHAVTILD-LPPAYlQQQAEELRHAGRRIA-VRTCILGgeawdASLLTQQAVqaEAWFNA-------- 2275
Cdd:PRK05605 296 APDIDLILDAMKKHPPTWLPgVPPLY-EKIAEAAEERGVDLSgVRNAFSG-----AMALPVSTV--ELWEKLtggllveg 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTE----AVITPLAWHCRAQEGGAP--------AIGRALGARRAcildaalqpcaPGMIGELYIGGQCLARGYLGRPG 2343
Cdd:PRK05605 368 YGLTEtspiIVGNPMSDDRRPGYVGVPfpdtevriVDPEDPDETMP-----------DGEEGELLVRGPQVFKGYWNRPE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2344 QTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGP 2422
Cdd:PRK05605 437 ETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpREDGSE 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2423 LLAAYLVGRDamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRK 2477
Cdd:PRK05605 509 EVVAAVVLEP---GAALDPEgLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1944-2457 |
1.07e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 109.96 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1944 HLLHLLQRMAETPQAALGELALLDAGerqeALRDWQAPLealprgGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRA 2023
Cdd:PRK08279 3 TLMDLAARLPRRLPDLPGILRGLKRT----ALITPDSKR------SLGDVFEEAAARHPDRPALLFEDQSISYAELNARA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2024 ERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-PCP 2102
Cdd:PRK08279 73 NRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFeEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2103 AEVERLPLETAAWPASADTRPL-------------------PEVAGETLAYVIYTSGSTGQPKgvavsqAALVAH--CQA 2161
Cdd:PRK08279 153 ADLARPPRLWVAGGDTLDDPEGyedlaaaaagapttnpasrSGVTAKDTAFYIYTSGTTGLPK------AAVMSHmrWLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGV----GPGD---CQLQF-----ASISFDAAaeqlfvpLLAGARVLLGDagQWSAQHLADEVERHAVT------- 2222
Cdd:PRK08279 227 AMGGFGGllrlTPDDvlyCCLPLyhntgGTVAWSSV-------LAAGATLALRR--KFSASRFWDDVRRYRATafqyige 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2223 ----ILDLPPaylqqQAEELRHagrriAVRTCI---LGGEAWDAsLLTQQAVQ--AEAW---------FNAYGPTEAV-I 2283
Cdd:PRK08279 298 lcryLLNQPP-----KPTDRDH-----RLRLMIgngLRPDIWDE-FQQRFGIPriLEFYaasegnvgfINVFNFDGTVgR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2284 TPLAWHCRA------QEGGAPAIGRalgarracilDAALQPCAPGMIGELyiggqcLAR--------GYlGRPGQTAERF 2349
Cdd:PRK08279 367 VPLWLAHPYaivkydVDTGEPVRDA----------DGRCIKVKPGEVGLL------IGRitdrgpfdGY-TDPEASEKKI 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2350 VADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAY 2427
Cdd:PRK08279 430 LRDVFK-KGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAA 508
|
570 580 590
....*....|....*....|....*....|.
gi 2310915810 2428 LVGRDamrGEDL-LAELRTWLAGRLPAYMQP 2457
Cdd:PRK08279 509 IVLAD---GAEFdLAALAAHLYERLPAYAVP 536
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
3059-3532 |
1.31e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 110.12 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3059 FGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVEL 3138
Cdd:PRK06060 26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3139 LLSQShlklPLAQGVQRIDLDRGAPWFEDYSEANPDIH--LDGENLAYVIYTSGSTGKPKGAGNRHS---ALSNRLCwmQ 3213
Cdd:PRK06060 106 VVTSD----ALRDRFQPSRVAEAAELMSEAARVAPGGYepMGGDALAYATYTSGTTGPPKAAIHRHAdplTFVDAMC--R 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3214 QAYGLGVGDTVLQKTPFSFDV----SVWeffWPLMSGARLVVAA-PGDHRDPAKLVAlinREGVDTLHFVPSMLQAFLQD 3288
Cdd:PRK06060 180 KALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSaPVTPEAAAILSA---RFGPSVLYGVPNFFARVIDS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCTSLKRIVCSGEAL-PADAQQ--QVFAKLPqagLYNLYGPTE-----AAIDVTHWTCVEEGKDAVPIG-RPIANl 3359
Cdd:PRK06060 254 CSPDSFRSLRCVVSAGEALeLGLAERlmEFFGGIP---ILDGIGSTEvgqtfVSNRVDEWRLGTLGRVLPPYEiRVVAP- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 acyilDGnlEPVPVGVLGELYLAGQGLARGYHQRPgltaerfvaSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:PRK06060 330 -----DG--TTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVdgRQLVGYVVLES----ESGDWREALAA-----HLAASLPEYMVPAQWLALE 3510
Cdd:PRK06060 394 GGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTLQAflvaTSGATIDGSVMrdlhrGLLNRLSAFKVPHRFAVVD 471
|
490 500
....*....|....*....|..
gi 2310915810 3511 RMPLSPNGKLDRKALpRPQAAA 3532
Cdd:PRK06060 472 RLPRTPNGKLVRGAL-RKQSPT 492
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1097-1512 |
1.42e-23 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 107.47 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEP--- 1171
Cdd:cd19539 1 RIPLSFAQErlWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAple 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1172 ---LWRRQAGSEEALLALCEEAQ-RSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLD-- 1245
Cdd:cd19539 81 vrdLSDPDSDRERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1246 --ADLGPRSSSYQTWSRHLHEQAGA-RLDEL-DYWQAQLHDA-PHALPCENPHGALENRHERKLVLTLDAERTRQLLQEA 1320
Cdd:cd19539 161 paAPLPELRQQYKEYAAWQREALAApRAAELlDFWRRRLRGAePTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1321 PAAyRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDlgeaIDLSRTVGWFTSLFPVR--LTPAADLGESLKAIKEQ 1398
Cdd:cd19539 241 KRA-RSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH----PRFESTVGFFVNLLPLRvdVSDCATFRDLIARVRKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1399 LrgvpdkgvgygLLRYLAGEEAATRLAALPQPR----------ITFNYLGRFDRQFDGAALLVPATES---AGAAQDpca 1465
Cdd:cd19539 316 L-----------VDAQRHQELPFQQLVAELPVDrdagrhplvqIVFQVTNAPAGELELAGGLSYTEGSdipDGAKFD--- 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2310915810 1466 planwLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHAL 1512
Cdd:cd19539 382 -----LNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQL 423
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
536-945 |
1.72e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 107.55 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEypeerqaymledsgvqllLSQ 615
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 616 SHLKlplaqgvQRIDLDQADAWLenhaennpGIELNGENLAyVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05910 64 KNLK-------QCLQEAEPDAFI--------GIPKADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 696 TVLQKTPfsfdvsVWEFFWPLMSGArlVVAAPGDHR-----DPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCT 768
Cdd:cd05910 128 VDLATFP------LFALFGPALGLT--SVIPDMDPTrparaDPQKLVGAIRQYGVSIVFGSPALLERVARycAQHGITLP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 769 SLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEA---------AIDVTHWTCVEEGKDTVpIGRPIGNLGCYILD 838
Cdd:cd05910 200 SLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTC-VGRPIPGVRVRIIE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 839 GNLEP---------VPVGVLGELYLAGRGLARGYHQRPglTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:cd05910 279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRP--VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
410 420 430
....*....|....*....|....*....|....*...
gi 2310915810 910 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD--GRQL 945
Cdd:cd05910 357 VITTGGTLYTEPVERVFNTHPGVRRSALVGVGkpGCQL 394
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1129-1515 |
1.76e-23 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 106.90 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1129 PLDGDRLGRALERLQAQHDALRLRFR-EERGAWHQAYAEQAgEPLWRRQ-------AGSEEALLALCEEAQ-RSLDLEQG 1199
Cdd:cd19543 35 PLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDR-KLPWRELdlshlseAEQEAELEALAEEDReRGFDLARA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADL------DADLGPRSSSYQTW-SRHLHEQAgarlde 1272
Cdd:cd19543 114 PLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALgegqppSLPPVRPYRDYIAWlQRQDKEAA------ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1273 LDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAYRTQVNDLLLTALARATCRWSGDASVL 1350
Cdd:cd19543 188 EAYWREYLagFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1351 VQLEGHGREdlgeaIDLS---RTVGWFTSLFPVR--LTPAADLGESLKAIKEQlrgvpdkgvgygllrylageeaatRLA 1425
Cdd:cd19543 267 FGTTVSGRP-----AELPgieTMVGLFINTLPVRvrLDPDQTVLELLKDLQAQ------------------------QLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1426 ALPqpritFNYLGRFDRQ---------FDgaALLV----PATESAGAAQDPCAPLANWLSIEGQV-Y--------GGELS 1483
Cdd:cd19543 318 LRE-----HEYVPLYEIQawsegkqalFD--HLLVfenyPVDESLEEEQDEDGLRITDVSAEEQTnYpltvvaipGEELT 390
|
410 420 430
....*....|....*....|....*....|..
gi 2310915810 1484 LHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19543 391 IKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
522-941 |
2.09e-23 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 107.26 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 602 YMLEDSGVQLLLSQSHLKLPLAQG---VQRIDLDQADAWlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRHSA- 677
Cdd:PRK09029 94 ELLPSLTLDFALVLEGENTFSALTslhLQLVEGAHAVAW-------------QPQRLATMTLTSGSTGLPKAAVHTAQAh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 678 LSNR---LCWMQqaygLGVGDTVLQKTPFsFDVS----VWEffWpLMSGARLVVaapgdhRDPAKLVELInrEGVDTLHF 750
Cdd:PRK09029 161 LASAegvLSLMP----FTAQDSWLLSLPL-FHVSgqgiVWR--W-LYAGATLVV------RDKQPLEQAL--AGCTHASL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 751 VPSMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQvfakLPQAGL--YNLYGPTEAAIDVthwtCVEE--GKDTVpiG 826
Cdd:PRK09029 225 VPTQLWRLLDNRSEP--LSLKAVLLGGAAIPVELTEQ----AEQQGIrcWCGYGLTEMASTV----CAKRadGLAGV--G 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 827 RPIGNLGCYILDgnlepvpvgvlGELYLAGRGLARGYHQRPGLTaerfvasPFVAGERMYRTGDLARYRaDGVIEYAGRI 906
Cdd:PRK09029 293 SPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRL 353
|
410 420 430
....*....|....*....|....*....|....*
gi 2310915810 907 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD 941
Cdd:PRK09029 354 DNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
520-998 |
2.43e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 107.59 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 520 QVERTPTAPA---LAFGEeRLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK09088 4 HARLQPQRLAavdLALGR-RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 597 EERQAYMLEDSGVQLLLSQSHLKlplAQGVQRIDLDQADAWLENHaENNPGIELNGENLAYVIYTSGSTGKPKGAgnrhs 676
Cdd:PRK09088 83 ASELDALLQDAEPRLLLGDDAVA---AGRTDVEDLAAFIASADAL-EPADTPSIPPERVSLILFTSGTSGQPKGV----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 677 ALSNRlCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFwPLMSGARLVVAAPG-----DHRDPAKLVELINREGVDTLHF- 750
Cdd:PRK09088 154 MLSER-NLQQTAHNFGVLGRVDAHSSFLCDAPMFHII-GLITSVRPVLAVGGsilvsNGFEPKRTLGRLGDPALGITHYf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 751 -VPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADaqqQVFAKLPQA-GLYNLYGPTEAAidvthwTCVEEGKDTVPI- 825
Cdd:PRK09088 232 cVPQMAQAFRAqpGFDAAALRHLTALFTGGAPHAAE---DILGWLDDGiPMVDGFGMSEAG------TVFGMSVDCDVIr 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 826 ------GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGV 899
Cdd:PRK09088 303 akagaaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 900 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGYVVLESEGGDWR--EALAAHLAASLPEYMV 975
Cdd:PRK09088 377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgeVGYLAIVPADGAPLdlERIRSHLSTRLAKYKV 456
|
490 500
....*....|....*....|...
gi 2310915810 976 PAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK09088 457 PKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
516-998 |
2.83e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 108.05 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEER--LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:PRK05852 21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 EYPEERQAYMLEDSGVQLLL----------SQSHLKLPLAQGVQRiDLDQADAWLENH----AENNPGIELN---GENLA 656
Cdd:PRK05852 101 ALPIAEQRVRSQAAGARVVLidadgphdraEPTTRWWPLTVNVGG-DSGPSGGTLSVHldaaTEPTPATSTPeglRPDDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 657 YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGdhRDPAK 735
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARG--RFSAH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 736 LV-ELINREGVDTLHFVPSMLQAFLQ---DEDVASCTSLKRIV--CSGEALPADAQ--QQVFAklpqAGLYNLYGPTEAA 807
Cdd:PRK05852 258 TFwDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIrsCSAPLTAETAQalQTEFA----APVVCAFGMTEAT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 808 IDVTHWTCVEEGKD------TVPIGRPIGnLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFva 881
Cdd:PRK05852 334 HQVTTTQIEGIGQTenpvvsTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 882 germyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGD 957
Cdd:PRK05852 411 -----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdqlyGEAVAAVIVPRESAPP 485
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2310915810 958 WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK05852 486 TAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
533-1001 |
2.87e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 107.48 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 613 LSQSHLKLPLA----QGVQ--------------RIDLDQA---------DAWLENHAennPGIELNGENLAYVIYTSGST 665
Cdd:PRK12406 88 IAHADLLHGLAsalpAGVTvlsvptppeiaaayRISPALLtppagaidwEGWLAQQE---PYDGPPVPQPQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 666 GKPKGAGNRHSALSNRLCWMQ---QAYGLGVGDTVL------QKTPFSFDVSVWEFfwplmsGARLVVAApgdHRDPAKL 736
Cdd:PRK12406 165 GHPKGVRRAAPTPEQAAAAEQmraLIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 737 VELINREGVDTLHFVPSMLQAFLQ--DE-----DVascTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAId 809
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKlpEEvrakyDV---SSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 810 VTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLAR-GYHQRPGLTAE----RFVASpfvager 884
Cdd:PRK12406 311 VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITS------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 885 myrtGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWRE 960
Cdd:PRK12406 384 ----GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPdaefGEALMAVVEPQPGATLDEA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2310915810 961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:PRK12406 460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
3064-3465 |
3.05e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 106.50 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVdpeypeerqaymledsgvELLLSQS 3143
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------------TTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3144 HLKlplaqgvQRIDLDRGApwfedYSEANPDIHLDGENLAYviYTSGSTGKPKGAGNRHSA-----LSNrLCWMqqayGL 3218
Cdd:cd05974 63 DLR-------DRVDRGGAV-----YAAVDENTHADDPMLLY--FTSGTTSKPKLVEHTHRSypvghLST-MYWI----GL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3219 GVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSL 3297
Cdd:cd05974 124 KPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3298 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAVP--IGRPIANLACYILDGNLEPVPVG- 3374
Cdd:cd05974 203 REVVGAGEPLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGN----SPGQPVKAgsMGRPLPGYRVALLDPDGAPATEGe 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3375 ---VLGELYLAGqgLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 3451
Cdd:cd05974 278 valDLGDTRPVG--LMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410
....*....|....
gi 2310915810 3452 RLLEHPWVREAAVL 3465
Cdd:cd05974 349 VLIEHPAVAEAAVV 362
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
4551-5040 |
3.05e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 107.76 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDS--------------RAHLLLTHSHLLERL----PIPEGlsclsVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGST 4692
Cdd:PRK06188 106 EDAgistlivdpapfveRALALLARVPSLKHVltlgPVPDG-----VDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4693 GMPKGVAVSHGPLIAHIVATGERYEMtPEDceLHFMSFAfDGSHEGwmhplinGARV---LIRDDSLWL-----PERTYA 4764
Cdd:PRK06188 181 GKPKGVMGTHRSIATMAQIQLAEWEW-PAD--PRFLMCT-PLSHAG-------GAFFlptLLRGGTVIVlakfdPAEVLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVFPPVYLQQLAEHAE-RDGNPPPVRVYCFGGDAVAQASYDLAWRALKPkYLFNGYGPTET--VVTPLLWK 4841
Cdd:PRK06188 250 AIEEQRITATFLVPTMIYALLDHPDlRTRDLSSLETVYYGASPMSPVRLAEAIERFGP-IFAQYYGQTEApmVITYLRKR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 ARAGD------ACGaayMPIgtlLGNRSGyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgaPGSR 4915
Cdd:PRK06188 329 DHDPDdpkrltSCG---RPT---PGLRVA-LLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4916 LyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSP 4994
Cdd:PRK06188 395 L-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEAVTAVVVLRPGAAVDAA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 4995 EAQAecraqlktALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06188 474 ELQA--------HVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
537-998 |
3.74e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 106.45 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS 616
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 617 hlklplaqgVQRIDLDqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDT 696
Cdd:cd05973 81 ---------ANRHKLD--------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 697 vlqktpfsfdvsvwefFW-----------------PLMSGARLVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFL 759
Cdd:cd05973 132 ----------------FWnaadpgwayglyyaitgPLALGHPTILLEGG--FSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 760 QDEDVASCT---SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV-THWTC---VEEGKdtvpIGRPIGNL 832
Cdd:cd05973 194 AAGAEVPARpkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLaNHHALehpVHAGS----AGRAMPGW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 833 GCYILDGNLEPVPVGVLGELYLAGRGLA----RGYHQRPgltaerfvaSPFVAGeRMYRTGDLARYRADGVIEYAGRIDH 908
Cdd:cd05973 269 RVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPD---------TPAIDG-GYYLTGDTVEFDPDGSFSFIGRADD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 909 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES--EGG-DWREALAAHLAASLPEYMVPAQWLA 981
Cdd:cd05973 339 VITMSGYRIGPFDVESALIEHPAVAEAAVIGVPdperTEVVKAFVVLRGghEGTpALADELQLHVKKRLSAHAYPRTIHF 418
|
490
....*....|....*..
gi 2310915810 982 LERMPLSPNGKLDRKAL 998
Cdd:cd05973 419 VDELPKTPSGKIQRFLL 435
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
521-957 |
4.16e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 107.08 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 521 VERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:PRK13391 7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 599 RQAYMLEDSGVQLLLSqSHLKLPLAQGV--------QRIDLDQADAW-----LENHAENNPGIELNGENL-AYVIYTSGS 664
Cdd:PRK13391 87 EAAYIVDDSGARALIT-SAAKLDVARALlkqcpgvrHRLVLDGDGELegfvgYAEAVAGLPATPIADESLgTDMLYSSGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 665 TGKPKG--AGNRHSALSNRL---CWMQQAYGLGVGDTVLQKTPF-----SFDVSVweffwPLMSGARLVVAapgDHRDPA 734
Cdd:PRK13391 166 TGRPKGikRPLPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPLyhsapQRAVML-----VIRLGGTVIVM---EHFDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 735 KLVELINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA---- 806
Cdd:PRK13391 238 QYLALIEEYGVTHTQLVPTMFSRMLKlPEEVRDkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGlgft 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 807 AIDVTHWTcveEGKDTVpiGRPI-GNLgcYILDGNLEPVPVGVLGELYLAGrGLARGYHQRPGLTAERFVASPfvageRM 885
Cdd:PRK13391 317 ACDSEEWL---AHPGTV--GRAMfGDL--HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----TW 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGD 957
Cdd:PRK13391 384 STVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVpneDLGEEVKAVVQPVDGVD 458
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
4560-5040 |
4.17e-23 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 107.37 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL----DIEYPRERLLYMMQDSRA 4635
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvppTYDEPNARLRKLRHIWQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4636 HLLLTHSHLLERLPIPEGLSCLS---VDREEEWAGFPAHDPEVALH---GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd05906 117 LGSPVVLTDAELVAEFAGLETLSglpGIRVLSIEELLDTAADHDLPqsrPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCELHFMsfAFD---GSHEGWMHPLINGAR-------VLIRDDSLWLpertyAEMHRHGVTVGVFPPV 4779
Cdd:cd05906 197 AGKIQHNGLTPQDVFLNWV--PLDhvgGLVELHLRAVYLGCQqvhvpteEILADPLRWL-----DLIDRYRVTITWAPNF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4780 YLQQLAEHAER----DGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFN-----GYGPTETV------VTPLLWKARA 4844
Cdd:cd05906 270 AFALLNDLLEEiedgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCsgviysRSFPTYDHSQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 GD---ACGAAYMPIGTLlgnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGD 4921
Cdd:cd05906 350 ALefvSLGRPIPGVSMR-------IVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4922 LTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE----AVVVAQPGAVGQQL-VGYVVAQEPAVADSPEA 4996
Cdd:cd05906 416 LGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELaIFFVPEYDLQDALSETL 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 4997 QAecraqLKTALRERL---PEYMVPshllfLAR--MPLTPNGKLDRKGL 5040
Cdd:cd05906 495 RA-----IRSVVSREVgvsPAYLIP-----LPKeeIPKTSLGKIQRSKL 533
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1106-1288 |
4.52e-23 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 105.62 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1106 WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAwHQAYaeQA--GEPLWR---RQAGSE 1180
Cdd:cd19532 12 WFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPED-GEPM--QGvlASSPLRlehVQISDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1181 EALLALCEE-AQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAdlDADLGPRSSSYQTWS 1259
Cdd:cd19532 89 AEVEEEFERlKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--GQPLLPPPLQYLDFA 166
|
170 180 190
....*....|....*....|....*....|.
gi 2310915810 1260 RHLHEQ--AGARLDELDYWQAQLHDAPHALP 1288
Cdd:cd19532 167 ARQRQDyeSGALDEDLAYWKSEFSTLPEPLP 197
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4679-5036 |
4.69e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 104.77 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLaYVIYTSGSTGMPKGVAVSHGPLiaHIVATGERYEMTPEDCELHFMSFAfDGSHEG--WMH--PLINGA------- 4747
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDI--FRMLMGGADFGTGEFTPSEDAHKA-AAAAAGtvMFPapPLMHGTgswtafg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4748 ------RVLIRDDSLwLPERTYAEMHRHGVTVGVF-PPVYLQQLAEhAERDGNP---PPVRVYCFGGDAVAQASYDLAWR 4817
Cdd:cd05924 79 gllggqTVVLPDDRF-DPEEVWRTIEKHKVTSMTIvGDAMARPLID-ALRDAGPydlSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 ALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLgnrsgyILDGQLNLLPVGVAGELYLGGEG-VARGYLER 4896
Cdd:cd05924 157 LVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV------VLDDDGRVVPPGSGGVGWIARRGhIPLGYYGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4897 PALTAERFVPdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-V 4975
Cdd:cd05924 231 EAKTAETFPE----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDErW 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4976 GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd05924 307 GQEVVAVVQLREGAGVD--------LEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
3657-3933 |
5.14e-23 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 105.75 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRF-HETDGTWH-AEHAEATLGGALL-WRAEAVDRQ--ALESLCEESQ-RSLDLTDGPL 3730
Cdd:cd19543 36 LDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLqVVLKDRKLPWRELdLSHLSEAEQeaELEALAEEDReRGFDLARAPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3731 LRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPgKTSPFKAWAGRVSEHARGESmkaqLQF 3810
Cdd:cd19543 116 MRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLP-PVRPYRDYIAWLQRQDKEAA----EAY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3811 WRELLEG--APAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQL 3888
Cdd:cd19543 191 WREYLAGfeEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGT 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2310915810 3889 EGHGREelfADID-LSRTVGWFTSLFPVR--LSPVADLGESLKAIKEQ 3933
Cdd:cd19543 270 TVSGRP---AELPgIETMVGLFINTLPVRvrLDPDQTVLELLKDLQAQ 314
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1995-2445 |
1.04e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 106.52 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1995 AHQVASA---PEAIALVCGD----------EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKA 2061
Cdd:PRK09274 10 RHLPRAAqerPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2062 GAGYLPLDPNYPAERLAYMLRDSGARWLICQE--TLAERL--PCPAEVERL------------PLETAAWPASADTRPLP 2125
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPkaHLARRLfgWGKPSVRRLvtvggrllwggtTLATLLRDGAAAPFPMA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2126 EVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FAsisfdaaaeqLFVPLLaGARVLL 2201
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtfplFA----------LFGPAL-GMTSVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 GDA-----GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLLTQ-QAV---QAEA 2271
Cdd:PRK09274 239 PDMdptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpSLRRVISAGAPVPIAVIERfRAMlppDAEI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 WfNAYGPTEAVitPLA-----------WHcRAQEGGAPAIGRALGARRACI--LDAALQP-------CAPGMIGELYIGG 2331
Cdd:PRK09274 319 L-TPYGATEAL--PISsiesreilfatRA-ATDNGAGICVGRPVDGVEVRIiaISDAPIPewddalrLATGEIGEIVVAG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2332 QCLARGYLGRPGQTAERFVADpfsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK09274 395 PMVTRSYYNRPEATRLAKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
|
490 500 510
....*....|....*....|....*....|....*.
gi 2310915810 2412 AVVALDGVGG--PLLAAYLVGRDAMRGEDLLAELRT 2445
Cdd:PRK09274 472 ALVGVGVPGAqrPVLCVELEPGVACSKSALYQELRA 507
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
4538-5038 |
1.20e-22 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 106.42 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4538 LVHQRVAERARMAPDAVAVIFDEEK-----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:cd05968 62 IVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER----LPIPE----GLSCLSVD---------REEEWA--GFPAHDP 4673
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRgrevNLKEEadkaCAQCPTVEkvvvvrhlgNDFTPAkgRDLSYDE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4674 EVALHGDNLA--------YVIYTSGSTGMPKGVAVSHG--PLIAHIVAtGERYEMTPEDCELHFmsfafdgSHEGWMH-- 4741
Cdd:cd05968 222 EKETAGDGAErtesedplMIIYTSGTTGKPKGTVHVHAgfPLKAAQDM-YFQFDLKPGDLLTWF-------TDLGWMMgp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4742 -----PLINGARVLIRDDSLWLP--ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP---PPVRVYCFGGDAVAQAS 4811
Cdd:cd05968 294 wlifgGLILGATMVLYDGAPDHPkaDRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAhdlSSLRVLGSTGEPWNPEP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 YDLAWRAL----KPkyLFNGYGPTETvvtpllwkaRAGDACGAAYMPI------GTLLGNRSGyILDGQLNLLPVGVaGE 4881
Cdd:cd05968 374 WNWLFETVgkgrNP--IINYSGGTEI---------SGGILGNVLIKPIkpssfnGPVPGMKAD-VLDESGKPARPEV-GE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4882 LYLGGE--GVARGYLERPaltaERFVPDPFgapgSRL---YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:cd05968 441 LVLLAPwpGMTRGFWRDE----DRYLETYW----SRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAqEPAVADSPEaqaecraqLKTALRERLPEYM----VPSHLLFLARMPLTP 5031
Cdd:cd05968 513 LNAHPAVLESAAIGVPHPVkGEAIVCFVVL-KPGVTPTEA--------LAEELMERVADELgkplSPERILFVKDLPKTR 583
|
....*..
gi 2310915810 5032 NGKLDRK 5038
Cdd:cd05968 584 NAKVMRR 590
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3184-3521 |
1.67e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 102.85 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3184 YVIYTSGSTGKPKGAGNRH-----SALSNRL---------CWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 3249
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrMLMGGADfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS----CTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 3325
Cdd:cd05924 87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpydLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3326 NLYGPTEAAIDVTHWTcveegKDAVPIGRPIANLA--CYILDGNLEPVPVGVLGELYLAGQGL-ARGYHQRPGLTAERFv 3402
Cdd:cd05924 165 DAFGSSETGFTGSGHS-----AGSGPETGPFTRANpdTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3403 asPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL 3478
Cdd:cd05924 239 --PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPderwGQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2310915810 3479 ESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:cd05924 317 REGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1583-1956 |
1.85e-22 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 103.94 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWP----QP-LQVVFEQATLelrlapPGSDPQRQAEAEREAG---FDPAR 1654
Cdd:cd20484 34 SKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPfqkiEPsKPLSFQEEDI------SSLKESEIIAYLREKAkepFVLEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1655 APLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEVAATV--GRYRDYIGW----LQGRDAMAT 1724
Cdd:cd20484 108 GPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqGKQPTLASspASYYDFVAWeqdmLAGAEGEEH 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1725 EFFWRDRLAS----LEMPTRLARQARTEQPGQgEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVA 1800
Cdd:cd20484 188 RAYWKQQLSGtlpiLELPADRPRSSAPSFEGQ-TYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDII 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1801 FGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAG----HGGEALFD 1876
Cdd:cd20484 267 VGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNiprsQANSPVFQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1877 SILVFENFPVAEALRQAPADLEFSTPSN-----HEQTNYPLTLGV-TLGERLSLQYVYARRDFDAADIAELDRHLLHLLQ 1950
Cdd:cd20484 345 VAFFYQNFLQSTSLQQFLAEYQDVLSIEfvegiHQEGEYELVLEVyEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAE 424
|
....*.
gi 2310915810 1951 RMAETP 1956
Cdd:cd20484 425 ELIANP 430
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3179-3525 |
1.92e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 102.56 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3179 GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWMQQAYGL-GVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGD 3256
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLfDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3257 HRDPA---KLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD--AQQQVFAKLPqagLYNLYGPT 3331
Cdd:cd05944 80 YRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVElrARFEDATGLP---VVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3332 EAaidvthwTCV--------EEGKDAVPIGRPIANLACYILDGN---LEPVPVGVLGELYLAGQGLARGYHQRPGltaer 3400
Cdd:cd05944 157 EA-------TCLvavnppdgPKRPGSVGLRLPYARVRIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTEG----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3401 fvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYV 3476
Cdd:cd05944 225 --NKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAGELPVAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3477 VLESESGDWREALAAHLAASLPEY-MVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05944 303 QLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
516-991 |
2.17e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 105.21 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 596 PEERQAYMLEDSGVQLLLSQSHLK---------------LPLAQGVQRIDLDQAD-------AWLENHAENNP------G 647
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVVWPGFKgidfaailaavppdaLPPLRAIAVVDDAADAtpapapgARVQLFALPDPappaaaG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 648 IELNGENLAYVIYT-SGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAa 726
Cdd:PRK06164 175 ERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCE- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 727 pgDHRDPAKLVELINREGVDtlHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPT 804
Cdd:PRK06164 254 --PVFDAARTARALRRHRVT--HTFGNdeMLRRILDTAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGSS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 805 EAAIDVTHWTCVEEGKDT-VPIGRPIGNLG----CYILDGNLepVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF 879
Cdd:PRK06164 330 EVQALVALQPATDPVSVRiEGGGRPASPEArvraRDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 880 vagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR-QLVGYVVLESEGG 956
Cdd:PRK06164 408 ------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrDGKtVPVAFVIPTDGAS 481
|
490 500 510
....*....|....*....|....*....|....*..
gi 2310915810 957 DWREALAAHLAASLPEYMVPAQWLALERMP--LSPNG 991
Cdd:PRK06164 482 PDEAGLMAACREALAGFKVPARVQVVEAFPvtESANG 518
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1998-2479 |
2.37e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 104.77 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCG--DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE 2075
Cdd:PRK13391 7 AQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2076 RLAYMLRDSGARWLICQ-------ETLAERLP---------CPAEVER---LPLETAAWPASadtrPLP-EVAGETLayv 2135
Cdd:PRK13391 87 EAAYIVDDSGARALITSaakldvaRALLKQCPgvrhrlvldGDGELEGfvgYAEAVAGLPAT----PIAdESLGTDM--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2136 IYTSGSTGQPKGV--------AVSQAALVAHCQaaaRTYGVGPGDCQLQFASISFdaAAEQLFVPLL--AGARVLLGDAg 2205
Cdd:PRK13391 160 LYSSGTTGRPKGIkrplpeqpPDTPLPLTAFLQ---RLWGFRSDMVYLSPAPLYH--SAPQRAVMLVirLGGTVIVMEH- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 qWSAQHLADEVERHAVT-----------ILDLPpaylqqqaEELRhagrriavrtcilggEAWDASLLtQQAVQAEA--- 2271
Cdd:PRK13391 234 -FDAEQYLALIEEYGVThtqlvptmfsrMLKLP--------EEVR---------------DKYDLSSL-EVAIHAAApcp 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 ---------WFNA-----YGPTEAVitpLAWHCRAQEGGAP--AIGRAL-GARRacILDAALQPCAPGMIGELYIGGQcL 2334
Cdd:PRK13391 289 pqvkeqmidWWGPiiheyYAATEGL---GFTACDSEEWLAHpgTVGRAMfGDLH--ILDDDGAELPPGEPGTIWFEGG-R 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2335 ARGYLGRPGQTAERFVADPfsgsgeRLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV- 2413
Cdd:PRK13391 363 PFEYLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVf 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2414 -VALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK13391 437 gVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
2023-2479 |
2.71e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 105.88 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2023 AERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCP 2102
Cdd:PRK06060 40 AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2103 AEVERLPL-ETAAWPASADTRPlpeVAGETLAYVIYTSGSTGQPKGvAVSQAALV-----AHCQAAARtygVGPGDCQLQ 2176
Cdd:PRK06060 120 RVAEAAELmSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKA-AIHRHADPltfvdAMCRKALR---LTPEDTGLC 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2177 FASISFD-AAAEQLFVPLLAGARVLLGDAgQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGE 2255
Cdd:PRK06060 193 SARMYFAyGLGNSVWFPLATGGSAVINSA-PVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFR-SLRCVVSAGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2256 AWDASLltqqavqAEAWFNAYGPTeavitPLAWHCRAQEGGAPAIGRALGARRACILDAALQP------------CAPGM 2323
Cdd:PRK06060 271 ALELGL-------AERLMEFFGGI-----PILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPyeirvvapdgttAGPGV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2324 IGELYIGGQCLARGYLGRPgqtaerfvaDPFSGSGERLyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:PRK06060 339 EGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLII 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAYLV-GRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06060 409 EDEAVAEAAVVAVrESTGASTLQAFLVaTSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
652-998 |
2.79e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 102.17 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 652 GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWMQQAYGL-GVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGD 729
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLfDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 730 HRDPA---KLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD--AQQQVFAKLPqagLYNLYGPT 804
Cdd:cd05944 80 YRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVElrARFEDATGLP---VVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 805 EAaidvthwTCVEEgkdTVPIGRP--IGNLG---------CYILDGN---LEPVPVGVLGELYLAGRGLARGYHQRPGlt 870
Cdd:cd05944 157 EA-------TCLVA---VNPPDGPkrPGSVGlrlpyarvrIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTEG-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 871 aerfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLV 946
Cdd:cd05944 225 -----NKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAGELPV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 947 GYVVLESEGGDWREALAAHLAASLPEY-MVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05944 300 AYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
3060-3528 |
2.88e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 104.40 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:PRK12406 8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQSHLKLPLA----QGVQ--------------RIDLDRGAP---------WFEDYSEANPdihLDGENLAYVIYTSGST 3192
Cdd:PRK12406 88 IAHADLLHGLAsalpAGVTvlsvptppeiaaayRISPALLTPpagaidwegWLAQQEPYDG---PPVPQPQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3193 GKPKGAGNRHSALSNRLCWMQ---QAYGLGVGDTVL------QKTPFSFDVSVWEFfwplmsGARLVVAApgdHRDPAKL 3263
Cdd:PRK12406 165 GHPKGVRRAAPTPEQAAAAEQmraLIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGVDTLHFVPSMLQAFLQ--DE-----DVascTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAId 3336
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKlpEEvrakyDV---SSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3337 VThwTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLAR-GYHQRPGLTAE----RFVASpfvag 3409
Cdd:PRK12406 311 VT--FATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITS----- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3410 ermyrtGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDW 3485
Cdd:PRK12406 384 ------GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPdaefGEALMAVVEPQPGATLD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 3486 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:PRK12406 458 EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
3035-3525 |
2.88e-22 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 104.67 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3035 PLQR--GVHRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVA 3104
Cdd:cd05906 1 PLHRpeGAPRTLLELLLRAAERGPTKGityidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3105 LMAILKAGG--AYVPVDPEYPEE-------RQAYMLEDSGVelLLSQSHLKLPLA-----QGVQRIDLDRgapwFEDYSE 3170
Cdd:cd05906 81 FWACVLAGFvpAPLTVPPTYDEPnarlrklRHIWQLLGSPV--VLTDAELVAEFAgletlSGLPGIRVLS----IEELLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 ANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSG 3246
Cdd:cd05906 155 TAADHDLpqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVAAPGDH-RDPAKLVALINREGVdTLHFVPSMLQAFLQD--EDVASCT----SLKRIVCSGEALPADAQQQVFAKL 3319
Cdd:cd05906 235 CQQVHVPTEEIlADPLRWLDLIDRYRV-TITWAPNFAFALLNDllEEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLLRLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3320 PQAGL-------------------YNLYGPTEAAIDVTHWTCVeegkdavpiGRPIANLACYILDGNLEPVPVGVLGELY 3380
Cdd:cd05906 314 EPYGLppdairpafgmtetcsgviYSRSFPTYDHSQALEFVSL---------GRPIPGVSMRIVDDEGQLLPEGEVGRLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3381 LAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 3460
Cdd:cd05906 385 VRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3461 EAAVLAVDGR-------QLVGYVVLESESGDWR-------EALAAHLAASLPEYMVPaqwLALERMPLSPNGKLDRKAL 3525
Cdd:cd05906 458 PSFTAAFAVRdpgaeteELAIFFVPEYDLQDALsetlraiRSVVSREVGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2006-2479 |
2.97e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 104.38 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK08008 25 ALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETL-----AERLPCPAEVERLPLETAAWPA--------------SADTRPLPEVAGETLAYVIYTSGS 2141
Cdd:PRK08008 105 LQNSQASLLVTSAQFypmyrQIQQEDATPLRHICLTRVALPAddgvssftqlkaqqPATLCYAPPLSTDDTAEILFTSGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2142 TGQPKGVAVSQAALV-----AHCQAAAR---TY-GVGPG---DCQLqfasisfdAAAEQLFVpllAGARVLLGDagQWSA 2209
Cdd:PRK08008 185 TSRPKGVVITHYNLRfagyySAWQCALRdddVYlTVMPAfhiDCQC--------TAAMAAFS---AGATFVLLE--KYSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVTILDLPPAYLQ------QQAEELRHAGRRIAVRTCILGGEAWDasLLTQQAVQAeawFNAYGPTEAVI 2283
Cdd:PRK08008 252 RAFWGQVCKYRATITECIPMMIRtlmvqpPSANDRQHCLREVMFYLNLSDQEKDA--FEERFGVRL---LTSYGMTETIV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2284 -----TPlawhcrAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGG---QCLARGYLGRPGQTAERFVADPFS 2355
Cdd:PRK08008 327 giigdRP------GDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 GSGERLYRTGDLARYRVDgqveylgRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPL----LAAYLVGR 2431
Cdd:PRK08008 401 HTGDTGYVDEEGFFYFVD-------RRCNMIKRGGENVSCVELENIIATHPKIQDIVVV---GIKDSIrdeaIKAFVVLN 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 2432 DamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK08008 471 E---GETLsEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
532-1013 |
3.14e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 105.88 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 532 FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK06060 26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 612 LLSQSHLKLPLAQG--VQRIDLdQADAWLENHAENNPgieLNGENLAYVIYTSGSTGKPKGAGNRHS---ALSNRLCwmQ 686
Cdd:PRK06060 106 VVTSDALRDRFQPSrvAEAAEL-MSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHAdplTFVDAMC--R 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 687 QAYGLGVGDTVLQKTPFSFDV----SVWeffWPLMSGARLVVAAPGDHRDPAKLveLINREGVDTLHFVPSMLQAFLQDE 762
Cdd:PRK06060 180 KALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVIDSC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 763 DVASCTSLKRIVCSGEAL-PADAQQ--QVFAKLPqagLYNLYGPTEAAidvthWTCVEegkDTVPIGRPiGNLGCYILDG 839
Cdd:PRK06060 255 SPDSFRSLRCVVSAGEALeLGLAERlmEFFGGIP---ILDGIGSTEVG-----QTFVS---NRVDEWRL-GTLGRVLPPY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 840 NLEPVP-------VGVLGELYLAGRGLARGYHQRPgltaerfvaSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:PRK06060 323 EIRVVApdgttagPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 913 RGLRIELGEIEARLLEHPWVREAAVLAVdgRQLVGYVVLES----------EGGDWREALAAHLAASLPeYMVPAQWLAL 982
Cdd:PRK06060 394 GGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTLQAflvatsgatiDGSVMRDLHRGLLNRLSA-FKVPHRFAVV 470
|
490 500 510
....*....|....*....|....*....|....*...
gi 2310915810 983 ERMPLSPNGKLDRKAL-------PAPEVSVAQAGYSAP 1013
Cdd:PRK06060 471 DRLPRTPNGKLVRGALrkqsptkPIWELSLTEPGSGVR 508
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
4546-5035 |
3.33e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 104.39 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK13391 6 HAQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLP-----IPEGLSCLSVDREEEWAGFPAHDPEVA-----------LHGDNLayviY 4687
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARallkqCPGVRHRLVLDGDGELEGFVGYAEAVAglpatpiadesLGTDML----Y 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGV-------AVSHGPLIAHIVAtgERYEMTPEDCEL------HFMSFAFDGShegwMHPLinGARVLIRDD 4754
Cdd:PRK13391 162 SSGTTGRPKGIkrplpeqPPDTPLPLTAFLQ--RLWGFRSDMVYLspaplyHSAPQRAVML----VIRL--GGTVIVMEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4755 slWLPERTYAEMHRHGVTVGVFPP------------------VYLQQLAEHAerdGNPPPVRvycfggdaVAQASYDLaW 4816
Cdd:PRK13391 234 --FDAEQYLALIEEYGVTHTQLVPtmfsrmlklpeevrdkydLSSLEVAIHA---AAPCPPQ--------VKEQMIDW-W 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKYlfngYGPTE----TVVTPLLWKARAGdACGAAYMpiGTLlgnrsgYILDGQLNLLPVGVAGELYLGGeGVARG 4892
Cdd:PRK13391 300 GPIIHEY----YAATEglgfTACDSEEWLAHPG-TVGRAMF--GDL------HILDDDGAELPPGEPGTIWFEG-GRPFE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4893 YLERPALTAERFVPDPfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP 4972
Cdd:PRK13391 366 YLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4973 GA-VGQQlVGYVVAQEPAVADSPEAQAECRAqlktALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK13391 440 NEdLGEE-VKAVVQPVDGVDPGPALAAELIA----FCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3187-3482 |
3.34e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 101.59 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3187 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDvSVWEFFWPLMSGARLVVAAPGdhRDPAKLV 3264
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPS--FDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 ALINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 3342
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAELEHPDFDkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS-PVSTQTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEG--KDAVPIGRPIANLACYILD--GNLEPvPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDL 3418
Cdd:cd05917 165 TDDSieKRVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWLHTGDL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3419 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESES 3482
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPderyGEEVCAWIRLKEGA 305
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1554-1956 |
3.35e-22 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 103.11 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLF-HSLHGTEGDYVNQLRMDIGG-LDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRL 1631
Cdd:cd19538 3 PLSFAQRRLWFlHQLEGPSATYNIPLVIKLKGkLDVQALQQALYDVVERHESLRTVFPEEDG--VPYQLILEEDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1632 APPGSDPQRQAEAEREA---GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY-------AGQE 1701
Cdd:cd19538 81 EIKEVDEEELESEINEAvryPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarckgeAPEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1702 VAATVgRYRDYIGWLQ--------GRDAMATEF-FWRDRLASL----EMPTRLARQARTEQpgQGEHLR-ELDPQTTRQL 1767
Cdd:cd19538 161 APLPV-QYADYALWQQellgdesdPDSLIARQLaYWKKQLAGLpdeiELPTDYPRPAESSY--EGGTLTfEIDSELHQQL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1768 ASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLpVI---AAPQPqqSVADYLQG 1844
Cdd:cd19538 238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTL-VLrtdTSGNP--SFRELLER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1845 MQALNLALREHEHTPLYDI------QRWAGHggEALFDSILVFENFPVAE-ALRQAPADLEfstPSNHEQTNYPLTLgvT 1917
Cdd:cd19538 313 VKETNLEAYEHQDIPFERLvealnpTRSRSR--HPLFQIMLALQNTPQPSlDLPGLEAKLE---LRTVGSAKFDLTF--E 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1918 LGERLS----------LQYvyaRRD-FDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19538 386 LREQYNdgtpngiegfIEY---RTDlFDHETIEALAQRYLLLLESAVENP 432
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
660-955 |
3.53e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 101.59 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDvSVWEFFWPLMSGARLVVAAPGdhRDPAKLV 737
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPS--FDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 738 ELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 815
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAELEHPDFDkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS-PVSTQTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 816 VEEG--KDTVPIGRPIGNLGCYILD--GNLEPvPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDL 891
Cdd:cd05917 165 TDDSieKRVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWLHTGDL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 892 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEG 955
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPderyGEEVCAWIRLKEGA 305
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
4680-5040 |
4.84e-22 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 103.57 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFDGSheGWMhPLINGARVLIRDDS 4755
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALpffhSFGLTGC--LWL-PLLSGIKVVFHPNP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4756 lwLPERTYAEM-HRHGVTVGVFPPVYLQQLAEHAERDgNPPPVRVYCFGGDAVAQASYDLaWRALKPKYLFNGYGPTETv 4834
Cdd:cd05909 224 --LDYKKIPELiYDKKATILLGTPTFLRGYARAAHPE-DFSSLRLVVAGAEKLKDTLRQE-FQEKFGIRILEGYGTTEC- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 vTPLLwkaragdACGAAYMP-----IGTLLGNRSGYILDGQ-LNLLPVGVAGELYLGGEGVARGYLERPALTAErfvpdp 4908
Cdd:cd05909 299 -SPVI-------SVNTPQSPnkegtVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF------ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4909 fgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH-PAVREAVVVAQPGAV-GQQLVGYVVAQ 4986
Cdd:cd05909 365 --AFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRkGEKIVLLTTTT 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4987 EPAVadspeaqAECRAQLKTAlreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05909 443 DTDP-------SSLNDILKNA---GISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1999-2496 |
4.96e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 104.65 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1999 ASAPEAIAL---VCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYlPLDP 2070
Cdd:PRK07529 36 ARHPDAPALsflLDADpldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLIC-------------QET--------------LAERLPCPAEVERLPL------------- 2110
Cdd:PRK07529 115 LLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVlaalpelrtvvevdLARYLPGPKRLAVPLIrrkaharildfda 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2111 ETAAWPASADTRPLPEVAGETLAYViYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQ----FASISfd 2183
Cdd:PRK07529 195 ELARQPGDRLFSGRPIGPDDVAAYF-HTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDtvfCGLPlfhvNALLV-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2184 aaaeQLFVPLLAGARVLLGDAGQWSAQHLADE----VERHAVTILD-LPPAY---LQQQAEelrhaGRRI-AVRTCILGG 2254
Cdd:PRK07529 272 ----TGLAPLARGAHVVLATPQGYRGPGVIANfwkiVERYRINFLSgVPTVYaalLQVPVD-----GHDIsSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 EAWDASLLTQ-QAVQAEAWFNAYGPTEAVitplAWHCRAQEGGAPAIGrALGAR------RACILDAA---LQPCAPGMI 2324
Cdd:PRK07529 343 APLPVEVFRRfEAATGVRIVEGYGLTEAT----CVSSVNPPDGERRIG-SVGLRlpyqrvRVVILDDAgryLRDCAVDEV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQCLARGYLgRPGQTAERFVadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIkIR-GFRIEIGEIESQLL 2403
Cdd:PRK07529 418 GVLCIAGPNVFSGYL-EAAHNKGLWL-------EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAY--LV-GRDAMrgedlLAELRTWLAGRLP---AymQPTAWQVLSSLPLNANGKLDR 2476
Cdd:PRK07529 489 RHPAVALAAAVGRpDAHAGELPVAYvqLKpGASAT-----EAELLAFARDHIAeraA--VPKHVRILDALPKTAVGKIFK 561
|
570 580
....*....|....*....|....*.
gi 2310915810 2477 KALpKVDAAAR------RQAGEPPRE 2496
Cdd:PRK07529 562 PAL-RRDAIRRvlraalRDAGVEAEV 586
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
4547-5042 |
5.21e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 103.32 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEvRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSvdreEEWAGFPAHDPEVALHGDNLA----YVIYTSGSTGMPKGVAVSH 4702
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLPDEEGRVIEI----DEWKRMIEKYLPTYAPIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAHIVATGERYEMTPEDCEL--------HFMSfafdgsheGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVG 4774
Cdd:PRK07638 166 QSWLHSFDCNVHDFHMKREDSVLiagtlvhsLFLY--------GAISTLYVGQTVHLMRK--FIPNQVLDKLETENISVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4775 VFPPVYLQQLAEHAERDGNppPVRVYCFGGDAVAQASYDLA--WRALKpkyLFNGYGPTE-TVVTPLLWK--ARAGDACG 4849
Cdd:PRK07638 236 YTVPTMLESLYKENRVIEN--KMKIISSGAKWEAEAKEKIKniFPYAK---LYEFYGASElSFVTALVDEesERRPNSVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4850 AAYMPIGTLLGNRSGYILDGqlnllpvGVAGELYLGGEGVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADG 4929
Cdd:PRK07638 311 RPFHNVQVRICNEAGEEVQK-------GEIGTVYVKSPQFFMGYIIGGVLARE--------LNADGWMTVRDVGYEDEEG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4930 VVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPavadspeaqaecRAQLKTAL 5008
Cdd:PRK07638 376 FIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEKPVAIIKGSAT------------KQQLKSFC 443
|
490 500 510
....*....|....*....|....*....|....
gi 2310915810 5009 RERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK07638 444 LQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
3064-3525 |
6.69e-22 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 103.18 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAhALIERGVGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYP--EERQAYMLEDSGVELLLS 3141
Cdd:cd05909 8 LTYRKLLTGAIALA-RKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 qSHLKLPLAQGVQRIDLDRGAPW--FED---------------YSEANPDIHL--------DGENLAYVIYTSGSTGKPK 3196
Cdd:cd05909 85 -SKQFIEKLKLHHLFDVEYDARIvyLEDlrakiskadkckaflAGKFPPKWLLrifgvapvQPDDPAVILFTSGSEGLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3197 GAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP----FSFDVSVWeffWPLMSGARLVVAApgDHRDPAKLVALINREGV 3272
Cdd:cd05909 164 GVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCLW---LPLLSGIKVVFHP--NPLDYKKIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3273 DTLHFVPSMLQAFL---QDEDVAsctSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDA 3349
Cdd:cd05909 239 TILLGTPTFLRGYAraaHPEDFS---SLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTECS-PVISVNTPQSPNKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3350 VPIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAerfvaspFVAGERMYRTGDLARYRADGVIE 3428
Cdd:cd05909 314 GTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3429 YAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV-DGR---QLVgyVVLESESGDWREALAAHLAASLPEYMVP 3503
Cdd:cd05909 387 ITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRkgeKIV--LLTTTTDTDPSSLNDILKNAGISNLAKP 464
|
490 500
....*....|....*....|..
gi 2310915810 3504 AQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05909 465 SYIHQVEEIPLLGTGKPDYVTL 486
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1128-1400 |
6.78e-22 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 102.18 E-value: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1128 QPLDGDRLGRALERLQAQHDALRLRFREERgawHQAYAEQAGEPLWR-------RQAGSEEALLALCEE-AQRSLDLEQG 1199
Cdd:cd19535 35 EDLDPDRLERAWNKLIARHPMLRAVFLDDG---TQQILPEVPWYGITvhdlrglSEEEAEAALEELRERlSHRVLDVERG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDE-LDYWQA 1278
Cdd:cd19535 112 PLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPLPPLELSFRDYLLAEQALRETAYERaRAYWQE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1279 QLHDAPHA--LPCENPHGALENRHERKLVLTLDAERtRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:cd19535 192 RLPTLPPApqLPLAKDPEEIKEPRFTRREHRLSAEQ-WQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLF 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2310915810 1357 GREDLGEAIDlsRTVGWFTS--LFPVRLTPAADLGESLKAIKEQLR 1400
Cdd:cd19535 271 NRLPLHPDVN--DVVGDFTSllLLEVDGSEGQSFLERARRLQQQLW 314
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
2997-3526 |
8.16e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 103.15 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2997 LLRGMLENPQASVDSLPMLDAEERG--QLLEGWNATAAEYPlqrgvhrlfeeqvERTptapALAFGEERLDYAELNRRAN 3074
Cdd:PRK13383 9 LVRSGLLNPPSPRAVLRLLREASRGgtNPYTLLAVTAARWP-------------GRT----AIIDDDGALSYRELQRATE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3075 RLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQ 3154
Cdd:PRK13383 72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3155 RIDLDRGAPWFEDYSEANPDIHLDGEnlaYVIYTSGSTGKPKGAgNRHSALSNrlcwmqqayGLGVGDTVLQKTpfsfdv 3234
Cdd:PRK13383 152 AVAVIDPATAGAEESGGRPAVAAPGR---IVLLTSGTTGKPKGV-PRAPQLRS---------AVGVWVTILDRT------ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3235 svweffwPLMSGARLVVAAP----------------------GDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA 3292
Cdd:PRK13383 213 -------RLRTGSRISVAMPmfhglglgmlmltialggtvltHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3293 SCTS----LKRIVCSGEAL-PADAQQqvFAKLPQAGLYNLYGPTEAAIDVThwTCVEEGKDAV-PIGRPIANLACYILDG 3366
Cdd:PRK13383 286 RARNplpqLRVVMSSGDRLdPTLGQR--FMDTYGDILYNGYGSTEVGIGAL--ATPADLRDAPeTVGKPVAGCPVRILDR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3367 NLEPVPVGVLGELYLAGQGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 3446
Cdd:PRK13383 362 NNRPVGPRVTGRIFVGGELAGTRYTDGGG--------KAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3447 GEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:PRK13383 432 RAVENALAAHPAVADNAVIGVPderfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLR 511
|
....
gi 2310915810 3523 KALP 3526
Cdd:PRK13383 512 KELP 515
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
3047-3478 |
8.80e-22 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 103.80 E-value: 8.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVERTPTAPALAF-GEE-----RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd05966 62 HLKERGDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLLS---------QSHLK------LPLAQGVQRI----DLDRGAPWFE-----------DYSE 3170
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITadggyrggkVIPLKeivdeaLEKCPSVEKVlvvkRTGGEVPMTEgrdlwwhdlmaKQSP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 ANPDIHLDGENLAYVIYTSGSTGKPKGAgnRHSalsnrlcwmQQAYGLGVGDTvlqkTPFSFDVSVWEFFW--------- 3241
Cdd:cd05966 222 ECEPEWMDSEDPLFILYTSGSTGKPKGV--VHT---------TGGYLLYAATT----FKYVFDYHPDDIYWctadigwit 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3242 --------PLMSGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASC--TSLKRIVCSGEAL 3307
Cdd:cd05966 287 ghsyivygPLANGATTVMfeGTP-TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHdlSSLRVLGSVGEPI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3308 PADAQQQvfaklpqagLYNLYGPTEAAIDVTHW-TcvEEG-------KDAVPI-----GRPIANLACYILDGNLEPVPVG 3374
Cdd:cd05966 366 NPEAWMW---------YYEVIGKERCPIVDTWWqT--ETGgimitplPGATPLkpgsaTRPFFGIEPAILDEEGNEVEGE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3375 VLGelYLAGQ----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd05966 435 VEG--YLVIKrpwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVE 508
|
490 500 510
....*....|....*....|....*....|..
gi 2310915810 3451 ARLLEHPWVREAAVLAVD----GRQLVGYVVL 3478
Cdd:cd05966 509 SALVAHPAVAEAAVVGRPhdikGEAIYAFVTL 540
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
4551-5037 |
9.35e-22 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 103.80 E-value: 9.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIF------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLA---------VLKAGGAYV 4615
Cdd:cd05966 67 GDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFAGFSAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PLdieypRERLlymmQDSRAHLL----------------LTHSHLLERLPIPEglSCLSVDR---------------EEE 4664
Cdd:cd05966 147 SL-----ADRI----NDAQCKLVitadggyrggkviplkEIVDEALEKCPSVE--KVLVVKRtggevpmtegrdlwwHDL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4665 WAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeryemtpedcelhfMSFAFDgSHE------- 4737
Cdd:cd05966 216 MAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATT---------------FKYVFD-YHPddiywct 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4738 ---GWM--H------PLINGARVLIRDDSLWLPE--RTYAEMHRHGVTVGVFPPVYLQQLAehaeRDGNPPPVRvycfgg 4804
Cdd:cd05966 280 adiGWItgHsyivygPLANGATTVMFEGTPTYPDpgRYWDIVEKHKVTIFYTAPTAIRALM----KFGDEWVKK------ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4805 davaqasYDL----------------AWRALKpKYLFNGYGP-------TET---VVTPL--LWKARAGdacgAAYMPig 4856
Cdd:cd05966 350 -------HDLsslrvlgsvgepinpeAWMWYY-EVIGKERCPivdtwwqTETggiMITPLpgATPLKPG----SATRP-- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 tLLGNRSGyILDGQLNLLPVGVAGELYLGGE--GVARGYLERPaltaERFVPDPFGA-PGsrLYRSGDLTRGRADGVVDY 4933
Cdd:cd05966 416 -FFGIEPA-ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKfPG--YYFTGDGARRDEDGYYWI 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVaqepaVADSPEAQAECRAQLKTALRERL 5012
Cdd:cd05966 488 TGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIkGEAIYAFVT-----LKDGEEPSDELRKELRKHVRKEI 562
|
570 580
....*....|....*....|....*
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd05966 563 GPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
2011-2491 |
1.56e-21 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 103.02 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA-------GYlpldpnyPAERLAYMLRD 2083
Cdd:cd05966 82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhsvvfaGF-------SAESLADRIND 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQ----------------ETLAERLPCPAEV---ERLPLETAAWP----------ASADTRPLPE-VAGETLA 2133
Cdd:cd05966 155 AQCKLVITAdggyrggkviplkeivDEALEKCPSVEKVlvvKRTGGEVPMTEgrdlwwhdlmAKQSPECEPEwMDSEDPL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQlqfASI------SFdaaaeQLFVPLLAGARVLL-- 2201
Cdd:cd05966 235 FILYTSGSTGKPKGVVHTTGGYLLYAATTFKyVFDYHPDDiywCT---ADIgwitghSY-----IVYGPLANGATTVMfe 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 G-----DAGQWsaqhlADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRtcILG--GE-----AWDaslltqqa 2266
Cdd:cd05966 307 GtptypDPGRY-----WDIVEKHKVTIFYTAPTairALMKFGDEWVKKHDLSSLR--VLGsvGEpinpeAWM-------- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2267 vqaeaWFN------------AYGPTE---AVITPLAWHCRAQEGGApaiGRALGARRACILDAALQPCAPGMIGELYI-- 2329
Cdd:cd05966 372 -----WYYevigkercpivdTWWQTEtggIMITPLPGATPLKPGSA---TRPFFGIEPAILDEEGNEVEGEVEGYLVIkr 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2330 ---GgqcLARGYLGRPgqtaERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:cd05966 444 pwpG---MARTIYGDH----ERYEDtyfSKFPG----YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:cd05966 513 AHPAVAEAAVVGRpHDIKGEAIYAFVTLKDGEEPSDELRkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
570
....*....|
gi 2310915810 2482 VdAAARRQAG 2491
Cdd:cd05966 593 I-AAGEEELG 601
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
537-938 |
1.59e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 101.11 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVdpeypeerqaymledsgvQLLLSQS 616
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------------TTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 617 HLKlplaqgvQRIDLDQA--DAWLENHAENNPGIelngenlayVIYTSGSTGKPKGAGNRHSA-----LSNrLCWMqqay 689
Cdd:cd05974 63 DLR-------DRVDRGGAvyAAVDENTHADDPML---------LYFTSGTTSKPKLVEHTHRSypvghLST-MYWI---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 690 GLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT 768
Cdd:cd05974 122 GLKPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 769 SLKRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDTVP--IGRPIGNLGCYILDGNLEPVPV 846
Cdd:cd05974 201 KLREVVGAGEPLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGN----SPGQPVKAgsMGRPLPGYRVALLDPDGAPATE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 847 GVLGELYLAGR--GLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 924
Cdd:cd05974 276 GEVALDLGDTRpvGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410
....*....|....
gi 2310915810 925 RLLEHPWVREAAVL 938
Cdd:cd05974 349 VLIEHPAVAEAAVV 362
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
520-951 |
1.95e-21 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 102.64 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 520 QVERTPTAPALAF-GEE-----RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd05966 62 HLKERGDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 594 EYPEERQAYMLEDSGVQLLLS---------QSHLK------LPLAQGVQRI-----------DLDQADAWLE----NHAE 643
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITadggyrggkVIPLKeivdeaLEKCPSVEKVlvvkrtggevpMTEGRDLWWHdlmaKQSP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 644 NNPGIELNGENLAYVIYTSGSTGKPKGAgnRHSalsnrlcwmQQAYGLGVGDTvlqkTPFSFDVSVWEFFW--------- 714
Cdd:cd05966 222 ECEPEWMDSEDPLFILYTSGSTGKPKGV--VHT---------TGGYLLYAATT----FKYVFDYHPDDIYWctadigwit 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 715 --------PLMSGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASC--TSLKRIVCSGEAL 780
Cdd:cd05966 287 ghsyivygPLANGATTVMfeGTP-TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHdlSSLRVLGSVGEPI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 781 PADAQQQvfaklpqagLYNLYGPTEAAIDVTHW---------TCVEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:cd05966 366 NPEAWMW---------YYEVIGKERCPIVDTWWqtetggimiTPLPGATPLKPgsATRPFFGIEPAILDEEGNEVEGEVE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 850 GelYLAGR----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEAR 925
Cdd:cd05966 437 G--YLVIKrpwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
|
490 500 510
....*....|....*....|....*....|
gi 2310915810 926 LLEHPWVREAAVLAVD----GRQLVGYVVL 951
Cdd:cd05966 511 LVAHPAVAEAAVVGRPhdikGEAIYAFVTL 540
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1102-1515 |
1.96e-21 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 100.46 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1102 PVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREE--RGAWHQAYAEQaGEPLWRRQAGS 1179
Cdd:cd19542 6 PMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESsaEGTFLQVVLKS-LDPPIEEVETD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1180 EEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYadlDADLGPRSSSYQTWS 1259
Cdd:cd19542 85 EDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY---NGQLLPPAPPFSDYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1260 RHLHEQagARLDELDYWQAQLHDA-PHALPCENPhgalenrhERKLVLTLDAE-RTRQLLQEAPAAYRTQVNDLLLTALA 1337
Cdd:cd19542 162 SYLQSQ--SQEESLQYWRKYLQGAsPCAFPSLSP--------KRPAERSLSSTrRSLAKLEAFCASLGVTLASLFQAAWA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1338 RATCRWSGDASVLVqleGH---GREDLGEAIDlsRTVGWFTSLFPVRLTPAADL--GESLKAIKEQlrgvpdkgvgygLL 1412
Cdd:cd19542 232 LVLARYTGSRDVVF---GYvvsGRDLPVPGID--DIVGPCINTLPVRVKLDPDWtvLDLLRQLQQQ------------YL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1413 RYLAGE--------EAATRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAplanwLSIEGQVYGGELSL 1484
Cdd:cd19542 295 RSLPHQhlslreiqRALGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYP-----VAVEVEPSGDSLKV 369
|
410 420 430
....*....|....*....|....*....|.
gi 2310915810 1485 HWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19542 370 SLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
2001-2481 |
2.88e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 101.01 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK07638 14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETLAERLPCpaeVERLPLETAAWPA---SADTRPLP-EVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK07638 93 LAISNADMIVTERYKLNDLPD---EEGRVIEIDEWKRmieKYLPTYAPiENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTYGVGPGDCQL----QFASISFDAAAEQLFVpllaGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLq 2232
Cdd:PRK07638 170 HSFDCNVHDFHMKREDSVLiagtLVHSLFLYGAISTLYV----GQTVHL--MRKFIPNQVLDKLETENISVMYTVPTML- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 qqaEELRHAGRRI-AVRTCILGGEAWDASlltQQAVQAEAWFNA-----YGPTE-AVITPLawHCRAQEGGAPAIGRALG 2305
Cdd:PRK07638 243 ---ESLYKENRVIeNKMKIISSGAKWEAE---AKEKIKNIFPYAklyefYGASElSFVTAL--VDEESERRPNSVGRPFH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRpgqtaerfVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK07638 315 NVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG--------GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgedllaELRTWLAGRLPAYMQPTAWQVLS 2464
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVpDSYWGEKPVAIIKGSATKQ------QLKSFCLQRLSSFKIPKEWHFVD 460
|
490
....*....|....*..
gi 2310915810 2465 SLPLNANGKLDRKALPK 2481
Cdd:PRK07638 461 EIPYTNSGKIARMEAKS 477
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
2006-2487 |
3.08e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 101.31 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSG 2085
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2086 ARWLICQETLAERLP--CPAEVERLPLET-----AAWPASADTRPLPEVA-----------------GETLAYVIYTSGS 2141
Cdd:PRK12406 84 ARVLIAHADLLHGLAsaLPAGVTVLSVPTppeiaAAYRISPALLTPPAGAidwegwlaqqepydgppVPQPQSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2142 TGQPKGV-----AVSQAAlvAHCQAAARTYGVGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLgdaGQWSAQHLADE 2215
Cdd:PRK12406 164 TGHPKGVrraapTPEQAA--AAEQMRALIYGLKPGIRALLTGPLYHSAPnAYGLRAGRLGGVLVLQ---PRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVT-----------ILDLPPAYLQQ-QAEELRHagrriavrtcILGGEAWDASLLTQQAVqaEAW----FNAYGPT 2279
Cdd:PRK12406 239 IERHRIThmhmvptmfirLLKLPEEVRAKyDVSSLRH----------VIHAAAPCPADVKRAMI--EWWgpviYEYYGST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EavITPLAWHCRAQEGGAPA-IGRALGARRACILDAALQPCAPGMIGELYiggqCLARG-----YLGRPGQTAErfvadp 2353
Cdd:PRK12406 307 E--SGAVTFATSEDALSHPGtVGKAAPGAELRFVDEDGRPLPQGEIGEIY----SRIAGnpdftYHNKPEKRAE------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 fSGSGErLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLvgrD 2432
Cdd:PRK12406 375 -IDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIpDAEFGEALMAVV---E 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2433 AMRGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL--PKVDAAAR 2487
Cdd:PRK12406 450 PQPGATLdEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLrdPYWANAGR 507
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
2056-2481 |
3.62e-21 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 101.39 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2056 LGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-----PCPAEVERLPLETAAWPASADTRPLPEVAGE 2130
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVdsvasECPSLKTKLLVSEKSRDGWLNFKELLNEAST 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYV---------IY-TSGSTGQPKGVAVSQAALVAHCQAAARTY-GVGPGDCQLQFASISF-DAAAEQLFVPLLAGAR 2198
Cdd:cd05928 165 EHHCVetgsqepmaIYfTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGAC 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2199 VLLGDAGQWSAQHLADEVERHAVTIL-DLPPAY---LQQ-----QAEELRHagrriavrtCILGGEAWDASLLTQQAVQA 2269
Cdd:cd05928 245 VFVHHLPRFDPLVILKTLSSYPITTFcGAPTVYrmlVQQdlssyKFPSLQH---------CVTGGEPLNPEVLEKWKAQT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2270 EA-WFNAYGPTEAVITplawhCRAQEG---GAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQ-----CLARGYLG 2340
Cdd:cd05928 316 GLdIYEGYGQTETGLI-----CANFKGmkiKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVD 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGV 2419
Cdd:cd05928 391 NPEKTAATIRGD--------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSpDPI 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2420 GGPLLAAYLVGRDAMRGED---LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:cd05928 463 RGEVVKAFVVLAPQFLSHDpeqLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
653-995 |
3.63e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 98.49 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 653 ENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW------MQQAYGLGVGDTVLQKTPFSFDVSVWeffWPLM----SGARL 722
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAV-----LLANKTFFavpdilQKEGLNWVVGDVTYLPLPATHIGGLW---WILTclihGGLCV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 723 VVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAF--LQDEDVASCTSLkRIVCSGEALPADAQQQVFAKLPQAGLYNL 800
Cdd:cd17635 73 TG---GENTTYKSLFKILTTNAVTTTCLVPTLLSKLvsELKSANATVPSL-RLIGYGGSRAIAADVRFIEATGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 801 YGPTEaaidVTHWTCVEEGKDTVPI---GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVas 877
Cdd:cd17635 149 YGLSE----TGTALCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 878 pfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGD 957
Cdd:cd17635 223 -----DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2310915810 958 WRE-----ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:cd17635 298 ELDenairALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
78-285 |
4.85e-21 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 99.63 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 78 VRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFE--DCSGLPEAEQEARLREEAQREslqpF 155
Cdd:cd19534 28 LRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEvvDLSSLAQAAAIEALAAEAQSS----L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 156 DLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSrfySAYATGAEPGLPALP--IQYADYALWQRSWLEA 233
Cdd:cd19534 104 DLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLE---AAYEQALAGEPIPLPskTSFQTWAELLAEYAQS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 234 GEQERQLEYWRGKLGErhPVLELPTDHPRpvvpSYRGSRYE-FSIEPALAEAL 285
Cdd:cd19534 181 PALLEELAYWRELPAA--DYWGLPKDPEQ----TYGDARTVsFTLDEEETEAL 227
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
2001-2479 |
5.81e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 100.83 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGDEHLSYAELDMRAERLARGLRARGVVA--EALVAIAAERSFDLVvgLLGILKAGAgyLPLDPNYPAERL- 2077
Cdd:PRK10946 36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPgdTALVQLGNVAEFYIT--FFALLKLGV--APVNALFSHQRSe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 --AYMlRDSGARWLICQ------------ETLAERLPCPAEV----ERLPLETAAWPASADT--RPLPEVAGEtLAYVIY 2137
Cdd:PRK10946 112 lnAYA-SQIEPALLIADrqhalfsdddflNTLVAEHSSLRVVlllnDDGEHSLDDAINHPAEdfTATPSPADE-VAFFQL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVA-------VSQAALVAHCQAAARTYGVgpgdCQLQfASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQ 2210
Cdd:PRK10946 190 SGGSTGTPKLIPrthndyyYSVRRSVEICGFTPQTRYL----CALP-AAHNYPMSSPGALGVFLAGGTVVL--APDPSAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDL-PPA---YLQQQAEelrhAGRRIAVRTCIL---GGEAWDASLLTQ---------QAV--QAEAW 2272
Cdd:PRK10946 263 LCFPLIEKHQVNVTALvPPAvslWLQAIAE----GGSRAQLASLKLlqvGGARLSETLARRipaelgcqlQQVfgMAEGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 FNaY----GPTEAVITplawhcrAQeggapaiGRAL-GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAE 2347
Cdd:PRK10946 339 VN-YtrldDSDERIFT-------TQ-------GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNAS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2348 RFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAA 2426
Cdd:PRK10946 404 AFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMeDELMGEKSCA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2427 YLVGRDAMRGedllAELRTWLAGRLPA-YMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK10946 477 FLVVKEPLKA----VQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
2135-2474 |
5.88e-21 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 97.57 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLlgDAGQWSAQ 2210
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAG---IVACLLTGATVV--PVAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIA----VRTCILGGEAWDASLL--TQQAVQAEAWFNAYGPTEAVIT 2284
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSL---LDHPGRKKFdlssLRAAVTGAATVPVELVrrMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 PLawhCRAQEGG---APAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerl 2361
Cdd:cd17638 157 TM---CRPGDDAetvATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2362 YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDA--MRGED 2438
Cdd:cd17638 217 LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpDERMGEVGKAFVVARPGvtLTEED 296
|
330 340 350
....*....|....*....|....*....|....*.
gi 2310915810 2439 LLAelrtWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:cd17638 297 VIA----WCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
3180-3522 |
6.17e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 97.72 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 ENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW------MQQAYGLGVGDTVLQKTPFSFDVSVWeffWPLM----SGARL 3249
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAV-----LLANKTFFavpdilQKEGLNWVVGDVTYLPLPATHIGGLW---WILTclihGGLCV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAF--LQDEDVASCTSLkRIVCSGEALPADAQQQVFAKLPQAGLYNL 3327
Cdd:cd17635 73 TG---GENTTYKSLFKILTTNAVTTTCLVPTLLSKLvsELKSANATVPSL-RLIGYGGSRAIAADVRFIEATGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3328 YGPTEaaidVTHWTCVEEGKDAVPI---GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVas 3404
Cdd:cd17635 149 YGLSE----TGTALCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3405 pfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGD 3484
Cdd:cd17635 223 -----DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2310915810 3485 WRE-----ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:cd17635 298 ELDenairALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
3657-4049 |
7.08e-21 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 99.06 E-value: 7.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRFHETDG----TWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLR 3732
Cdd:cd19536 36 LNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvQVVHRQAQVPVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3733 SLLVDMADGGQRLL-LVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPgKTSPFKAWAGRVSEHARGEsmkAQLQFW 3811
Cdd:cd19536 116 AALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEYKPLSLP-PAQPYRDFVAHERASIQQA---ASERYW 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3812 RELLEGA---PAELPCEHPQGALEQRFATsvqsRFDRSLTERllkQAPAAYRTQVN--DLLLTALARVVCRWSGASSSLV 3886
Cdd:cd19536 192 REYLAGAtlaTLPALSEAVGGGPEQDSEL----LVSVPLPVR---SRSLAKRSGIPlsTLLLAAWALVLSRHSGSDDVVF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3887 QLEGHGREELFADIDlsRTVGWFTSLFPVRLS-PVADLGESLKAIKEQLRaipdkglgyGLLRYLAGE--ESARVLAGLP 3963
Cdd:cd19536 265 GTVVHGRSEETTGAE--RLLGLFLNTLPLRVTlSEETVEDLLKRAQEQEL---------ESLSHEQVPlaDIQRCSEGEP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3964 QARITFNYLgQFDAQFDEMALLDPAGE---SAGAEMDPGAPLdnWLSLNGRvfDGELSIDWSFSSQMFGEDQVRRLADDY 4040
Cdd:cd19536 334 LFDSIVNFR-HFDLDFGLPEWGSDEGMrrgLLFSEFKSNYDV--NLSVLPK--QDRLELKLAYNSQVLDEEQAQRLAAYY 408
|
....*....
gi 2310915810 4041 VAELTALVD 4049
Cdd:cd19536 409 KSAIAELAT 417
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
4532-5037 |
8.04e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 100.62 E-value: 8.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4532 GYPATPLVHQRVAER----ARMAPDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PRK12583 9 GGGDKPLLTQTIGDAfdatVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4606 AVLKAGGAYVPLDIEYPRERLLYMMQDSRA-------------------------HLLLTHSHLLERLPIPEGLSCLSVD 4660
Cdd:PRK12583 89 ATARIGAILVNINPAYRASELEYALGQSGVrwvicadafktsdyhamlqellpglAEGQPGALACERLPELRGVVSLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4661 REEEWAGFPA-------------HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL-- 4725
Cdd:PRK12583 169 PPPGFLAWHElqargetvsrealAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4726 --HFMSFAFDGSHEGWMhplINGARVLIRDDSlWLPERTYAEMHRHGVTV--GVfPPVYLQQLaEHAERDG-NPPPVRVY 4800
Cdd:PRK12583 249 vpLYHCFGMVLANLGCM---TVGACLVYPNEA-FDPLATLQAVEEERCTAlyGV-PTMFIAEL-DHPQRGNfDLSSLRTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGdavAQASYDLAWRALKPKYLFN---GYGPTETvvTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVG 4877
Cdd:PRK12583 323 IMAG---APCPIEVMRRVMDEMHMAEvqiAYGMTET--SPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4878 VAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARL 4957
Cdd:PRK12583 398 EIGELCTRGYSVMKGYWNNPEATAESIDEDGW-------MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4958 REHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSPEAQAECRAQLKtalrerlpEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK12583 471 FTHPAVADVQVFGVPDEkYGEEIVAWVRLHPGHAASEEELREFCKARIA--------HFKVPRYFRFVDEFPMTVTGKVQ 542
|
.
gi 2310915810 5037 R 5037
Cdd:PRK12583 543 K 543
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
4685-5036 |
8.36e-21 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 97.37 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------H--FMSFAFDGSHEGwmhplinGARVLIRDDSl 4756
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLnsgplfHigTLMFTLATFHAG-------GTNVFVRRVD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 wlPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNPPPVRVYCFggdavaqaSYDLAWRALKP------KYLFNGYGP 4830
Cdd:cd17636 77 --AEEVLELIEAERCTHAFLLPPTIDQIVE-LNADGLYDLSSLRSS--------PAAPEWNDMATvdtspwGRKPGGYGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4831 TEtVVTPLLWKARAGDACGAAYMPiGTLLGNRsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfg 4910
Cdd:cd17636 146 TE-VMGLATFAALGGGAIGGAGRP-SPLVQVR---ILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4911 apgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAV 4990
Cdd:cd17636 216 ---GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2310915810 4991 ADSPEAQAE-CRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd17636 293 SVTEAELIEhCRA--------RIASYKKPKSVEFADALPRTAGGADD 331
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
4122-4498 |
8.50e-21 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 98.87 E-value: 8.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4122 DIPRFRAAWQSALDRHAILRSGFAWQGE--LQQPLQIVyrqrQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPL 4199
Cdd:cd20483 37 DVNLLQKALSELVRRHEVLRTAYFEGDDfgEQQVLDDP----SFHLIVIDLSEAADPEAALDQLVRNLRRQELDIEEGEV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4200 LRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AGRSP---EQPRDGrYSDYI----AWLQRQDAAATE 4268
Cdd:cd20483 113 IRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLatvPPPPVQ-YIDFTlwhnALLQSPLVQPLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4269 AFWREQMAALDEPTRLVE-ALAQPGLTSANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVV 4347
Cdd:cd20483 192 DFWKEKLEGIPDASKLLPfAKAERPPVKDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4348 FGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQglQRQNLALREQEHTplfelqrwagfggEAVFDNLL- 4426
Cdd:cd20483 272 IGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLE--STKTTCLEAYEHS-------------AVPFDYIVd 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4427 ------------VFE---NYPVDEVLERSSAGGVRFGAVAmHEQ--TNYPLAL-ALGGGD-SLSLQFSYDRGLFPAATIE 4487
Cdd:cd20483 335 aldvprstshfpIGQiavNYQVHGKFPEYDTGDFKFTDYD-HYDipTACDIALeAEEDPDgGLDLRLEFSTTLYDSADME 413
|
410
....*....|.
gi 2310915810 4488 RLGRHLTTLLE 4498
Cdd:cd20483 414 RFLDNFVTFLT 424
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
3042-3479 |
9.34e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 100.27 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGVGA-DRlVGV-AMERsIEMVVALMAILKAGGAYVP 3117
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKgDR-VGIwAPNV-PEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEYPEERQAYMLEDSGVELLLSQSHLK---------------------------LPLAQGVQRIDlDRGAPWFEDYSE 3170
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelapelatcepgqlqsarLPELRRVIFLG-DEKHPGMLNFDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 -ANPDIHLDGENLAY---------VI---YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvw 3237
Cdd:PRK08315 177 lLALGRAVDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3238 eF--FWPLM-------SGARLVVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEA 3306
Cdd:PRK08315 250 -YhcFGMVLgnlacvtHGATMVY--PGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARfdLSSLRTGIMAGSP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3307 LPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEgkdavPI-------GRPIANLACYILDGNL-EPVPVGVLGE 3378
Cdd:PRK08315 327 CPIEVMKRVIDKMHMSEVTIAYGMTETS-PVSTQTRTDD-----PLekrvttvGRALPHLEVKIVDPETgETVPRGEQGE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVkLRGlrielG------EIEAR 3452
Cdd:PRK08315 401 LCTRGYSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEF 468
|
490 500 510
....*....|....*....|....*....|.
gi 2310915810 3453 LLEHPWVREAAVLAVD----GRQLVGYVVLE 3479
Cdd:PRK08315 469 LYTHPKIQDVQVVGVPdekyGEEVCAWIILR 499
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
3052-3527 |
1.04e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 100.30 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPAL--AFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PLN02574 53 NGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQ-------SHLKLPLAQGVQRIDLDRGAPWFEDY-------SEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:PLN02574 133 KRVVDCSVGLAFTSpenveklSPLGVPVIGVPENYDFDSKRIEFPKFyelikedFDFVPKPVIKQDDVAAIMYSSGTTGA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSN------RLCWMQQAYGlGVGDTVLQKTPFSFDVSVWEFFWPLMS-GARLVVAAPGDHRDpakLVALI 3267
Cdd:PLN02574 213 SKGVVLTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASD---MVKVI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3268 NREGVDTLHFVPSMLQAFLQDEDVASCTSLK--RIVCSGEALPADAQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVE 3344
Cdd:PLN02574 289 DRFKVTHFPVVPPILMALTKKAKGVCGEVLKslKQVSCGAAPLSGKFIQDFVQtLPHVDFIQGYGMTESTAVGTRGFNTE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3345 EGKDAVPIGRPIANLACYILD---GNLepVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARY 3421
Cdd:PLN02574 369 KLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3422 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PLN02574 441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPdkecGEIPVAFVVRRQGSTLSQEAVINYVAKQV 520
|
490 500 510
....*....|....*....|....*....|
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PLN02574 521 APYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
4550-5042 |
1.10e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 99.68 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4550 APDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGgaYVPLDIEYPRERL--- 4626
Cdd:PRK10946 36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSeln 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQ-------DSRAHLLLTHSHLLERL----PIPE--------GLSCLSVDREEEWAGFPAhDPEVAlhgDNLAYVIY 4687
Cdd:PRK10946 114 AYASQiepalliADRQHALFSDDDFLNTLvaehSSLRvvlllnddGEHSLDDAINHPAEDFTA-TPSPA---DEVAFFQL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CEL---HFMSFAFDGS----HEGwmhplinGARVLIRDDSlw 4757
Cdd:PRK10946 190 SGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTrylCALpaaHNYPMSSPGAlgvfLAG-------GTVVLAPDPS-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 lPERTYAEMHRHGVTV-GVFPP---VYLQQLAEHAERDgNPPPVRVYCFGGdavAQASYDLAWRAlkPKYLfnG------ 4827
Cdd:PRK10946 261 -ATLCFPLIEKHQVNVtALVPPavsLWLQAIAEGGSRA-QLASLKLLQVGG---ARLSETLARRI--PAEL--Gcqlqqv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4828 YGPTETVVTpllwKARAGDACGAAYMPIGT-LLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVP 4906
Cdd:PRK10946 332 FGMAEGLVN----YTRLDDSDERIFTTQGRpMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 DPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVA 4985
Cdd:PRK10946 408 NGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEKSCAFLVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4986 QEPAVAdspeaqaecrAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK10946 481 KEPLKA----------VQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
3061-3478 |
1.12e-20 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 100.47 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGA-DRLVgVAMERSIEMVVALMAILKAG-------GAYVP---------VDPEY- 3122
Cdd:cd05967 80 ERTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGaihsvvfGGFAAkelasriddAKPKLi 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 --------PEERQAYM-LEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFeDYSEA------NPDIHLDGENLAYVIY 3187
Cdd:cd05967 159 vtascgiePGKVVPYKpLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDL-DWSELlakaepVDCVPVAATDPLYILY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGA----GNRHSALSnrlcW-MQQAYGLGVGDTvlqktpfsfdvsvwefFW-----------------PLMS 3245
Cdd:cd05967 238 TSGTTGKPKGVvrdnGGHAVALN----WsMRNIYGIKPGDV----------------WWaasdvgwvvghsyivygPLLH 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVV--AAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVA-----SCTSLKRIVCSGEALPADAQQQVFA 3317
Cdd:cd05967 298 GATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKeDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAEN 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 KLPQAGLYNlYGPTEAAIDVTHwTCVEEGKDAVPIGRPIANLACY---ILDGNLEPVPVGVLGELYLAGQgLARGYHQRP 3394
Cdd:cd05967 378 TLGVPVIDH-WWQTETGWPITA-NPVGLEPLPIKAGSPGKPVPGYqvqVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3395 GLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GR 3470
Cdd:cd05967 455 WKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRdelkGQ 534
|
....*...
gi 2310915810 3471 QLVGYVVL 3478
Cdd:cd05967 535 VPLGLVVL 542
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
653-998 |
1.18e-20 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 99.33 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP----FSFDVSVWeffWPLMSGARLVVAApg 728
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCLW---LPLLSGIKVVFHP-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 729 DHRDPAKLVELINREGVDTLHFVPSMLQAFL---QDEDVAsctSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTE 805
Cdd:cd05909 222 NPLDYKKIPELIYDKKATILLGTPTFLRGYAraaHPEDFS---SLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 806 AAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAerfvaspFVAGER 884
Cdd:cd05909 298 CS-PVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV-DGR---QLVgyVVLESEGGDWR 959
Cdd:cd05909 370 WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRkgeKIV--LLTTTTDTDPS 447
|
330 340 350
....*....|....*....|....*....|....*....
gi 2310915810 960 EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05909 448 SLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
806-1078 |
1.24e-20 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 95.97 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 806 AAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLArgYHQRPGLTAERFVASPFVAGERM 885
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLL--LRIRLLAAAARAPFIPVPYPAQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESEGGDWRE 960
Cdd:COG3433 79 GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaalrgAGVGLLLIVGAVAALDGLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERT-----LAEIWQDLLGV--ER 1033
Cdd:COG3433 159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRADVAELLGVdpEE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2310915810 1034 VGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSL 1078
Cdd:COG3433 239 IDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAW 283
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2014-2422 |
1.34e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 98.69 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRA----RGVVAEALVAIAAErSFDLVVGLLgilKAGAGYLPLDPNYPAERLAymlrdsgarwl 2089
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAygirRGMRAVLMVPPGPD-FFALTFALF---KAGAVPVLIDPGMGRKNLK----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 icqetlaerlPCPAEVErlpletaawPASADTRPLpevAGETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVG 2169
Cdd:cd05910 68 ----------QCLQEAE---------PDAFIGIPK---ADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2170 PGDCQLQfasiSFDAAAeqLFVPLLAGARVLLG-DA---GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI 2245
Cdd:cd05910 125 PGEVDLA----TFPLFA--LFGPALGLTSVIPDmDPtrpARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2246 -AVRTCILGGEAWDASLLTQ--QAVQAEA-WFNAYGPTEAV-ITPLAWH-CRAQEGGAPA------IGRALGARRACILD 2313
Cdd:cd05910 199 pSLRRVLSAGAPVPIALAARlrKMLSDEAeILTPYGATEALpVSSIGSReLLATTTAATSggagtcVGRPIPGVRVRIIE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2314 AALQPCA---------PGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQ 2384
Cdd:cd05910 279 IDDEPIAewddtlelpRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
|
410 420 430
....*....|....*....|....*....|....*...
gi 2310915810 2385 QIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP 2422
Cdd:cd05910 356 RVITTGGTLYTEPVERVFNTHPGVRRSALV---GVGKP 390
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1999-2479 |
1.38e-20 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 98.99 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1999 ASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVvaealvAIAAERSFDLVVGLLGILKAGAGYLPLDPnyPAERLA 2078
Cdd:cd05929 3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGV------WIADGVYIYLINSILTVFAAAAAWKCGAC--PAYKSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2079 YMLRDSGarwlicqETLAERLPCPAEVERLPLETAAW--------PASADTRPLPEVAGETlaYVIYTSGSTGQPKGVav 2150
Cdd:cd05929 75 RAPRAEA-------CAIIEIKAAALVCGLFTGGGALDgledyeaaEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGI-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2151 sQAAL------VAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTIL 2224
Cdd:cd05929 144 -KRGLpggppdNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME--KFDPEEFLRLIERYRVTFA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPAYLQQQA---EELRHAGRRIAVRTCILGGeAWDASLLTQQAVqaeAW-----FNAYGPTEAVitPLAWhCRAQE-- 2294
Cdd:cd05929 221 QFVPTMFVRLLklpEAVRNAYDLSSLKRVIHAA-APCPPWVKEQWI---DWggpiiWEYYGGTEGQ--GLTI-INGEEwl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2295 ---GgapAIGRALGARrACILDAALQPCAPGMIGELYIGGQClARGYLGRPGQTAERFVADPFSGsgerlyrTGDLARYR 2371
Cdd:cd05929 294 thpG---SVGRAVLGK-VHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWST-------LGDVGYLD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2372 VDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAG 2449
Cdd:cd05929 362 EDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVpdEELGQRVHAVVQPAPGADAGTALAEELIAFLRD 441
|
490 500 510
....*....|....*....|....*....|
gi 2310915810 2450 RLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05929 442 RLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
3631-3827 |
1.58e-20 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 98.11 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRLFF----EQPIPNrqhWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATLGgALLWR 3703
Cdd:cd19538 9 RRLWFlhqlEGPSAT---YNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYqliLEEDEATPK-LEIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3704 aeaVDRQALESLCEES-QRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR-- 3780
Cdd:cd19538 85 ---VDEEELESEINEAvRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPEla 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3781 -LPGKTSPFKAWAGRVSEHARGE--SMKAQLQFWRELLEGAPA--ELPCEHP 3827
Cdd:cd19538 162 pLPVQYADYALWQQELLGDESDPdsLIARQLAYWKKQLAGLPDeiELPTDYP 213
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
3041-3553 |
2.73e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 99.26 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAG 3112
Cdd:PRK07529 28 YELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3113 GAyVPVDPEYPEERQAYMLEDSGVELLLS-------------QSHL-KLPLAQGVQRIDLDRGAPW-------------- 3164
Cdd:PRK07529 108 IA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVLaALPELRTVVEVDLARYLPGpkrlavplirrkah 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3165 --FEDYSEA---NPDIHLD------GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWM-QQAYGLGVGDTVLQKTP-FS 3231
Cdd:PRK07529 187 arILDFDAElarQPGDRLFsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLgALLLGLGPGDTVFCGLPlFH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 FDVSVWEFFWPLMSGARLVVAAPGDHRDP---AKLVALINREGVDTLHFVPSMLQAFLQ----DEDVascTSLKRIVCSG 3304
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQvpvdGHDI---SSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3305 EALPADAQQQvFAKLPQAGLYNLYGPTEAaidvthwTCV--------EEGKDAVPIGRPIANLACYILDGN---LEPVPV 3373
Cdd:PRK07529 343 APLPVEVFRR-FEAATGVRIVEGYGLTEA-------TCVssvnppdgERRIGSVGLRLPYQRVRVVILDDAgryLRDCAV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3374 GVLGELYLAGQGLARGYhqrpgLTAERfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 3453
Cdd:PRK07529 415 DEVGVLCIAGPNVFSGY-----LEAAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3454 LEHPWVREAAVL----AVDGRQLVGYVVL-------ESESGDWrealaahLAASLPE-YMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK07529 488 LRHPAVALAAAVgrpdAHAGELPVAYVQLkpgasatEAELLAF-------ARDHIAErAAVPKHVRILDALPKTAVGKIF 560
|
570 580 590
....*....|....*....|....*....|..
gi 2310915810 3522 RKALPRPQAAAGQTHVAPQNEMERRIAAVWAD 3553
Cdd:PRK07529 561 KPALRRDAIRRVLRAALRDAGVEAEVVDVVED 592
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
4533-5040 |
2.73e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 98.95 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4533 YPATPLvHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:PRK06710 21 YDIQPL-HKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------------LPIPEGL---------SCL----- 4657
Cdd:PRK06710 100 IVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRvtnvqsatkiehvivtriadfLPFPKNLlypfvqkkqSNLvvkvs 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4658 ---------SVDREEEWAGFPAHDPEvalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM 4728
Cdd:PRK06710 180 esetihlwnSVEKEVNTGVEVPCDPE-----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4729 SFAFdgSHEGWMHPLINGA------RVLIRDDSLwlpERTYAEMHRHGVTV--GVfPPVYLQQLAEHAERDGNPPPVRVy 4800
Cdd:PRK06710 255 VLPF--FHVYGMTAVMNLSimqgykMVLIPKFDM---KMVFEAIKKHKVTLfpGA-PTIYIALLNSPLLKEYDISSIRA- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGDAVAQASYDLAWRALKPKYLFNGYGPTET---VVTPLLWKARAGDACGAAYMPI-GTLLGNRSGyildgqlNLLPV 4876
Cdd:PRK06710 328 CISGSAPLPVEVQEKFETVTGGKLVEGYGLTESspvTHSNFLWEKRVPGSIGVPWPDTeAMIMSLETG-------EALPP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4877 GVAGELYLGGEGVARGYLERPALTAErFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:PRK06710 401 GEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK06710 473 LYEHEKVQEVVTIGVPDPYrGETVKAFVVLKEGTECSEEE--------LNQFARKYLAAYKVPKVYEFRDELPKTTVGKI 544
|
....*
gi 2310915810 5036 DRKGL 5040
Cdd:PRK06710 545 LRRVL 549
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
534-951 |
3.20e-20 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 98.93 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 534 EERLDYAELNRRANRLAHALIERGIGA-DRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd05967 80 ERTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 613 LSQS---------------HLKLPLAQ-----------GVQRIDLDQADAWLENH-----AENNPGIELNGENLAYVIYT 661
Cdd:cd05967 159 VTAScgiepgkvvpykpllDKALELSGhkphhvlvlnrPQVPADLTKPGRDLDWSellakAEPVDCVPVAATDPLYILYT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 662 SGSTGKPKGA----GNRHSALSnrlcW-MQQAYGLGVGDTvlqktpfsfdvsvwefFW-----------------PLMSG 719
Cdd:cd05967 239 SGTTGKPKGVvrdnGGHAVALN----WsMRNIYGIKPGDV----------------WWaasdvgwvvghsyivygPLLHG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 720 ARLVV--AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVA-----SCTSLKRIVCSGEALPADAQQQVFAK 791
Cdd:cd05967 299 ATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKeDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAENT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 792 LPQAGLYNlYGPTEaaidvTHW--TCVEEGKDTVPI-----GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRgLARGYH 864
Cdd:cd05967 379 LGVPVIDH-WWQTE-----TGWpiTANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 865 QRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--- 941
Cdd:cd05967 452 LTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRdel 531
|
490
....*....|.
gi 2310915810 942 -GRQLVGYVVL 951
Cdd:cd05967 532 kGQVPLGLVVL 542
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
3050-3525 |
3.22e-20 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 97.83 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:cd05929 4 RDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEdsgvelllsqsHLKLPLaqgVQRIDLDRGAPW-FEDYSEA---NPDIHLDGE-NLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:cd05929 84 IIE-----------IKAAAL---VCGLFTGGGALDgLEDYEAAeggSPETPIEDEaAGWKMLYSGGTTGRPKGIKRGLPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 -LSNRLCWMQQAYGLG--VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:cd05929 150 gPPDNDTLMAAALGFGpgADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDPEEFLRLIERYRVTFAQFVPTM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AIDVTHWTcveegKDAVPIG 3353
Cdd:cd05929 227 FVRLLKLPEAVrnayDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGqgltIINGEEWL-----THPGSVG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3354 RPIANLACyILDGNLEPVPVGVLGELYLAGqGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRI 3433
Cdd:cd05929 301 RAVLGKVH-ILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTDRR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV--VLESESGD-WREALAAHLAASLPEYMVPAQW 3506
Cdd:cd05929 373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPdeelGQRVHAVVqpAPGADAGTaLAEELIAFLRDRLSRYKCPRSI 452
|
490
....*....|....*....
gi 2310915810 3507 LALERMPLSPNGKLDRKAL 3525
Cdd:cd05929 453 EFVAELPRDDTGKLYRRLL 471
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
4534-5015 |
3.34e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 98.96 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVIFDE------EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAV 4607
Cdd:PRK12582 46 PYPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4608 LKAGGAYVPLDIEY------------------PRerlLYMMQDS------RAHLLLTHSHLLERLPIPEGLSCLSVDree 4663
Cdd:PRK12582 126 MQAGVPAAPVSPAYslmshdhaklkhlfdlvkPR---VVFAQSGapfaraLAALDLLDVTVVHVTGPGEGIASIAFA--- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4664 EWAGFPAhDPEV-----ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIvATGERYEMTPEDCE----LHFM--SFAF 4732
Cdd:PRK12582 200 DLAATPP-TAAVaaaiaAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANI-AMQEQLRPREPDPPppvsLDWMpwNHTM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4733 DGSHEgwMHPLINGARVLIRDDSLWLP---ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDgnpPPVRVYCF------- 4802
Cdd:PRK12582 278 GGNAN--FNGLLWGGGTLYIDDGKPLPgmfEETIRNLREISPTVYGNVPAGYAMLAEAMEKD---DALRRSFFknlrlma 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4803 -GGDAVAQASYD----LAWRALKPKYLF-NGYGPTETvvtpllwkarAGDACGAAYMPigtllgNRSGYI---LDG-QLN 4872
Cdd:PRK12582 353 yGGATLSDDLYErmqaLAVRTTGHRIPFyTGYGATET----------APTTTGTHWDT------ERVGLIglpLPGvELK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTR-----GRADGVVdYLGRVDHQVKI-RGF 4946
Cdd:PRK12582 417 LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARfvdpdDPEKGLI-FDGRVAEDFKLsTGT 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4947 RIELGEiearLREH------PAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAE---CRAQLKTALRERLPEY 5015
Cdd:PRK12582 489 WVSVGT----LRPDavaacsPVIHDAVVAGQDRAFIGLLAWPNPAACRQLAGDPDAAPEdvvKHPAVLAILREGLSAH 562
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
4563-5037 |
4.54e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 96.87 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPldieyprerllymmqdsrAHLLLTHS 4642
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLPIPEGLSCLSVDreeewagfpahdpevALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05974 63 DLRDRVDRGGAVYAAVDE---------------NTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFmsfafdgSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNP 4794
Cdd:cd05974 128 VHWNI-------SSPGWakhawscfFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGDAVAQASYDLAWRALKpKYLFNGYGPTETVvtpllwkARAGDACGAAYMPiGTLLGNRSGY---ILDgql 4871
Cdd:cd05974 200 VKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETT-------ALVGNSPGQPVKA-GSMGRPLPGYrvaLLD--- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4872 nllPVGVA---GE--LYLGGE---GVARGYLERPALTAerfvpdpfGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:cd05974 268 ---PDGAPateGEvaLDLGDTrpvGLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4944 RGFRIELGEIEARLREHPAVREAVVVAQPG----AVGQQLVGYVVAQEPavadSPEAQAEcraqLKTALRERLPEYMVPS 5019
Cdd:cd05974 337 SDYRISPFELESVLIEHPAVAEAAVVPSPDpvrlSVPKAFIVLRAGYEP----SPETALE----IFRFSRERLAPYKRIR 408
|
490
....*....|....*...
gi 2310915810 5020 HLLFlARMPLTPNGKLDR 5037
Cdd:cd05974 409 RLEF-AELPKTISGKIRR 425
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
511-943 |
4.94e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 98.41 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 511 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA--- 587
Cdd:PRK08279 37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 588 --------------------YVPVDPEYpeeRQAYmlEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPG 647
Cdd:PRK08279 117 lntqqrgavlahslnlvdakHLIVGEEL---VEAF--EEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 648 I--ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDV-------SVweffwpLMS 718
Cdd:PRK08279 192 SrsGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTggtvawsSV------LAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 719 GARLVVA----APGDHRDpaklvelINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD---AQQQVFAk 791
Cdd:PRK08279 266 GATLALRrkfsASRFWDD-------VRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDiwdEFQQRFG- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 792 LPQagLYNLYGPTEA------------------AIDVTHWTCVEEGKDTvpiGRPIGNlgcyiLDGNLEPVPVGVLGELY 853
Cdd:PRK08279 338 IPR--ILEFYAASEGnvgfinvfnfdgtvgrvpLWLAHPYAIVKYDVDT---GEPVRD-----ADGRCIKVKPGEVGLLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 854 --LAGRGLARGYHQrPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:PRK08279 408 grITDRGPFDGYTD-PEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPG 486
|
490
....*....|....*..
gi 2310915810 932 VREAAVLAV-----DGR 943
Cdd:PRK08279 487 VEEAVVYGVevpgtDGR 503
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
515-952 |
5.74e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 97.57 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 515 RLFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGA-DRlVGV-AMERsIEMVVALMAILKAGGAYVP 590
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKgDR-VGIwAPNV-PEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 591 VDPEYPEERQAYMLEDSGVQLLLSQSHLK---------------------------LPLAQGVQRIDLDQADAWLENHAE 643
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelapelatcepgqlqsarLPELRRVIFLGDEKHPGMLNFDEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 644 NNPGIELNGENLAY---------VI---YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvwe 711
Cdd:PRK08315 178 LALGRAVDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL-------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 712 F--FWPLM-------SGARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEAL 780
Cdd:PRK08315 250 YhcFGMVLgnlacvtHGATMVY--PGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARfdLSSLRTGIMAGSPC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 781 PADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKD----TVpiGRPIGNLGCYILDGNL-EPVPVGVLGELYLA 855
Cdd:PRK08315 328 PIEVMKRVIDKMHMSEVTIAYGMTETS-PVSTQTRTDDPLEkrvtTV--GRALPHLEVKIVDPETgETVPRGEQGELCTR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 856 GRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVkLRGlrielG------EIEARLLEH 929
Cdd:PRK08315 405 GYSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTH 472
|
490 500
....*....|....*....|....*..
gi 2310915810 930 PWVREAAVLAVD----GRQLVGYVVLE 952
Cdd:PRK08315 473 PKIQDVQVVGVPdekyGEEVCAWIILR 499
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1989-2480 |
6.60e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.52 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1989 GVAAAFAHQVASAPEAIALVcgDE--HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYL 2066
Cdd:PRK13382 44 GPTSGFAIAAQRCPDRPGLI--DElgTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2067 PLDPNYPAERLAYMLRDSGARWLICQETLAERLP-----CPAeverlPLETAAWPASADTRPL-----------PEVAGE 2130
Cdd:PRK13382 122 LLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDraladCPQ-----ATRIVAWTDEDHDLTVevliaahagqrPEPTGR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYVIYTSGSTGQPKGVAVSQA--ALVAHC-------QAAARTYGVGP-----GDCQLQFA-SISFDAAAEQLFVPlla 2195
Cdd:PRK13382 197 KGRVILLTSGTTGTPKGARRSGPggIGTLKAildrtpwRAEEPTVIVAPmfhawGFSQLVLAaSLACTIVTRRRFDP--- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLLgdagqwsaqhladeVERHAVT-----------ILDLPPAYLQqqaeelRHAGR--RIAvrtcilggeAWDASLL 2262
Cdd:PRK13382 274 EATLDL--------------IDRHRATglavvpvmfdrIMDLPAEVRN------RYSGRslRFA---------AASGSRM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2263 TQQAVQA------EAWFNAYGPTE----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK13382 325 RPDVVIAfmdqfgDVIYNNYNATEagmiATATPADLRAAPDTAGRPAEGTEIR-----ILDQDFREVPTGEVGTIFVRND 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYL-GRPGQTAERFVAdpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK13382 400 TQFDGYTsGSTKDFHDGFMA------------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2412 AVVALDGVG-GPLLAAYLVGRDAMRG--EDLLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PRK13382 468 AVIGVDDEQyGQRLAAFVVLKPGASAtpETLKQHVRDNLAN----YKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
3655-3936 |
7.07e-20 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 96.02 E-value: 7.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3655 EALNAKALEAALQALVEHHDALRLRFHEtDGT--WHAEHAEAT-----LGGALLWRAEavdrQALESLCEE-SQRSLDLT 3726
Cdd:cd19535 35 EDLDPDRLERAWNKLIARHPMLRAVFLD-DGTqqILPEVPWYGitvhdLRGLSEEEAE----AALEELRERlSHRVLDVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3727 DGPLLR---SLLvdmADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslRGEAPRLPGKTspFKAWAGRVSEHARGES 3803
Cdd:cd19535 110 RGPLFDirlSLL---PEGRTRLHLSIDLLVADALSLQILLRELAALYED--PGEPLPPLELS--FRDYLLAEQALRETAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3804 MKAQlQFWRELLE---GAPaELP-CEHPQGALEQRFaTSVQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWS 3879
Cdd:cd19535 183 ERAR-AYWQERLPtlpPAP-QLPlAKDPEEIKEPRF-TRREHRLSAEQWQRLKERA-RQHGVTPSMVLLTAYAEVLARWS 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3880 GASSSLVQLEGHGREELFADIDlsRTVGWFTS--LFPVRLSPVADLGESLKAIKEQLRA 3936
Cdd:cd19535 259 GQPRFLLNLTLFNRLPLHPDVN--DVVGDFTSllLLEVDGSEGQSFLERARRLQQQLWE 315
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
523-998 |
7.69e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 97.37 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYPEER--- 599
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRsel 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 600 QAYMLEDSGVQLLLSQSHlklPLAQGVQRIDLDQA-------------------DAWLENHAENNPGIELNGENLAYVIY 660
Cdd:PRK10946 113 NAYASQIEPALLIADRQH---ALFSDDDFLNTLVAehsslrvvlllnddgehslDDAINHPAEDFTATPSPADEVAFFQL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 661 TSGSTGKPKGAGNRHSAL------SNRLCWMQQAY----GLGVGDTVLQKTPFSFDVsvweffwpLMSGARLVVAApgdh 730
Cdd:PRK10946 190 SGGSTGTPKLIPRTHNDYyysvrrSVEICGFTPQTrylcALPAAHNYPMSSPGALGV--------FLAGGTVVLAP---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 731 rDPAKLV--ELINREGVDTLHFVPSM----LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPT 804
Cdd:PRK10946 258 -DPSATLcfPLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 805 EAAIDVTHWTCVEEGKDTVPiGRPI-GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvage 883
Cdd:PRK10946 336 EGLVNYTRLDDSDERIFTTQ-GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF---- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 884 rmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV--------- 950
Cdd:PRK10946 411 --YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEdelmGEKSCAFLVvkeplkavq 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 951 ----LESEGgdwrealaahlaasLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK10946 489 lrrfLREQG--------------IAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
4542-5024 |
9.56e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 97.25 E-value: 9.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4542 RVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG--AYV---- 4615
Cdd:PRK08279 42 VFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntqq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 -------PLDIEYPR-----ERLLYMMQDSRAHLLLTHS---HLLERLPIPEGLSCLsvdrEEEWAGFPAHDPEV--ALH 4678
Cdd:PRK08279 122 rgavlahSLNLVDAKhlivgEELVEAFEEARADLARPPRlwvAGGDTLDDPEGYEDL----AAAAAGAPTTNPASrsGVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CEL---HFMsfafdGSHEGWMHPLINGARVLIR 4752
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDvlyCCLplyHNT-----GGTVAWSSVLAAGATLALR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4753 D----DSLWlpertyAEMHRHGVTvgVFppVY--------LQQLAEHAERDGnppPVRVyCFG----GDavaqasydlAW 4816
Cdd:PRK08279 273 RkfsaSRFW------DDVRRYRAT--AF--QYigelcrylLNQPPKPTDRDH---RLRL-MIGnglrPD---------IW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKY----LFNGYGPTETVVTPLLWKARAGdACGaaympIGTLLGNRSGYIL-------------DGQLNLLPVGVA 4879
Cdd:PRK08279 330 DEFQQRFgiprILEFYAASEGNVGFINVFNFDG-TVG-----RVPLWLAHPYAIVkydvdtgepvrdaDGRCIKVKPGEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4880 GELYlgGEGVARGYLE---RPALTAERFVPDPFgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqvkirgFR-----I 4948
Cdd:PRK08279 404 GLLI--GRITDRGPFDgytDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGhaqFVDRLGDT--------FRwkgenV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4949 ELGEIEARLREHPAVREAVV--VAQPGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPshlLFL 5024
Cdd:PRK08279 473 ATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADGAEFD--------LAALAAHLYERLPAYAVP---LFV 539
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
470-1000 |
9.87e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 96.60 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 470 LLRGMLENPQASVDSLPMLDAEERG--QLLEGWNATAAEYPlqrgvhrlfeeqvERTptapALAFGEERLDYAELNRRAN 547
Cdd:PRK13383 9 LVRSGLLNPPSPRAVLRLLREASRGgtNPYTLLAVTAARWP-------------GRT----AIIDDDGALSYRELQRATE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 548 RLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLKLPLA---Q 624
Cdd:PRK13383 72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAgadD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 625 GVQRIDLDQADAwleNHAENNPGIELNGEnlaYVIYTSGSTGKPKGAgNRHSALSNrlcwmqqayGLGVGDTVLQKTPfs 704
Cdd:PRK13383 152 AVAVIDPATAGA---EESGGRPAVAAPGR---IVLLTSGTTGKPKGV-PRAPQLRS---------AVGVWVTILDRTR-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 705 fdvsvweffwpLMSGARLVVAAP----------------------GDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE 762
Cdd:PRK13383 214 -----------LRTGSRISVAMPmfhglglgmlmltialggtvltHRHFDAEAALAQASLHRADAFTAVPVVLARILELP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 763 DVASCTS----LKRIVCSGEAL-PADAQQqvFAKLPQAGLYNLYGPTEAAIDVTHWTC-VEEGKDTVpiGRPIGNLGCYI 836
Cdd:PRK13383 283 PRVRARNplpqLRVVMSSGDRLdPTLGQR--FMDTYGDILYNGYGSTEVGIGALATPAdLRDAPETV--GKPVAGCPVRI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:PRK13383 359 LDRNNRPVGPRVTGRIFVGGELAGTRYTDGGG--------KAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGEN 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 917 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:PRK13383 429 VYPRAVENALAAHPAVADNAVIGVPderfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGK 508
|
....*...
gi 2310915810 993 LDRKALPA 1000
Cdd:PRK13383 509 VLRKELPG 516
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
527-940 |
1.00e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 96.67 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 527 APALAFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 605
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 606 DSGVQLLLSQS---HLKLPLAQGVQRIDLDqADAW---LENHAENNPG-IELNGENLAYVIYTSGSTGKPKGAGNRHSAL 678
Cdd:PRK07867 99 HADCQLVLTESahaELLDGLDPGVRVINVD-SPAWadeLAAHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 679 SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweffwplMSGARLVVAAPGDHRDPAK-----LVELINREGVDTLHFVPS 753
Cdd:PRK07867 178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV-------MAGWAVALAAGASIALRRKfsasgFLPDVRRYGATYANYVGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 754 MLQAFL---QDEDVAScTSLkRIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVThWTcveegKDTVP--IGRP 828
Cdd:PRK07867 251 PLSYVLatpERPDDAD-NPL-RIVYGNEGAPGDIAR--FARRFGCVVVDGFGSTEGGVAIT-RT-----PDTPPgaLGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 829 IGNLGcyILDGN-LEPVPVGVL------------GELY-LAGRGLARGYHQRPGLTAERFVASpfvagerMYRTGDLARY 894
Cdd:PRK07867 321 PPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYR 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2310915810 895 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK07867 392 DADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
2014-2482 |
1.28e-19 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 97.00 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGV------------VAEALVA------IAAERSfdLVVGLLG---------------ILK 2060
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVvkgdrviiympmIPEAAIAmlacarIGAIHS--VVFGGFAakelasriddakpklIVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2061 AGAG--------YLPLdpnypaerLAYMLRDSG---ARWLICQetlaeRLPCPAEVERlPLETAAWP---ASADTRPLPE 2126
Cdd:cd05967 161 ASCGiepgkvvpYKPL--------LDKALELSGhkpHHVLVLN-----RPQVPADLTK-PGRDLDWSellAKAEPVDCVP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2127 VAGETLAYVIYTSGSTGQPKGV-------AVSQAALVAHCqaaartYGVGPGDcqlqfasiSFDAAAEQLFV-------- 2191
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVvrdngghAVALNWSMRNI------YGIKPGD--------VWWAASDVGWVvghsyivy 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2192 -PLLAGARVLL--------GDAGQWSAQhladeVERHAVT-ILDLPPAY--LQQQAEELRHaGRRI---AVRTCILGGEA 2256
Cdd:cd05967 293 gPLLHGATTVLyegkpvgtPDPGAFWRV-----IEKYQVNaLFTAPTAIraIRKEDPDGKY-IKKYdlsSLRTLFLAGER 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2257 WDASllTQQAVQA-------EAWFNaygpTEAViTPLAWHCRAQEGGAP---AIGRALGARRACILDAALQPCAPGMIGE 2326
Cdd:cd05967 367 LDPP--TLEWAENtlgvpviDHWWQ----TETG-WPITANPVGLEPLPIkagSPGKPVPGYQVQVLDEDGEPVGPNELGN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2327 LYIGGQcLARGYLGRPGQTAERFVADPFSGSgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:cd05967 440 IVIKLP-LPPGCLLTLWKNDERFKKLYLSKF-PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHP 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2407 YVAEAAVVAL-DGVGGPLLAAYLVGRDAMR--GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKV 2482
Cdd:cd05967 518 AVAECAVVGVrDELKGQVPLGLVVLKEGVKitAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
4545-5040 |
1.74e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 95.90 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4545 ERARMAPDAVAVIF-----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:PRK08008 15 DLADVYGHKTALIFessggVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4620 EYPRERLLYMMQDSRAhllLTHSHLLERLPI-----PEGLSCLS---VDREEEWAGFPAHD-------------PEVALH 4678
Cdd:PRK08008 95 RLLREESAWILQNSQA---SLLVTSAQFYPMyrqiqQEDATPLRhicLTRVALPADDGVSSftqlkaqqpatlcYAPPLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM-SFAFDGSHEGWMHPLINGAR-VLIRDDS- 4755
Cdd:PRK08008 172 TDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMpAFHIDCQCTAAMAAFSAGATfVLLEKYSa 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4756 --LWLPERTYAEMHRHGV-----TVGVFPPVYLQQlaEHAERDgnpppVRVYCfggdAVAQASYDLAWRALKPKyLFNGY 4828
Cdd:PRK08008 252 raFWGQVCKYRATITECIpmmirTLMVQPPSANDR--QHCLRE-----VMFYL----NLSDQEKDAFEERFGVR-LLTSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GPTETVVTPLlwkaraGDACGAA--YMPIGtllgnRSGY-----ILDGQLNLLPVGVAGELYLGGE---GVARGYLERPA 4898
Cdd:PRK08008 320 GMTETIVGII------GDRPGDKrrWPSIG-----RPGFcyeaeIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4899 LTAERFVPDPFGAPGSRLYRSgdltrgrADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK08008 389 ATAKVLEADGWLHTGDTGYVD-------EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4979 LVGYVVAQEPAVADSPEA-QAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08008 462 AIKAFVVLNEGETLSEEEfFAFC--------EQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
2133-2479 |
1.78e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 93.96 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2133 AYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGvGPGdcQLQFASISFDAAAEQLFV-PLLAGARVLLGDAgqwSAQH 2211
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPG--QWLLALPAHHIAGLQVLVrSVIAGSEPVELDV---SAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERhAVTILDLPPAYLQ----QQAEELRHAGRRIAVRT---CILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVit 2284
Cdd:PRK07824 112 DPTALPR-AVAELGGGRRYTSlvpmQLAKALDDPAATAALAEldaVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETS-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 plawhcraqeGGAPAIGRALGARRACILDaalqpcapgmiGELYIGGQCLARGYLGRPgqtaerfVADPFSGSGerLYRT 2364
Cdd:PRK07824 189 ----------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV-------DPDPFAEPG--WFRT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYrVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAAYLVgrdAMRGEDLLAE 2442
Cdd:PRK07824 239 DDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLpdDRLGQRVVAAVVG---DGGPAPTLEA 314
|
330 340 350
....*....|....*....|....*....|....*..
gi 2310915810 2443 LRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07824 315 LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
3058-3525 |
2.34e-19 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 95.67 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3058 AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVE 3137
Cdd:cd17642 39 AHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3138 LLLSQS---------HLKLPLAQGVQRIDLD---RGAPWFEDYSEANPDIHLDG-----------ENLAYVIYTSGSTGK 3194
Cdd:cd17642 119 IVFCSKkglqkvlnvQKKLKIIKTIIILDSKedyKGYQCLYTFITQNLPPGFNEydfkppsfdrdEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSNRLCWMQQ-AYGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdHRDPAKL-VALINRE 3270
Cdd:cd17642 199 PKGVQLTHKNIVARFSHARDpIFGNQIipDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM----YKFEEELfLRSLQDY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTE--AAIDVTHWTCVEEG 3346
Cdd:cd17642 275 KVQSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEttSAILITPEGDDKPG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3347 KdavpIGRPIANLACYILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAErfvaspFVAGERMYRTGDLARYRADG 3425
Cdd:cd17642 355 A----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDIAYYDEDG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESESGDWREALAAHLAASLpeyMV 3502
Cdd:cd17642 425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdeDAGELPAAVVVLEAGKTMTEKEVMDYVASQ---VS 501
|
490 500
....*....|....*....|....*...
gi 2310915810 3503 PAQWLA-----LERMPLSPNGKLDRKAL 3525
Cdd:cd17642 502 TAKRLRggvkfVDEVPKGLTGKIDRRKI 529
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
3038-3632 |
2.84e-19 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 96.70 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEYPEERQAYMLEDSGVELLLSQ---SHLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:COG3319 81 LAALALALAAAAAALLLAALALLLAllaALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDT 3274
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3275 LHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGR 3354
Cdd:COG3319 241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPF--VAGERMYRTGDLARYRADGVIEYAGR 3432
Cdd:COG3319 321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAgaGARGRLRRGGDRGRRLGGGLLLGLGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLAL 3509
Cdd:COG3319 401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAaaaAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3510 ERMPLSPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIq 3589
Cdd:COG3319 481 LLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLL- 559
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2310915810 3590 ftpkdLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQR 3632
Cdd:COG3319 560 -----RLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRA 597
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
525-992 |
3.76e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 94.67 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQSHLKLP--LAQGvqridlDQADAWLENHAENNPgIELNgenlayviYTSGSTGKPKGAGNRH-----SA 677
Cdd:cd12118 98 RHSEAKVLFVDREFEYEdlLAEG------DPDFEWIPPADEWDP-IALN--------YTSGTTGRPKGVVYHHrgaylNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 678 LSNRLCW-MQQayglgvgDTVLQKTPFSFDVSVWEFFWPlmsgarlVVAAPGDH---R--DPAKLVELINREGVDtlHF- 750
Cdd:cd12118 163 LANILEWeMKQ-------HPVYLWTLPMFHCNGWCFPWT-------VAAVGGTNvclRkvDAKAIYDLIEKHKVT--HFc 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 751 ----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLY--NLYGPTEAAIDVThwTCVE-EGKDTV 823
Cdd:cd12118 227 gaptVLNML-ANAPPSDARPLPHRVHVMTAGAPPPA----AVLAKMEELGFDvtHVYGLTETYGPAT--VCAWkPEWDEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 824 PIG-----------RPIGNLGCYILDGN-LEPVPV-GV-LGELYLAGRGLARGYHQRPGLTAERFvaspfvAGErMYRTG 889
Cdd:cd12118 300 PTEerarlkarqgvRYVGLEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG-WFHSG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLEsEGGDWREALAAH 965
Cdd:cd12118 373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPdekwGEVPCAFVELK-EGAKVTEEEIIA 451
|
490 500
....*....|....*....|....*...
gi 2310915810 966 -LAASLPEYMVPAQWLALErMPLSPNGK 992
Cdd:cd12118 452 fCREHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
4556-4971 |
4.73e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 94.05 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4556 VIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRA 4635
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4636 hlllthshllerlpipeglSCLSVDREEEwagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHiVATGER 4715
Cdd:cd05914 81 -------------------KAIFVSDEDD-----------------VALINYTSGTTGNSKGVMLTYRNIVSN-VDGVKE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4716 YEM-TPEDCEL------HFMSFAFDGshegwMHPLINGARVLIRDDS---------------------LWLPERTY--AE 4765
Cdd:cd05914 124 VVLlGKGDKILsilplhHIYPLTFTL-----LLPLLNGAHVVFLDKIpsakiialafaqvtptlgvpvPLVIEKIFkmDI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4766 MHRHGVTVGVF----PPVYLQ--QLAEHAERDGNPPPVRVYCFGGDAV-AQASYDLawRALKPKYLFnGYGPTETvvTPL 4838
Cdd:cd05914 199 IPKLTLKKFKFklakKINNRKirKLAFKKVHEAFGGNIKEFVIGGAKInPDVEEFL--RTIGFPYTI-GYGMTET--API 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LwkaragdacgaAYMPIGTLLGNRSGYILDGQ----LNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:cd05914 274 I-----------SYSPPNRIRLGSAGKVIDGVevriDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW----- 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4915 rlYRSGDLTRGRADGVVDYLGRVDHQ-VKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:cd05914 338 --FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQ 393
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
3061-3464 |
4.90e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 94.96 E-value: 4.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVG-ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:PRK04319 71 KEKYTYKELKELSNKFANVLKELGVEkGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQSHL-------KLPLAQGVQRIDLDRGAP-----WFEDYSEANPDI---HLDGENLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:PRK04319 150 ITTPALlerkpadDLPSLKHVLLVGEDVEEGpgtldFNALMEQASDEFdieWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 lsnrlcwMQQAYglGVGDTVLQKTPfsFDVsvwefFW-----------------PLMSGARLVVAapGDHRDPAKLVALI 3267
Cdd:PRK04319 230 -------MLQHY--QTGKYVLDLHE--DDV-----YWctadpgwvtgtsygifaPWLNGATNVID--GGRFSPERWYRIL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3268 NREGVDTLHFVPS---MLQAflQDEDVASC---TSLKRIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDV 3337
Cdd:PRK04319 292 EDYKVTVWYTAPTairMLMG--AGDDLVKKydlSSLRHILSVGEPLNPEVvrwGMKVF-GLP---IHDNWWMTEtGGIMI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVeegkDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAgQG---LARGYHQRPgltaERFvASPFVAGerM 3412
Cdd:PRK04319 366 ANYPAM----DIKPgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNP----EKY-ESYFAGD--W 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 3464
Cdd:PRK04319 434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
525-998 |
5.18e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.91 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPAL--AFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PLN02574 53 NGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 602 YMLEDSGVQLLLS--QSHLKLPlAQGVQRIDLDQADAWLENHAENNPGIEL-------------NGENLAYVIYTSGSTG 666
Cdd:PLN02574 133 KRVVDCSVGLAFTspENVEKLS-PLGVPVIGVPENYDFDSKRIEFPKFYELikedfdfvpkpviKQDDVAAIMYSSGTTG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 667 KPKGAGNRHSALSN------RLCWMQQAYGlGVGDTVLQKTPFSFDVSVWEFFWPLMS-GARLVVAAPGDHRDpakLVEL 739
Cdd:PLN02574 212 ASKGVVLTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASD---MVKV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 740 INREGVDTLHFVPSMLQAFLQDEDVASCTSLK--RIVCSGEALPADAQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCV 816
Cdd:PLN02574 288 IDRFKVTHFPVVPPILMALTKKAKGVCGEVLKslKQVSCGAAPLSGKFIQDFVQtLPHVDFIQGYGMTESTAVGTRGFNT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 817 EEGKDTVPIGRPIGNLGCYILD---GNLepVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLAR 893
Cdd:PLN02574 368 EKLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAAS 969
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPdkecGEIPVAFVVRRQGSTLSQEAVINYVAKQ 519
|
490 500
....*....|....*....|....*....
gi 2310915810 970 LPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PLN02574 520 VAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
4559-5040 |
5.36e-19 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 94.45 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALI-ARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHL 4637
Cdd:cd05928 38 DEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKC 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 LLTHSHLLERL-------PIPEGLSCLSVDREEEWAGF-----PAHDPEVALH-GDNLAYVIY-TSGSTGMPKGVAVSHG 4703
Cdd:cd05928 118 IVTSDELAPEVdsvasecPSLKTKLLVSEKSRDGWLNFkellnEASTEHHCVEtGSQEPMAIYfTSGTTGSPKMAEHSHS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERY-EMTPEDcelhfmsFAFDGSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVG 4774
Cdd:cd05928 198 SLGLGLKVNGRYWlDLTASD-------IMWNTSDTGWiksawsslFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4775 VFPPVYLQQLAEHAERDGNPPPVRvYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKaraGDACGAAYMP 4854
Cdd:cd05928 271 CGAPTVYRMLVQQDLSSYKFPSLQ-HCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFK---GMKIKPGSMG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IGTllgnrSGY---ILDGQLNLLPVGVAGELYLGGE-----GVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGR 4926
Cdd:cd05928 347 KAS-----PPYdvqIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD--------FYLTGDRGIMD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4927 ADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaECRAQLK 5005
Cdd:cd05928 414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIrGEVVKAFVVLAPQFLSHDPE---QLTKELQ 490
|
490 500 510
....*....|....*....|....*....|....*
gi 2310915810 5006 TALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05928 491 QHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4687-5037 |
6.26e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 91.96 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4687 YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED--CELHFMSFAFdGSHEGWMHPLINGARVLirddslwLPERTY- 4763
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDrlCIPVPLFHCF-GSVLGVLACLTHGATMV-------FPSPSFd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 -----AEMHR------HGVtvgvfPPVYLQQLaEHAERDGNPP-PVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPT 4831
Cdd:cd05917 81 plavlEAIEKekctalHGV-----PTMFIAEL-EHPDFDKFDLsSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4832 ETvvTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLN-LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfg 4910
Cdd:cd05917 155 ET--SPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4911 apgsRLYRSGDLTRGRADGVVDYLGRVDHQVkIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVaqep 4988
Cdd:cd05917 230 ----GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDErYGEEVCAWIR---- 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2310915810 4989 aVADSPEAQAEcraQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd05917 301 -LKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1990-2473 |
6.53e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 94.49 E-value: 6.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHL--SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:PRK08315 18 IGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLIC---------QETLAERLP----CPA---EVERLP----------------LETAAW 2115
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAadgfkdsdyVAMLYELAPelatCEPgqlQSARLPelrrviflgdekhpgmLNFDEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2116 PASADTRPLPEVA--GETLAY--VI---YTSGSTGQPKGVAVSQ------AALVAHCQA--------------------- 2161
Cdd:PRK08315 178 LALGRAVDDAELAarQATLDPddPIniqYTSGTTGFPKGATLTHrnilnnGYFIGEAMKlteedrlcipvplyhcfgmvl 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 ---AARTYG---VGPGDcqlqfasiSFDaaaeqlfvPLLAGARVllgdagqwsaqhladEVER----HAV-----TILDL 2226
Cdd:PRK08315 258 gnlACVTHGatmVYPGE--------GFD--------PLATLAAV---------------EEERctalYGVptmfiAELDH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 P--PAYlqqqaeELRHagrriaVRTCILGG-----EawdasllTQQAVQAEawFN------AYGPTEA--VIT------P 2285
Cdd:PRK08315 307 PdfARF------DLSS------LRTGIMAGspcpiE-------VMKRVIDK--MHmsevtiAYGMTETspVSTqtrtddP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2286 LAWHCRaqeggapAIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLARGYLGRPGQTAErfVADPfsgsgERLYRT 2364
Cdd:PRK08315 366 LEKRVT-------TVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDA-----DGWMHT 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYRVDGQVEYLGRadqqIK---IRGfrieiG------EIESQLLAHPYVAEAAVValdGVG----GPLLAAYLVGR 2431
Cdd:PRK08315 432 GDLAVMDEEGYVNIVGR----IKdmiIRG-----GeniyprEIEEFLYTHPKIQDVQVV---GVPdekyGEEVCAWIILR 499
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2310915810 2432 DamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNANGK 2473
Cdd:PRK08315 500 P---GATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
4563-5040 |
7.80e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 94.32 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY-PRErLLYMMQDSRAHL---- 4637
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYtPRE-LEHQLKDSGAEAivvl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 ---LLTHSHLLERLPIPE----------GLSCLSVD---RE-----EEWAgFPAHDP--------------EVALHGDNL 4682
Cdd:PRK07059 128 enfATTVQQVLAKTAVKHvvvasmgdllGFKGHIVNfvvRRvkkmvPAWS-LPGHVRfndalaegarqtfkPVKLGPDDV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHIVATG----ERYEMTPEDCELHFMS-------FAFdgSHEGWMHPLINGARVLI 4751
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqPAFEKKPRPDQLNFVCalplyhiFAL--TVCGLLGMRTGGRNILI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 ---RDDSLWLpertyAEMHRHGVTVgvFPPV--YLQQLAEHAE-RDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLF 4825
Cdd:PRK07059 285 pnpRDIPGFI-----KELKKYQVHI--FPAVntLYNALLNNPDfDKLDFSKLIVANGGGMAVQRPVAE-RWLEMTGCPIT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYGPTETVVTPLLWKARAGDACGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERF 4904
Cdd:PRK07059 357 EGYGLSETSPVATCNPVDATEFSGTIGLPLpSTEVS-----IRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVM 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4905 VPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYV 4983
Cdd:PRK07059 432 TADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPdEHSGEAVKLFV 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 4984 VAQEPAVADspeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK07059 505 VKKDPALTE---------EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
531-998 |
8.49e-19 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 93.75 E-value: 8.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 531 AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS--- 607
Cdd:cd17642 39 AHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISkpt 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 608 -------GVQLLLS-QShlKLPLAQGVQRIDLD---QADAWLENHAENNPGIELNG-----------ENLAYVIYTSGST 665
Cdd:cd17642 119 ivfcskkGLQKVLNvQK--KLKIIKTIIILDSKedyKGYQCLYTFITQNLPPGFNEydfkppsfdrdEQVALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 666 GKPKGAGNRHSALSNRLCWMQQ-AYGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdHRDPAKL-VELIN 741
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARDpIFGNQIipDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM----YKFEEELfLRSLQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 742 REGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTE--AAIDVTHWTCVE 817
Cdd:cd17642 273 DYKVQSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEttSAILITPEGDDK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 818 EGKdtvpIGRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAErfvaspFVAGERMYRTGDLARYRA 896
Cdd:cd17642 353 PGA----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDIAYYDE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 897 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGDWREALAAHLAASLpey 973
Cdd:cd17642 423 DGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdeDAGELPAAVVVLEAGKTMTEKEVMDYVASQ--- 499
|
490 500 510
....*....|....*....|....*....|
gi 2310915810 974 MVPAQWLA-----LERMPLSPNGKLDRKAL 998
Cdd:cd17642 500 VSTAKRLRggvkfVDEVPKGLTGKIDRRKI 529
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3027-3523 |
9.60e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 93.91 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3027 WNATAAEYPLQRGVHrLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVAL 3105
Cdd:PRK05605 22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDR-VAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3106 MAILKAGGAYVPVDPEYPEERQAYMLEDSG----------------------------VEL-----LLSQSHLKLPL-AQ 3151
Cdd:PRK05605 100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGarvaivwdkvaptverlrrttpletivsVNMiaampLLQRLALRLPIpAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3152 GVQRIDLDRGAPWFEDYSE-------------ANPDIHLDgeNLAYVIYTSGSTGKPKGA----GNRHSALSNRLCWMQq 3214
Cdd:PRK05605 180 RKARAALTGPAPGTVPWETlvdaaiggdgsdvSHPRPTPD--DVALILYTSGTTGKPKGAqlthRNLFANAAQGKAWVP- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3215 ayGLGVGD-TVLQKTPF--SFDVSVWEFFWPLMsGARLVV-AAPgdhrDPAKLVALINREGVDTLHFVPSMLQAFLQ--D 3288
Cdd:PRK05605 257 --GLGDGPeRVLAALPMfhAYGLTLCLTLAVSI-GGELVLlPAP----DIDLILDAMKKHPPTWLPGVPPLYEKIAEaaE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVThwtCVEEGKDAVP--IGRPIANLACYILD- 3365
Cdd:PRK05605 330 ERGVDLSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTEVRIVDp 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3366 GNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 3444
Cdd:PRK05605 406 EDPdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3445 ELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLpreDGSEeVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
...
gi 2310915810 3521 DRK 3523
Cdd:PRK05605 559 RRR 561
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
2130-2476 |
9.77e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 91.17 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVA---HCQAAARTYGVGpgDCQLQFASISFDAAAEQLFVPLLA-GARVLLGDAG 2205
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAvpdILQKEGLNWVVG--DVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAqhLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGeawdASLLTQQAVQAEAWF------NAYGPT 2279
Cdd:cd17635 79 TYKS--LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYG----GSRAIAADVRFIEATgltntaQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 E-AVITPLAWHCRAQEGGApaIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsG 2358
Cdd:cd17635 153 EtGTALCLPTDDDSIEINA--VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------D 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2359 ERLYrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVgRDAMRGE 2437
Cdd:cd17635 224 GWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIsDEEFGELVGLAVV-ASAELDE 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 2310915810 2438 DLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd17635 302 NAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
3054-3467 |
1.01e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 93.59 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3132
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3133 DSGVELLLSQS---HLKLPLAQGVQRIDLDrGAPWFED---YSEANPD-IHLDGENLAYVIYTSGSTGKPKGAGNRHSAL 3205
Cdd:PRK07867 99 HADCQLVLTESahaELLDGLDPGVRVINVD-SPAWADElaaHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3206 SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweffwplMSGARLVVAAPGDHRDPAKLVAL-----INREGVDTLHFVPS 3280
Cdd:PRK07867 178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV-------MAGWAVALAAGASIALRRKFSASgflpdVRRYGATYANYVGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFL---QDEDVAScTSLkRIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAVPIGRPIA 3357
Cdd:PRK07867 251 PLSYVLatpERPDDAD-NPL-RIVYGNEGAPGDIAR--FARRFGCVVVDGFGSTEGGVAITR----TPDTPPGALGPLPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3358 NLAcyILDGN-LEPVPVGVL------------GELY-LAGQGLARGYHQRPGLTAERFVASpfvagerMYRTGDLARYRA 3423
Cdd:PRK07867 323 GVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2310915810 3424 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK07867 394 DGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2134-2475 |
1.07e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 91.67 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAAlVAHCQAAARTYGVGP-------GDCQLQFASISFDAA------AEQL--FVPLLAGAR 2198
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQED-IFRMLMGGADFGTGEftpsedaHKAAAAAAGTVMFPApplmhgTGSWtaFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2199 VLLGDAGqWSAQHLADEVERHAVTILDL-PPAYLQQQAEELRHAGRR--IAVRTCILGGEAWdaSLLTQQAVQAE----A 2271
Cdd:cd05924 86 VVLPDDR-FDPEEVWRTIEKHKVTSMTIvGDAMARPLIDALRDAGPYdlSSLFAISSGGALL--SPEVKQGLLELvpniT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 WFNAYGPTEAVITPLAwhcRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCL-ARGYLGRPGQTAERFV 2350
Cdd:cd05924 163 LVDAFGSSETGFTGSG---HSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2351 adpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV 2429
Cdd:cd05924 240 ----EVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRpDERWGQEVVAVVQ 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2310915810 2430 GRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd05924 316 LREGAGVD--LEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
4559-4971 |
1.10e-18 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 92.81 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhll 4638
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 lthshllerlpipeglSCLSVDReeewagfpahdpevalHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEM 4718
Cdd:cd17640 79 ----------------VALVVEN----------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4719 TPEDcelHFMSF-----AFDGSHEGW-----MHPLINGARVLIRDDSLWLPE------RTYaEMHRHGV--TVGVFPPVY 4780
Cdd:cd17640 127 QPGD---RFLSIlpiwhSYERSAEYFifacgCSQAYTSIRTLKDDLKRVKPHyivsvpRLW-ESLYSGIqkQVSKSSPIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 lQQLAEHAERDGNpppVRVYCFGGDAVAQaSYDLAWRALKPKYLfNGYGPTET--VVTP-LLWKARAGdACGAaymPI-G 4856
Cdd:cd17640 203 -QFLFLFFLSGGI---FKFGISGGGALPP-HVDTFFEAIGIEVL-NGYGLTETspVVSArRLKCNVRG-SVGR---PLpG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 T---LLGNRSGyildgqlNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDY 4933
Cdd:cd17640 273 TeikIVDPEGN-------VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVL 338
|
410 420 430
....*....|....*....|....*....|....*....
gi 2310915810 4934 LGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:cd17640 339 TGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQ 377
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
3333-3615 |
1.11e-18 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 90.19 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3333 AAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLArgYHQRPGLTAERFVASPFVAGERM 3412
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLL--LRIRLLAAAARAPFIPVPYPAQP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGDWRE 3487
Cdd:COG3433 79 GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaalrgAGVGLLLIVGAVAALDGLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVAP------QNEMERRIAAVWADVLKL--EE 3559
Cdd:COG3433 159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASpapaleTALTEEELRADVAELLGVdpEE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3560 VGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQ 3615
Cdd:COG3433 239 IDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
4685-5037 |
1.61e-18 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 90.41 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------HFM--SFAFDGSHEGwmhplinGARVLI-RDDs 4755
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLnmlplfHIAglNLALATFHAG-------GANVVMeKFD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4756 lwlPERTYAEMHRHGVTV-GVFPPVyLQQLAEHAERDGNPPPVRVYCFGGDAVAQASydlAWRALKPKYLFNGYGPTET- 4833
Cdd:cd17637 77 ---PAEALELIEEEKVTLmGSFPPI-LSNLLDAAEKSGVDLSSLRHVLGLDAPETIQ---RFEETTGATFWSLYGQTETs 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4834 -VVTpllwKARAGDACGAAympiGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgap 4912
Cdd:cd17637 150 gLVT----LSPYRERPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4913 gsR--LYRSGDLTRGRADGVVDYLGRVDHQ--VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEP 4988
Cdd:cd17637 214 --RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2310915810 4989 AVADSPEAQAECRAqlktalrERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17637 292 GATLTADELIEFVG-------SRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3038-3198 |
1.73e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 93.40 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA--- 3114
Cdd:PRK08279 37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 --------------------YVPVDPEYpeeRQAYmlEDSGVELLLSQSHLKLPLAQGVQR---IDLDRGApwfEDYSEA 3171
Cdd:PRK08279 117 lntqqrgavlahslnlvdakHLIVGEEL---VEAF--EEARADLARPPRLWVAGGDTLDDPegyEDLAAAA---AGAPTT 188
|
170 180
....*....|....*....|....*....
gi 2310915810 3172 NPDIH--LDGENLAYVIYTSGSTGKPKGA 3198
Cdd:PRK08279 189 NPASRsgVTAKDTAFYIYTSGTTGLPKAA 217
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
2134-2479 |
1.78e-18 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 93.47 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGV-------AVSQAALVAHcqaaarTYGVGPGDCQLQFASI------SFDAAAeqlfvPLLAGARVL 2200
Cdd:PRK10524 237 YILYTSGTTGKPKGVqrdtggyAVALATSMDT------IFGGKAGETFFCASDIgwvvghSYIVYA-----PLLAGMATI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2201 L-------GDAGQWSAQhladeVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRTCILGGEAWDASllTQQavqae 2270
Cdd:PRK10524 306 MyeglptrPDAGIWWRI-----VEKYKVNRMFSAPTairVLKKQDPALLRKHDLSSLRALFLAGEPLDEP--TAS----- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2271 aWFnaygpTEAVITPLAWHCRAQEGGAP--AIGRALGAR--------------RACILDAAL-QPCAPGMIGELYIGGQc 2333
Cdd:PRK10524 374 -WI-----SEALGVPVIDNYWQTETGWPilAIARGVEDRptrlgspgvpmygyNVKLLNEVTgEPCGPNEKGVLVIEGP- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2334 LARGYLgrpgQTA----ERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVA 2409
Cdd:PRK10524 447 LPPGCM----QTVwgddDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVA 522
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2410 EAAVVAL-DGVGGPLLAAYLVGRDAMRGED------LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK10524 523 EVAVVGVkDALKGQVAVAFVVPKDSDSLADrearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1981-2473 |
2.45e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 91.98 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGgvAAAFahqvasaPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILK 2060
Cdd:cd12118 6 PLSFLERA--AAVY-------PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2061 AGAGYLPLDPNYPAERLAYMLRDSGARWLICQEtlaerlpcpaeverlPLETAAWPASADTRPLPEVAG---ETLAyVIY 2137
Cdd:cd12118 77 AGAVLNALNTRLDAEEIAFILRHSEAKVLFVDR---------------EFEYEDLLAEGDPDFEWIPPAdewDPIA-LNY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQ--AALVAhcQAAARTYGVGPGDCQL----QF--ASISFDAAaeqlfVPLLAGARVLLGDAgqwSA 2209
Cdd:cd12118 141 TSGTTGRPKGVVYHHrgAYLNA--LANILEWEMKQHPVYLwtlpMFhcNGWCFPWT-----VAAVGGTNVCLRKV---DA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVTILDLPPAYL----QQQAEELRHAGRRIAVRTcilGGEAWDASLLtqQAVQAEAW--FNAYGPTEA-- 2281
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLnmlaNAPPSDARPLPHRVHVMT---AGAPPPAAVL--AKMEELGFdvTHVYGLTETyg 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VITPLAWHcRAQEGGAPAIGRALGARRAC---------ILDAALQPCAPG---MIGELYIGGQCLARGYLGRPGQTAERF 2349
Cdd:cd12118 286 PATVCAWK-PEWDELPTEERARLKARQGVryvgleevdVLDPETMKPVPRdgkTIGEIVFRGNIVMKGYLKNPEATAEAF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2350 vADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL 2428
Cdd:cd12118 365 -RGGW-------FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDEKWGEVPCAFV 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 2429 VGRDamrGEDLLA-ELRTWLAGRLPAYMQPTAWqVLSSLPLNANGK 2473
Cdd:cd12118 437 ELKE---GAKVTEeEIIAFCREHLAGFMVPKTV-VFGELPKTSTGK 478
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
3052-3467 |
2.80e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 91.98 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLKLP--LAQGvqridlDRGAPWFEDYSEANPdIHLDgenlayviYTSGSTGKPKGAGNRH-----SA 3204
Cdd:cd12118 98 RHSEAKVLFVDREFEYEdlLAEG------DPDFEWIPPADEWDP-IALN--------YTSGTTGRPKGVVYHHrgaylNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 LSNRLCW-MQQayglgvgDTVLQKTPFSFDVSVWEFFWPlmsgarlVVAAPGDH---R--DPAKLVALINREGVDtlHF- 3277
Cdd:cd12118 163 LANILEWeMKQ-------HPVYLWTLPMFHCNGWCFPWT-------VAAVGGTNvclRkvDAKAIYDLIEKHKVT--HFc 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 ----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLY--NLYGPTEAAIDVThwTCVE-EGKDAV 3350
Cdd:cd12118 227 gaptVLNML-ANAPPSDARPLPHRVHVMTAGAPPPA----AVLAKMEELGFDvtHVYGLTETYGPAT--VCAWkPEWDEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3351 PIG-----------RPIANLACYILDGN-LEPVPV-GV-LGELYLAGQGLARGYHQRPGLTAERFvaspfvAGErMYRTG 3416
Cdd:cd12118 300 PTEerarlkarqgvRYVGLEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG-WFHSG 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd12118 373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVAR 423
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
514-1034 |
3.02e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 92.71 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 514 HRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAG 585
Cdd:PRK07529 28 YELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 586 GAyVPVDPEYPEERQAYMLEDSGVQLLLS-------------QSHL-KLPLAQGVQRIDL--------DQADAWLENHAE 643
Cdd:PRK07529 108 IA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVLaALPELRTVVEVDLarylpgpkRLAVPLIRRKAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 644 NN-----------PGIEL------NGENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWM-QQAYGLGVGDTVLQKTP-FS 704
Cdd:PRK07529 187 ARildfdaelarqPGDRLfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLgALLLGLGPGDTVFCGLPlFH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 705 FDVSVWEFFWPLMSGARLVVAAPGDHRDP---AKLVELINREGVDTLHFVPSMLQAFLQ----DEDVascTSLKRIVCSG 777
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQvpvdGHDI---SSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 778 EALPADAQQQvFAKLPQAGLYNLYGPTEAaidvthwTCVEEgkdTVPIGRP--IGNLG---------CYILDGN---LEP 843
Cdd:PRK07529 343 APLPVEVFRR-FEAATGVRIVEGYGLTEA-------TCVSS---VNPPDGErrIGSVGlrlpyqrvrVVILDDAgryLRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 844 VPVGVLGELYLAGRGLARGYhqrpgLTAERfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:PRK07529 412 CAVDEVGVLCIAGPNVFSGY-----LEAAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 924 ARLLEHPWVREAAVL----AVDGRQLVGYVVL-------ESEGGDWrealaahLAASLPE-YMVPAQWLALERMPLSPNG 991
Cdd:PRK07529 485 EALLRHPAVALAAAVgrpdAHAGELPVAYVQLkpgasatEAELLAF-------ARDHIAErAAVPKHVRILDALPKTAVG 557
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2310915810 992 KLDRKALPAPEVsvaqagysapRNAVERTLAEIWQDLLGVERV 1034
Cdd:PRK07529 558 KIFKPALRRDAI----------RRVLRAALRDAGVEAEVVDVV 590
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
3050-3525 |
3.69e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 91.98 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYPEER--- 3126
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRsel 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3127 QAYMLEDSGVELLLSQSHlklPLAQGVQRID------------LDRGAP-------WFEDYSEANPDIHLDGENLAYVIY 3187
Cdd:PRK10946 113 NAYASQIEPALLIADRQH---ALFSDDDFLNtlvaehsslrvvLLLNDDgehslddAINHPAEDFTATPSPADEVAFFQL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSAL------SNRLCWMQQAY----GLGVGDTVLQKTPFSFDVsvweffwpLMSGARLVVAApgdh 3257
Cdd:PRK10946 190 SGGSTGTPKLIPRTHNDYyysvrrSVEICGFTPQTrylcALPAAHNYPMSSPGALGV--------FLAGGTVVLAP---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 rDPAKLV--ALINREGVDTLHFVPSM----LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPT 3331
Cdd:PRK10946 258 -DPSATLcfPLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3332 EAAIDvthWTCVEEGKDAV--PIGRPIA-NLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFva 3408
Cdd:PRK10946 336 EGLVN---YTRLDDSDERIftTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3409 germYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---- 3480
Cdd:PRK10946 411 ----YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEdelmGEKSCAFLVVKEplka 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3481 --------ESGdwrealaahlaasLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK10946 487 vqlrrflrEQG-------------IAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2129-2487 |
4.09e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 89.85 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2129 GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASIsfDAAAEQLFVPLLAGARVLLGDAG 2205
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDvllCGLPLFHV--NGSVVTLLTPLASGAHVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADE----VERHAVTILDLPPAYLQQQAEelRHAGRRI-AVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPT 2279
Cdd:cd05944 79 GYRNPGLFDNfwklVERYRITSLSTVPTVYAALLQ--VPVNADIsSLRFAMSGAAPLPVELRARfEDATGLPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EAVITplawHCRAQEGGAPAIGrALGAR------RACILDA---ALQPCAPGMIGELYIGGQCLARGYLgrpgQTAERFV 2350
Cdd:cd05944 157 EATCL----VAVNPPDGPKRPG-SVGLRlpyarvRIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYL----YTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2351 ADpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL- 2428
Cdd:cd05944 228 AF----VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQpDAHAGELPVAYVq 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2429 VGRDAMRGEdllAELRTWLAGRLPAYMQ-PTAWQVLSSLPLNANGKLDRKALpKVDAAAR 2487
Cdd:cd05944 304 LKPGAVVEE---EELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL-RADAIHR 359
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
2011-2457 |
4.42e-18 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 90.88 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 cqetlaerlpcpaeverlpletaawpasADTrplpevagetlAYVIYTSGSTGQPKgvavsqAALVAHCQAAARTYGvgp 2170
Cdd:cd05940 81 ----------------------------VDA-----------ALYIYTSGTTGLPK------AAIISHRRAWRGGAF--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 gdcqlqFASISFDAAAEQLF--VPL--------------LAGARVLLGDagQWSAQHLADEVERHAVTIL----DLPPAY 2230
Cdd:cd05940 113 ------FAGSGGALPSDVLYtcLPLyhstalivgwsaclASGATLVIRK--KFSASNFWDDIRKYQATIFqyigELCRYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEELRhagRRIAVRtCILG----GEAWDaSLLTQQAVQAEAWFnaYGPTEAVITplAWHCRAQEGgapAIGRALGA 2306
Cdd:cd05940 185 LNQPPKPTE---RKHKVR-MIFGnglrPDIWE-EFKERFGVPRIAEF--YAATEGNSG--FINFFGKPG---AIGRNPSL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRACILDAALQ-----------------PCAPGMIGEL--YIGGQCLARGYLGrPGQTAERFVADPFSgSGERLYRTGDL 2367
Cdd:cd05940 253 LRKVAPLALVKydlesgepirdaegrciKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFK-KGDAWFNTGDL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2368 ARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAYLVgrDAMRGEDLLAELRT 2445
Cdd:cd05940 331 MRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIV--LQPNEEFDLSALAA 408
|
490
....*....|..
gi 2310915810 2446 WLAGRLPAYMQP 2457
Cdd:cd05940 409 HLEKNLPGYARP 420
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
3037-3525 |
7.14e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 92.29 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3037 QRGVHRLFEEQVERTPTAPALA-FGEERLDYAELNRRANRLAHaLIERGVGADRLVGVAMERSIEMVVALMAILKAGgaY 3115
Cdd:PRK08633 614 LPPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLALLLAG--K 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3116 VPVDPEYPEERQAYM--LEDSGVE-LLLSQSHL-KLPLAQGVQRIDLDRGAPWFEDYSEA-------------------- 3171
Cdd:PRK08633 691 VPVNLNYTASEAALKsaIEQAQIKtVITSRKFLeKLKNKGFDLELPENVKVIYLEDLKAKiskvdkltallaarllparl 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 -----NPDIHLDgeNLAYVIYTSGSTGKPKGAG-NRHSALSNrLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFwPL 3243
Cdd:PRK08633 771 lkrlyGPTFKPD--DTATIIFSSGSEGEPKGVMlSHHNILSN-IEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWL-PL 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3244 MSGARLV-VAAPGDHRDPAKLVAlinREGVDTLHFVPSMLQAFLQD-----EDVASctsLKRIVCSGEALP---ADAQQQ 3314
Cdd:PRK08633 847 LEGIKVVyHPDPTDALGIAKLVA---KHRATILLGTPTFLRLYLRNkklhpLMFAS---LRLVVAGAEKLKpevADAFEE 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3315 VFAKLPQAGlynlYGPTE----AAIDVTHwtcVEEGKDAV-------PIGRPIANLACYILD-GNLEPVPVGVLGELYLA 3382
Cdd:PRK08633 921 KFGIRILEG----YGATEtspvASVNLPD---VLAADFKRqtgskegSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3383 GQGLARGYHQRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 3462
Cdd:PRK08633 994 GPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEV 1070
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3463 --AVLAVD----GRQLVgyVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK08633 1071 vfAVTAVPdekkGEKLV--VLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
500-996 |
7.94e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 91.21 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 500 WNATAAEYPLQRGVHrLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVAL 578
Cdd:PRK05605 22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDR-VAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 579 MAILKAGGAYVPVDPEYPEERQAYMLEDSG----------------------------VQL-----LLSQSHLKLPL-AQ 624
Cdd:PRK05605 100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGarvaivwdkvaptverlrrttpletivsVNMiaampLLQRLALRLPIpAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 625 GVQRIDL----DQADAW--LENHAENNPGI-----ELNGENLAYVIYTSGSTGKPKGA----GNRHSALSNRLCWMQqay 689
Cdd:PRK05605 180 RKARAALtgpaPGTVPWetLVDAAIGGDGSdvshpRPTPDDVALILYTSGTTGKPKGAqlthRNLFANAAQGKAWVP--- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 690 GLGVGD-TVLQKTPF--SFDVSVWEFFWPLMsGARLVV-AAPgdhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DED 763
Cdd:PRK05605 257 GLGDGPeRVLAALPMfhAYGLTLCLTLAVSI-GGELVLlPAP----DIDLILDAMKKHPPTWLPGVPPLYEKIAEaaEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 764 VASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVThwtCVEEGKDTVP--IGRPIGNLGCYILD-GN 840
Cdd:PRK05605 332 GVDLSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTEVRIVDpED 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 841 L-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 919
Cdd:PRK05605 408 PdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 920 GEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLEsEGGDW-REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK05605 481 AEVEEVLREHPGVEDAAVVGLpreDGSEeVVAAVVLE-PGAALdPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVR 559
|
..
gi 2310915810 995 RK 996
Cdd:PRK05605 560 RR 561
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2137-2476 |
9.15e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 88.49 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVA------VSQAALVAHCQA------------------------AARTYGvgpgdCQLQFASISFDAAA 2186
Cdd:cd05917 9 FTSGTTGSPKGATlthhniVNNGYFIGERLGlteqdrlcipvplfhcfgsvlgvlACLTHG-----ATMVFPSPSFDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2187 eqlfvpllagarVLLgdagqwsaqhladEVERHAVTIL-DLPPAYLqqqaEELRHAGRR----IAVRTCILGGEAWDASL 2261
Cdd:cd05917 84 ------------VLE-------------AIEKEKCTALhGVPTMFI----AELEHPDFDkfdlSSLRTGIMAGAPCPPEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2262 LTQ--QAVQAEAWFNAYGPTEAviTPLAWHCRA---QEGGAPAIGRALGARRACILDAALQP-CAPGMIGELYIGGQCLA 2335
Cdd:cd05917 135 MKRviEVMNMKDVTIAYGMTET--SPVSTQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYLGRPGQTAErfvadpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIkIRGFR-IEIGEIESQLLAHPYVAEAAVV 2414
Cdd:cd05917 213 KGYWNDPEKTAE-------AIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVV 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2415 AL-DGVGGPLLAAYLVGRDamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd05917 285 GVpDERYGEEVCAWIRLKE---GAELTEEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
3656-3827 |
9.47e-18 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 89.79 E-value: 9.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3656 ALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATLGgallWRAEAVDRQAL-ESLCEESQRSLDLTDGPLL 3731
Cdd:cd19540 35 ALDVDALRAALADVVARHESLRTVFPEDDGGPYqvvLPAAEARPD----LTVVDVTEDELaARLAEAARRGFDLTAELPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3732 RSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR---LPGKTSPFKAWAGRV--SEHARGESMKA 3806
Cdd:cd19540 111 RARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDwapLPVQYADYALWQRELlgDEDDPDSLAAR 190
|
170 180
....*....|....*....|...
gi 2310915810 3807 QLQFWRELLEGAPAE--LPCEHP 3827
Cdd:cd19540 191 QLAYWRETLAGLPEEleLPTDRP 213
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
536-993 |
9.79e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 90.54 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 536 RLDYAELNRRANRLAHALIERGIGA-DRLVGVAME--RSIEMvvaLMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPgDRVGTLAWNgyRHLEA---YYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 613 LSQSHLkLPLAQGV---------------------QRIDLDQADAWLENHAENNPGIELNgENLA-YVIYTSGSTGKPKG 670
Cdd:PRK07008 116 LFDLTF-LPLVDALapqcpnvkgwvamtdaahlpaGSTPLLCYETLVGAQDGDYDWPRFD-ENQAsSLCYTSGTTGNPKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 671 A--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFWPL-MSGARLVVaaPGDHRDPAKLVELINREGVDT 747
Cdd:PRK07008 194 AlySHRSTVLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSApLTGAKLVL--PGPDLDGKSLYELIEAERVTF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 748 LHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPAdAQQQVFAKLPQAGLYNLYGPTE-------AAIDVTHWTCVEE 818
Cdd:PRK07008 271 SAGVPTVWLGLLNhmREAGLRFSTLRRTVIGGSACPP-AMIRTFEDEYGVEVIHAWGMTEmsplgtlCKLKWKHSQLPLD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 819 GKDTVPI--GRPIGNLGCYILDGNLEPVPV-GV-LGELYLAGRGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARY 894
Cdd:PRK07008 350 EQRKLLEkqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFPTGDVATI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 895 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESEGGDW-REALAAHLAA 968
Cdd:PRK07008 420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkwDERPLL--VVVKRPGAEVtREELLAFYEG 497
|
490 500
....*....|....*....|....*
gi 2310915810 969 SLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:PRK07008 498 KVAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
3052-3467 |
1.10e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 90.32 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPAL-AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:PRK07514 16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQSHL-----KLPLAQGVQRI---DLDRGAPWFE---DYSEANPDIHLDGENLAYVIYTSGSTGKPKGAG 3199
Cdd:PRK07514 96 IGDAEPALVVCDPANfawlsKIAAAAGAPHVetlDADGTGSLLEaaaAAPDDFETVPRGADDLAAILYTSGTTGRSKGAM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSAL-SNRLCwMQQAYGLGVGDTVLQKTPF--------SFDVSvweffwpLMSGARLVVAApgdHRDPAKLVALINRE 3270
Cdd:PRK07514 176 LSHGNLlSNALT-LVDYWRFTPDDVLIHALPIfhthglfvATNVA-------LLAGASMIFLP---KFDPDAVLALMPRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVdtLHFVPSMLQAFLQDEDV-ASCTSLKRIVCSGEA-LPADAQQQVFAKLPQAGLyNLYGPTEAAIDVTHwtcVEEGkD 3348
Cdd:PRK07514 245 TV--MMGVPTFYTRLLQEPRLtREAAAHMRLFISGSApLLAETHREFQERTGHAIL-ERYGMTETNMNTSN---PYDG-E 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3349 AVP--IGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADG 3425
Cdd:PRK07514 318 RRAgtVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERG 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2310915810 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK07514 392 YVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
2001-2474 |
1.18e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 90.07 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGD--EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLA 2078
Cdd:PRK13390 10 APDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2079 YMLRDSGARWLICQETL---AERLPCPAEVeRLPL--------ETAAWPASADTRPLPEVAGetlAYVIYTSGSTGQPKG 2147
Cdd:PRK13390 90 YIVGDSGARVLVASAALdglAAKVGADLPL-RLSFggeidgfgSFEAALAGAGPRLTEQPCG---AVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 V-------AVSQAA--LVAhcqAAARTYGVGPGDCQLQFASIsFDAAAEQL--FVPLLAGARVLlgdAGQWSAQHLADEV 2216
Cdd:PRK13390 166 IqpdlpgrDVDAPGdpIVA---IARAFYDISESDIYYSSAPI-YHAAPLRWcsMVHALGGTVVL---AKRFDAQATLGHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGgeAWDASLLTQQAVQaeAW-----FNAYGPTEA----VIT 2284
Cdd:PRK13390 239 ERYRITVTQMVPTMfvrLLKLDADVRTRYDVSSLRAVIHA--AAPCPVDVKHAMI--DWlgpivYEYYSSTEAhgmtFID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 PLAWhcRAQEGgapAIGRA-LGARRACILDAALQPCapGMIGELYIGGQCLARGYLGRPGQTAE-RFVADPFSGSgerly 2362
Cdd:PRK13390 315 SPDW--LAHPG---SVGRSvLGDLHICDDDGNELPA--GRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWTT----- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2363 rTGDLARYRVDGqveYLGRADQQ---IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGED 2438
Cdd:PRK13390 383 -VGDLGSVDEDG---YLYLADRKsfmIISGGVNIYPQETENALTMHPAVHDVAVIGVpDPEMGEQVKAVIQLVEGIRGSD 458
|
490 500 510
....*....|....*....|....*....|....*..
gi 2310915810 2439 LLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK13390 459 ELArELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
3060-3472 |
1.29e-17 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 89.73 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQShlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLG 3219
Cdd:cd17640 82 VVEN----------------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3220 VGDTVLQKTP--FSFDVSVwEFFWPLMSGARL---VVAAPGDHRD--PAKLVAlinregvdtlhfVPSMLQAF---LQDE 3289
Cdd:cd17640 128 PGDRFLSILPiwHSYERSA-EYFIFACGCSQAytsIRTLKDDLKRvkPHYIVS------------VPRLWESLysgIQKQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLKRI-------------VCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT---HWtCVEEGKdavpIG 3353
Cdd:cd17640 195 VSKSSPIKQFLflfflsggifkfgISGGGALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSarrLK-CNVRGS----VG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3354 RPIANLACYILD--GNlEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAG 3431
Cdd:cd17640 268 RPLPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTG 340
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2310915810 3432 RI-DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL 3472
Cdd:cd17640 341 RAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRL 382
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
4534-5041 |
1.31e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 90.06 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLvhqrvAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:PRK13383 37 PYTLL-----AVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGAD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPiPEGLSCLSVDREEEWAGFPAHDPEVALHGdnlAYVIYTSGSTG 4693
Cdd:PRK13383 112 VVPISTEFRSDALAAALRAHHISTVVADNEFAERIA-GADDAVAVIDPATAGAEESGGRPAVAAPG---RIVLLTSGTTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGV----------AVSHGPLIAHIVATGERyeMTPEDCELHFMSFAFdgshegWMHPLINGARVLIRDDslWLPERTY 4763
Cdd:PRK13383 188 KPKGVprapqlrsavGVWVTILDRTRLRTGSR--ISVAMPMFHGLGLGM------LMLTIALGGTVLTHRH--FDAEAAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVTVGVFPPVYLQQLAEHAE--RDGNP-PPVRVYCFGGDAVAQAsydLAWRALKP--KYLFNGYGPTETVVTPL 4838
Cdd:PRK13383 258 AQASLHRADAFTAVPVVLARILELPPrvRARNPlPQLRVVMSSGDRLDPT---LGQRFMDTygDILYNGYGSTEVGIGAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAAYMPIGTLlgnrSGYILDgqLNLLPVG--VAGELYLGGEgvargylerpaLTAERFVPDPFGAPGSRL 4916
Cdd:PRK13383 335 ATPADLRDAPETVGKPVAGC----PVRILD--RNNRPVGprVTGRIFVGGE-----------LAGTRYTDGGGKAVVDGM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSpe 4995
Cdd:PRK13383 398 TSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErFGHRLAAFVVLHPGSGVDA-- 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 4996 aqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:PRK13383 476 ------AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
4875-5129 |
1.36e-17 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 86.73 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4875 PVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIE 4954
Cdd:COG3433 40 FGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4955 ARLREHPAVREAVVVAQPGAVGQQLVGYVVAqepavadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGK 5034
Cdd:COG3433 120 LVLRAAAVVRVAVLAALRGAGVGLLLIVGAV---------AALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5035 LDRKGLPQPDASLLQQVYVAPRSDLE-----QQVAGIWAEVLQL--QQVGLDDNFFELGGHSLLAIQVTARMQsEVGVEL 5107
Cdd:COG3433 191 VVARAAPALAAAEALLAAASPAPALEtalteEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERWR-KAGLDV 269
|
250 260
....*....|....*....|..
gi 2310915810 5108 PLAALFQTESLQAYAELAAAQT 5129
Cdd:COG3433 270 SFADLAEHPTLAAWWALLAAAQ 291
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3657-3936 |
1.55e-17 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 88.67 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRF--HETDG----------TWHAEHAEATlggallwRAEAVDRqALESLCeesQRSLD 3724
Cdd:cd19532 36 LDVARLERAVRAVGQRHEALRTCFftDPEDGepmqgvlassPLRLEHVQIS-------DEAEVEE-EFERLK---NHVYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3725 LTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeaPRLPGKTSPFKAWAGRVSEHARGESM 3804
Cdd:cd19532 105 LESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG------QPLLPPPLQYLDFAARQRQDYESGAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3805 KAQLQFWRELLEGAPAELP--------CEHPQGALEQRfatSVQSRFDRSLTERlLKQAPAAYRTQVNDLLLTALARVVC 3876
Cdd:cd19532 179 DEDLAYWKSEFSTLPEPLPllpfakvkSRPPLTRYDTH---TAERRLDAALAAR-IKEASRKLRVTPFHFYLAALQVLLA 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3877 RWSGAssslvqleghgrEELF--------ADIDLSRTVGWFTSLFPVRLSPVAD--LGESLKAIKEQLRA 3936
Cdd:cd19532 255 RLLDV------------DDICigiadanrTDEDFMETIGFFLNLLPLRFRRDPSqtFADVLKETRDKAYA 312
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
2012-2417 |
1.56e-17 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 89.34 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 qetlaerlpcpaeverlpletaawpasadtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPG 2171
Cdd:cd17640 84 ----------------------------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2172 DCQLQFASI--SFDAAAEqlFVPLLAGA-------RVLLGDAGQWSAQHLAdEVERHAVTIldlppaYLQQQaEELRH-- 2240
Cdd:cd17640 130 DRFLSILPIwhSYERSAE--YFIFACGCsqaytsiRTLKDDLKRVKPHYIV-SVPRLWESL------YSGIQ-KQVSKss 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRIAVRTCILGGEawdasllTQQAV--------QAEAWFNA--------YGPTEAviTPLAWHCRAQEGGAPAIGRAL 2304
Cdd:cd17640 200 PIKQFLFLFFLSGGI-------FKFGIsgggalppHVDTFFEAigievlngYGLTET--SPVVSARRLKCNVRGSVGRPL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2305 GARRACILDA-ALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRAD 2383
Cdd:cd17640 271 PGTEIKIVDPeGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRAK 343
|
410 420 430
....*....|....*....|....*....|....*
gi 2310915810 2384 QQIKIR-GFRIEIGEIESQLLAHPYVAEAAVVALD 2417
Cdd:cd17640 344 DTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
525-993 |
1.57e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:PRK13390 11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQA-DAWLENHAENNPGIELNGENL------AYVIYTSGSTGKPKG----- 670
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKVGADLPLRLSfGGEIDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKGiqpdl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 671 AGNRHSALSNRLCWMQQA-YGLGVGDTVLQKTPFSFDVSVWeffWPLMS---GARLVVAAPGDHRDPAKLVElinREGVD 746
Cdd:PRK13390 171 PGRDVDAPGDPIVAIARAfYDISESDIYYSSAPIYHAAPLR---WCSMVhalGGTVVLAKRFDAQATLGHVE---RYRIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 747 TLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AIDVTHWTCvEE 818
Cdd:PRK13390 245 VTQMVPTMFVRLLKlDADVRTrydVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAhgmtFIDSPDWLA-HP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 819 GKdtvpIGRPI-GNLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAE-RFVASPFVAgermyRTGDLARYRA 896
Cdd:PRK13390 323 GS----VGRSVlGDL--HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWT-----TVGDLGSVDE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 897 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL---VGYVVLESEGGDWREALAAH----LAAS 969
Cdd:PRK13390 392 DGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMgeqVKAVIQLVEGIRGSDELARElidyTRSR 471
|
490 500
....*....|....*....|....
gi 2310915810 970 LPEYMVPAQWLALERMPLSPNGKL 993
Cdd:PRK13390 472 IAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
534-937 |
1.88e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 89.95 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 534 EERLDYAELNRRANRLAHALIERGIG-ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK04319 71 KEKYTYKELKELSNKFANVLKELGVEkGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 613 LSQSHL-------KLPLAQGVQRIDLDQA--------DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:PRK04319 150 ITTPALlerkpadDLPSLKHVLLVGEDVEegpgtldfNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 678 lsnrlcwMQQAYglGVGDTVLQKTPfsFDVsvwefFW-----------------PLMSGARLVVAapGDHRDPAKLVELI 740
Cdd:PRK04319 230 -------MLQHY--QTGKYVLDLHE--DDV-----YWctadpgwvtgtsygifaPWLNGATNVID--GGRFSPERWYRIL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 741 NREGVDTLHFVPS---MLQAflQDEDVASC---TSLKRIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDV 810
Cdd:PRK04319 292 EDYKVTVWYTAPTairMLMG--AGDDLVKKydlSSLRHILSVGEPLNPEVvrwGMKVF-GLP---IHDNWWMTEtGGIMI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 811 THWTCVeegkDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAgRG---LARGYHQRPgltaERFvASPFVAGerM 885
Cdd:PRK04319 366 ANYPAM----DIKPgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNP----EKY-ESYFAGD--W 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 937
Cdd:PRK04319 434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
3654-4049 |
1.93e-17 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 88.12 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3654 REALNAKALEAALQALVEHHDALRLRFHETD--GTWHAEHAEATLGgallWRaeavDRQALESLCEE-SQRSLDLtDGPL 3730
Cdd:cd19545 31 PPDIDLARLQAAWEQVVQANPILRTRIVQSDsgGLLQVVVKESPIS----WT----ESTSLDEYLEEdRAAPMGL-GGPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3731 LRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeapRLPGKTSPFKawagRVSEHARGESMKAQLQF 3810
Cdd:cd19545 102 VRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG-------EPVPQPPPFS----RFVKYLRQLDDEAAAEF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3811 WRELLEGA-PAELPC-------EHPQGALEQRFATSVQSRFDRSLTErllkqapaayrtqvndLLLTALARVVCRWSGAS 3882
Cdd:cd19545 171 WRSYLAGLdPAVFPPlpssryqPRPDATLEHSISLPSSASSGVTLAT----------------VLRAAWALVLSRYTGSD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3883 SSLVQLEGHGREELFADIDlsRTVG-WFTSL-FPVRLSPVADLGESLKAIKEQL-RAIPDKGLGyglLRylageesaRVL 3959
Cdd:cd19545 235 DVVFGVTLSGRNAPVPGIE--QIVGpTIATVpLRVRIDPEQSVEDFLQTVQKDLlDMIPFEHTG---LQ--------NIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3960 AGLPQARITFNylgqfdaqFDEMALLDPAGESAGAEMDPG---------APLDNW-LSLNGRVFDGELSIDWSFSSQMFG 4029
Cdd:cd19545 302 RLGPDARAACN--------FQTLLVVQPALPSSTSESLELgieeesedlEDFSSYgLTLECQLSGSGLRVRARYDSSVIS 373
|
410 420
....*....|....*....|
gi 2310915810 4030 EDQVRRLADDYVAELTALVD 4049
Cdd:cd19545 374 EEQVERLLDQFEHVLQQLAS 393
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1994-2479 |
4.00e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 88.94 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASA-PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:PRK06710 29 YVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2073 PAERLAYMLRDSGARWLICQE---------------------TLAERLPCP-------------------AEVERLPLET 2112
Cdd:PRK06710 109 TERELEYQLHDSGAKVILCLDlvfprvtnvqsatkiehvivtRIADFLPFPknllypfvqkkqsnlvvkvSESETIHLWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2113 AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD----CQLQFASISFDAAAE 2187
Cdd:PRK06710 189 SVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEGEevvlGVLPFFHVYGMTAVM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2188 QLfvPLLAGARVLLgdAGQWSAQHLADEVERHAVTIL-DLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQ-Q 2265
Cdd:PRK06710 269 NL--SIMQGYKMVL--IPKFDMKMVFEAIKKHKVTLFpGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKfE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2266 AVQAEAWFNAYGPTEAviTPLAWHCRAQEGGAP-AIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLARGYLGRPG 2343
Cdd:PRK06710 345 TVTGGKLVEGYGLTES--SPVTHSNFLWEKRVPgSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIMKGYWNKPE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2344 QTAErFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGP 2422
Cdd:PRK06710 423 ETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVpDPYRGE 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2423 LLAAYLVGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06710 495 TVKAFVVLKEGTECSE--EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
2287-2572 |
4.41e-17 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 85.57 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 AWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGD 2366
Cdd:COG3433 7 PPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2367 LARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVgrdAMRGEDLLAELRTW 2446
Cdd:COG3433 87 LLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGA---VAALDGLAAAAALA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2447 LAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPR-----EGLERSVAAIWEALLGV--EGIARDE 2519
Cdd:COG3433 164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPApaletALTEEELRADVAELLGVdpEEIDPDD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 2520 HFFELGGHSLSATRVVSRLRQDlELDVPLRILFERPVLADFAASLESQAASVA 2572
Cdd:COG3433 244 NLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
4537-4987 |
4.54e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 88.50 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4537 PLvHQRVAERARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA- 4613
Cdd:PLN02246 24 PL-HDYCFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 ------YVPLDIEYprerllyMMQDSRAHLLLTHSHLLERLP---IPEGLSCLSVDREEE-----WAGFPAHD---PEVA 4676
Cdd:PLN02246 103 ttanpfYTPAEIAK-------QAKASGAKLIITQSCYVDKLKglaEDDGVTVVTIDDPPEgclhfSELTQADEnelPEVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4677 LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV--ATGE--RYEMTPED---CEL---HFMSFafdgsHEGWMHPLING 4746
Cdd:PLN02246 176 ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqVDGEnpNLYFHSDDvilCVLpmfHIYSL-----NSVLLCGLRVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4747 ARVLIrddslwLPERTYAEM----HRHGVTVGVF-PPVYLqQLAEhaerdgNPppvrvycfggdavAQASYDL------- 4814
Cdd:PLN02246 251 AAILI------MPKFEIGALleliQRHKVTIAPFvPPIVL-AIAK------SP-------------VVEKYDLssirmvl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4815 ------------AWRALKPKYLF-NGYGPTETvvTPLL----------WKARAGdACgaaympiGTLLGNRSGYILDGQL 4871
Cdd:PLN02246 305 sgaaplgkeledAFRAKLPNAVLgQGYGMTEA--GPVLamclafakepFPVKSG-SC-------GTVVRNAELKIVDPET 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4872 NL-LPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLtrGRADG-----VVDylgRVDHQVKIRG 4945
Cdd:PLN02246 375 GAsLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW-------LHTGDI--GYIDDddelfIVD---RLKELIKYKG 442
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQE 4987
Cdd:PLN02246 443 FQVAPAELEALLISHPSIADAAVVPMKDEVaGEVPVAFVVRSN 485
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
657-998 |
4.80e-17 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 87.82 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 657 YVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLG--VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDP 733
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPGgPPDNDTLMAAALGFGpgADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 734 AKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA--- 806
Cdd:cd05929 206 EEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVrnayDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGqgl 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 807 -AIDVTHWTcveEGKDTVpiGRPIGNlGCYILDGNLEPVPVGVLGELYLAGrGLARGYHQRPGLTAERFVASPFVAgerm 885
Cdd:cd05929 285 tIINGEEWL---THPGSV--GRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST---- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 886 yrTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGDWREAL 962
Cdd:cd05929 354 --LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVpdeELGQRVHAVVQPAPGADAGTAL 431
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2310915810 963 AAHLAA----SLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05929 432 AEELIAflrdRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
4563-4990 |
5.71e-17 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 88.04 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGgayVPLDIEYP---RERLLYMMQDSRAhlll 4639
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETEC---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 thshllerlpipEGLSClsvdreeewagfpahDPEvalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY--E 4717
Cdd:cd17639 79 ------------SAIFT---------------DGK----PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4718 MTPEDCEL------HFMSFAFD------GSHEGWMHPlingaRVLIrDDSLwlpERTYAEMH--RHGVTVGVfPPVY--- 4780
Cdd:cd17639 128 LGPDDRYLaylplaHIFELAAEnvclyrGGTIGYGSP-----RTLT-DKSK---RGCKGDLTefKPTLMVGV-PAIWdti 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 --------------LQQLAEHAE-------RDGNPPP-----------------VRVYCFGGDAVAQASYDLAWRALKPk 4822
Cdd:cd17639 198 rkgvlaklnpmgglKRTLFWTAYqsklkalKEGPGTPlldelvfkkvraalggrLRYMLSGGAPLSADTQEFLNIVLCP- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 yLFNGYGPTETVvtpllwkaragdaCGAAYMPIGTLLGNRSGYILDG-QLNLLPVGVA----------GELYLGGEGVAR 4891
Cdd:cd17639 277 -VIQGYGLTETC-------------AGGTVQDPGDLETGRVGPPLPCcEIKLVDWEEGgystdkppprGEILIRGPNVFK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4892 GYLERPALTAERFVPDpfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREAVVVA 4970
Cdd:cd17639 343 GYYKNPEKTKEAFDGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500
....*....|....*....|
gi 2310915810 4971 QPGAVgqQLVGYVVAQEPAV 4990
Cdd:cd17639 416 DPDKS--YPVAIVVPNEKHL 433
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
533-945 |
6.24e-17 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 87.41 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 613 LsqshlklplaqgvqridldqadawLENHaennpgielnGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLG 692
Cdd:cd17640 82 V------------------------VEND----------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 693 VGDTVLQKTP--FSFDVSVwEFFWPLMSGARL---VVAAPGDHRD--PAKLVElinregvdtlhfVPSMLQAF---LQDE 762
Cdd:cd17640 128 PGDRFLSILPiwHSYERSA-EYFIFACGCSQAytsIRTLKDDLKRvkPHYIVS------------VPRLWESLysgIQKQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 763 DVASCTSLKRI-------------VCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT---HWtCVEEGKdtvpIG 826
Cdd:cd17640 195 VSKSSPIKQFLflfflsggifkfgISGGGALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSarrLK-CNVRGS----VG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 827 RPIGNLGCYILD--GNlEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAG 904
Cdd:cd17640 268 RPLPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTG 340
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2310915810 905 RI-DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL 945
Cdd:cd17640 341 RAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRL 382
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1990-2479 |
6.57e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 88.01 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PRK08751 27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGdRVALMMPNCLQYPIATFGVLRAGLTVVNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 DPNYPAERLAYMLRDSGARWLIC--------QETLAER---------------LPCPAEVE-------------RLP--- 2109
Cdd:PRK08751 107 NPLYTPRELKHQLIDSGASVLVVidnfgttvQQVIADTpvkqvittglgdmlgFPKAALVNfvvkyvkklvpeyRINgai 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2110 -LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAA----ARTYGVGPGdCQLQFASIS--- 2181
Cdd:PRK08751 187 rFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwlAGTGKLEEG-CEVVITALPlyh 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2182 -FDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTI----------LDLPPAYLQQQAEELRhagrriavrtC 2250
Cdd:PRK08751 266 iFALTANGLVFMKIGGCNHLISNPRDMPG--FVKELKKTRFTAftgvntlfngLLNTPGFDQIDFSSLK----------M 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2251 ILGGeawdaSLLTQQAVqAEAW--------FNAYGPTE----AVITPLAWhcrAQEGGApaIGRALGARRACILDAALQP 2318
Cdd:PRK08751 334 TLGG-----GMAVQRSV-AERWkqvtgltlVEAYGLTEtspaACINPLTL---KEYNGS--IGLPIPSTDACIKDDAGTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:PRK08751 403 LAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2399 ESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:PRK08751 476 EDVIAMMPGVLEVAAVGVpDEKSGEIVKVVIVKKDpALTAEDVKAHARANLTG----YKQPRIIEFRKELPKTNVGKILR 551
|
...
gi 2310915810 2477 KAL 2479
Cdd:PRK08751 552 REL 554
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
4675-5040 |
7.37e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 87.96 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS--------------FAFDGShegWM 4740
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEgqevmiaplplyhiYAFTAN---CM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4741 HPLINGAR-VLI---RDDSLWLPE----RTYAEMHRHGVTVGvfppvylqqLAEHAE-RDGNPPPVRVYCFGGDAVAQAS 4811
Cdd:PRK12492 279 CMMVSGNHnVLItnpRDIPGFIKElgkwRFSALLGLNTLFVA---------LMDHPGfKDLDFSALKLTNSGGTALVKAT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 YDlAWRALKPKYLFNGYGPTET--VVT--PLLWKARagdaCGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGG 4886
Cdd:PRK12492 350 AE-RWEQLTGCTIVEGYGLTETspVAStnPYGELAR----LGTVGIPVpGTALK-----VIDDDGNELPLGERGELCIKG 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4887 EGVARGYLERPALTAErfVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4966
Cdd:PRK12492 420 PQVMKGYWQQPEATAE--ALDAEG-----WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANC 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4967 VVVAQPGA-VGQQLVGYVVAQEPAVAdspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK12492 493 AAIGVPDErSGEAVKLFVVARDPGLS---------VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
4541-5042 |
7.70e-17 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 87.58 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd17642 21 HKAMKRYASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSRAHLLLTHSHLLER-------LPIPEGLSCLS--VDREE-----------EWAGFPAHD--PEVA 4676
Cdd:cd17642 101 DIYNERELDHSLNISKPTIVFCSKKGLQKvlnvqkkLKIIKTIIILDskEDYKGyqclytfitqnLPPGFNEYDfkPPSF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4677 LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIA---HIVATGERYEMTPEDCELHFMSFafdgsHEGW-----MHPLINGAR 4748
Cdd:cd17642 181 DRDEQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPF-----HHGFgmfttLGYLICGFR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4749 VLIR---DDSLWLpertyAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKYL 4824
Cdd:cd17642 256 VVLMykfEEELFL-----RSLQDYKVQSALLVPTLFAFFAKSTLVDKyDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4825 FNGYGPTET----VVTPllwkaRAGDACGAaympIGTLLGNRSGYILDGQL-NLLPVGVAGELYLGGEGVARGYLERPAL 4899
Cdd:cd17642 331 RQGYGLTETtsaiLITP-----EGDDKPGA----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFVPDPFgapgsrlYRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG 4976
Cdd:cd17642 402 TKALIDKDGW-------LHSGDIAYYDEDGhffIVD---RLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 4977 QQLVG-YVVAQEPAVADSPEAQAECRAQLKTALRERlpeymvpSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:cd17642 472 GELPAaVVVLEAGKTMTEKEVMDYVASQVSTAKRLR-------GGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
3063-3520 |
8.74e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 87.45 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGA-DRLVGVAME--RSIEMvvaLMAILKAGGAYVPVDPE-YPEE--------RQAYM 3130
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPgDRVGTLAWNgyRHLEA---YYGVSGSGAVCHTINPRlFPEQiayivnhaEDRYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQSHLKLPLAQG-VQRIDLDR----GAPW--FEDYSEANPDIH----LDgENLA-YVIYTSGSTGKPKGA 3198
Cdd:PRK07008 116 LFDLTFLPLVDALAPQCPNVKGwVAMTDAAHlpagSTPLlcYETLVGAQDGDYdwprFD-ENQAsSLCYTSGTTGNPKGA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3199 --GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFWPL-MSGARLVVaaPGDHRDPAKLVALINREGVDTL 3275
Cdd:PRK07008 195 lySHRSTVLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSApLTGAKLVL--PGPDLDGKSLYELIEAERVTFS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3276 HFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPAdAQQQVFAKLPQAGLYNLYGPTEAAIDVThwTCVEEGK-DAVPI 3352
Cdd:PRK07008 272 AGVPTVWLGLLNhmREAGLRFSTLRRTVIGGSACPP-AMIRTFEDEYGVEVIHAWGMTEMSPLGT--LCKLKWKhSQLPL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 ----------GRPIANLACYILDGNLEPVPV-GV-LGELYLAGQGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLAR 3420
Cdd:PRK07008 349 deqrkllekqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFPTGDVAT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESESGDW-REALAAHLA 3494
Cdd:PRK07008 419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkwDERPLL--VVVKRPGAEVtREELLAFYE 496
|
490 500
....*....|....*....|....*.
gi 2310915810 3495 ASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:PRK07008 497 GKVAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
4121-4504 |
1.24e-16 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 86.38 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4121 LDIPRFRAAWQSALDRHAILRSGFAWQG-ELQQPLQIVYRQRQ----LPFAEEDLSQAANRDAALLalaaaerergFELQ 4195
Cdd:cd19546 39 LDRDALEAALGDVAARHEILRTTFPGDGgDVHQRILDADAARPelpvVPATEEELPALLADRAAHL----------FDLT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4196 RAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AGRSPEQ-PRDGRYSDYIAWLQRQDAAATE-- 4268
Cdd:cd19546 109 RETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarrEGRAPERaPLPLQFADYALWERELLAGEDDrd 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4269 -------AFWREQMAALDEPTRLVEALAQPGLTSANGVGEHLReVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYT 4341
Cdd:cd19546 189 sligdqiAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLR-LDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4342 GQHTVVFGaTVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEA- 4420
Cdd:cd19546 268 AGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSAd 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4421 ---VFDNLLVFENYPVDEvLERSSAGGVRFGAVAM-HEQTNYPLALAL-------GGGDSLSLQFSYDRGLFPAATIERL 4489
Cdd:cd19546 347 rhpVFQVALDVRDDDNDP-WDAPELPGLRTSPVPLgTEAMELDLSLALterrnddGDPDGLDGSLRYAADLFDRATAAAL 425
|
410
....*....|....*
gi 2310915810 4490 GRHLTTLLEAFAEHP 4504
Cdd:cd19546 426 ARRLVRVLEQVAADP 440
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
3046-3477 |
1.46e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 86.96 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3046 EQVERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY- 3122
Cdd:PLN02246 31 ERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYt 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 -PE-ERQAymlEDSGVELLLSQSHL-----KLPLAQGVQRIDLDR---GAPWFEDYSEAN----PDIHLDGENLAYVIYT 3188
Cdd:PLN02246 111 pAEiAKQA---KASGAKLIITQSCYvdklkGLAEDDGVTVVTIDDppeGCLHFSELTQADenelPEVEISPDDVVALPYS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3189 SGSTGKPKGAGNRHSALSNrlCWMQQAYG------LGVGDTVLQKTP----FSFDvSVweFFWPLMSGARLVVAApgdHR 3258
Cdd:PLN02246 188 SGTTGLPKGVMLTHKGLVT--SVAQQVDGenpnlyFHSDDVILCVLPmfhiYSLN-SV--LLCGLRVGAAILIMP---KF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 DPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEAAI 3335
Cdd:PLN02246 260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKydLSSI-RMVLSGAApLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVThwTCVEEGKDAVPI-----GRPIANLACYILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAG 3409
Cdd:PLN02246 339 VLA--MCLAFAKEPFPVksgscGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATANT------IDK 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3410 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGRQLVGYVV 3477
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPmkdeVAGEVPVAFVV 482
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1100-1515 |
1.61e-16 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 85.50 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL----W 1173
Cdd:cd19533 4 LTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIrhidL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1174 RRQAGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRS 1252
Cdd:cd19533 84 SGDPDPEGAAQQWMqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1253 SSYQTWSRHLHE-----QAGARLDELDYWQAQLHDAP--HALPCENPHGALENRhERKLVLTLDAERTrqlLQEAPAAYR 1325
Cdd:cd19533 164 APFGSFLDLVEEeqayrQSERFERDRAFWTEQFEDLPepVSLARRAPGRSLAFL-RRTAELPPELTRT---LLEAAEAHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1326 TQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIdlsrTVGWFTSLFPVRLT--PAADLGESLKAIKEQLRGV- 1402
Cdd:cd19533 240 ASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQ----TPGMVANTLPLRLTvdPQQTFAELVAQVSRELRSLl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1403 -PDKGVGYGLLRYLAGEEAATRLAalpqpRITFNYLgRFDRQFD-GAALLVPATESAGAAQDpcaplanwLSIegQVY-- 1478
Cdd:cd19533 316 rHQRYRYEDLRRDLGLTGELHPLF-----GPTVNYM-PFDYGLDfGGVVGLTHNLSSGPTND--------LSI--FVYdr 379
|
410 420 430
....*....|....*....|....*....|....*....
gi 2310915810 1479 --GGELSLHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19533 380 ddESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
3648-3922 |
1.62e-16 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 85.99 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3648 SLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTD 3727
Cdd:cd19546 30 SVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPVVPATEEELPALLADRAAHLFDLTR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3728 GPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR---LPGKTSPFKAWAGRV--SEHARGE 3802
Cdd:cd19546 110 ETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPErapLPLQFADYALWERELlaGEDDRDS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3803 SMKAQLQFWRELLEGAPAE--LPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNdLLLTALARVVCRWSG 3880
Cdd:cd19546 190 LIGDQIAYWRDALAGAPDEleLPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFT-VVQAALAMLLTRLGA 268
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2310915810 3881 ASSSLVQLEGHGREELfadIDLSRTVGWFTSLFPVRLSPVAD 3922
Cdd:cd19546 269 GTDVTVGTVLPRDDEE---GDLEGMVGPFARPLALRTDLSGD 307
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
2134-2476 |
1.87e-16 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 83.99 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAALVA---------HCQAAARTYGVGPgdcqLQFaSISFDAAAEQLFvplLAGARVLLgda 2204
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIEsfvcnedlfNISGEDAILAPGP----LSH-SLFLYGAISALY---LGGTFIGQ--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAgrrIAVRTCILGGEAWDASL---LTQQAVQAEAwFNAYGPTEA 2281
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE---SKIKSIFSSGQKLFESTkkkLKNIFPKANL-IEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VItpLAWHCRAQEGGAPAIGRALGARRACILDAalqpcAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgsgerl 2361
Cdd:cd17633 149 SF--ITYNFNQESRPPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2362 YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgedll 2440
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpDARFGEIAVALYSGDKLTY----- 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 2310915810 2441 AELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd17633 285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
4533-5035 |
1.88e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 86.22 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4533 YPATplvhqrvaeRARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK13390 2 YPGT---------HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNL------AY 4684
Cdd:PRK13390 73 GLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLteqpcgAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKG---------VAVSHGPLIAhivATGERYEMTPEDceLHFMSFA-FDGSHEGW--MHPLINGARVLI- 4751
Cdd:PRK13390 153 MLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVA---IARAFYDISESD--IYYSSAPiYHAAPLRWcsMVHALGGTVVLAk 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 RDDSlwlpERTYAEMHRHGVTVGVFPP---VYLQQLAEHAERDGNPPPVRVYCFGGDA----VAQASYDlaWraLKPkYL 4824
Cdd:PRK13390 228 RFDA----QATLGHVERYRITVTQMVPtmfVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdVKHAMID--W--LGP-IV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4825 FNGYGPTE----TVVTPLLWKARAGDACGAAympIGTLlgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:PRK13390 299 YEYYSSTEahgmTFIDSPDWLAHPGSVGRSV---LGDL------HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVP-DPFGAPgsrlyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQ 4978
Cdd:PRK13390 370 AAAQHPaHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPeMGEQ 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 4979 lVGYVVAQEPAVADSPEAQAEcraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK13390 444 -VKAVIQLVEGIRGSDELARE----LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1997-2479 |
1.93e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 86.57 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1997 QVASAPEAIALVCGDEHlSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAER 2076
Cdd:PLN02246 35 EFSDRPCLIDGATGRVY-TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2077 LAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPA----------SADTRPLPEV--AGETLAYVIYTSGSTGQ 2144
Cdd:PLN02246 114 IAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPegclhfseltQADENELPEVeiSPDDVVALPYSSGTTGL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2145 PKGVAVSQAALVAhcQAAARTYGVGP------GD---CQLQFASI-SFDAAaeqLFVPLLAGARVLLGDAGQWSAqhLAD 2214
Cdd:PLN02246 194 PKGVMLTHKGLVT--SVAQQVDGENPnlyfhsDDvilCVLPMFHIySLNSV---LLCGLRVGAAILIMPKFEIGA--LLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2215 EVERHAVTILDL-PPAYLQQQAEELRHAGRRIAVRTCI-----LGGEAWDA-SLLTQQAVQAEawfnAYGPTEAviTPLA 2287
Cdd:PLN02246 267 LIQRHKVTIAPFvPPIVLAIAKSPVVEKYDLSSIRMVLsgaapLGKELEDAfRAKLPNAVLGQ----GYGMTEA--GPVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRA--------QEGGAPAIGRALGARracILD----AALQPCAPgmiGELYIGGQCLARGYLGRPGQTAERFVADPFs 2355
Cdd:PLN02246 341 AMCLAfakepfpvKSGSCGTVVRNAELK---IVDpetgASLPRNQP---GEICIRGPQIMKGYLNDPEATANTIDKDGW- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 gsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAM 2434
Cdd:PLN02246 414 ------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMkDEVAGEVPVAFVVRSNGS 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 2435 R-GEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN02246 488 EiTED---EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
4560-5034 |
2.74e-16 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 85.10 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLll 4639
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 thshllerlpipeglscLSVDReeewagfpahdpevalhgdnlAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT 4719
Cdd:cd05940 79 -----------------LVVDA---------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4720 PEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTvgVFPPV-----YL-QQLAEHAERDG 4792
Cdd:cd05940 121 PSDVLYTCLPlYHSTALIVGWSACLASGATLVIRKK--FSASNFWDDIRKYQAT--IFQYIgelcrYLlNQPPKPTERKH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4793 NpppVRVYCfgGDAVAQAsydlAWRALKPKY----LFNGYGPTETVVTPLLWKARAGdACGAaympIGTLLGNRSGYIL- 4867
Cdd:cd05940 197 K---VRMIF--GNGLRPD----IWEEFKERFgvprIAEFYAATEGNSGFINFFGKPG-AIGR----NPSLLRKVAPLALv 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4868 -------------DGQLNLLPVGVAGEL--YLGGEGVARGYLErPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVD 4932
Cdd:cd05940 263 kydlesgepirdaEGRCIKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLDGEGFWY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADSPEAQAECRAqLKTALRE 5010
Cdd:cd05940 341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGR-------AGMAAIVLQPNEEFDLSA-LAAHLEK 412
|
490 500
....*....|....*....|....
gi 2310915810 5011 RLPEYMVPSHLLFLARMPLTPNGK 5034
Cdd:cd05940 413 NLPGYARPLFLRLQPEMEITGTFK 436
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
3057-3470 |
3.18e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 85.19 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3057 LAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3136
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 ELLLSQshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCWMQQAY 3216
Cdd:cd05914 81 KAIFVS-----------------------------------DEDDVALINYTSGTTGNSKGV-----MLTYRNIVSNVDG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3217 G-----LGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLhfvpsMLQAFLQDED 3290
Cdd:cd05914 121 VkevvlLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFL---DKIPSAKIIALAFAQVTPTL-----GVPVPLVIEK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3291 VASCTSLKRIVCSGE----ALPADAQQ---QVF------------------AKLPQ---AGLYNL-------YGPTEAA- 3334
Cdd:cd05914 193 IFKMDIIPKLTLKKFkfklAKKINNRKirkLAFkkvheafggnikefviggAKINPdveEFLRTIgfpytigYGMTETAp 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3335 -IDVTHWTCVEEGKdavpIGRPIANLACYILDgnlePVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMY 3413
Cdd:cd05914 273 iISYSPPNRIRLGS----AGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWF 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3414 RTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGR 3470
Cdd:cd05914 339 HTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKK 396
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
2135-2414 |
3.27e-16 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 83.51 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ-----------FASISFDAAAEQLFVPllagaRVllgd 2203
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplfhigtlmFTLATFHAGGTNVFVR-----RV---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2204 agqwSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLltqqAVQAEAWFNA---YGPTE 2280
Cdd:cd17636 76 ----DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMA----TVDTSPWGRKpggYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2281 AV-ITPLAWHCRAQEGGApaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVAdpfsgsge 2359
Cdd:cd17636 148 VMgLATFAALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2360 RLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVV 2414
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
4122-4503 |
3.57e-16 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 84.16 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4122 DIPRFRAAWQSALDRHAILRSGF-AWQGELQQPLQIVYRQRQLPfAEEDLSQAANRDaallalaaaerergFELQRAPLL 4200
Cdd:cd19537 37 DRDRLASAWNTVLARHRILRSRYvPRDGGLRRSYSSSPPRVQRV-DTLDVWKEINRP--------------FDLEREDPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4201 RLLLVKTaegehHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPEQPRDgRYSDYIAWlQRQDAAATEAFWREQMA---A 4277
Cdd:cd19537 102 RVFISPD-----TLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRR-EYLDSTAW-SRPASPEDLDFWSEYLSglpL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4278 LDEPTRLvealaqpGLTSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPA 4357
Cdd:cd19537 175 LNLPRRT-------SSKSYRG-TSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4358 dlPGVENQVGLFINTLPVVVTL--APQMTLDELLQGLQR--QNlALreqEHT-PLFELQRWAG----FGGEAVFDNLLVF 4428
Cdd:cd19537 247 --EEDMETVGLFLEPLPIRIRFpsSSDASAADFLRAVRRssQA-AL---AHAiPWHQLLEHLGlppdSPNHPLFDVMVTF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4429 -ENYPVDEVLE-------RSSAGGVRFGavAMHEQTnyplALAlggGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAF 4500
Cdd:cd19537 321 hDDRGVSLALPipgveplYTWAEGAKFP--LMFEFT----ALS---DDSLLLRLEYDTDCFSEEEIDRIESLILAALELL 391
|
...
gi 2310915810 4501 AEH 4503
Cdd:cd19537 392 VEG 394
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
3181-3520 |
3.67e-16 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 83.32 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3181 NLAYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVvaaPGDH 3257
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAI 3335
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DvthwTCVEEGKDAVPI----GRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVASPFVager 3411
Cdd:cd17638 156 A----TMCRPGDDAETVattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESESGDWRE 3487
Cdd:cd17638 218 --HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgeVGkaFVVARPGVTLTEE 295
|
330 340 350
....*....|....*....|....*....|...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17638 296 DVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
519-950 |
3.74e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 85.42 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 519 EQVERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY- 595
Cdd:PLN02246 31 ERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYt 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 596 -PE-ERQAymlEDSGVQLLLSQSHL-----KLPLAQGVQRIDLDQADA-----WLENHAENN--PGIELNGENLAYVIYT 661
Cdd:PLN02246 111 pAEiAKQA---KASGAKLIITQSCYvdklkGLAEDDGVTVVTIDDPPEgclhfSELTQADENelPEVEISPDDVVALPYS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 662 SGSTGKPKGAGNRHSALSNrlCWMQQAYG------LGVGDTVLQKTP----FSFDvSVweFFWPLMSGARLVVAApgdHR 731
Cdd:PLN02246 188 SGTTGLPKGVMLTHKGLVT--SVAQQVDGenpnlyFHSDDVILCVLPmfhiYSLN-SV--LLCGLRVGAAILIMP---KF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 732 DPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEAAI 808
Cdd:PLN02246 260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKydLSSI-RMVLSGAApLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 809 DVThwTCVEEGKDTVPI-----GRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAG 882
Cdd:PLN02246 339 VLA--MCLAFAKEPFPVksgscGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATANT------IDK 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 883 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGRQLVGYVV 950
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPmkdeVAGEVPVAFVV 482
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
3185-3467 |
4.09e-16 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 83.09 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSalsNRLCWMQQ---AYGLGVGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDP 3260
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHG---NLIAANLQlihAMGLTEADVYLNMLPL-FHIAgLNLALATFHAGGANVVM---EKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLkRIVcSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT 3338
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNLLDaaEKSGVDLSSL-RHV-LGLDAPETIQR--FEETTGATFWSLYGQTETSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3339 HWTCVEEGKDAvpiGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvageR--MYRTG 3416
Cdd:cd17637 154 LSPYRERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWHHTG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQ--VKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGV 274
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
4546-5040 |
4.29e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 85.46 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALI--ARGVGPeVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDieyPR 4623
Cdd:PRK13388 10 RDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIalADPDRP-LHVGVLLGNTPEMLFWLAAAALGGYVLVGLN---TT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLPIPEGLScLSVDR-----EEEWAGF--PAHD--PEVALHGDNLAYVIYTSGSTGM 4694
Cdd:PRK13388 86 RRGAALAADIRRADCQLLVTDAEHRPLLDGLD-LPGVRvldvdTPAYAELvaAAGAltPHREVDAMDPFMLIFTSGTTGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4695 PKGVAVSHGPLIAHIVATGERYEMTPED-CELHFMSFAFDGSHEGWMHPLINGARVLIRDD---SLWLPertyaEMHRHG 4770
Cdd:PRK13388 165 PKAVRCSHGRLAFAGRALTERFGLTRDDvCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKfsaSGFLD-----DVRRYG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4771 VT----VGVfPPVYLQQLAEHAERDGNppPVRVyCFGGDAVA--QASYDLAWRAlkpkYLFNGYGPTETVVTPLLWKARA 4844
Cdd:PRK13388 240 ATyfnyVGK-PLAYILATPERPDDADN--PLRV-AFGNEASPrdIAEFSRRFGC----QVEDGYGSSEGAVIVVREPGTP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 GDACG------AAYMPIGTLLGNRSGYILDGQLnLLPVGVAGELY-LGGEGVARGYLERPALTAERFvpdpfgAPGsrLY 4917
Cdd:PRK13388 312 PGSIGrgapgvAIYNPETLTECAVARFDAHGAL-LNADEAIGELVnTAGAGFFEGYYNNPEATAERM------RHG--MY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSPEA 4996
Cdd:PRK13388 383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErVGDQVMAALVLRDGATFDPDAF 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2310915810 4997 QAECRAQlktalrERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK13388 463 AAFLAAQ------PDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
3052-3520 |
4.36e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGE--ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:PRK13390 11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEDSGVELLLSQSHLKLPLAQGVQ----RIDLDRGAPWFEDYSEAnpdIHLDGENL------AYVIYTSGSTGKPKGAg 3199
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKVGAdlplRLSFGGEIDGFGSFEAA---LAGAGPRLteqpcgAVMLYSSGTTGFPKGI- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 nrHSALSNRLcwMQQAyglgvGDTVLQKTPFSFDVSVWEFFWplmSGARLVVAAP----------------GDHRDPAKL 3263
Cdd:PRK13390 167 --QPDLPGRD--VDAP-----GDPIVAIARAFYDISESDIYY---SSAPIYHAAPlrwcsmvhalggtvvlAKRFDAQAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AI 3335
Cdd:PRK13390 235 LGHVERYRITVTQMVPTMFVRLLKlDADVRTrydVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAhgmtFI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTCvEEGKdavpIGRPIANlACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAE-RFVASPFVAgermyR 3414
Cdd:PRK13390 314 DSPDWLA-HPGS----VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWT-----T 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3415 TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---ESGDWRE 3487
Cdd:PRK13390 383 VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPdpemGEQVKAVIQLVEgirGSDELAR 462
|
490 500 510
....*....|....*....|....*....|...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:PRK13390 463 ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
526-940 |
4.44e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 85.46 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 526 TAPALAFGEERLDYAELNRRANRLAHALIERGIGADRL-VGVAMERSIEMVVALMAILKAGGAYVPVDPEypeERQAYML 604
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 ED---SGVQLLLS-QSHLKLpLA----QGVQRIDLDqADAWLE---NHAENNPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:PRK13388 93 ADirrADCQLLVTdAEHRPL-LDgldlPGVRVLDVD-TPAYAElvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVELINREGVDTLHFVP 752
Cdd:PRK13388 171 SHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALPA---KFSASGFLDDVRRYGATYFNYVG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 753 SMLQAFL----QDEDVAscTSLkRIVCSGEALPADaqQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDTVPIGRP 828
Cdd:PRK13388 248 KPLAYILatpeRPDDAD--NPL-RVAFGNEASPRD--IAEFSRRFGCQVEDGYGSSEGAVIVVR----EPGTPPGSIGRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 829 IGNLGCYILDGnLEPVPVGVL-------------GELY-LAGRGLARGYHQRPGLTAERFvaspfvageR--MYRTGDLA 892
Cdd:PRK13388 319 APGVAIYNPET-LTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAERM---------RhgMYWSGDLA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2310915810 893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK13388 389 YRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAV 436
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
653-998 |
4.85e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 86.13 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 653 ENLAYVIYTSGSTGKPKGAG-NRHSALSNrLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFwPLMSGARlVVAAPgD 729
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMlSHHNILSN-IEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWL-PLLEGIK-VVYHP-D 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 730 HRDPAKLVELINREGVDTLHFVPSMLQAFLQD-----EDVASctsLKRIVCSGEALP---ADAQQQVFAKLPQAGlynlY 801
Cdd:PRK08633 858 PTDALGIAKLVAKHRATILLGTPTFLRLYLRNkklhpLMFAS---LRLVVAGAEKLKpevADAFEEKFGIRILEG----Y 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 802 GPTE----AAIDVTHwtcVEEGKDTVPIGRPIGNLG-------CYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGL 869
Cdd:PRK08633 931 GATEtspvASVNLPD---VLAADFKRQTGSKEGSVGmplpgvaVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 870 TAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA--AVLAVD----GR 943
Cdd:PRK08633 1008 TAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVvfAVTAVPdekkGE 1084
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 944 QLVgyVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK08633 1085 KLV--VLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
4517-5034 |
5.00e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 85.39 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4517 AELSAIGAI-WnrSDSGYPATplVHQRVAERARMAPDAVAVIF--------DEEKLTYAELDSRANRLAHALIARGVGPE 4587
Cdd:PRK07529 8 ADIEAIEAVpL--AARDLPAS--TYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4588 VRVAIAMQRSAEIMVAFLA---------------------VLKAGGAYV-----PL---DIEYPRERLLYMMQDSRAHLL 4638
Cdd:PRK07529 84 DVVAFLLPNLPETHFALWGgeaagianpinpllepeqiaeLLRAAGAKVlvtlgPFpgtDIWQKVAEVLAALPELRTVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 LTHShllERLPIPEGLSCLSVDRE---------EEWAGFPA--HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIA 4707
Cdd:PRK07529 164 VDLA---RYLPGPKRLAVPLIRRKaharildfdAELARQPGdrLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4708 HIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLI------RDDSLWlpERTYAEMHRHGVT--VGVfPP 4778
Cdd:PRK07529 241 NAWLGALLLGLGPGDTVFCGLPlFHVNALLVTGLAPLARGAHVVLatpqgyRGPGVI--ANFWKIVERYRINflSGV-PT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 VYLQQLA-----------EHAERDGNPPPVRVYcfggdavaqasydlawRALKPKY---LFNGYGPTETvvtpllwkara 4844
Cdd:PRK07529 318 VYAALLQvpvdghdisslRYALCGAAPLPVEVF----------------RRFEAATgvrIVEGYGLTEA----------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 gdACGAAYMPIGTLL-----GNRSGY------ILDGQLNLL---PVGVAGELYLGGEGVARGYLE----RPALTAERFVp 4906
Cdd:PRK07529 371 --TCVSSVNPPDGERrigsvGLRLPYqrvrvvILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLEaahnKGLWLEDGWL- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 dpfgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVkIR-GFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVV 4984
Cdd:PRK07529 448 -----------NTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAhAGELPVAYVQ 515
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4985 AQEPAVADSPEAQAECRAQlktaLRERLPeymVPSHLLFLARMPLTPNGK 5034
Cdd:PRK07529 516 LKPGASATEAELLAFARDH----IAERAA---VPKHVRILDALPKTAVGK 558
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
530-943 |
5.45e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 84.42 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 530 LAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 609
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 610 QLLLSQshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCWMQQAY 689
Cdd:cd05914 81 KAIFVS-----------------------------------DEDDVALINYTSGTTGNSKGV-----MLTYRNIVSNVDG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 690 G-----LGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAApgdhRDPAKLVELINREGVDTLHFVPSMLQAflqdED 763
Cdd:cd05914 121 VkevvlLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPTLGVPVPLVI----EK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 764 VASCTSLKRIVCSGE----ALPADAQQ---QVF------------------AKLPQ---AGLYNL-------YGPTEAAI 808
Cdd:cd05914 193 IFKMDIIPKLTLKKFkfklAKKINNRKirkLAFkkvheafggnikefviggAKINPdveEFLRTIgfpytigYGMTETAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 809 DVTHWTCVEEGKDTVpiGRPIGNLGCYILDgnlePVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRT 888
Cdd:cd05914 273 IISYSPPNRIRLGSA--GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWFHT 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 889 GDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGR 943
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKK 396
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3631-4048 |
5.75e-16 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 84.23 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRLFFEQP-IPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHEtdGTWHAEHAEATLGGALL----WRAE 3705
Cdd:cd20483 9 RRLWFLHNfLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFE--GDDFGEQQVLDDPSFHLividLSEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3706 AVDRQALESLCEESQRS-LDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG----EAPR 3780
Cdd:cd20483 87 ADPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGrdlaTVPP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3781 LPGKTSPFKAWAgrvSEHARGESMKAQLQFWRELLEGAPAE---LPCEHPQGALEQRFATS-VQSRFDRSLTERlLKQAP 3856
Cdd:cd20483 167 PPVQYIDFTLWH---NALLQSPLVQPLLDFWKEKLEGIPDAsklLPFAKAERPPVKDYERStVEATLDKELLAR-MKRIC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3857 AAYRTQVNDLLLTALARVVCRWSGASSSLVQL----EGHGreelfadiDLSRTVGWFTSLFPVRL-----SPVADLGES- 3926
Cdd:cd20483 243 AQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMvdgdRPHP--------DFDDLVGFFVNMLPIRCrmdcdMSFDDLLESt 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3927 ----LKAIKEqlRAIPdkglgyglLRYLAGEESA-RVLAGLPQARITFNYL--GQF------DAQFDEMALLD--PAGES 3991
Cdd:cd20483 315 kttcLEAYEH--SAVP--------FDYIVDALDVpRSTSHFPIGQIAVNYQvhGKFpeydtgDFKFTDYDHYDipTACDI 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3992 A-GAEMDPgapldnwlslngrvfDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALV 4048
Cdd:cd20483 385 AlEAEEDP---------------DGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVI 427
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1554-1843 |
6.89e-16 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 83.39 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLFHSLHGTEGD-----YVNQLRMDIgglDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQAtle 1628
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSsfnvsFACRLSGDV---DRDRLASAWNTVLARHRILRSRYVPRDG--GLRRSYSSSP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1629 lrlappgsdPQRQ--------AEAEREagFDPARAPLQRlVLVPlangRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ 1700
Cdd:cd19537 75 ---------PRVQrvdtldvwKEINRP--FDLEREDPIR-VFIS----PDTLLVVMSHIICDLTTLQLLLREVSAAYNGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1701 EVAATVGRYRDYIGWLQgRDAMATEFFWRDRLA---SLEMPTRLARQARteqpgQGE-HLRELDPQTTRQLASFAQGQKV 1776
Cdd:cd19537 139 LLPPVRREYLDSTAWSR-PASPEDLDFWSEYLSglpLLNLPRRTSSKSY-----RGTsRVFQLPGSLYRSLLQFSTSSGI 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 1777 TLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLPV-IAAPQPQQ-SVADYLQ 1843
Cdd:cd19537 213 TLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGLFLEPLPIrIRFPSSSDaSAADFLR 279
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
2010-2476 |
7.62e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 84.03 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL 2089
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVG 2169
Cdd:cd05914 84 FVSDE-----------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2170 PGDCQLQFASIS------FDaaaeqLFVPLLAGA---------------------RVLLGDAGQWSAQHLA--DEVERHA 2220
Cdd:cd05914 129 KGDKILSILPLHhiypltFT-----LLLPLLNGAhvvfldkipsakiialafaqvTPTLGVPVPLVIEKIFkmDIIPKLT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2221 VTI----LDLPPAYLQqqaeeLRHAGRRIA-------VRTCILGGEAWDAslltqqavQAEAWFN--------AYGPTEA 2281
Cdd:cd05914 204 LKKfkfkLAKKINNRK-----IRKLAFKKVheafggnIKEFVIGGAKINP--------DVEEFLRtigfpytiGYGMTET 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 viTPLAWHCRAQEGGAPAIGRALGARRACILDaalqPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerl 2361
Cdd:cd05914 271 --APIISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2362 YRTGDLARYRVDGQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRG---- 2436
Cdd:cd05914 338 FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALkqrn 417
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 2437 --EDLLAELRTWLAGRLPAYMQPTAWQ-VLSSLPLNANGKLDR 2476
Cdd:cd05914 418 iiDAIKWEVRDKVNQKVPNYKKISKVKiVKEEFEKTPKGKIKR 460
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
4561-5040 |
7.96e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 84.51 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDieyPRERLLYMMQ---DSRAH 4636
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMN---PSSSLGEIKKrvvDCSVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4637 LLLTHSHLLERLPiPEGLSCLSV-------DREEEWAGFPA---HDPEVA----LHGDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:PLN02574 142 LAFTSPENVEKLS-PLGVPVIGVpenydfdSKRIEFPKFYElikEDFDFVpkpvIKQDDVAAIMYSSGTTGASKGVVLTH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAhIVATGERYEMTpedcelhfmSFAFDGSHEGWMHPL----INGARV----LIRDDSLWLPERTY--AEM----HR 4768
Cdd:PLN02574 221 RNLIA-MVELFVRFEAS---------QYEYPGSDNVYLAALpmfhIYGLSLfvvgLLSLGSTIVVMRRFdaSDMvkviDR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 HGVT-VGVFPPVyLQQLAEHAERDGNPP--PVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVV-------TPL 4838
Cdd:PLN02574 291 FKVThFPVVPPI-LMALTKKAKGVCGEVlkSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAvgtrgfnTEK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKaragdacgaaYMPIGTLLGNRSGYILDGQL-NLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:PLN02574 370 LSK----------YSSVGLLAPNMQAKVVDWSTgCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW-------L 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadsPEA 4996
Cdd:PLN02574 433 RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKeCGEIPVAFVVRR-------QGS 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2310915810 4997 QAECrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN02574 506 TLSQ-EAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
2010-2479 |
8.44e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 84.31 E-value: 8.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEH--LSYAELDMRAERLARGLRARGVVAEAL--------VAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAY 2079
Cdd:PRK13388 14 GDDTiaVRYGDRTWTWREVLAEAAARAAALIALadpdrplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2080 MLRDSGARWLIcqeTLAERLPCPA-----EVERLPLETAAWP----ASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAV 2150
Cdd:PRK13388 94 DIRRADCQLLV---TDAEHRPLLDgldlpGVRVLDVDTPAYAelvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2151 SQAALVAHCQAAARTYGVGPGD-CQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDL--- 2226
Cdd:PRK13388 171 SHGRLAFAGRALTERFGLTRDDvCYVSMPLFHSNAVMAGWAPAVASGAAVALPA--KFSASGFLDDVRRYGATYFNYvgk 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 PPAYLQQQAEE-------LRHAgrriavrtciLGGEAWD---ASLLTQQAVQAeawFNAYGPTEAVITPlawhcrAQEGG 2296
Cdd:PRK13388 249 PLAYILATPERpddadnpLRVA----------FGNEASPrdiAEFSRRFGCQV---EDGYGSSEGAVIV------VREPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 AP--AIGRalGARRACILDAA-LQPCAPGM-------------IGELY-IGGQCLARGYLGRPGQTAERFvadpfsgsge 2359
Cdd:PRK13388 310 TPpgSIGR--GAPGVAIYNPEtLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEATAERM---------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2360 R--LYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrG 2436
Cdd:PRK13388 378 RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVpDERVGDQVMAALVLRD---G 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2310915810 2437 EDLL-AELRTWLAGR--LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK13388 455 ATFDpDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
4547-5134 |
9.24e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 84.70 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVavifdeeklTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06060 24 AFYAADVV---------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPevaLHGDNLAYVIYTSGSTGMPKGVAVSHGPLI 4706
Cdd:PRK06060 95 ALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHADPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4707 AHIVATGER-YEMTPEDCELHF--MSFAFDGSHEGWMhPLINGARVLIrdDSLWLPERTYAEMHRH---GVTVGVfpPVY 4780
Cdd:PRK06060 172 TFVDAMCRKaLRLTPEDTGLCSarMYFAYGLGNSVWF-PLATGGSAVI--NSAPVTPEAAAILSARfgpSVLYGV--PNF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 LQQLAEHAERDgNPPPVRVYCFGGDAVAQAsydLAWRALK-----PkyLFNGYGPTE---TVVTPLLWKARAGDacgaay 4852
Cdd:PRK06060 247 FARVIDSCSPD-SFRSLRCVVSAGEALELG---LAERLMEffggiP--ILDGIGSTEvgqTFVSNRVDEWRLGT------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 mpIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERpaltaerfvPDPFGAPGSRLyRSGDLTRGRADGVVD 4932
Cdd:PRK06060 315 --LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWL-DTRDRVCIDSDGWVT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVaqePAVADSPEAQAecRAQLKTALRER 5011
Cdd:PRK06060 383 YRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGaSTLQAFLV---ATSGATIDGSV--MRDLHRGLLNR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL--------------------------PQPDASLLQQVYVAPRSDLEQQVAG 5065
Cdd:PRK06060 458 LSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsptkpiwelsltepgsgvraqrdDLSASNMTIAGGNDGGATLRERLVA 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5066 IWAEVLQL------------------QQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAA 5127
Cdd:PRK06060 538 LRQERQRLvvdavcaeaakmlgepdpWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEA 617
|
....*..
gi 2310915810 5128 QTSSNDT 5134
Cdd:PRK06060 618 ELAGGHG 624
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
2130-2482 |
1.53e-15 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 83.15 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLLGdAG 2205
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVVFH-PN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADEVERHAVTILDLPPAYLQQ-----QAEELRhagrriAVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPT 2279
Cdd:cd05909 223 PLDYKKIPELIYDKKATILLGTPTFLRGyaraaHPEDFS------SLRLVVAGAEKLKDTLRQEfQEKFGIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EAviTPLAWHCRAQEGGAP-AIGRALGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgs 2357
Cdd:cd05909 297 EC--SPVISVNTPQSPNKEgTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAH-PYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR 2435
Cdd:cd05909 367 GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRKGEKIVLLTTTTDTDP 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2310915810 2436 gEDLLAELRTwlAGrLPAYMQPTAWQVLSSLPLNANGKLDRKALPKV 2482
Cdd:cd05909 447 -SSLNDILKN--AG-ISNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
4674-5040 |
1.55e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 83.66 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4674 EVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeRYEMTP---EDCEL--------HFMSFAFdgsHEGWMHp 4742
Cdd:PRK05677 201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC--RALMGSnlnEGCEIliaplplyHIYAFTF---HCMAMM- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 LINGARVLI---RDdslwLPERTyAEMHRHGVT--VGVfPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLaWR 4817
Cdd:PRK05677 275 LIGNHNILIsnpRD----LPAMV-KELGKWKFSgfVGL-NTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAER-WK 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 ALKPKYLFNGYGPTET--VVTpllWKARAGDACGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:PRK05677 348 EVTGCAICEGYGMTETspVVS---VNPSQAIQVGTIGIPVpSTLCK-----VIDDDGNELPLGEVGELCVKGPQVMKGYW 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4895 ERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA 4974
Cdd:PRK05677 420 QRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4975 VGQQLVGYVVAQEPAVADSPEaqaecraQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK05677 493 KSGEAIKVFVVVKPGETLTKE-------QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
2012-2428 |
1.79e-15 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 83.29 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGAR---- 2087
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKalfv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2088 -----WLICQETLAERLP-CPAEVERLPLETAAWPASADTRPL----PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05932 85 gklddWKAMAPGVPEGLIsISLPPPSAANCQYQWDDLIAQHPPleerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2158 HCQAAARTYGVGPGDCQLQFASISFdaAAEQLFV---PLLAGARVLLGDagqwSAQHLADEVERHAVTIL---------- 2224
Cdd:cd05932 165 AAQAGIEHIGTEENDRMLSYLPLAH--VTERVFVeggSLYGGVLVAFAE----SLDTFVEDVQRARPTLFfsvprlwtkf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 ------DLPPAYLQQQAeELRHAGRriAVRTCILGGEAWDAS--LLTQQAVQAEA---WFN--------AYGPTEA-VIT 2284
Cdd:cd05932 239 qqgvqdKIPQQKLNLLL-KIPVVNS--LVKRKVLKGLGLDQCrlAGCGSAPVPPAlleWYRslglnileAYGMTENfAYS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 PLAWHCRAQEGgapAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRT 2364
Cdd:cd05932 316 HLNYPGRDKIG---TVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF-------LRT 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2365 GDLARYRVDGQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYVaEAAVVALDGVGGPLLAAYL 2428
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPAPLALVVL 439
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
4685-5037 |
2.14e-15 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 81.15 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIA---HIVATGEryEMTPEDCELHFMSFAFDGShEGWMHPLI--NGARVLIRDDSLWlp 4759
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAvpdILQKEGL--NWVVGDVTYLPLPATHIGG-LWWILTCLihGGLCVTGGENTTY-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4760 ERTYAEMHRHGVTVGVFPPVYLQQLA-EHAERDGNPPPVRVYCFGGDAVAQASYDLAwRALKPKYLFNGYGPTETVVTPL 4838
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVsELKSANATVPSLRLIGYGGSRAIAADVRFI-EATGLTNTAQVYGLSETGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyR 4918
Cdd:cd17635 160 LPTDDDSIEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------N 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4919 SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVG-YVVAQEpaVADSPEAQ 4997
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGlAVVASA--ELDENAIR 305
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2310915810 4998 AecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17635 306 A-----LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
658-940 |
2.22e-15 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 81.16 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 658 VIYTSGSTGKPKGAGNRHSalsNRLCWMQQ---AYGLGVGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDP 733
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHG---NLIAANLQlihAMGLTEADVYLNMLPL-FHIAgLNLALATFHAGGANVVM---EKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 734 AKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLkRIVcSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT 811
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNLLDaaEKSGVDLSSL-RHV-LGLDAPETIQR--FEETTGATFWSLYGQTETSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 812 HWTCVEEGKDTvpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvageR--MYRTG 889
Cdd:cd17637 154 LSPYRERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWHHTG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 890 DLARYRADGVIEYAGRIDHQ--VKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGV 274
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1581-1847 |
3.43e-15 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 81.77 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1581 DIGGLDPDRFRAAWQATLDAHEILRSGFLwKDGWPQPLQVVFEQ--ATLELRLAPPgSDPQRQAEAEREA----GFDPAR 1654
Cdd:cd19535 33 DGEDLDPDRLERAWNKLIARHPMLRAVFL-DDGTQQILPEVPWYgiTVHDLRGLSE-EEAEAALEELRERlshrVLDVER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1655 APLQRLVLVPLANGRMHLiytyhHI-----LMDGWSNAQLLAEVLQRYAGQEVA-ATVG-RYRDYIGWLQGRDAMATEF- 1726
Cdd:cd19535 111 GPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPGEPlPPLElSFRDYLLAEQALRETAYERa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1727 --FWRDRLASL----EMPtrLARQ-ARTEQPGQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETV 1799
Cdd:cd19535 186 raYWQERLPTLppapQLP--LAKDpEEIKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRF 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2310915810 1800 AFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQA 1847
Cdd:cd19535 264 LLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQ 311
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
4673-5040 |
3.71e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 82.41 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 PEVAlhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI----------VATGERYEMTPedCELHFMsFAFDGSHEGWMHp 4742
Cdd:PRK08974 201 PELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakaaygplLHPGKELVVTA--LPLYHI-FALTVNCLLFIE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 lINGARVLI---RDdslwLPErTYAEMHRHGVTV--GV---FPPvyLQQLAEHAERDGNPppVRVYCFGGDAVAQASYDl 4814
Cdd:PRK08974 275 -LGGQNLLItnpRD----IPG-FVKELKKYPFTAitGVntlFNA--LLNNEEFQELDFSS--LKLSVGGGMAVQQAVAE- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4815 AWRALKPKYLFNGYGPTETvvTPLLwkaragdAC---------GAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLG 4885
Cdd:PRK08974 344 RWVKLTGQYLLEGYGLTEC--SPLV-------SVnpydldyysGS----IGLPVPSTEIKLVDDDGNEVPPGEPGELWVK 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4886 GEGVARGYLERPALTAErFVPDPFGApgsrlyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4965
Cdd:PRK08974 411 GPQVMLGYWQRPEATDE-VIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4966 AVVVAQPGAVGQQLVG-YVVAQEPAVAdspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08974 483 VAAVGVPSEVSGEAVKiFVVKKDPSLT---------EEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
4555-5043 |
3.87e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 82.05 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4555 AVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSR 4634
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4635 AHLLLTHSHLLERLP--IPEGLSCLSVDREEE--------------------WAGF-PAHDPEVALHGDNLAYVIYTSGS 4691
Cdd:PRK12406 84 ARVLIAHADLLHGLAsaLPAGVTVLSVPTPPEiaaayrispalltppagaidWEGWlAQQEPYDGPPVPQPQSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGV---------AVSHGPLIAHI---------VATGERYEMTPEdcelhfmsfAFdgsheGWMHPLINGARVLI-R 4752
Cdd:PRK12406 164 TGHPKGVrraaptpeqAAAAEQMRALIyglkpgiraLLTGPLYHSAPN---------AY-----GLRAGRLGGVLVLQpR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4753 DDslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHaerdgnPPPVRvycfggdavaqASYDLA----------------- 4815
Cdd:PRK12406 230 FD----PEELLQLIERHRITHMHMVPTMFIRLLKL------PEEVR-----------AKYDVSslrhvihaaapcpadvk 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4816 ------WRALKPKYlfngYGPTE----TVVTPLLWKARAGD----ACGAAYMPIGTllgnrsgyilDGqlNLLPVGVAGE 4881
Cdd:PRK12406 289 ramiewWGPVIYEY----YGSTEsgavTFATSEDALSHPGTvgkaAPGAELRFVDE----------DG--RPLPQGEIGE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4882 LYLGGEGVAR-GYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH 4960
Cdd:PRK12406 353 IYSRIAGNPDfTYHNKPEKRAE--------IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4961 PAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADspeaQAECRAQLKtalrERLPEYMVPSHLLFLARMPLTPNGKLDRKG 5039
Cdd:PRK12406 425 PGVHDCAVFGIPDAeFGEALMAVVEPQPGATLD----EADIRAQLK----ARLAGYKVPKHIEIMAELPREDSGKIFKRR 496
|
....
gi 2310915810 5040 LPQP 5043
Cdd:PRK12406 497 LRDP 500
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
2585-2945 |
4.11e-15 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 81.33 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHV--RGVLDQ--AALQQAFDwlvlRHETLRTRF--EEVDgQARQTIL--ANM 2656
Cdd:cd19544 3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFdsRARLDAflAALQQVID----RHDILRTAIlwEGLS-EPVQVVWrqAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2657 PLRIVLEDCAGASEATLRQRVAEEiRQPFDLARGP-LLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDElLQAYAAA 2735
Cdd:cd19544 78 PVEELTLDPGDDALAQLRARFDPR-RYRLDLRQAPlLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEE-IQAILAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2736 RRGEQPTLAPlklqYADYAAwhRAWLDSGEGARQlDYWRERLGA-EQPVleLPADrVRPAQASGRG-QRLDMALPVPLSE 2813
Cdd:cd19544 156 RAAALPPPVP----YRNFVA--QARLGASQAEHE-AFFREMLGDvDEPT--APFG-LLDVQGDGSDiTEARLALDAELAQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2814 ELLACARREGVTPFMLLLASFQVLLKRYSGQSDI--------RVGvpianrNRAEVERLIGFFVNTQVLRCQVDAglafr 2885
Cdd:cd19544 226 RLRAQARRLGVSPASLFHLAWALVLARCSGRDDVvfgtvlsgRMQ------GGAGADRALGMFINTLPLRVRLGG----- 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2886 dllGRVREAAlgAQAHQDL----PFEQ--LVDALQpernlsHS------PLFQVM--YNHQSGERQDAQVDGLH 2945
Cdd:cd19544 295 ---RSVREAV--RQTHARLaellRHEHasLALAQR------CSgvpaptPLFSALlnYRHSAAAAAAAALAAWE 357
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
525-940 |
4.12e-15 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 81.85 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPAL-AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:PRK07514 16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 604 LEDSGVQLLLSQSHL-----KLPLAQGVQRI---DLDQADAWLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAG 672
Cdd:PRK07514 96 IGDAEPALVVCDPANfawlsKIAAAAGAPHVetlDADGTGSLLEAAAAAPDDFETvprGADDLAAILYTSGTTGRSKGAM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 673 NRHSAL-SNRLCwMQQAYGLGVGDTVLQKTPF--------SFDVSvweffwpLMSGARLVVAApgdHRDPAKLVELINRE 743
Cdd:PRK07514 176 LSHGNLlSNALT-LVDYWRFTPDDVLIHALPIfhthglfvATNVA-------LLAGASMIFLP---KFDPDAVLALMPRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 744 GVdtLHFVPSMLQAFLQDEDV-ASCTSLKRIVCSGEA-LPADAQQQVFAKLPQAGLyNLYGPTEAAIDVTHWTCVEEGKD 821
Cdd:PRK07514 245 TV--MMGVPTFYTRLLQEPRLtREAAAHMRLFISGSApLLAETHREFQERTGHAIL-ERYGMTETNMNTSNPYDGERRAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 822 TVpiGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVI 900
Cdd:PRK07514 322 TV--GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2310915810 901 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK07514 394 HIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
4952-5034 |
4.44e-15 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 72.96 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4952 EIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLT 5030
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELkGEAPVAFVVLKPGVELL--------EEELVAHVREELGPYAVPKEVVFVDELPKT 72
|
....
gi 2310915810 5031 PNGK 5034
Cdd:pfam13193 73 RSGK 76
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
4542-5040 |
5.11e-15 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 82.36 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4542 RVAERARmaPDAVAVIFD------EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG---- 4611
Cdd:cd05967 58 RHVEAGR--GDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihs 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 ---GAYVP----LDIEYPRERLL----YMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREE------------EWAGF 4668
Cdd:cd05967 136 vvfGGFAAkelaSRIDDAKPKLIvtasCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQvpadltkpgrdlDWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4669 PA----HDPeVALHGDNLAYVIYTSGSTGMPKGVAVSHGpliAHIVATgeRYEM-TPEDCelHFMSFAFDGSHEGWM--H 4741
Cdd:cd05967 216 LAkaepVDC-VPVAATDPLYILYTSGTTGKPKGVVRDNG---GHAVAL--NWSMrNIYGI--KPGDVWWAASDVGWVvgH 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4742 ------PLINGARVLIRDDslwLPERT------YAEMHRHGVTvGVF--PPVY--LQQLAEHAE--RDGNPPPVRVYCFG 4803
Cdd:cd05967 288 syivygPLLHGATTVLYEG---KPVGTpdpgafWRVIEKYQVN-ALFtaPTAIraIRKEDPDGKyiKKYDLSSLRTLFLA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4804 GDAVAQASYDLAWRALKpKYLFNGYGPTETVvtpllWkARAGDACGAAYMPIGTLLGNRS--GY---ILDGQLNLLPVGV 4878
Cdd:cd05967 364 GERLDPPTLEWAENTLG-VPVIDHWWQTETG-----W-PITANPVGLEPLPIKAGSPGKPvpGYqvqVLDEDGEPVGPNE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4879 AGELYLGGEgVARGYLERPALTAERFVPDPFGA-PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARL 4957
Cdd:cd05967 437 LGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSKfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4958 REHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd05967 514 LSHPAVAECAVVGVRDELkGQVPLGLVVLKEGVKITAEELEKELVAL----VREQIGPVAAFRLVIFVKRLPKTRSGKIL 589
|
....
gi 2310915810 5037 RKGL 5040
Cdd:cd05967 590 RRTL 593
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
3053-3467 |
5.32e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 82.00 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3053 TAPALAFGEERLDYAELNRRANRLAHALIERGVGADRL-VGVAMERSIEMVVALMAILKAGGAYVPVDPEypeERQAYML 3131
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 ED---SGVELLLS-QSHLKLpLA----QGVQRIDLDrGAPWFE---DYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:PRK13388 93 ADirrADCQLLVTdAEHRPL-LDgldlPGVRVLDVD-TPAYAElvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVaapgdhrdPAKLVAL-----INREGVDT 3274
Cdd:PRK13388 171 SHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVAL--------PAKFSASgflddVRRYGATY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3275 LHFVPSMLQAFL----QDEDVAscTSLkRIVCSGEALPADaqQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAV 3350
Cdd:PRK13388 243 FNYVGKPLAYILatpeRPDDAD--NPL-RVAFGNEASPRD--IAEFSRRFGCQVEDGYGSSEGAVIVVR----EPGTPPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3351 PIGRPIANLACYILDGnLEPVPVGVL-------------GELY-LAGQGLARGYHQRPGLTAERFvaspfvageR--MYR 3414
Cdd:PRK13388 314 SIGRGAPGVAIYNPET-LTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAERM---------RhgMYW 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3415 TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK13388 384 SGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAV 436
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
4534-5035 |
5.57e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.92 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLvhqRVAER-ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:PRK08162 17 PLTPL---SFLERaAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLT----HSHLLERLPIPEGLSCLSVD------------REEEWAGFPAH-DPEV 4675
Cdd:PRK08162 94 VLNTLNTRLDAASIAFMLRHGEAKVLIVdtefAEVAREALALLPGPKPLVIDvddpeypggrfiGALDYEAFLASgDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4676 ALHG-----DNLAyVIYTSGSTGMPKGVAVSH-GPL---IAHIVATGeryeMTPEDCELHFMSFaFdgsH-EGWMHP--- 4742
Cdd:PRK08162 174 AWTLpadewDAIA-LNYTSGTTGNPKGVVYHHrGAYlnaLSNILAWG----MPKHPVYLWTLPM-F---HcNGWCFPwtv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 -LINGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQL--AEHAERDGNPPPVRVYCFGG-------DAVAQASY 4812
Cdd:PRK08162 245 aARAGTNVCLRKVD---PKLIFDLIREHGVTHYCGAPIVLSALinAPAEWRAGIDHPVHAMVAGAappaaviAKMEEIGF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4813 DLAwralkpkylfNGYGPTETV--VTPLLWKARAGDacgaayMPIG--TLLGNRSG--YILDGQLNLL------PVG--- 4877
Cdd:PRK08162 322 DLT----------HVYGLTETYgpATVCAWQPEWDA------LPLDerAQLKARQGvrYPLQEGVTVLdpdtmqPVPadg 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4878 -VAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrLYRSGDLTRGRADGVVdylgrvdhQVKIR--------GFRI 4948
Cdd:PRK08162 386 eTIGEIMFRGNIVMKGYLKNPKATEEAF------AGG--WFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPSHLLFlARM 5027
Cdd:PRK08162 450 SSIEVEDVLYRHPAVLVAAVVAKPDPKwGEVPCAFVELKDGASATEEEIIAHC--------REHLAGFKVPKAVVF-GEL 520
|
....*...
gi 2310915810 5028 PLTPNGKL 5035
Cdd:PRK08162 521 PKTSTGKI 528
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3028-3525 |
6.23e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 81.56 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3028 NATAAEYPLQRGvhRLFEEQVERTPTAPALAFgeerlDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMA 3107
Cdd:PLN02330 27 KLTLPDFVLQDA--ELYADKVAFVEAVTGKAV-----TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 ILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS-------HLKLPL--------AQGVQRIDLDRGAPWFEDYSeAN 3172
Cdd:PLN02330 100 IMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygkvkGLGLPVivlgeekiEGAVNWKELLEAADRAGDTS-DN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 PDIHldGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCwmQQAYGLG---VGD-TVLQKTPFsFDVS--VWEFFWPLMSG 3246
Cdd:PLN02330 179 EEIL--QTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGpemIGQvVTLGLIPF-FHIYgiTGICCATLRNK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVAAPGDHRdpAKLVALINREgVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQA 3322
Cdd:PLN02330 254 GKVVVMSRFELR--TFLNALITQE-VSFAPIVPPIILNLVKNPIVEefdlSKLKLQAIMTAAAPLAPELLTAFEAKFPGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3323 GLYNLYGPTE-AAIDVTHWTcVEEGKDAV---PIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLT 3397
Cdd:PLN02330 331 QVQEAYGLTEhSCITLTHGD-PEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEET 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3398 AERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLV 3473
Cdd:PLN02330 410 DRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPdeeaGEIPA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3474 GYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PLN02330 484 ACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
2138-2421 |
6.66e-15 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 80.58 E-value: 6.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQ------AALVAHCQAAArtyGVGPGD-CQLQF------ASISFDAAAEQLfvpllaGARVLLGDA 2204
Cdd:COG1541 91 SSGTTGKPTVVGYTRkdldrwAELFARSLRAA---GVRPGDrVQNAFgyglftGGLGLHYGAERL------GATVIPAGG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQwsaqhladeVERHAVTILDLP-------PAYLQQQAEELRHAG---RRIAVRTCILGGEAWDASLltQQAVqAEAW-- 2272
Cdd:COG1541 162 GN---------TERQLRLMQDFGptvlvgtPSYLLYLAEVAEEEGidpRDLSLKKGIFGGEPWSEEM--RKEI-EERWgi 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 --FNAYGPTEavITP-LAWHCRAQEGgapaigraL----GARRACILD-AALQPCAPGMIGELYI-----GGQCLARgyl 2339
Cdd:COG1541 230 kaYDIYGLTE--VGPgVAYECEAQDG--------LhiweDHFLVEIIDpETGEPVPEGEEGELVVttltkEAMPLIR--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2340 grpgqtaerfvadpfsgsgerlYRTGDLARY------------RVDGqveYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:COG1541 297 ----------------------YRTGDLTRLlpepcpcgrthpRIGR---ILGRADDMLIIRGVNVFPSQIEEVLLRIPE 351
|
330
....*....|....
gi 2310915810 2408 VAEAAVVALDGVGG 2421
Cdd:COG1541 352 VGPEYQIVVDREGG 365
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
522-939 |
6.91e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.53 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 522 ERT----PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVAL----MA------------- 580
Cdd:PRK08162 25 ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHfgvpMAgavlntlntrlda 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 581 -----ILKAGGAYV-PVDPEYPEERQAYMLEDSGVQLLLsqSHLKLPLAQGVQRIDLDQADAWLenhAENNPG------- 647
Cdd:PRK08162 105 asiafMLRHGEAKVlIVDTEFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIGALDYEAFL---ASGDPDfawtlpa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 648 -----IELNgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPlm 717
Cdd:PRK08162 180 dewdaIALN--------YTSGTTGNPKGVVYHHrgaylNALSNILAW-----GMPKHPVYLWTLPM-FHCNGWCFPWT-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 718 sgarlVVAAPGDH---R--DPAKLVELINREGVDtlHF-----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQ 787
Cdd:PRK08162 244 -----VAARAGTNvclRkvDPKLIFDLIREHGVT--HYcgapiVLSAL-INAPAEWRAGIDHPVHAMVAGAAPPA----A 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 788 VFAKLPQAG--LYNLYGPTE----AAIdvthwtCVE-EGKDTVPI----------GRPIGNL-GCYILDGN-LEPVPVG- 847
Cdd:PRK08162 312 VIAKMEEIGfdLTHVYGLTEtygpATV------CAWqPEWDALPLderaqlkarqGVRYPLQeGVTVLDPDtMQPVPADg 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 848 -VLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 926
Cdd:PRK08162 386 eTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
490
....*....|...
gi 2310915810 927 LEHPWVREAAVLA 939
Cdd:PRK08162 459 YRHPAVLVAAVVA 471
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
539-940 |
7.26e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 81.27 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:PRK08008 40 YLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 619 kLPLAQGVQR----------------------IDLDQADAwlENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:PRK08008 120 -YPMYRQIQQedatplrhicltrvalpaddgvSSFTQLKA--QQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 677 ALsnRLCWMQQAY--GLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVelinREGVDTL-HFVP 752
Cdd:PRK08008 197 NL--RFAGYYSAWqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQV----CKYRATItECIP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 753 SMLQAFLqdedVASCTSLKRIVCSGEAL----PADAQQQVFAKLPQAGLYNLYGPTEAAI--------DVTHWTcveegk 820
Cdd:PRK08008 271 MMIRTLM----VQPPSANDRQHCLREVMfylnLSDQEKDAFEERFGVRLLTSYGMTETIVgiigdrpgDKRRWP------ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 821 dtvPIGRPignlG-CY---ILDGNLEPVPVGVLGELYL---AGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLAR 893
Cdd:PRK08008 341 ---SIGRP----GfCYeaeIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEADGWL------HTGDTGY 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2310915810 894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK08008 408 VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
4563-5040 |
7.57e-15 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 80.88 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05929 18 LLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCGLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLPIPEGLsclsvDREEEWAGFPAHDPEVAlhGDnlaYVIYTSGSTGMPKGV--AVSHGPL-IAHIVATGERYEMT 4719
Cdd:cd05929 98 TGGGALDGLEDY-----EAAEGGSPETPIEDEAA--GW---KMLYSGGTTGRPKGIkrGLPGGPPdNDTLMAAALGFGPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4720 PEDCELHFMSFAFDGSHEGWMHPLINGARVLI--RDDslwlPERTYAEMHRHGVTVGVFPPVYLQQLA--EHAERDG-NP 4794
Cdd:cd05929 168 ADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLmeKFD----PEEFLRLIERYRVTFAQFVPTMFVRLLklPEAVRNAyDL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGdAVAQASYDLAWRALKPKYLFNGYGPTE----TVVTPLLWKARAGDacgaaympIGTLLGNRSgYILDGQ 4870
Cdd:cd05929 244 SSLKRVIHAA-APCPPWVKEQWIDWGGPIIWEYYGGTEgqglTIINGEEWLTHPGS--------VGRAVLGKV-HILDED 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4871 LNLLPVGVAGELYLGGeGVARGYLERPALTAERFVPDPFgapgsrlyRS-GDLTRGRADGVVDYLGRVDHQVKIRGFRIE 4949
Cdd:cd05929 314 GNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGW--------STlGDVGYLDEDGYLYLTDRRSDMIISGGVNIY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4950 LGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVvaqEPavADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMP 5028
Cdd:cd05929 385 PQEIENALIAHPKVLDAAVVGVPDEeLGQRVHAVV---QP--APGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELP 459
|
490
....*....|..
gi 2310915810 5029 LTPNGKLDRKGL 5040
Cdd:cd05929 460 RDDTGKLYRRLL 471
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
2015-2494 |
8.53e-15 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 80.94 E-value: 8.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLR-ARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD- 2172
Cdd:cd05937 87 ------------------------------------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDr 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2173 ---CQLQFASISFDAAAEQLfvpLLAGARVLLGDagQWSAQHLADEVERHAVTILdlppAYLQQQAEELRHA-----GRR 2244
Cdd:cd05937 131 tytCMPLYHGTAAFLGACNC---LMSGGTLALSR--KFSASQFWKDVRDSGATII----QYVGELCRYLLSTppspyDRD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2245 IAVRtCILG----GEAWDAsllTQQAVQAEAWFNAYGPTEAVITplAWHCRAQEGGAPAIGRAlGARRACILDAALQPCA 2320
Cdd:cd05937 202 HKVR-VAWGnglrPDIWER---FRERFNVPEIGEFYAATEGVFA--LTNHNVGDFGAGAIGHH-GLIRRWKFENQVVLVK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2321 ------------------------PG-MIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQ 2375
Cdd:cd05937 275 mdpetddpirdpktgfcvrapvgePGeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFR-KGDIYFRTGDLLRQDADGR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2376 VEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-----DGVGGpLLAAYLVGRDAMRGEDLLAELRTWLAGR 2450
Cdd:cd05937 354 WYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGRAG-CAAITLEESSAVPTEFTKSLLASLARKN 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2310915810 2451 LPAYMQPTAWQVLSSLPLNANGKLDRKALpkvdaaarRQAGEPP 2494
Cdd:cd05937 433 LPSYAVPLFLRLTEEVATTDNHKQQKGVL--------RDEGVDP 468
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
654-993 |
1.01e-14 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 654 NLAYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVvaaPGDH 730
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 731 RDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAI 808
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 809 DvthwTCVEEGKDTVPI----GRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVASPFVager 884
Cdd:cd17638 156 A----TMCRPGDDAETVattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 885 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESEGGDWRE 960
Cdd:cd17638 218 --HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgeVGkaFVVARPGVTLTEE 295
|
330 340 350
....*....|....*....|....*....|...
gi 2310915810 961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17638 296 DVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
4681-5037 |
1.11e-14 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 78.60 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIrdDSLWLPE 4760
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG--QRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4761 RTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGnppPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTET-VVTPLL 4839
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQALARTLEPES---KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELsFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4840 WK--ARAGDacgaaympIGTLLGNRSGYILDGQlnllpVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgapgsrlY 4917
Cdd:cd17633 156 NQesRPPNS--------VGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------M 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVadspeaq 4997
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLT------- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2310915810 4998 aecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17633 284 ---YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1092-1400 |
1.21e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 81.63 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1092 GPASGEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAG 1169
Cdd:PRK10252 2 EPMSQHLPLVAAQPgiWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1170 EPLW-----RRQAGSEEALLALCE-EAQRSLDLEQG-PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYA 1242
Cdd:PRK10252 82 FPLPeiidlRTQPDPHAAAQALMQaDLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1243 DLDADLGPRSSSYQTWSRHLHEQAGARLDEL-----DYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQ 1315
Cdd:PRK10252 162 AWLRGEPTPASPFTPFADVVEEYQRYRASEAwqrdaAFWAEQRRQLPPPasLSPAPLPGRSASADILRLKLEFTDGAFRQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1316 LLQEAPAAYRTqvnDLLLTALARATCRWSGDASVLVQLEGHGRedLGEAIdlSRTVGWFTSLFP--VRLTPAADLGESLK 1393
Cdd:PRK10252 242 LAAQASGVQRP---DLALALVALWLGRLCGRMDYAAGFIFMRR--LGSAA--LTATGPVLNVLPlrVHIAAQETLPELAT 314
|
....*..
gi 2310915810 1394 AIKEQLR 1400
Cdd:PRK10252 315 RLAAQLK 321
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3046-3525 |
1.33e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 80.44 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3046 EQVERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK05857 22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EE---------RQAYML--EDSGVElllSQSHLKLPLAQGVQRIDLDRGAPWFE-----DYSEANPDIHLDgENLAyVIY 3187
Cdd:PRK05857 102 IAaierfcqitDPAAALvaPGSKMA---SSAVPEALHSIPVIAVDIAAVTRESEhsldaASLAGNADQGSE-DPLA-MIF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAgnrhsALSNRLCW----MQQAYGLG-----VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHr 3258
Cdd:PRK05857 177 TSGTTGEPKAV-----LLANRTFFavpdILQKEGLNwvtwvVGETTYSPLPATHIGGLWWILTCLMHGGLCVTG--GEN- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 dPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSG-EALPADAQ---------QQVFAkLPQAGLYN 3326
Cdd:PRK05857 249 -TTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGsRAIAADVRfieatgvrtAQVYG-LSETGCTA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3327 LYGPTeaaiDVTHWTCVEEGKdavpIGRPIANLACYILDGN------LEPVPVGVLGELYLAGQGLARGYHQRPGLTAEr 3400
Cdd:PRK05857 327 LCLPT----DDGSIVKIEAGA----VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3401 fvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH-PWVREAAVLAVDGRQ---LVGYV 3476
Cdd:PRK05857 398 ------VLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVREAACYEIPDEEfgaLVGLA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3477 VL------ESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK05857 471 VVasaeldESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
2012-2479 |
1.61e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 80.60 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRAR-GVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CQETLAERL-------PC--------------PAEVERLPLETAAWPASADTRPL----PEVAGETLAYVIYTSGSTGQP 2145
Cdd:PRK05620 117 ADPRLAEQLgeilkecPCvravvfigpsdadsAAAHMPEGIKVYSYEALLDGRSTvydwPELDETTAAAICYSTGTTGAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2146 KGVAVSQAALVAHCQA--AARTYGVGPGD----CQLQFASISFDaaaeqlfVPL---LAGARVLLGDAgQWSAQHLADEV 2216
Cdd:PRK05620 197 KGVVYSHRSLYLQSLSlrTTDSLAVTHGEsflcCVPIYHVLSWG-------VPLaafMSGTPLVFPGP-DLSAPTLAKII 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ER------HAVtildlPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTqqavqaeAWFNAYG------------- 2277
Cdd:PRK05620 269 ATamprvaHGV-----PTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIK-------AWEERYGvdvvhvwgmtets 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2278 PTEAVITPLA-------WHCRAQEGGAPAI--------GRALGA--RRAcildaalqpcapgmiGELYIGGQCLARGYLG 2340
Cdd:PRK05620 337 PVGTVARPPSgvsgearWAYRVSQGRFPASleyrivndGQVMEStdRNE---------------GEIQVRGNWVTASYYH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQT----AERFVADPFSGSGERL-----YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK05620 402 SPTEEgggaASTFRGEDVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVEC 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2412 AVVAL--DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK05620 482 AVIGYpdDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
2006-2479 |
1.66e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 80.11 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEHLSYAELDMRAERLARGLRAR---------GVVAEAlvaiAAERSFDLVVGLLGilkagaGYLPLDPNyPAER 2076
Cdd:PRK07867 21 GLYFEDSFTSWREHIRGSAARAAALRARldptrpphvGVLLDN----TPEFSLLLGAAALS------GIVPVGLN-PTRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2077 LAYMLRDsgARWLICQETLAERL------PCPAEVERLPLETAAW----PASADTRPLPEVAG-ETLAYVIYTSGSTGQP 2145
Cdd:PRK07867 90 GAALARD--IAHADCQLVLTESAhaelldGLDPGVRVINVDSPAWadelAAHRDAEPPFRVADpDDLFMLIFTSGTSGDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2146 KGVAVSQAALVAHCQAAARTYGVGPGD-CQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTIL 2224
Cdd:PRK07867 168 KAVRCTHRKVASAGVMLAQRFGLGPDDvCYVSMPLFHSNAVMAGWAVALAAGASIAL--RRKFSASGFLPDVRRYGATYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DL---PPAYLQQQAEEL--RHAGRRIAvrtciLGGEAWDASLLTQQAVQAEAWFNAYGPTE--AVITplawhcRAQEGGA 2297
Cdd:PRK07867 246 NYvgkPLSYVLATPERPddADNPLRIV-----YGNEGAPGDIARFARRFGCVVVDGFGSTEggVAIT------RTPDTPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2298 PAIGRALGARRacILDAA-LQPCAPG------------MIGELY-IGGQCLARGYLGRPGQTAERFVadpfsgsgERLYR 2363
Cdd:PRK07867 315 GALGPLPPGVA--IVDPDtGTECPPAedadgrllnadeAIGELVnTAGPGGFEGYYNDPEADAERMR--------GGVYW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2364 TGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAE 2442
Cdd:PRK07867 385 SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVpDPVVGDQVMAALVLAP---GAKFDPD 461
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2310915810 2443 -LRTWLAGR--LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07867 462 aFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
4528-5040 |
2.04e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 80.27 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4528 RSDSGYPA-TPLVhqrVAERARMA-PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PLN02479 12 KNAANYTAlTPLW---FLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4606 AVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHShllERLPIPEG-LSCLSVDREEEW-------AGFPAHDP---E 4674
Cdd:PLN02479 89 GVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQ---EFFTLAEEaLKILAEKKKSSFkppllivIGDPTCDPkslQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 VALHGDNLAY------------------------VIYTSGSTGMPKGVAVSH---------GPLIAHiVATGERYEMTpe 4721
Cdd:PLN02479 166 YALGKGAIEYekfletgdpefawkppadewqsiaLGYTSGTTASPKGVVLHHrgaylmalsNALIWG-MNEGAVYLWT-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4722 dcelhFMSFAFDGSHEGWMHPLINGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQLAEH-AERDGNPPPVRVY 4800
Cdd:PLN02479 243 -----LPMFHCNGWCFTWTLAALCGTNICLRQVT---AKAIYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGDAVAQASY-----DLAWRALKPKYLFNGYGPTeTVVT--------PLLWKARAGDACGAAYMPIGTLlgnrsgYIL 4867
Cdd:PLN02479 315 VMTAGAAPPPSVlfamsEKGFRVTHTYGLSETYGPS-TVCAwkpewdslPPEEQARLNARQGVRYIGLEGL------DVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4868 DGQlNLLPV----GVAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:PLN02479 388 DTK-TMKPVpadgKTMGEIVMRGNMVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIIS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4944 RGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcrAQLKTALRERLPEYMVPSHLLF 5023
Cdd:PLN02479 459 GGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALA--EDIMKFCRERLPAYWVPKSVVF 536
|
570
....*....|....*..
gi 2310915810 5024 lARMPLTPNGKLDRKGL 5040
Cdd:PLN02479 537 -GPLPKTATGKIQKHVL 552
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
2012-2476 |
2.14e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 80.05 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD-PNYPAERLAY------MLRDS 2084
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2085 GARWLICQETLAERLPcpAEVERLPLETAAWPASADTRP-----LPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC 2159
Cdd:PRK09192 128 QPAAIITPDELLPWVN--EATHGNPLLHVLSHAWFKALPeadvaLPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2160 QAAAR-TYGVGPGD-----------------------CQLqfasiSFDAAAEQLFV--PLlagarvllgdagQWsaqhlA 2213
Cdd:PRK09192 206 RAISHdGLKVRPGDrcvswlpfyhdmglvgflltpvaTQL-----SVDYLPTRDFArrPL------------QW-----L 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2214 DEVERHAVTILDLPP-AY--LQQQAEELRHAGR-----RIAVrtciLGGEAWDASLLTQQAVQ-AEAWFNA------YGP 2278
Cdd:PRK09192 264 DLISRNRGTISYSPPfGYelCARRVNSKDLAELdlscwRVAG----IGADMIRPDVLHQFAEAfAPAGFDDkafmpsYGL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 TEAV----ITPLAWHCRAQ-------EGGAPAIGRALGARRA-----C----------ILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK09192 340 AEATlavsFSPLGSGIVVEevdrdrlEYQGKAVAPGAETRRVrtfvnCgkalpgheieIRNEAGMPLPERVVGHICVRGP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYLGRPgQTAERFVADPFsgsgerlYRTGDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV--AE 2410
Cdd:PRK09192 420 SLMSGYFRDE-ESQDVLAADGW-------LDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGD 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2411 AAVVALDGVGGPLLAAYLVGR--DAMRGEDLLAELRTWLAGR---------LPAYmqptawqvlsSLPLNANGKLDR 2476
Cdd:PRK09192 491 AAAFSIAQENGEKIVLLVQCRisDEERRGQLIHALAALVRSEfgveaavelVPPH----------SLPRTSSGKLSR 557
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
5054-5130 |
2.30e-14 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 71.04 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5054 APRSDLEQQVAGIWAEVLQL--QQVGLDDNFF-ELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQTS 5130
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
3185-3467 |
3.53e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 77.34 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSAL---SNRLCWMQQaygLGVGDTVLQKTPFsFDVSVWEFFWP--LMSGARLVVAAPgdhrD 3259
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVdTLHFV--PSMLQ--AFLQDE--DVASCTSLKRIVCSGEALPADAQQqVFAKLPQaglynlYGPTE- 3332
Cdd:cd17636 77 AEEVLELIEAERC-THAFLlpPTIDQivELNADGlyDLSSLRSSPAAPEWNDMATVDTSP-WGRKPGG------YGQTEv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3333 AAIDVTHWTcveeGKDAVPI-GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvageR 3411
Cdd:cd17636 149 MGLATFAAL----GGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------G 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd17636 218 WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
2134-2482 |
3.84e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 79.41 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAA-LVahcQAAARTYGVgpgdcqlqfasisFDAAAEQLF---------------V--PLLA 2195
Cdd:PRK00174 249 FILYTSGSTGKPKGVLHTTGGyLV---YAAMTMKYV-------------FDYKDGDVYwctadvgwvtghsyiVygPLAN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLL--G-----DAGQWsaqhlADEVERHAVTILdlppaY--------LQQQAEELRHAGRRIAVRtcILG--GEAwd 2258
Cdd:PRK00174 313 GATTLMfeGvpnypDPGRF-----WEVIDKHKVTIF-----YtaptairaLMKEGDEHPKKYDLSSLR--LLGsvGEP-- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2259 aslltqqaVQAEAW---FNAYG----P-------TE---AVITPLAwhcraqegGAPAI-----GRALGARRACILDAAL 2316
Cdd:PRK00174 379 --------INPEAWewyYKVVGgercPivdtwwqTEtggIMITPLP--------GATPLkpgsaTRPLPGIQPAVVDEEG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 QPCAPGMIGELYIG----GQclARGYLGRPgqtaERFVADPFS---GsgerLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:PRK00174 443 NPLEGGEGGNLVIKdpwpGM--MRTIYGDH----ERFVKTYFStfkG----MYFTGDGARRDEDGYYWITGRVDDVLNVS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2390 GFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGRDAMRGED-LLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:PRK00174 513 GHRLGTAEIESALVAHPKVAEAAVVgRPDDIKGQGIYAFVTLKGGEEPSDeLRKELRNWVRKEIGPIAKPDVIQFAPGLP 592
|
410
....*....|....*
gi 2310915810 2468 LNANGKLDRKALPKV 2482
Cdd:PRK00174 593 KTRSGKIMRRILRKI 607
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1100-1401 |
3.85e-14 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 78.26 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQRWFFEQSI--PNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAW-----HQAYAEQAGEPL 1172
Cdd:cd19536 4 LSSLQEGMLFHSLlnPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQpvqvvHRQAQVPVTELD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 WRRQAGSEEALLALCEEAQ-RSLDLEQGPLLRALLVdMADGSQRLLLVI--HHLAVDGVSWRILLEDLQRLYADLdADLG 1249
Cdd:cd19536 84 LTPLEEQLDPLRAYKEETKiRRFDLGRAPLVRAALV-RKDERERFLLVIsdHHSILDGWSLYLLVKEILAVYNQL-LEYK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 PRSSSYQTWSRHL--HEQAGARLDELD-YWQAQLHDAPHA-LPCENPHGALENRHERKLVLTLD-AERTRQLlqeapaAY 1324
Cdd:cd19536 162 PLSLPPAQPYRDFvaHERASIQQAASErYWREYLAGATLAtLPALSEAVGGGPEQDSELLVSVPlPVRSRSL------AK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1325 RTQVN--DLLLTALARATCRWSGDASVLVQLEGHGRedLGEAIDLSRTVGWFTSLFPVRLT-PAADLGESLKAIKEQLRG 1401
Cdd:cd19536 236 RSGIPlsTLLLAAWALVLSRHSGSDDVVFGTVVHGR--SEETTGAERLLGLFLNTLPLRVTlSEETVEDLLKRAQEQELE 313
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
3033-3525 |
4.09e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.04 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3033 EYPlqrGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLA-----HALIERGvgaDRlVGVAMERSIEMVVALMA 3107
Cdd:PRK05677 22 EYP---NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAawlqqHTDLKPG---DR-IAVQLPNVLQYPVAVFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 ILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL---SQSHLK---LP--------------------------------- 3148
Cdd:PRK05677 95 AMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAekvLPktgvkhvivtevadmlpplkrllinavvkhvkk 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3149 ------LAQGVQRID-LDRGAPwfEDYSEANPDihldGENLAYVIYTSGSTGKPKGAGNRHSAL-SNRL-CWMQQAYGLG 3219
Cdd:PRK05677 175 mvpayhLPQAVKFNDaLAKGAG--QPVTEANPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLqCRALMGSNLN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3220 VG-DTVLQKTP----FSFDVSVweFFWPLMSGARLVVAAPGDH----RDPAK------------LVALINREGVDTLHFv 3278
Cdd:PRK05677 249 EGcEILIAPLPlyhiYAFTFHC--MAMMLIGNHNILISNPRDLpamvKELGKwkfsgfvglntlFVALCNNEAFRKLDF- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 psmlqaflqdedvascTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGKdavpIGRPI 3356
Cdd:PRK05677 326 ----------------SALKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSpvVSVNPSQAIQVGT----IGIPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:PRK05677 385 PSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDM 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:PRK05677 459 ILVSGFNVYPNELEDVLAALPGVLQCAAIGVpdekSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDEL 538
|
570
....*....|...
gi 2310915810 3513 PLSPNGKLDRKAL 3525
Cdd:PRK05677 539 PTTNVGKILRREL 551
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
506-998 |
4.42e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.04 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 506 EYPlqrGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLA-----HALIERGigaDRlVGVAMERSIEMVVALMA 580
Cdd:PRK05677 22 EYP---NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAawlqqHTDLKPG---DR-IAVQLPNVLQYPVAVFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 581 ILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL---SQSHLK---LP------------------------------LAQ 624
Cdd:PRK05677 95 AMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAekvLPktgvkhvivtevadmlpplkrllinavvkhVKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 625 GVQRIDLDQA----DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSAL-SNRL-CWMQQAYGLGVG-DTV 697
Cdd:PRK05677 175 MVPAYHLPQAvkfnDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLqCRALMGSNLNEGcEIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 698 LQKTP----FSFDVSVweFFWPLMSGARLVVAAPgdhRD-PAKLVELINRE-----GVDTLhFVpsmlqAFLQDEDVASC 767
Cdd:PRK05677 255 IAPLPlyhiYAFTFHC--MAMMLIGNHNILISNP---RDlPAMVKELGKWKfsgfvGLNTL-FV-----ALCNNEAFRKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 768 --TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGNLEP 843
Cdd:PRK05677 324 dfSALKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSpvVSVNPSQAIQVGT----IGIPVPSTLCKVIDDDGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 844 VPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:PRK05677 399 LPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 924 ARLLEHPWVREAAVLAV----DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK05677 473 DVLAALPGVLQCAAIGVpdekSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
2014-2415 |
5.06e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 78.41 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGagyLPLDPNYP---AERLAYMLRDSGARWLI 2090
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CqetlaerlpcpaeverlpletaawpasaDTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--V 2168
Cdd:cd17639 83 T----------------------------DGKP------DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2169 GPGD---CQLQFASIsFDAAAEQLFvpLLAGARVllgdaGQWSAQHLADEVERH--------------AV-TILDL---- 2226
Cdd:cd17639 129 GPDDrylAYLPLAHI-FELAAENVC--LYRGGTI-----GYGSPRTLTDKSKRGckgdltefkptlmvGVpAIWDTirkg 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 ------PPAYLQQQAEELRHAGRRIAVR----TCIL---------------------GGEAWDASllTQQavqaeaWFN- 2274
Cdd:cd17639 201 vlaklnPMGGLKRTLFWTAYQSKLKALKegpgTPLLdelvfkkvraalggrlrymlsGGAPLSAD--TQE------FLNi 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 -------AYGPTEAVitplawhCRA--QEGGAPAIGRAlGARRACIlDAALQPC--------APGMIGELYIGGQCLARG 2337
Cdd:cd17639 273 vlcpviqGYGLTETC-------AGGtvQDPGDLETGRV-GPPLPCC-EIKLVDWeeggystdKPPPRGEILIRGPNVFKG 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2338 YLGRPGQTAERFvadpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIR-GFRIEIGEIESQLLAHPYVAEAAVVA 2415
Cdd:cd17639 344 YYKNPEKTKEAF-------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1104-1383 |
5.49e-14 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 78.07 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1104 QR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL----WRRQA 1177
Cdd:cd20483 8 QRrlWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLividLSEAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1178 GSEEALLALCEEAQRS-LDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY------ADLDADLGP 1250
Cdd:cd20483 88 DPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalragRDLATVPPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1251 RSS--SYQTWSRHLHEQAgARLDELDYWQAQLHDAPHA---LP---CENPhgaLENRHERKLV-LTLDAE---RTRQLLQ 1318
Cdd:cd20483 168 PVQyiDFTLWHNALLQSP-LVQPLLDFWKEKLEGIPDAsklLPfakAERP---PVKDYERSTVeATLDKEllaRMKRICA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1319 EA---PAAYrtqvndlLLTALARATCRWSGDASVLVQL----EGHGredlgeaiDLSRTVGWFTSLFPVRLT 1383
Cdd:cd20483 244 QHavtPFMF-------LLAAFRAFLYRYTEDEDLTIGMvdgdRPHP--------DFDDLVGFFVNMLPIRCR 300
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
2397-2473 |
5.60e-14 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 69.88 E-value: 5.60e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGK 2473
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVpDELKGEAPVAFVVLKPG--VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1980-2479 |
6.34e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 78.52 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1980 APLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGIL 2059
Cdd:PRK07059 15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2060 KAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcpAEVERLPLE---------------------------- 2111
Cdd:PRK07059 95 RAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQ--QVLAKTAVKhvvvasmgdllgfkghivnfvvrrvkkm 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2112 TAAWP---------ASADTRPL----PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAA---RTYGVGPGDCQ 2174
Cdd:PRK07059 173 VPAWSlpghvrfndALAEGARQtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlQMEAwlqPAFEKKPRPDQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASI-----SFDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTILdlpPAYLQQQAEELRHAG-RRIAVR 2248
Cdd:PRK07059 253 LNFVCAlplyhIFALTVCGLLGMRTGGRNILIPNPRDIPG--FIKELKKYQVHIF---PAVNTLYNALLNNPDfDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 TCIL---GGEAwdasllTQQAVqAEAWFN--------AYGPTEAviTPLAwHCRAQEGGA--PAIGRALGARRACILDAA 2315
Cdd:PRK07059 328 KLIVangGGMA------VQRPV-AERWLEmtgcpiteGYGLSET--SPVA-TCNPVDATEfsGTIGLPLPSTEVSIRDDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:PRK07059 398 GNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTwlagRLPAYMQPTAWQVLSSLPLNANGK 2473
Cdd:PRK07059 471 NEIEEVVASHPGVLEVAAVGVpDEHSGEAVKLFVVKKDpALTEEDVKAFCKE----RLTNYKRPKFVEFRTELPKTNVGK 546
|
....*.
gi 2310915810 2474 LDRKAL 2479
Cdd:PRK07059 547 ILRREL 552
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
511-998 |
7.25e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 78.33 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 511 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG--IGADRlVGVAMERSIEMVVALMAILKAGGAY 588
Cdd:PRK12492 24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDR-IAVQMPNVLQYPIAVFGALRAGLIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 589 VPVDPEYPEERQAYMLEDSG-------------VQLLLSQSHLK----------LPLAQG-------------VQRIDLD 632
Cdd:PRK12492 103 VNTNPLYTAREMRHQFKDSGaralvylnmfgklVQEVLPDTGIEylieakmgdlLPAAKGwlvntvvdkvkkmVPAYHLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 633 QA----DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGlgvgdTVLQKTPFSFdvs 708
Cdd:PRK12492 183 QAvpfkQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHG---NLVANMLQVRA-----CLSQLGPDGQ--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 709 vweffwPLMSGARLVVAAP-------------------GDH-------RDPAKLVELINRE------GVDTLhFVPSMLQ 756
Cdd:PRK12492 252 ------PLMKEGQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPGFIKELGKWrfsallGLNTL-FVALMDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 757 AFLQDEDVascTSLKRIVCSGEALpADAQQQVFAKLPQAGLYNLYGPTEAAIDVT---HWTCVEEGKdtvpIGRPIGNLG 833
Cdd:PRK12492 325 PGFKDLDF---SALKLTNSGGTAL-VKATAERWEQLTGCTIVEGYGLTETSPVAStnpYGELARLGT----VGIPVPGTA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 834 CYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLR 913
Cdd:PRK12492 397 LKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 914 GLRIELGEIEARLLEHPWVREAAVLAV-DGR--QLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:PRK12492 471 GFNVYPNEIEDVVMAHPKVANCAAIGVpDERsgEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPV 550
|
....*...
gi 2310915810 991 GKLDRKAL 998
Cdd:PRK12492 551 GKILRREL 558
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
658-940 |
9.13e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 76.19 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 658 VIYTSGSTGKPKGAGNRHSAL---SNRLCWMQQaygLGVGDTVLQKTPFsFDVSVWEFFWP--LMSGARLVVAAPgdhrD 732
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 733 PAKLVELINREGVdTLHFV--PSMLQ--AFLQDE--DVASCTSLKRIVCSGEALPADAQQqVFAKLPQaglynlYGPTE- 805
Cdd:cd17636 77 AEEVLELIEAERC-THAFLlpPTIDQivELNADGlyDLSSLRSSPAAPEWNDMATVDTSP-WGRKPGG------YGQTEv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 806 AAIDVTHWTcveEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvageRM 885
Cdd:cd17636 149 MGLATFAAL---GGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GW 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1981-2479 |
9.30e-14 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 77.95 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGGVAAAFAHQVASAPEAIALVcgDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLL 2056
Cdd:cd17642 10 PLEDGTAGEQLHKAMKRYASVPGTIAFT--DAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2057 GILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE-------TLAERLPCPAEVERLPLETAAWPASAD----TRPLP 2125
Cdd:cd17642 88 AGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKkglqkvlNVQKKLKIIKTIIILDSKEDYKGYQCLytfiTQNLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2126 EVAG------------ETLAYVIYTSGSTGQPKGVAVSQAALVA---HCQAAARTYGVGPGDCQLQFASISFDAAAEQLF 2190
Cdd:cd17642 168 PGFNeydfkppsfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2191 VPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPP---AYLQQQAEELRHAGRRIAVRTCilGGeawdASLLTQQAV 2267
Cdd:cd17642 248 GYLICGFRVVL--MYKFEEELFLRSLQDYKVQSALLVPtlfAFFAKSTLVDKYDLSNLHEIAS--GG----APLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2268 QAEAWFN------AYGPTEA----VITPlawhcraQEGGAP-AIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLA 2335
Cdd:cd17642 320 AVAKRFKlpgirqGYGLTETtsaiLITP-------EGDDKPgAVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA 2415
Cdd:cd17642 393 KGYVNNPEATKALIDKDGW-------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2416 L-DGVGGPLLAAYLVGRDamrGEDLLA-ELRTWLAGRL-PAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd17642 466 IpDEDAGELPAAVVVLEA---GKTMTEkEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
4543-5040 |
9.90e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.80 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAE--RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEimvaFLAVLKAG--GAYVPL 4617
Cdd:PRK07867 7 VAEllLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPE----FSLLLGAAalSGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 DIEyPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGL----SCLSVDRE---EEWAGFPAHDPE-VALHGDNLAYVIYTS 4689
Cdd:PRK07867 83 GLN-PTRRGAALARDIAHADCQLVLTESAHAELLDGLdpgvRVINVDSPawaDELAAHRDAEPPfRVADPDDLFMLIFTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDceLHFMS---FAFDGSHEGWMHPLINGARVLIR---DDSLWLPErty 4763
Cdd:PRK07867 162 GTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD--VCYVSmplFHSNAVMAGWAVALAAGASIALRrkfSASGFLPD--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 aeMHRHGVT----VGVfPPVYLqqLAEHAERDGNPPPVRVyCFGGDAVAQASYDLAWRalkpkylF-----NGYGPTETV 4834
Cdd:PRK07867 237 --VRRYGATyanyVGK-PLSYV--LATPERPDDADNPLRI-VYGNEGAPGDIARFARR-------FgcvvvDGFGSTEGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 VTpllwKARAGDACGAAympIGTLLGNRSgyILDGQ-LNLLPVGVA------------GELY-LGGEGVARGYLERPALT 4900
Cdd:PRK07867 304 VA----ITRTPDTPPGA---LGPLPPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVpdpfgapGSRlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQL 4979
Cdd:PRK07867 375 AERMR-------GGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4980 VGYVVAQEPAVADsPEAQAECRAQlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK07867 447 MAALVLAPGAKFD-PDAFAEFLAA-----QPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
4544-5043 |
1.37e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 77.49 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK13382 50 AIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLPipEGLS-CLSVDREEEWAGFPA---HDPEVALH--------GDNLAYVIYTSGS 4691
Cdd:PRK13382 130 PALAEVVTREGVDTVIYDEEFSATVD--RALAdCPQATRIVAWTDEDHdltVEVLIAAHagqrpeptGRKGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIAHIVATGERyemTPEDCELHFMSFAFDGSHEGWMHPLINGA-RVLIRDDSLWLPERTYAEMHRHG 4770
Cdd:PRK13382 208 TGTPKGARRSGPGGIGTLKAILDR---TPWRAEEPTVIVAPMFHAWGFSQLVLAASlACTIVTRRRFDPEATLDLIDRHR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4771 VTVGVFPPVYLQQLAEHAERDGNPppvrvYCFGGDAVAQASYDlawrALKPKY-----------LFNGYGPTE----TVV 4835
Cdd:PRK13382 285 ATGLAVVPVMFDRIMDLPAEVRNR-----YSGRSLRFAAASGS----RMRPDVviafmdqfgdvIYNNYNATEagmiATA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4836 TPLLWKArAGDACGAAymPIGTLLgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYleRPALTAErfVPDPFGApgsr 4915
Cdd:PRK13382 356 TPADLRA-APDTAGRP--AEGTEI-----RILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD--FHDGFMA---- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4916 lyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAqEPAVADSP 4994
Cdd:PRK13382 420 ---SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEqYGQRLAAFVVL-KPGASATP 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 4995 EAqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQP 5043
Cdd:PRK13382 496 ET-------LKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1106-1320 |
1.39e-13 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 76.53 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1106 WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGE--PLWRRQAGSEEAL 1183
Cdd:cd19538 12 WFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEAtpKLEIKEVDEEELE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1184 LALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY----ADLDADLGPRSSSY---- 1255
Cdd:cd19538 92 SEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarcKGEAPELAPLPVQYadya 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1256 ---QTWSRHLHEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEA 1320
Cdd:cd19538 172 lwqQELLGDESDPDSLIARQLAYWKKQLAGLPDEieLPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
4558-5042 |
1.41e-13 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 77.09 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4558 FDEEKLTYAELDSRANRLAHALI-ARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYmmqdsrah 4636
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIH-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4637 lllthshllerlpipeglsCLSVDReeewAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY 4716
Cdd:cd05937 73 -------------------CLKLSG----SRFVIVDP------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4717 EMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV-LIRDDSLwlpERTYAEMHRHGVTVgvfppvyLQQLAEHAERDGNP 4794
Cdd:cd05937 124 NLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLaLSRKFSA---SQFWKDVRDSGATI-------IQYVGELCRYLLST 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPV------RVYCFGGDAVaqaSYDLaWRALKPKylFN------GYGPTETVVTplLWKARAGD----ACGAAYMPIGTL 4858
Cdd:cd05937 194 PPSpydrdhKVRVAWGNGL---RPDI-WERFRER--FNvpeigeFYAATEGVFA--LTNHNVGDfgagAIGHHGLIRRWK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNrsGYIL---------------DGQLNLLPVGVAGE----LYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRS 4919
Cdd:cd05937 266 FEN--QVVLvkmdpetddpirdpkTGFCVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVF-RKGDIYFRT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADSPEAQ 4997
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGR-------AGCAAITLEESSA 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2310915810 4998 ---AECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:cd05937 416 vptEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
2002-2416 |
1.47e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.15 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE------ 2075
Cdd:PLN02860 21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEeaksam 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2076 ---RLAYMLRDSGAR-WliCQETLAERLP---------------CPAEVERLPLETAAWPASADTRPLPEVAGETLAYVI 2136
Cdd:PLN02860 101 llvRPVMLVTDETCSsW--YEELQNDRLPslmwqvflespsssvFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLIC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGA-RVLLgdaGQWSAQHLADE 2215
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAcHVLL---PKFDAKAALQA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTC---ILGGEAWDASLLTQQAVQ---AEAWFNAYGPTEAV--ITPLA 2287
Cdd:PLN02860 256 IKQHNVTSMITVPAMMADLISLTRKSMTW-KVFPSvrkILNGGGSLSSRLLPDAKKlfpNAKLFSAYGMTEACssLTFMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRAQEGGApaigRALGARRACILDAALQP---C----APGMigELYIG-------GQCLARG---YLGRPGQTAErfv 2350
Cdd:PLN02860 335 LHDPTLESPK----QTLQTVNQTKSSSVHQPqgvCvgkpAPHV--ELKIGldessrvGRILTRGphvMLGYWGQNSE--- 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2351 aDPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL 2416
Cdd:PLN02860 406 -TASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1096-1387 |
1.55e-13 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 76.75 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1096 GEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAY--AEQAGEP 1171
Cdd:cd19546 3 DEVPATAGQLrtWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldADAARPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1172 LWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY-------ADL 1244
Cdd:cd19546 83 LPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarregrAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1245 DADLGPRSSSYQTWSRHL----HEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQ 1318
Cdd:cd19546 163 RAPLPLQFADYALWERELlageDDRDSLIGDQIAYWRDALAGAPDEleLPTDRPRPVLPSRRAGAVPLRLDAEVHARLME 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 1319 EAPAAYRTQVNdLLLTALARATCRWSGDASVLVQLEGHGREDLGeaiDLSRTVGWFTSLFPVRLTPAAD 1387
Cdd:cd19546 243 AAESAGATMFT-VVQAALAMLLTRLGAGTDVTVGTVLPRDDEEG---DLEGMVGPFARPLALRTDLSGD 307
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
3062-3439 |
1.71e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.39 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvelLLS 3141
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS---------------LMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 QSHLKL------------------PLAQGVQRIDLDrGAPWF--EDYSEANPDIHLDG-------------------ENL 3182
Cdd:PRK12582 144 HDHAKLkhlfdlvkprvvfaqsgaPFARALAALDLL-DVTVVhvTGPGEGIASIAFADlaatpptaavaaaiaaitpDTV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3183 AYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE--------FFWPLMSGARLvvaap 3254
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDPPPPVSLDWMPWNhtmggnanFNGLLWGGGTL----- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3255 gdHRDPAKLVALINREGVDTLH--------FVP---SMLQAFLQdEDVASCTS----LKRIVCSGEALPADAQQQVFA-- 3317
Cdd:PRK12582 294 --YIDDGKPLPGMFEETIRNLReisptvygNVPagyAMLAEAME-KDDALRRSffknLRLMAYGGATLSDDLYERMQAla 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 ------KLPqagLYNLYGPTEAA--IDVTHWTCVEEGKdavpIGRPIANLAcyildgnLEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK12582 371 vrttghRIP---FYTGYGATETAptTTGTHWDTERVGL----IGLPLPGVE-------LKLAPVGDKYEVRVKGPNVTPG 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3390 YHQRPGLTAERFVASPFvagermYRTGDLARY-----RADGVIeYAGRIDHQVKL 3439
Cdd:PRK12582 437 YHKDPELTAAAFDEEGF------YRLGDAARFvdpddPEKGLI-FDGRVAEDFKL 484
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
2135-2476 |
1.78e-13 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 75.38 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQHLAD 2214
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVV--MEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2215 EVERHAVTIL-DLPPAyLQQQAEELRHAGRRIAVRTCILGGEAWDasllTQQAVQAE---AWFNAYGPTEAviTPLAWHC 2290
Cdd:cd17637 83 LIEEEKVTLMgSFPPI-LSNLLDAAEKSGVDLSSLRHVLGLDAPE----TIQRFEETtgaTFWSLYGQTET--SGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2291 RAQE--GGApaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLA 2368
Cdd:cd17637 156 PYRErpGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--------WHHTGDLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQ--IKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP-----LLAAYLVGRDAMRGEDlla 2441
Cdd:cd17637 225 RFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI---GVPDPkwgegIKAVCVLKPGATLTAD--- 298
|
330 340 350
....*....|....*....|....*....|....*
gi 2310915810 2442 ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd17637 299 ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
3049-3466 |
1.91e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.91 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERT----PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVAL----MA------------- 3107
Cdd:PRK08162 25 ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHfgvpMAgavlntlntrlda 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 -----ILKAGGAYV-PVDPEYPEERQAYMLEDSGVELLLsqSHLKLPLAQGVQRI------------DLDRGAPWFEDYS 3169
Cdd:PRK08162 105 asiafMLRHGEAKVlIVDTEFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIgaldyeaflasgDPDFAWTLPADEW 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3170 EAnpdIHLDgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPlm 3244
Cdd:PRK08162 183 DA---IALN--------YTSGTTGNPKGVVYHHrgaylNALSNILAW-----GMPKHPVYLWTLPM-FHCNGWCFPWT-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3245 sgarlVVAAPGDH---R--DPAKLVALINREGVDtlHF-----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQ 3314
Cdd:PRK08162 244 -----VAARAGTNvclRkvDPKLIFDLIREHGVT--HYcgapiVLSAL-INAPAEWRAGIDHPVHAMVAGAAPPA----A 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3315 VFAKLPQAG--LYNLYGPTE----AAIdvthwtCVE-EGKDAVPIGRPIANLA----CY-------ILDGN-LEPVPVG- 3374
Cdd:PRK08162 312 VIAKMEEIGfdLTHVYGLTEtygpATV------CAWqPEWDALPLDERAQLKArqgvRYplqegvtVLDPDtMQPVPADg 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3375 -VLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 3453
Cdd:PRK08162 386 eTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
490
....*....|...
gi 2310915810 3454 LEHPWVREAAVLA 3466
Cdd:PRK08162 459 YRHPAVLVAAVVA 471
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1981-2479 |
1.96e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.81 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRggvaAAFAHqvasaPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILK 2060
Cdd:PLN02479 22 PLWFLER----AAVVH-----PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2061 AGAGYLPLDPNYPAERLAYMLRDSGARWLICQE---TLAER-LPCPAEVE----RLPLETAAWPASADTRPL-------- 2124
Cdd:PLN02479 93 AGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQeffTLAEEaLKILAEKKkssfKPPLLIVIGDPTCDPKSLqyalgkga 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 ------------------PEVAGETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASI------ 2180
Cdd:PLN02479 173 ieyekfletgdpefawkpPADEWQSIA-LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMfhcngw 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2181 --SFDAAAeqlfvplLAGARVLLGdagQWSAQHLADEVERHAVTILDLPPAYLQQ-----QAEELRHAGRRIAVRTcilG 2253
Cdd:PLN02479 252 cfTWTLAA-------LCGTNICLR---QVTAKAIYSAIANYGVTHFCAAPVVLNTivnapKSETILPLPRVVHVMT---A 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2254 GEAWDASLLTQQAVQAEAWFNAYGPTEAV--ITPLAWhcRAQEGGAPAIGRA-LGARRAC---------ILDAALQPCAP 2321
Cdd:PLN02479 319 GAAPPPSVLFAMSEKGFRVTHTYGLSETYgpSTVCAW--KPEWDSLPPEEQArLNARQGVryiglegldVVDTKTMKPVP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2322 G---MIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:PLN02479 397 AdgkTMGEIVMRGNMVMKGYLKNPKANEEAFANG--------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2399 ESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAMRGED---LLAELRTWLAGRLPAYMQPTAwQVLSSLPLNANGKL 2474
Cdd:PLN02479 469 ENVVYTHPAVLEASVVArPDERWGESPCAFVTLKPGVDKSDeaaLAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKI 547
|
....*
gi 2310915810 2475 DRKAL 2479
Cdd:PLN02479 548 QKHVL 552
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4679-5040 |
1.98e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 75.59 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDSLW 4757
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 LPERTY------AEMHRHGVTVGVfPPVYLQQLAEHAERDGNPppVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPT 4831
Cdd:cd05944 81 RNPGLFdnfwklVERYRITSLSTV-PTVYAALLQVPVNADISS--LRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4832 ETvvtpllwkaragdACGAAYMPIGT-----LLGNRSGY------ILDGQLNLL---PVGVAGELYLGGEGVARGYLE-- 4895
Cdd:cd05944 157 EA-------------TCLVAVNPPDGpkrpgSVGLRLPYarvrikVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYte 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4896 --RPALTAERFVpdpfgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG 4973
Cdd:cd05944 224 gnKNAFVADGWL------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPD 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 4974 A-VGQQLVGYVVAQEPAVADSPEaqaecraqLKTALRERLPEY-MVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05944 292 AhAGELPVAYVQLKPGAVVEEEE--------LLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
501-1008 |
1.99e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 76.94 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 501 NATAAEYPLQRGvhRLFEEQVERTPTAPALAFgeerlDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMA 580
Cdd:PLN02330 27 KLTLPDFVLQDA--ELYADKVAFVEAVTGKAV-----TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 581 ILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS-------HLKLP-LAQGVQRID--------LDQADAWLENHAEN 644
Cdd:PLN02330 100 IMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygkvkGLGLPvIVLGEEKIEgavnwkelLEAADRAGDTSDNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 645 npgiELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCwmQQAYGLG---VGD-TVLQKTPFsFDVS--VWEFFWPLMS 718
Cdd:PLN02330 180 ----EILQTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGpemIGQvVTLGLIPF-FHIYgiTGICCATLRN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 719 GARLVVAAPGDHRdpAKLVELINREgVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQ 794
Cdd:PLN02330 253 KGKVVVMSRFELR--TFLNALITQE-VSFAPIVPPIILNLVKNPIVEefdlSKLKLQAIMTAAAPLAPELLTAFEAKFPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 795 AGLYNLYGPTE-AAIDVTHWTcVEEGKDTV---PIGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGL 869
Cdd:PLN02330 330 VQVQEAYGLTEhSCITLTHGD-PEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 870 TAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQL 945
Cdd:PLN02330 409 TDRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPdeeaGEIP 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 946 VGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQA 1008
Cdd:PLN02330 483 AACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKA 545
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
4551-5037 |
2.69e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 76.38 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:PLN02860 21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLT--------HSHLLERLP---------------IPEGLSCLSVDREEEWAGFPAhDPEVALHGDNLAYVIY 4687
Cdd:PLN02860 101 LLVRPVMLVTdetcsswyEELQNDRLPslmwqvflespsssvFIFLNSFLTTEMLKQRALGTT-ELDYAWAPDDAVLICF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAH------IVATGEryemtpEDCELHFMSFAFDGSHEGWMHPLINGA-RVLIR--DDSLWL 4758
Cdd:PLN02860 180 TSGTTGRPKGVTISHSALIVQslakiaIVGYGE------DDVYLHTAPLCHIGGLSSALAMLMVGAcHVLLPkfDAKAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4759 pertyAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP---PPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTE--- 4832
Cdd:PLN02860 254 -----QAIKQHNVTSMITVPAMMADLISLTRKSMTWkvfPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacs 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4833 -----TVVTPLLWKARAGDAC------GAAYMPIGTLLGNRSGYIldgQLNLLPVGVA--GELYLGGEGVARGYLERPAL 4899
Cdd:PLN02860 329 sltfmTLHDPTLESPKQTLQTvnqtksSSVHQPQGVCVGKPAPHV---ELKIGLDESSrvGRILTRGPHVMLGYWGQNSE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFVPDPFGApgsrlyrSGDLtrGRAD--GVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VG 4976
Cdd:PLN02860 406 TASVLSNDGWLD-------TGDI--GWIDkaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSrLT 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4977 QQLVGYVVAQEP---AVADSPEAQAE---CRAQLKTALRER-LPEYMVPShlLFLAR---MPLTPNGKLDR 5037
Cdd:PLN02860 477 EMVVACVRLRDGwiwSDNEKENAKKNltlSSETLRHHCREKnLSRFKIPK--LFVQWrkpFPLTTTGKIRR 545
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
3038-3525 |
2.85e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 76.40 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG--VGADRlVGVAMERSIEMVVALMAILKAGGAY 3115
Cdd:PRK12492 24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDR-IAVQMPNVLQYPIAVFGALRAGLIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3116 VPVDPEYPEERQAYMLEDSGVELLLsqsHLKLpLAQGVQRIDLDRGapwFEDYSEAN----------------------- 3172
Cdd:PRK12492 103 VNTNPLYTAREMRHQFKDSGARALV---YLNM-FGKLVQEVLPDTG---IEYLIEAKmgdllpaakgwlvntvvdkvkkm 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 -PDIHL-----------DG------------ENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGlgvgdTVLQKT 3228
Cdd:PRK12492 176 vPAYHLpqavpfkqalrQGrglslkpvpvglDDIAVLQYTGGTTGLAKGAMLTHG---NLVANMLQVRA-----CLSQLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3229 PFSFdvsvweffwPLMSGARLVVAAP-------------------GDH-------RDPA---------KLVALInreGVD 3273
Cdd:PRK12492 248 PDGQ---------PLMKEGQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPgfikelgkwRFSALL---GLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3274 TLhFVPSMLQAFLQDEDVascTSLKRIVCSGEALpADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVpIG 3353
Cdd:PRK12492 316 TL-FVALMDHPGFKDLDF---SALKLTNSGGTAL-VKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGT-VG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3354 RPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRI 3433
Cdd:PRK12492 390 IPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-DGR--QLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALE 3510
Cdd:PRK12492 464 KDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVpDERsgEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRD 543
|
570
....*....|....*
gi 2310915810 3511 RMPLSPNGKLDRKAL 3525
Cdd:PRK12492 544 SLPMTPVGKILRREL 558
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1990-2487 |
3.21e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 76.03 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PLN02574 43 VSFIFSHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGdVVLLLLPNSVYFPVIFLAVLSLGGIVTTM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 DPNYPAERLAYMLRDSGARWLICQETLAERLP--------CPAEVE----RLPLETAAWPASADTRPLPE--VAGETLAY 2134
Cdd:PLN02574 123 NPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSplgvpvigVPENYDfdskRIEFPKFYELIKEDFDFVPKpvIKQDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAAR---TYGVGPGDCQLQFASIS-FDAAAEQLFVPLLagarVLLGDA----GQ 2206
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFVRfeaSQYEYPGSDNVYLAALPmFHIYGLSLFVVGL----LSLGSTivvmRR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2207 WSAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGRRIAVRTC-----ILGGEAWDASLLTQQAVQAEA---WFNAYGP 2278
Cdd:PLN02574 279 FDASDMVKVIDRFKVTHFPVVPPILMA----LTKKAKGVCGEVLkslkqVSCGAAPLSGKFIQDFVQTLPhvdFIQGYGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 TEAVITPLAWHCRAQEGGAPAIGRALGARRACILD---AALQPcaPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFs 2355
Cdd:PLN02574 355 TESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwstGCLLP--PGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 gsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR--D 2432
Cdd:PLN02574 432 ------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVpDKECGEIPVAFVVRRqgS 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2433 AMRGEDLLaelrTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAAR 2487
Cdd:PLN02574 506 TLSQEAVI----NYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSV 556
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
535-912 |
3.28e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 76.24 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvqlLLS 614
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS---------------LMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 615 QSHLKL------------------PLAQGVQRIDLDQAD-AWLENHAENNPGI-------------------ELNGENLA 656
Cdd:PRK12582 144 HDHAKLkhlfdlvkprvvfaqsgaPFARALAALDLLDVTvVHVTGPGEGIASIafadlaatpptaavaaaiaAITPDTVA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 657 YVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE--------FFWPLMSGARLvvaapg 728
Cdd:PRK12582 224 KYLFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDPPPPVSLDWMPWNhtmggnanFNGLLWGGGTL------ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 729 dHRDPAK-LVELIN------REGVDTLHF-VP---SMLQAFLQdEDVASCTS----LKRIVCSGEALPADAQQQVFA--- 790
Cdd:PRK12582 294 -YIDDGKpLPGMFEetirnlREISPTVYGnVPagyAMLAEAME-KDDALRRSffknLRLMAYGGATLSDDLYERMQAlav 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 791 -----KLPqagLYNLYGPTEAA--IDVTHWTCVEEGKdtvpIGRPIGNLgcyildgNLEPVPVGVLGELYLAGRGLARGY 863
Cdd:PRK12582 372 rttghRIP---FYTGYGATETAptTTGTHWDTERVGL----IGLPLPGV-------ELKLAPVGDKYEVRVKGPNVTPGY 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 864 HQRPGLTAERFVASPFvagermYRTGDLARY-----RADGVIeYAGRIDHQVKL 912
Cdd:PRK12582 438 HKDPELTAAAFDEEGF------YRLGDAARFvdpddPEKGLI-FDGRVAEDFKL 484
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
536-998 |
3.46e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.94 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 536 RLDYAELNRRANRLAHALIERGIG-ADRLVGVA--MERSIEMVVALMAIlkaGGAYVPVDPEYPEERQAYML---EDSGV 609
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKlGDRVATIAwnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIInhaEDRVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 610 QL------LLSQSHLKLPlaqGVQR--IDLDQA-------------DAWLENHAENNPGIELNGENLAYVIYTSGSTGKP 668
Cdd:PRK06018 116 ITdltfvpILEKIADKLP---SVERyvVLTDAAhmpqttlknavayEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 669 KGA--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVW--EFFWPlMSGARLVVaaPGDHRDPAKLVELINREG 744
Cdd:PRK06018 193 KGVlySHRSNVLHALMANNGDALGTSAADTMLPVVPL-FHANSWgiAFSAP-SMGTKLVM--PGAKLDGASVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 745 VDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLpQAGLYNLYGPTE-------AAIDVTHWTC 815
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQymEKEGLKLPHLKMVVCGGSAMP-RSMIKAFEDM-GVEVRHAWGMTEmsplgtlAALKPPFSKL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 816 VEEGKDTVPI--GRPIGNLGCYILD--GNLEPVPVGVLGELYLAGRGLARGYHQRPG--LTAERFvaspfvagermYRTG 889
Cdd:PRK06018 347 PGDARLDVLQkqGYPPFGVEMKITDdaGKELPWDGKTFGRLKVRGPAVAAAYYRVDGeiLDDDGF-----------FDTG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESEGGD-WREALA 963
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpkwDERPLL--IVQLKPGETaTREEIL 493
|
490 500 510
....*....|....*....|....*....|....*
gi 2310915810 964 AHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06018 494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
4560-5040 |
3.56e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 76.47 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLL 4639
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 THSHLLERL-PIP--------------EGLS---CLSVD------REE-EW------------AGFPAHDPEVALHGDNL 4682
Cdd:PLN02654 198 TCNAVKRGPkTINlkdivdaaldesakNGVSvgiCLTYEnqlamkREDtKWqegrdvwwqdvvPNYPTKCEVEWVDAEDP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHiVATGERYEMTPEDCELHFMSfafdgSHEGWM--H------PLINGARVLIRDD 4754
Cdd:PLN02654 278 LFLLYTSGSTGKPKGVLHTTGGYMVY-TATTFKYAFDYKPTDVYWCT-----ADCGWItgHsyvtygPMLNGATVLVFEG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4755 SLWLPE--RTYAEMHRHGVTVGVFPPVYLQQLAehaeRDGNPPPVR-----VYCFGgdAVAQASYDLAWRalkpkYLFNG 4827
Cdd:PLN02654 352 APNYPDsgRCWDIVDKYKVTIFYTAPTLVRSLM----RDGDEYVTRhsrksLRVLG--SVGEPINPSAWR-----WFFNV 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4828 YGPTETVVTPLLWKARAGdacGAAYMPIGTLLGNRSGYILDGQLNLLPVgVAGELYLGGEGVARGYL----ERPAL---- 4899
Cdd:PLN02654 421 VGDSRCPISDTWWQTETG---GFMITPLPGAWPQKPGSATFPFFGVQPV-IVDEKGKEIEGECSGYLcvkkSWPGAfrtl 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 --TAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-G 4976
Cdd:PLN02654 497 ygDHERYETTYF-KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVkG 575
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4977 QQLVGYVvaqepAVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN02654 576 QGIYAFV-----TLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
3700-3941 |
3.79e-13 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 75.43 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3700 LLWRAEAVDRQA--LESLCEESQRS-LDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG 3776
Cdd:cd19547 82 LDWSGEDPDRRAelLERLLADDRAAgLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3777 EAPRLPgKTSPFKAWAGRV-SEHARGESMKaqlQFWRELL-EGAPAelPCEHPQGALEQRFATSVQsRFDRSLTeRLLKQ 3854
Cdd:cd19547 162 REPQLS-PCRPYRDYVRWIrARTAQSEESE---RFWREYLrDLTPS--PFSTAPADREGEFDTVVH-EFPEQLT-RLVNE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3855 APAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLsrTVGWFTSLFP--VRLSPVADLGESLKAIKE 3932
Cdd:cd19547 234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPlrIRLDPDQTVTGLLETIHR 311
|
....*....
gi 2310915810 3933 QLRAIPDKG 3941
Cdd:cd19547 312 DLATTAAHG 320
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
3066-3467 |
4.48e-13 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 75.49 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:PRK08008 40 YLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 kLPLAQGVQRID---------LDRGAPWFEDYS--------------EANPdihLDGENLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK08008 120 -YPMYRQIQQEDatplrhiclTRVALPADDGVSsftqlkaqqpatlcYAPP---LSTDDTAEILFTSGTTSRPKGVVITH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SALsnRLCWMQQAY--GLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLValinREGVDTL-HFV 3278
Cdd:PRK08008 196 YNL--RFAGYYSAWqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQV----CKYRATItECI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQAFLqdedVASCTSLKRIVCSGEAL----PADAQQQVFAKLPQAGLYNLYGPTEAAI--------DVTHWTcveeg 3346
Cdd:PRK08008 270 PMMIRTLM----VQPPSANDRQHCLREVMfylnLSDQEKDAFEERFGVRLLTSYGMTETIVgiigdrpgDKRRWP----- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3347 kdavPIGRPIANLACYILDGNLEPVPVGVLGELYL---AGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRA 3423
Cdd:PRK08008 341 ----SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEADGWL------HTGDTGYVDE 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2310915810 3424 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK08008 411 EGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
4671-5040 |
5.19e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.44 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPeVALHgdnlayviYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPedCELHFMSFAFDGSHeGWMHPLINGAR-- 4748
Cdd:PLN03102 186 HDP-ISLN--------YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGT--CPVYLWTLPMFHCN-GWTFTWGTAARgg 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4749 --VLIRddSLWLPErTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP--PPVRVYCFGGD---AVAQASYDLAWRALkp 4821
Cdd:PLN03102 254 tsVCMR--HVTAPE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPrsGPVHVLTGGSPppaALVKKVQRLGFQVM-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4822 kylfNGYGPTETVvTPLL---WKARAGDACGAAYMPIGTLLGNRsgyildgQLNLLPVGVA---------------GELY 4883
Cdd:PLN03102 329 ----HAYGLTEAT-GPVLfceWQDEWNRLPENQQMELKARQGVS-------ILGLADVDVKnketqesvprdgktmGEIV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4884 LGGEGVARGYLERPALTAERFvpdpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PLN03102 397 IKGSSIMKGYLKNPKATSEAF--------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4964 REAVVVAQPGAV-GQQLVGYVVAQ--EPAVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN03102 469 LETAVVAMPHPTwGETPCAFVVLEkgETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
65-436 |
5.95e-13 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 74.40 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 65 LEPQSGAYNLPSAVRLNgplDRQALER---AFASLVQRHETLRTVFprgADDSLAQaPLQ---RPLEVAFEDCSGLPEAE 138
Cdd:cd19544 17 LAEEGDPYLLRSLLAFD---SRARLDAflaALQQVIDRHDILRTAI---LWEGLSE-PVQvvwRQAELPVEELTLDPGDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 139 QEARLREEAQRESlQPFDLCEGPLLRVRLIR-LGEERHVLLLTLHHIVSDGWSMNVLIEEFsrfySAYATGAEPGLPAlP 217
Cdd:cd19544 90 ALAQLRARFDPRR-YRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI----QAILAGRAAALPP-P 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 218 IQYADYALWQRSWLEAGEQERqleYWRGKLGErhpvLELPT---------DHPRPVVpsyrgsRYEFSIEPALAEALRGT 288
Cdd:cd19544 164 VPYRNFVAQARLGASQAEHEA---FFREMLGD----VDEPTapfglldvqGDGSDIT------EARLALDAELAQRLRAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 289 ARRQGLTLFMLLLGGFNILLQRYSGQTD----------LRVGvpianrnrAEVEGLIGLFVNTQVLRSVFDGRtSVATLL 358
Cdd:cd19544 231 ARRLGVSPASLFHLAWALVLARCSGRDDvvfgtvlsgrMQGG--------AGADRALGMFINTLPLRVRLGGR-SVREAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 359 aglkdtvlgAQAHQdlpfeRLVEAFKVER-SLSH----------SPLFQVM--YNHQPLVADIEALDSVAGLSFgqLDWK 425
Cdd:cd19544 302 ---------RQTHA-----RLAELLRHEHaSLALaqrcsgvpapTPLFSALlnYRHSAAAAAAAALAAWEGIEL--LGGE 365
|
410
....*....|..
gi 2310915810 426 SRTT-QFDLSLD 436
Cdd:cd19544 366 ERTNyPLTLSVD 377
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
4673-5040 |
6.40e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 75.30 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT---PEDCELHFMSFA----FDGSHEGWMHPLIN 4745
Cdd:PRK08751 201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTgklEEGCEVVITALPlyhiFALTANGLVFMKIG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4746 GARVLI---RDDSLWLPErtyAEMHRHGVTVGVfpPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPK 4822
Cdd:PRK08751 281 GCNHLIsnpRDMPGFVKE---LKKTRFTAFTGV--NTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 YLFNGYGPTET----VVTPLLWKaragDACGAAYMPIGTllgnRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPA 4898
Cdd:PRK08751 356 TLVEAYGLTETspaaCINPLTLK----EYNGSIGLPIPS----TDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4899 LTAErfVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK08751 428 ETAK--VMDADG-----WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4979 LVGYVVAQEPAVADSPEAQAECRAQLKTalrerlpeYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08751 501 IVKVVIVKKDPALTAEDVKAHARANLTG--------YKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
4523-4924 |
7.81e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 75.30 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4523 GAIWNRSDSGYPATPL-VHQRVAERARMAPDAVAV---IFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQR 4596
Cdd:PRK08180 24 GTIYLRSAEPLGDYPRrLTDRLVHWAQEAPDRVFLaerGADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4597 SAEIMVAFLAVLKAGGAYVPLDIEYPR-----ERLLYMM----------QDSRAHLLLTHSHLLERLPI------PEGLS 4655
Cdd:PRK08180 104 SIEHALLALAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLelltpglvfaDDGAAFARALAAVVPADVEVvavrgaVPGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4656 CLSVDREEEWAGFPAHDPEV-ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYemtPEDCE-----LHFM- 4728
Cdd:PRK08180 184 ATPFAALLATPPTAAVDAAHaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF---PFLAEeppvlVDWLp 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4729 -SFAFDGSHE-GWMhpLINGARVLIrDDSLWLP---ERTYAEMHRhgvtvgVFPPVYL------QQLAEHAERD------ 4791
Cdd:PRK08180 261 wNHTFGGNHNlGIV--LYNGGTLYI-DDGKPTPggfDETLRNLRE------ISPTVYFnvpkgwEMLVPALERDaalrrr 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4792 --GNpppVRVYCFGGDAVAQASYD----LAWRALKPKYLF-NGYGPTETvvtpllwkaraGDACGAAYMPIgtllgNRSG 4864
Cdd:PRK08180 332 ffSR---LKLLFYAGAALSQDVWDrldrVAEATCGERIRMmTGLGMTET-----------APSATFTTGPL-----SRAG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4865 YI---LDG-QLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTR 4924
Cdd:PRK08180 393 NIglpAPGcEVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVR 449
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1019-1077 |
9.08e-13 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 66.05 E-value: 9.08e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1019 RTLAEIWQDLLGV--ERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRS 1077
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
3063-3525 |
1.10e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 74.40 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVG-ADRLVGVA--MERSIEMVVALMAIlkaGGAYVPVDPEYPEERQAYML---EDSGV 3136
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKlGDRVATIAwnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIInhaEDRVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 EL------LLSQSHLKLPlaqGVQR--IDLDR---------GAPWFEDY-SEANPDIH---LDGENLAYVIYTSGSTGKP 3195
Cdd:PRK06018 116 ITdltfvpILEKIADKLP---SVERyvVLTDAahmpqttlkNAVAYEEWiAEADGDFAwktFDENTAAGMCYTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3196 KGA--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVW--EFFWPlMSGARLVVaaPGDHRDPAKLVALINREG 3271
Cdd:PRK06018 193 KGVlySHRSNVLHALMANNGDALGTSAADTMLPVVPL-FHANSWgiAFSAP-SMGTKLVM--PGAKLDGASVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3272 VDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDA 3349
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQymEKEGLKLPHLKMVVCGGSAMP-RSMIKAFEDM-GVEVRHAWGMTEMSPLGTLAALKPPFSKL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3350 ---------VPIGRPIANLACYILD--GNLEPVPVGVLGELYLAGQGLARGYHQRPG--LTAERFvaspfvagermYRTG 3416
Cdd:PRK06018 347 pgdarldvlQKQGYPPFGVEMKITDdaGKELPWDGKTFGRLKVRGPAVAAAYYRVDGeiLDDDGF-----------FDTG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGDwREALAA 3491
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpkwDERPLLIVQLKPGETAT-REEILK 494
|
490 500 510
....*....|....*....|....*....|....
gi 2310915810 3492 HLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06018 495 YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
2358-2486 |
1.13e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.53 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGRDAMRg 2436
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrGKDPVAGERVKAKVISHEEID- 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2437 edlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAA 2486
Cdd:PRK08308 368 ---PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
4666-5036 |
1.15e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 75.00 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4666 AGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED----CELHFMSFAFDGsheGWMH 4741
Cdd:PRK06814 779 AGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDkvfnALPVFHSFGLTG---GLVL 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4742 PLINGARVLIRDDSL---WLPERTYAEmhrhGVTVGVFPPVYLQQLAEHAerdgNPPPVRV--YCFGGdavAQASYDLAW 4816
Cdd:PRK06814 856 PLLSGVKVFLYPSPLhyrIIPELIYDT----NATILFGTDTFLNGYARYA----HPYDFRSlrYVFAG---AEKVKEETR 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKY---LFNGYGPTET-----VVTPLLWKAragdacgaaympiGTLlgnrsGYILDG-QLNLLPV-GV--AGELYL 4884
Cdd:PRK06814 925 QTWMEKFgirILEGYGVTETapviaLNTPMHNKA-------------GTV-----GRLLPGiEYRLEPVpGIdeGGRLFV 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4885 GGEGVARGYL--ERPALtaerFVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPA 4962
Cdd:PRK06814 987 RGPNVMLGYLraENPGV----LEPPADG-----WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWP 1057
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4963 VREAVVVAQPGAV-GQQLVgyvvaqepAVADSPEAQaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK06814 1058 DALHAAVSIPDARkGERII--------LLTTASDAT---RAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
3052-3466 |
1.24e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 74.50 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLkLPLAQGVQRI-----------------------------DLDRGAPWFEDY-SEANPDIHL---- 3177
Cdd:PLN02479 114 EHSKSEVVMVDQEF-FTLAEEALKIlaekkkssfkppllivigdptcdpkslqyALGKGAIEYEKFlETGDPEFAWkppa 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 -DGENLAyVIYTSGSTGKPKGAGNRHS-----ALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPL--MSGARL 3249
Cdd:PLN02479 193 dEWQSIA-LGYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYLWTLPM-FHCNGWCFTWTLaaLCGTNI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVAapgdHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIV---CSGEALP----ADAQQQVFAKLPQA 3322
Cdd:PLN02479 266 CLR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPpsvlFAMSEKGFRVTHTY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3323 GLYNLYGPTEAAIDVTHWtcveegkDAVPIGRPiANLAC-----YI-LDG-------NLEPVPV--GVLGELYLAGQGLA 3387
Cdd:PLN02479 342 GLSETYGPSTVCAWKPEW-------DSLPPEEQ-ARLNArqgvrYIgLEGldvvdtkTMKPVPAdgKTMGEIVMRGNMVM 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3388 RGYHQRPGLTAERFVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 3466
Cdd:PLN02479 414 KGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1981-2417 |
1.28e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 74.31 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGgVAAAFAHQVASAPEAIALVCGD------EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVG 2054
Cdd:PRK12582 43 PLGPYPRS-IPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2055 LLGILKAGAGYLPLDPNYPA-----ERLAYM---------LRDSGARWLICQETLAERLPCPAEVERLPLETAAWP--AS 2118
Cdd:PRK12582 122 TLAAMQAGVPAAPVSPAYSLmshdhAKLKHLfdlvkprvvFAQSGAPFARALAALDLLDVTVVHVTGPGEGIASIAfaDL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2119 ADTRPLPEVAG-------ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASISFDAAAEQ 2188
Cdd:PRK12582 202 AATPPTAAVAAaiaaitpDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNHTMGGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2189 LFVPLLAGARVLLGDAGQWSAQHLADEV----ERHAVTILDLPPAY------LQQQAEELRHAGRRIavRTCILGGEAWD 2258
Cdd:PRK12582 282 NFNGLLWGGGTLYIDDGKPLPGMFEETIrnlrEISPTVYGNVPAGYamlaeaMEKDDALRRSFFKNL--RLMAYGGATLS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2259 ASLLTQ-QAVQAEA------WFNAYGPTEAVITPLAWHC---RAQEGGAPAIGRALgarracildaALQPCAPGMigELY 2328
Cdd:PRK12582 360 DDLYERmQALAVRTtghripFYTGYGATETAPTTTGTHWdteRVGLIGLPLPGVEL----------KLAPVGDKY--EVR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 IGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYrVDGQ-----VEYLGRADQQIKI-RGFRIEIGEIESQL 2402
Cdd:PRK12582 428 VKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARF-VDPDdpekgLIFDGRVAEDFKLsTGTWVSVGTLRPDA 499
|
490
....*....|....*..
gi 2310915810 2403 LA--HPYVAEAAVVALD 2417
Cdd:PRK12582 500 VAacSPVIHDAVVAGQD 516
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
525-998 |
1.28e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 74.29 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQSHLKlPLAQGVQRIdLDQADAWL--------ENHAENNPGI-ELNGENL-------------AYVI--- 659
Cdd:PLN03102 108 RHAKPKILFVDRSFE-PLAREVLHL-LSSEDSNLnlpvifihEIDFPKRPSSeELDYECLiqrgeptpslvarMFRIqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 660 -------YTSGSTGKPKGAGNRH-----SALSNRLCWMqqaygLGVGDTVLQKTPFsFDVSVWEFFWPlmSGARLVVAAP 727
Cdd:PLN03102 186 hdpislnYTSGTTADPKGVVISHrgaylSTLSAIIGWE-----MGTCPVYLWTLPM-FHCNGWTFTWG--TAARGGTSVC 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 728 GDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLYNL--YGP 803
Cdd:PLN03102 258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNslDLSPRSGPVHVLTGGSPPPA----ALVKKVQRLGFQVMhaYGL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 804 TEAAIDV------THWTCVEEGKDTVPIGRP-IGNLGCYILD----GNLEPVPVG--VLGELYLAGRGLARGYHQRPGLT 870
Cdd:PLN03102 334 TEATGPVlfcewqDEWNRLPENQQMELKARQgVSILGLADVDvknkETQESVPRDgkTMGEIVIKGSSIMKGYLKNPKAT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 871 AERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLV 946
Cdd:PLN03102 414 SEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwGETPC 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 947 GYVVLES--EGGDWREALAAHLA--------ASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PLN03102 487 AFVVLEKgeTTKEDRVDKLVTRErdlieycrENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
2011-2492 |
1.38e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 74.55 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CQETLaERLPCP-----------AEVER----------------LPLETAAWPASAD------------TRPLPEVAGET 2131
Cdd:PLN02654 198 TCNAV-KRGPKTinlkdivdaalDESAKngvsvgicltyenqlaMKREDTKWQEGRDvwwqdvvpnyptKCEVEWVDAED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2132 LAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQLQFASISfdAAAEQLFVPLLAGARVLL------ 2201
Cdd:PLN02654 277 PLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKyAFDYKPTDvywCTADCGWIT--GHSYVTYGPMLNGATVLVfegapn 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 -GDAGQ-WsaqhlaDEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRtcILG--GEAWDASlltqqavqaeAW-- 2272
Cdd:PLN02654 355 yPDSGRcW------DIVDKYKVTIFYTAPTLvrsLMRDGDEYVTRHSRKSLR--VLGsvGEPINPS----------AWrw 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 -FNAYG-----------PTEA---VITPL--AWHCRAQEGGAPAIGralgarracildaaLQPCAPGMIGElYIGGQCla 2335
Cdd:PLN02654 417 fFNVVGdsrcpisdtwwQTETggfMITPLpgAWPQKPGSATFPFFG--------------VQPVIVDEKGK-EIEGEC-- 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYL----GRPGQ------TAERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:PLN02654 480 SGYLcvkkSWPGAfrtlygDHERYETtyfKPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2403 LAHPYVAEAAVVALDG-VGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PLN02654 556 VSHPQCAEAAVVGIEHeVKGQGIYAFVTLVEGVPySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
570
....*....|..
gi 2310915810 2481 KVdaaARRQAGE 2492
Cdd:PLN02654 636 KI---ASRQLDE 644
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1012-1078 |
1.45e-12 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 66.03 E-value: 1.45e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 1012 APRNAVERTLAEIWQDLLGV--ERVGLDDNFFS-LGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRSL 1078
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADL 71
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2015-2479 |
1.51e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 73.86 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 LAER---LPCPAEV-ERLPLETA--------AWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCqaA 2162
Cdd:PLN02330 137 NYGKvkgLGLPVIVlGEEKIEGAvnwkelleAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANL--C 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2163 ARTYGVGPgDCQLQFASISF------DAAAEQLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDL-PPAYL---- 2231
Cdd:PLN02330 215 SSLFSVGP-EMIGQVVTLGLipffhiYGITGICCATLRNKGKVVV--MSRFELRTFLNALITQEVSFAPIvPPIILnlvk 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2232 QQQAEELRHAgrRIAVRTCILGGEAWDASLLTQ-----QAVQAEawfNAYGPTEAvitplawHCRAQEGGAPAIGRALGA 2306
Cdd:PLN02330 292 NPIVEEFDLS--KLKLQAIMTAAAPLAPELLTAfeakfPGVQVQ---EAYGLTEH-------SCITLTHGDPEKGHGIAK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRAC----------ILDAALQPCAP-GMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQ 2375
Cdd:PLN02330 360 KNSVgfilpnlevkFIDPDTGRSLPkNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW-------LHTGDIGYIDDDGD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2376 VEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV-GRDAMRGEDllaELRTWLAGRLPA 2453
Cdd:PLN02330 433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLpDEEAGEIPAACVViNPKAKESEE---DILNFVAANVAH 509
|
490 500
....*....|....*....|....*.
gi 2310915810 2454 YMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN02330 510 YKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
3050-3477 |
1.88e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 73.68 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP-EERQA 3128
Cdd:PLN02860 19 LRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfEEAKS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQS--HLKLPLAQGvqRI-----------DLDRGAPWFEDY-----------SEANPDIHLDGENLAY 3184
Cdd:PLN02860 99 AMLLVRPVMLVTDETcsSWYEELQND--RLpslmwqvflesPSSSVFIFLNSFlttemlkqralGTTELDYAWAPDDAVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrdpAKLV 3264
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFD----AKAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 -ALINREGVDTLHFVPSMLQAFLQ----DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:PLN02860 253 lQAIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTcVEEGKDAVPIGRPIANLACYILDGNLepvPVGV--------------LGELYLAGQGLARGYHQRPGLTAERFVASP 3405
Cdd:PLN02860 333 MT-LHDPTLESPKQTLQTVNQTKSSSVHQ---PQGVcvgkpaphvelkigLDESSRVGRILTRGPHVMLGYWGQNSETAS 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3406 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVV 3477
Cdd:PLN02860 409 VLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
4664-5040 |
2.08e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 74.19 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4664 EWAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELH----FMSFAFDGSHegW 4739
Cdd:PRK08633 772 KRLYGPTFKP------DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVTL--W 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4740 MhPLINGARVLIRDDSLwlPERTYAEM-HRHGVTVGVFPPVYLQQLAEH-----------------AERdgNPPPVRVyc 4801
Cdd:PRK08633 844 L-PLLEGIKVVYHPDPT--DALGIAKLvAKHRATILLGTPTFLRLYLRNkklhplmfaslrlvvagAEK--LKPEVAD-- 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4802 fggdavaqasydlawrALKPKY---LFNGYGPTET--VVTPLLWKARAGDAC-------GAAYMPI-GTllgnrSGYILD 4868
Cdd:PRK08633 917 ----------------AFEEKFgirILEGYGATETspVASVNLPDVLAADFKrqtgskeGSVGMPLpGV-----AVRIVD 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQ-LNLLPVGVAGELYLGGEGVARGYLERPALTAErFVPDpfgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqVKIR 4944
Cdd:PRK08633 976 PEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD---IDGIGWYVTGDKGHLDEDGfltITDRYSRF---AKIG 1048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4945 GFRIELGEIEARLREHPAVREAVVVAQpgAV-----GQQLVgyVVaqepaVADSPEAQAECRAQLKTAlreRLPEYMVPS 5019
Cdd:PRK08633 1049 GEMVPLGAVEEELAKALGGEEVVFAVT--AVpdekkGEKLV--VL-----HTCGAEDVEELKRAIKES---GLPNLWKPS 1116
|
410 420
....*....|....*....|.
gi 2310915810 5020 HLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08633 1117 RYFKVEALPLLGSGKLDLKGL 1137
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
518-951 |
2.66e-12 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 73.27 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 518 EEQVERtPTAPALAF----GEE-RLDYAELNRRANRLAHAL-----IERGigaDRlVGVAMERSIEMVVALMAILKAGGA 587
Cdd:cd05928 19 EKAGKR-PPNPALWWvngkGDEvKWSFRELGSLSRKAANVLsgacgLQRG---DR-VAVILPRVPEWWLVNVACIRTGLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 588 YVPVDPEYPEERQAYMLEDSGVQLLLSQSHLklplAQGVQRIDLD-------------QADAWLE-----NHAENNPGIE 649
Cdd:cd05928 94 FIPGTIQLTAKDILYRLQASKAKCIVTSDEL----APEVDSVASEcpslktkllvsekSRDGWLNfkellNEASTEHHCV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 650 LNGENLAYVIY-TSGSTGKPKGAGNRHSALSNRLC-----WMqqayGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARL 722
Cdd:cd05928 170 ETGSQEPMAIYfTSGTTGSPKMAEHSHSSLGLGLKvngryWL----DLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 723 VVaapgdHR----DPAKLVELINREGVDTLHFVPSMLQAFLQdEDVASCT--SLKRIVCSGEALPADAQQQVFAklpQAG 796
Cdd:cd05928 246 FV-----HHlprfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKfpSLQHCVTGGEPLNPEVLEKWKA---QTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 797 L--YNLYGPTEAAIdvthwTC-VEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR-----GLARGYHQR 866
Cdd:cd05928 317 LdiYEGYGQTETGL-----ICaNFKGMKIKPgsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 867 PGLTAERFVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDG 942
Cdd:cd05928 392 PEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspdpIRG 464
|
....*....
gi 2310915810 943 RQLVGYVVL 951
Cdd:cd05928 465 EVVKAFVVL 473
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
3052-3525 |
2.97e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.13 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLKlPLAQGVQRI---------------------------DLD------RGAP-------WFEDYSEA 3171
Cdd:PLN03102 108 RHAKPKILFVDRSFE-PLAREVLHLlssedsnlnlpvifiheidfpkrpsseELDyecliqRGEPtpslvarMFRIQDEH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 NPdIHLDgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWMqqaygLGVGDTVLQKTPFsFDVSVWEFFWPlmSG 3246
Cdd:PLN03102 187 DP-ISLN--------YTSGTTADPKGVVISHrgaylSTLSAIIGWE-----MGTCPVYLWTLPM-FHCNGWTFTWG--TA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL 3324
Cdd:PLN03102 250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNslDLSPRSGPVHVLTGGSPPPA----ALVKKVQRLGF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3325 YNL--YGPTEAAIDV------THWTCVEEGKDAVPIGRP-IANLACYILD----GNLEPVPVG--VLGELYLAGQGLARG 3389
Cdd:PLN03102 326 QVMhaYGLTEATGPVlfcewqDEWNRLPENQQMELKARQgVSILGLADVDvknkETQESVPRDgkTMGEIVIKGSSIMKG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3390 YHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD- 3468
Cdd:PLN03102 406 YLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPh 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3469 ---GRQLVGYVVLE-SESGDWREALAAHLAAS---------LPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PLN03102 479 ptwGETPCAFVVLEkGETTKEDRVDKLVTRERdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
4561-5012 |
4.05e-12 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 72.50 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLdieYPR---ERLLYMMQDSRAHL 4637
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 L---LTHSHLLERLPIPEGL-SCLS-----VDREEEWAGFPAHDP---EVALHG-DNLAYVIYTSGSTGMPKGVAVSHGP 4704
Cdd:cd05932 82 LfvgKLDDWKAMAPGVPEGLiSISLpppsaANCQYQWDDLIAQHPpleERPTRFpEQLATLIYTSGTTGQPKGVMLTFGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4705 LIAHIVATGERYEMTPEDCELHFMsfafdgshegwmhPLINGA-RVLIRDDSLWLPERTY---------AEMHRHGVTVG 4774
Cdd:cd05932 162 FAWAAQAGIEHIGTEENDRMLSYL-------------PLAHVTeRVFVEGGSLYGGVLVAfaesldtfvEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4775 VFPPvYLQQLAEHAERDGNPP---------PVRVYCFGGDAVAQASYDlawralKPKYLFNGYGPTETVVtpLLWKARAG 4845
Cdd:cd05932 229 FSVP-RLWTKFQQGVQDKIPQqklnlllkiPVVNSLVKRKVLKGLGLD------QCRLAGCGSAPVPPAL--LEWYRSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4846 -DACGA-------AYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrl 4916
Cdd:cd05932 300 lNILEAygmtenfAYSHLNYPGRDKIGTVGNaGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVrEAVVVAqpGAVGQQLVGYVVAQEPAVadsPE 4995
Cdd:cd05932 373 LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVI--GSGLPAPLALVVLSEEAR---LR 446
|
490
....*....|....*..
gi 2310915810 4996 AQAECRAQLKTALRERL 5012
Cdd:cd05932 447 ADAFARAELEASLRAHL 463
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1981-2166 |
4.07e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 72.99 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGgVAAAFAHQVASAPEAIALV--CGDE---HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGL 2055
Cdd:PRK08180 33 PLGDYPRR-LTDRLVHWAQEAPDRVFLAerGADGgwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2056 LGILKAGAGYLPLDPNYPA-----ERLAYMLR---------DSGARWlicQETLAErlPCPAEVERL-------PLETAA 2114
Cdd:PRK08180 112 LAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLElltpglvfaDDGAAF---ARALAA--VVPADVEVVavrgavpGRAATP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2115 WPASADTRPLPEVA-------GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTY 2166
Cdd:PRK08180 187 FAALLATPPTAAVDaahaavgPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF 245
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
3063-3480 |
4.23e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 72.87 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPV----DPEYPEERqaymLEDSGVE 3137
Cdd:PRK00174 98 KITYRELHREVCRFANALKSLGVKKgDR-VAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADR----IIDAGAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3138 LLL---------SQSHLK------LPLAQGVQR----------IDLDRGAP-WFEDYSEANPDIH----LDGENLAYVIY 3187
Cdd:PRK00174 173 LVItadegvrggKPIPLKanvdeaLANCPSVEKvivvrrtggdVDWVEGRDlWWHELVAGASDECepepMDAEDPLFILY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKG-----AGnrhsalsnrlcWMQQAYglgvgdtvlQKTPFSFDVSVWEFFW-----------------PLMS 3245
Cdd:PRK00174 253 TSGSTGKPKGvlhttGG-----------YLVYAA---------MTMKYVFDYKDGDVYWctadvgwvtghsyivygPLAN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVAScTSLK--RIVCS-GEalPADaqqqvfak 3318
Cdd:PRK00174 313 GATTLMfeGVP-NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKK-YDLSslRLLGSvGE--PIN-------- 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3319 lPQAGL--YNLYGPTEAAIDVTHW-TcvEEG-------KDAVPI-----GRPIANLACYILDGNLEPVPVGVLGELYLAG 3383
Cdd:PRK00174 381 -PEAWEwyYKVVGGERCPIVDTWWqT--ETGgimitplPGATPLkpgsaTRPLPGIQPAVVDEEGNPLEGGEGGNLVIKD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3384 Q--GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 3461
Cdd:PRK00174 458 PwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
|
490 500
....*....|....*....|...
gi 2310915810 3462 AAVL----AVDGRQLVGYVVLES 3480
Cdd:PRK00174 534 AAVVgrpdDIKGQGIYAFVTLKG 556
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
523-950 |
4.51e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.52 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP-EERQA 601
Cdd:PLN02860 19 LRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfEEAKS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 602 YMLEDSGVQLLLSQS------------------HLKLPLAQGVQRIDLDQA----DAWLENHAENNPGIELNGENLAYVI 659
Cdd:PLN02860 99 AMLLVRPVMLVTDETcsswyeelqndrlpslmwQVFLESPSSSVFIFLNSFltteMLKQRALGTTELDYAWAPDDAVLIC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrdpAKLV-E 738
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFD----AKAAlQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 739 LINREGVDTLHFVPSMLQAFLQ----DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWT 814
Cdd:PLN02860 255 AIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 815 cVEEGKDTVPIGRPIGNLGCYILDGNLepvPVGV--------------LGELYLAGRGLARGYHQRPGLTAERFVASPFV 880
Cdd:PLN02860 335 -LHDPTLESPKQTLQTVNQTKSSSVHQ---PQGVcvgkpaphvelkigLDESSRVGRILTRGPHVMLGYWGQNSETASVL 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVV 950
Cdd:PLN02860 411 SNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
2124-2479 |
5.07e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.03 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2124 LPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARV 2199
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVT---LWLPLLEGIKV 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2200 LLG----DAGQwsaqhLADEVERHAVTILDLPPAYLQ-----QQAEELRHAGRRIAVrtciLGGEawdaSLLTQQAVQAE 2270
Cdd:PRK08633 853 VYHpdptDALG-----IAKLVAKHRATILLGTPTFLRlylrnKKLHPLMFASLRLVV----AGAE----KLKPEVADAFE 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2271 AWFN-----AYGPTEavITPLA------------WHCRAQEGGApaIGRALGARRACILDA-ALQPCAPGMIGELYIGGQ 2332
Cdd:PRK08633 920 EKFGirileGYGATE--TSPVAsvnlpdvlaadfKRQTGSKEGS--VGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGP 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYLGRPGQTAErFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA- 2411
Cdd:PRK08633 996 QVMKGYLGDPEKTAE-VIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVv 1071
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2412 -AVVAL-DGVGGPLLAAyLVGRDAMRGEDLLAELrtwLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK08633 1072 fAVTAVpDEKKGEKLVV-LHTCGAEDVEELKRAI---KESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1554-1767 |
5.19e-12 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 71.51 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQgmLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDG-WpqplQVVFEQATLEL 1629
Cdd:cd19534 3 PLTPIQR--WFFEQNLAGRHHFNQsvlLRVP-QGLDPDALRQALRALVEHHDALRMRFRREDGgW----QQRIRGDVEEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 -RL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSnAQLLAEVL-----QRY 1697
Cdd:cd19534 76 fRLevvdlsSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVS-WRILLEDLeaayeQAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1698 AGQEVAA-TVGRYRDYIGWLQ---GRDAMATEF-FWRDRLASL--EMP---TRLARQARTEQpgqgehlRELDPQTTRQL 1767
Cdd:cd19534 155 AGEPIPLpSKTSFQTWAELLAeyaQSPALLEELaYWRELPAADywGLPkdpEQTYGDARTVS-------FTLDEEETEAL 227
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2002-2492 |
5.28e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.29 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIC--------QETLAE-----------RLPCPAEVERL-PLETAAWPASAD---TRPLPEVAGETLAyVIYT 2138
Cdd:PRK08162 112 RHGEAKVLIVdtefaevaREALALlpgpkplvidvDDPEYPGGRFIgALDYEAFLASGDpdfAWTLPADEWDAIA-LNYT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2139 SGSTGQPKGVAVSQ--AALVAhcQAAARTYGVGP--------------GDCqlqFASIsfdaaaeqlfVPLLAGARVLLG 2202
Cdd:PRK08162 191 SGTTGNPKGVVYHHrgAYLNA--LSNILAWGMPKhpvylwtlpmfhcnGWC---FPWT----------VAARAGTNVCLR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2203 DAgqwSAQHLADEVERHAVTILDLPPAYLQQ--QAEELRHAGRRIAVRTCIlGGEAWDASLLtqqAVQAEAWFN---AYG 2277
Cdd:PRK08162 256 KV---DPKLIFDLIREHGVTHYCGAPIVLSAliNAPAEWRAGIDHPVHAMV-AGAAPPAAVI---AKMEEIGFDlthVYG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2278 PTEAV--ITPLAWHcrAQEGGAPAIGRA-LGARR---------ACILDAA-LQPC-APG-MIGELYIGGQCLARGYLGRP 2342
Cdd:PRK08162 329 LTETYgpATVCAWQ--PEWDALPLDERAqLKARQgvryplqegVTVLDPDtMQPVpADGeTIGEIMFRGNIVMKGYLKNP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2343 GQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGG 2421
Cdd:PRK08162 407 KATEEAFAGGWF--------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKpDPKWG 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 2422 PLLAAYLVGRDAM--RGEDLLAELRTWLAGrlpaYMQPTAWqVLSSLPLNANGKLDRKALpkvdaaaRRQAGE 2492
Cdd:PRK08162 479 EVPCAFVELKDGAsaTEEEIIAHCREHLAG----FKVPKAV-VFGELPKTSTGKIQKFVL-------REQAKS 539
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
5061-5120 |
7.06e-12 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 63.35 E-value: 7.06e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 5061 QQVAGIWAEVLQL--QQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQA 5120
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
2276-2479 |
8.01e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 71.78 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTE----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVA 2351
Cdd:PRK12492 365 YGLTEtspvASTNPYGELARLGTVGIPVPGTALK-----VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVG 2430
Cdd:PRK12492 440 -------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVpDERSGEAVKLFVVA 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2310915810 2431 RDAMRGEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK12492 513 RDPGLSVE---ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
4564-5037 |
8.78e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 71.57 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR----------ERLLYMMQDS 4633
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRtdlavwaedtLRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4634 RAHLLLTHSHLLERLPiPEGLSCLSVDreEEWAGFPAHDPEVAlhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATG 4713
Cdd:PRK07768 111 AVVVGEPFLAAAPVLE-EKGIRVLTVA--DLLAADPIDPVETG--EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4714 ERYEMTPE-DCELHFMSFAFDGSHEGWMH-PLINGARVL-------IRDDSLWlpertyAEM-HRHGVTVGVFPP-VY-- 4780
Cdd:PRK07768 186 VAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVkvtpmdfLRDPLLW------AELiSKYRGTMTAAPNfAYal 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 ----LQQLAEHAERD---------G----NPPPVRVYC-----FG--GDAVAQAsYDLAWRALKPKYLFNGYGPTETVVT 4836
Cdd:PRK07768 260 larrLRRQAKPGAFDlsslrfalnGaepiDPADVEDLLdagarFGlrPEAILPA-YGMAEATLAVSFSPCGAGLVVDEVD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKA--RAGDACGA---AYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYlerpaLTAERFVP--DPF 4909
Cdd:PRK07768 339 ADLLAAlrRAVPATKGntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaqDAD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4910 GapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPA 4989
Cdd:PRK07768 414 G-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESN 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2310915810 4990 VADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PRK07768 489 AFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRR 536
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3645-3916 |
8.95e-12 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 70.81 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAE-HAEATLGgallwrAEAVDRQALES------LCE 3717
Cdd:cd20484 24 YNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKiEPSKPLS------FQEEDISSLKEseiiayLRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3718 ESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRL---PGKTSPFKAWAGR 3794
Cdd:cd20484 98 KAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLassPASYYDFVAWEQD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3795 VSEHARGESMKAqlqFWRELLEGA-PA-ELPCEHPqGALEQRFATSVQSrfdRSLTERLLKQAPA---AYRTQVNDLLLT 3869
Cdd:cd20484 178 MLAGAEGEEHRA---YWKQQLSGTlPIlELPADRP-RSSAPSFEGQTYT---RRLPSELSNQIKSfarSQSINLSTVFLG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2310915810 3870 ALARVVCRWSGASSSLVQLEGHGR-EELFADIdlsrtVGWFTSLFPVR 3916
Cdd:cd20484 251 IFKLLLHRYTGQEDIIVGMPTMGRpEERFDSL-----IGYFINMLPIR 293
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
3634-4038 |
8.97e-12 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 70.86 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3634 FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT---WHAEHAEATLGGALLWRAEAVDRQ 3710
Cdd:cd19533 13 FAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEpyqWIDPYTPVPIRHIDLSGDPDPEGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3711 ALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPrlpgKTSPFKA 3790
Cdd:cd19533 93 AQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA----PPAPFGS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3791 WAGRV-SEHARGESMKAQ--LQFWRELLEGAPaELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVNDLL 3867
Cdd:cd19533 169 FLDLVeEEQAYRQSERFErdRAFWTEQFEDLP-EPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAA-EAHGASWPSFF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3868 LTALARVVCRWSGASSSLVQLEGHGReelfADIDLSRTVGWFTSLFPVRL--SPVADLGESLKAIKEQLRAI-PDKGLGY 3944
Cdd:cd19533 247 IALVAAYLHRLTGANDVVLGVPVMGR----LGAAARQTPGMVANTLPLRLtvDPQQTFAELVAQVSRELRSLlRHQRYRY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3945 GLLRYLAGEESARVlaglPQARITFNYLgQFDAQFDEMallDPAGESAGAEMDPGAPLDNWLSlnGRVFDGELSIDWSFS 4024
Cdd:cd19533 323 EDLRRDLGLTGELH----PLFGPTVNYM-PFDYGLDFG---GVVGLTHNLSSGPTNDLSIFVY--DRDDESGLRIDFDAN 392
|
410
....*....|....
gi 2310915810 4025 SQMFGEDQVRRLAD 4038
Cdd:cd19533 393 PALYSGEDLARHQE 406
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
525-939 |
8.99e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.41 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 605 EDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLE-----------------NHAENNPGIE----LNGENLAYVI---- 659
Cdd:PLN02479 114 EHSKSEVVMVDQEF-FTLAEEALKILAEKKKSSFKppllivigdptcdpkslQYALGKGAIEyekfLETGDPEFAWkppa 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 660 ---------YTSGSTGKPKGAGNRHS-----ALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPL--MSGARLV 723
Cdd:PLN02479 193 dewqsialgYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYLWTLPM-FHCNGWCFTWTLaaLCGTNIC 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 724 VAapgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIV---CSGEALP----ADAQQQVFAKLPQAG 796
Cdd:PLN02479 267 LR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPpsvlFAMSEKGFRVTHTYG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 797 LYNLYGPTEAAIDVTHWtcveegkDTVPIG-----------RPIGNLGCYILD-GNLEPVPV--GVLGELYLAGRGLARG 862
Cdd:PLN02479 343 LSETYGPSTVCAWKPEW-------DSLPPEeqarlnarqgvRYIGLEGLDVVDtKTMKPVPAdgKTMGEIVMRGNMVMKG 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 863 YHQRPGLTAERFVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PLN02479 416 YLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3645-3883 |
9.31e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 72.38 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDG---TWH-AEHAEATLGGALLWRAEAVDRQALESLCEESQ 3720
Cdd:PRK10252 30 WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGevwQWVdPALTFPLPEIIDLRTQPDPHAAAQALMQADLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3721 RSLDLTDG-PLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRlpgkTSPFKAWAGRVSEHA 3799
Cdd:PRK10252 110 QDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTP----ASPFTPFADVVEEYQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3800 R---GESMKAQLQFWRELLEGAPAelPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVN--DLLLTALARV 3874
Cdd:PRK10252 186 RyraSEAWQRDAAFWAEQRRQLPP--PASLSPAPLPGRSASADILRLKLEFTDGAFRQL-AAQASGVQrpDLALALVALW 262
|
....*....
gi 2310915810 3875 VCRWSGASS 3883
Cdd:PRK10252 263 LGRLCGRMD 271
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
536-953 |
1.10e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 71.33 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 536 RLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPV----DPEYPEERqaymLEDSGVQ 610
Cdd:PRK00174 98 KITYRELHREVCRFANALKSLGVKKgDR-VAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADR----IIDAGAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 611 LLL---------SQSHLK------LPLAQGVQR----------IDLDQA-DAW----LENHAENNPGIELNGENLAYVIY 660
Cdd:PRK00174 173 LVItadegvrggKPIPLKanvdeaLANCPSVEKvivvrrtggdVDWVEGrDLWwhelVAGASDECEPEPMDAEDPLFILY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 661 TSGSTGKPKG-----AGnrhsalsnrlcWMQQAYglgvgdtvlQKTPFSFDVSVWEFFW-----------------PLMS 718
Cdd:PRK00174 253 TSGSTGKPKGvlhttGG-----------YLVYAA---------MTMKYVFDYKDGDVYWctadvgwvtghsyivygPLAN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 719 GARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVAScTSLK--RIVCS-GEalPADaqqqvfak 791
Cdd:PRK00174 313 GATTLMfeGVP-NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKK-YDLSslRLLGSvGE--PIN-------- 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 792 lPQAGL--YNLYGPTEAAIDVTHW-TcvEEG----------KDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGelYLAG 856
Cdd:PRK00174 381 -PEAWEwyYKVVGGERCPIVDTWWqT--ETGgimitplpgaTPLKPgsATRPLPGIQPAVVDEEGNPLEGGEGG--NLVI 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 857 R----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:PRK00174 456 KdpwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKV 531
|
490 500
....*....|....*....|....*
gi 2310915810 933 REAAVL----AVDGRQLVGYVVLES 953
Cdd:PRK00174 532 AEAAVVgrpdDIKGQGIYAFVTLKG 556
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
2321-2489 |
1.19e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 70.79 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2321 PGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIES 2400
Cdd:PRK07445 298 ANQTGNITIQAQSLALGYYPQILDSQGIFE-------------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2401 QLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07445 365 AILATGLVQDVCVLGLpDPHWGEVVTAIYVPKD---PSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
170
....*....|
gi 2310915810 2480 PKVdAAARRQ 2489
Cdd:PRK07445 442 QQI-AVQRLG 450
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
534-951 |
1.24e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 71.47 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 614 SQSHLKlplaQGVQRIDL-DQADAWLENHAEN--NPGIELNGENLA---------------------------------- 656
Cdd:PLN02654 198 TCNAVK----RGPKTINLkDIVDAALDESAKNgvSVGICLTYENQLamkredtkwqegrdvwwqdvvpnyptkcevewvd 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 657 -----YVIYTSGSTGKPKGAgnRHSAlsnrlcwmqqayglgVGDTVLQKTPF--SFDVSVWEFFW--------------- 714
Cdd:PLN02654 274 aedplFLLYTSGSTGKPKGV--LHTT---------------GGYMVYTATTFkyAFDYKPTDVYWctadcgwitghsyvt 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 715 --PLMSGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQ 786
Cdd:PLN02654 337 ygPMLNGATVLVfeGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLGSVGEPINPSAWR 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 787 QvfaklpqagLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGrpignlGCYILDGN--------LEPVPVG-----VLGEL- 852
Cdd:PLN02654 416 W---------FFNVVGDSRCPISDTWWQTETGGFMITPLP------GAWPQKPGsatfpffgVQPVIVDekgkeIEGECs 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 853 -YLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:PLN02654 481 gYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
|
490 500
....*....|....*....|....
gi 2310915810 932 VREAAVLAVD----GRQLVGYVVL 951
Cdd:PLN02654 561 CAEAAVVGIEhevkGQGIYAFVTL 584
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
519-1000 |
1.31e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.81 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 519 EQVERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK05857 22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 597 EERQAYMLEDSGVQLLL--------SQSHLKLPLAQGVQRIDLDQADAWLENHAENN-PGIELN---GENLAyVIYTSGS 664
Cdd:PRK05857 102 IAAIERFCQITDPAAALvapgskmaSSAVPEALHSIPVIAVDIAAVTRESEHSLDAAsLAGNADqgsEDPLA-MIFTSGT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 665 TGKPKGAgnrhsALSNRLCW----MQQAYGLG-----VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHrdPAK 735
Cdd:PRK05857 181 TGEPKAV-----LLANRTFFavpdILQKEGLNwvtwvVGETTYSPLPATHIGGLWWILTCLMHGGLCVTG--GEN--TTS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 736 LVELINREGVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSG-EALPADAQ---------QQVFAkLPQAGLYNLYGP 803
Cdd:PRK05857 252 LLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGsRAIAADVRfieatgvrtAQVYG-LSETGCTALCLP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 804 TeaaiDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGN------LEPVPVGVLGELYLAGRGLARGYHQRPGLTAErfvas 877
Cdd:PRK05857 331 T----DDGSIVKIEAGA----VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE----- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 878 pfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH-PWVREAAVLAVDGRQ---LVGYVV--- 950
Cdd:PRK05857 398 --VLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVREAACYEIPDEEfgaLVGLAVvas 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 951 --LESEGGDWREALAAHLAASLPEYMV-PAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:PRK05857 475 aeLDESAARALKHTIAARFRRESEPMArPSTIVIVTDIPRTQSGKVMRASLAA 527
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
3043-3467 |
1.33e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 70.85 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGvgaDRlVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLqnglgLKKG---DR-VALMMPNLLQYPIALFGILRAGMIVVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEY-PEERQaYMLEDSG-------------VELLLSQSHLK----------LPLAQG-------------VQRIDLDR 3160
Cdd:PRK08974 104 VNPLYtPRELE-HQLNDSGakaivivsnfahtLEKVVFKTPVKhviltrmgdqLSTAKGtlvnfvvkyikrlVPKYHLPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3161 GAPWFEDYSEA------NPDIhlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG--LGVG-DTVLQKTP-- 3229
Cdd:PRK08974 183 AISFRSALHKGrrmqyvKPEL--VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGkELVVTALPly 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3230 --FSFDVSVWEFFWplMSGARLVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGE 3305
Cdd:PRK08974 261 hiFALTVNCLLFIE--LGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGGM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3306 ALpadaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTcveeGKdavpIGRPIANLACYILDGNLEPVPVGV 3375
Cdd:PRK08974 336 AV----QQAVaerWVKLTGQYLLEGYGLTECSplvsvnpYDLDYYS----GS----IGLPVPSTEIKLVDDDGNEVPPGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3376 LGELYLAGQGLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:PRK08974 404 PGELWVKGPQVMLGYWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
|
490
....*....|..
gi 2310915810 3456 HPWVREAAVLAV 3467
Cdd:PRK08974 477 HPKVLEVAAVGV 488
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
4530-5034 |
1.43e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 71.00 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4530 DSGYPATPLVHQRVAER-ARMA---PDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVA 4603
Cdd:PRK08315 5 VRGPTDVPLLEQTIGQLlDRTAaryPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4604 FLAVLKAGGAYVPLDIEYPRERLLYMMQDS-------------------------RAHLLLTHSHLLERLPipeGLSCLS 4658
Cdd:PRK08315 85 QFATAKIGAILVTINPAYRLSELEYALNQSgckaliaadgfkdsdyvamlyelapELATCEPGQLQSARLP---ELRRVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4659 VDREEEWAGFP-----------AHDPEVA-----LHGDNLAYVIYTSGSTGMPKGVAVSH------GPLIahivatGERY 4716
Cdd:PRK08315 162 FLGDEKHPGMLnfdellalgraVDDAELAarqatLDPDDPINIQYTSGTTGFPKGATLTHrnilnnGYFI------GEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4717 EMTPED--------------------CELH-----FMSFAFDgshegwmhplingarvlirddslwlPERTYAEMHR--- 4768
Cdd:PRK08315 236 KLTEEDrlcipvplyhcfgmvlgnlaCVTHgatmvYPGEGFD-------------------------PLATLAAVEEerc 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 ---HGVtvgvfPPVYLQQLaEHAERD-------------GNPPPVRVycfggdavaqasydlAWRALKPKYLFN---GYG 4829
Cdd:PRK08315 291 talYGV-----PTMFIAEL-DHPDFArfdlsslrtgimaGSPCPIEV---------------MKRVIDKMHMSEvtiAYG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4830 PTETvvTPLLWKARAGDacgaaymPI-------GTLLGNRSGYILDGQLN-LLPVGVAGELYLGGEGVARGYLERPALTA 4901
Cdd:PRK08315 350 MTET--SPVSTQTRTDD-------PLekrvttvGRALPHLEVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4902 ERFVPDpfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVkIRGfrielG------EIEARLREHPAVREAVVVAQPGA- 4974
Cdd:PRK08315 421 EAIDAD-------GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVVGVPDEk 487
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4975 VGQQLVGYVVAQEPAVADSPEAQAECRAQLKTalrerlpeYMVPSHLLFLARMPLTPNGK 5034
Cdd:PRK08315 488 YGEEVCAWIILRPGATLTEEDVRDFCRGKIAH--------YKIPRYIRFVDEFPMTVTGK 539
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
4531-5040 |
1.62e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.81 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPLvhQRVAERARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVL 4608
Cdd:PRK05857 10 PQLPSTVL--DRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4609 KAGGAYVPLDIEYPRERLLYMMQDSR-AHLLLTHSHLLERLPIPEGLSCLSVDREE--EWAGFPAHDPEVALHGDNLAY- 4684
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIERFCQITDpAAALVAPGSKMASSAVPEALHSIPVIAVDiaAVTRESEHSLDAASLAGNADQg 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 ------VIYTSGSTGMPKGVAVSHGPLIAH---IVATGERYeMTPEDCELHFMSFAfdGSHEG--W--MHPLINGARVLI 4751
Cdd:PRK05857 168 sedplaMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNW-VTWVVGETTYSPLP--ATHIGglWwiLTCLMHGGLCVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 -RDDSLWLPERtyaeMHRHGVTVGVFPPVYLQQL-AEHAERDGNPPPVRVYCFGGDAVAQAsyDLAWRALKPKYLFNGYG 4829
Cdd:PRK05857 245 gGENTTSLLEI----LTTNAVATTCLVPTLLSKLvSELKSANATVPSLRLVGYGGSRAIAA--DVRFIEATGVRTAQVYG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4830 PTETVVTPL--------LWKARAGdACGAAYMPIGTLLGNRSGyildGQLNLLPVGVA---GELYLGGEGVARGYLERPA 4898
Cdd:PRK05857 319 LSETGCTALclptddgsIVKIEAG-AVGRPYPGVDVYLAATDG----IGPTAPGAGPSasfGTLWIKSPANMLGYWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4899 LTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK05857 394 RTAEVLI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGA 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4979 LVGYVVAqepAVADSPEAQAECRAQLKTALRERLPEYMV-PSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK05857 466 LVGLAVV---ASAELDESAARALKHTIAARFRRESEPMArPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1098-1317 |
1.63e-11 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 70.14 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1098 VALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAY--AEQAGEPLW 1173
Cdd:cd19540 2 IPLSFAQQrlWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1174 RRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSS 1253
Cdd:cd19540 82 VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 1254 S-------YQTWSRHL--HEQAGARL--DELDYWQAQLHDAP--HALPCENPHGALENRHERKLVLTLDAERTRQLL 1317
Cdd:cd19540 162 PlpvqyadYALWQRELlgDEDDPDSLaaRQLAYWRETLAGLPeeLELPTDRPRPAVASYRGGTVEFTIDAELHARLA 238
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
2012-2367 |
1.63e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 70.74 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPA---ERLAYMLRDSGARW 2088
Cdd:PRK05850 34 ETLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LI------------CQETLAERLPCPAEVERLPLETAAwPASADTRPLPEVAgetlaYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK05850 113 VLttsavvddvteyVAPQPGQSAPPVIEVDLLDLDSPR-GSDARPRDLPSTA-----YLQYTSGSTRTPAGVMVSHRNVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTY-----GVGPGDCqlqfASISF-----DAAAEQ-LFVPLLAGARVLLgdagqwsaqhladeveRHAVTILD 2225
Cdd:PRK05850 187 ANFEQLMSDYfgdtgGVPPPDT----TVVSWlpfyhDMGLVLgVCAPILGGCPAVL----------------TSPVAFLQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2226 LPPAYLQQQAE-------------ELrhAGRRI-----------AVRTCILGGEAWDASLLtQQAVQAEAWFN------- 2274
Cdd:PRK05850 247 RPARWMQLLASnphafsaapnfafEL--AVRKTsdddmagldlgGVLGIISGSERVHPATL-KRFADRFAPFNlretair 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 -AYGPTEAVI---------TPLAWHCRAQ-------EGGAPAIGRAL---GARRACIL-----DAALQpCAPGMIGELYI 2329
Cdd:PRK05850 324 pSYGLAEATVyvatrepgqPPESVRFDYEklsaghaKRCETGGGTPLvsyGSPRSPTVrivdpDTCIE-CPAGTVGEIWV 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2310915810 2330 GGQCLARGYLGRPGQTAERF---VADPFSGSGERLY-RTGDL 2367
Cdd:PRK05850 403 HGDNVAAGYWQKPEETERTFgatLVDPSPGTPEGPWlRTGDL 444
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
516-940 |
1.72e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 70.82 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK07059 28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 596 PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQ---------------------------ADAW-LENHAENNPG 647
Cdd:PRK07059 108 TPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHvvvasmgdllgfkghivnfvvrrvkkmVPAWsLPGHVRFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 648 I-----------ELNGENLAYVIYTSGSTGKPKGAGNRHS-ALSNRL---CWMQQAYGLGVGDTVLQ---KTP----FSF 705
Cdd:PRK07059 188 LaegarqtfkpvKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLqmeAWLQPAFEKKPRPDQLNfvcALPlyhiFAL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 706 DVSvweFFWPLMSGAR-LVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALpa 782
Cdd:PRK07059 268 TVC---GLLGMRTGGRnILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKldFSKLIVANGGGMAV-- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 783 daQQQV---FAKLPQAGLYNLYGPTEAAIDVThwtC--VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR 857
Cdd:PRK07059 340 --QRPVaerWLEMTGCPITEGYGLSETSPVAT---CnpVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 858 GLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 937
Cdd:PRK07059 415 QVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAA 488
|
...
gi 2310915810 938 LAV 940
Cdd:PRK07059 489 VGV 491
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
3538-3606 |
1.94e-11 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 62.95 E-value: 1.94e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3538 APQNEMERRIAAVWADVLKL--EEVGATDNFFA-LGGDSIVSIQVVSRCRAA-GIQFTPKDLFQQQTVQGLAR 3606
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLAD 73
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
4902-5040 |
2.03e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 70.75 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4902 ERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLV 4980
Cdd:PRK10524 460 DRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALkGQVAV 539
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4981 GYVVAQEPAVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK10524 540 AFVVPKDSDSLADREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
3061-3478 |
2.71e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 70.31 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 SQSHLKlplaQGVQRIDL--------DRGAP------------------------------WFEDYSEANP---DIH-LD 3178
Cdd:PLN02654 198 TCNAVK----RGPKTINLkdivdaalDESAKngvsvgicltyenqlamkredtkwqegrdvWWQDVVPNYPtkcEVEwVD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3179 GENLAYVIYTSGSTGKPKGAgnRHSAlsnrlcwmqqayglgVGDTVLQKTPF--SFDVSVWEFFW--------------- 3241
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGV--LHTT---------------GGYMVYTATTFkyAFDYKPTDVYWctadcgwitghsyvt 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3242 --PLMSGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQ 3313
Cdd:PLN02654 337 ygPMLNGATVLVfeGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLGSVGEPINPSAWR 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3314 QvfaklpqagLYNLYGPTEAAIDVTHWTCVEEGKDAVPIgrPIA-----NLACYILDGnLEPVPVGVLG-ELylagQGLA 3387
Cdd:PLN02654 416 W---------FFNVVGDSRCPISDTWWQTETGGFMITPL--PGAwpqkpGSATFPFFG-VQPVIVDEKGkEI----EGEC 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3388 RGY----HQRPGL------TAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:PLN02654 480 SGYlcvkKSWPGAfrtlygDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHP 559
|
490 500
....*....|....*....|....*
gi 2310915810 3458 WVREAAVLAVD----GRQLVGYVVL 3478
Cdd:PLN02654 560 QCAEAAVVGIEhevkGQGIYAFVTL 584
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
3043-3467 |
2.88e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 70.05 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK07059 28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLD-------------RGA--------------PW-------FEDY 3168
Cdd:PRK07059 108 TPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKhvvvasmgdllgfKGHivnfvvrrvkkmvpAWslpghvrFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3169 SEA------NPdIHLDGENLAYVIYTSGSTGKPKGAGNRHS-ALSNRL---CWMQQAYGLGVGDTVLQ---KTP----FS 3231
Cdd:PRK07059 188 LAEgarqtfKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLqmeAWLQPAFEKKPRPDQLNfvcALPlyhiFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 FDVSvweFFWPLMSGAR-LVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALp 3308
Cdd:PRK07059 267 LTVC---GLLGMRTGGRnILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKldFSKLIVANGGGMAV- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3309 adaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTCVeegkdavpIGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:PRK07059 340 ---QRPVaerWLEMTGCPITEGYGLSETSpvatcnpVDATEFSGT--------IGLPLPSTEVSIRDDDGNDLPLGEPGE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:PRK07059 409 ICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482
|
....*....
gi 2310915810 3459 VREAAVLAV 3467
Cdd:PRK07059 483 VLEVAAVGV 491
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
4546-5034 |
3.00e-11 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 69.99 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEE----KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV---P-- 4616
Cdd:cd05943 78 RHADADDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSscsPdf 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4617 -----LD----IEyPreRLL-----YMMQDSRAHLLLTHSHLLERLP-------IPEGLSCLSVDREEE-----WAGFPA 4670
Cdd:cd05943 158 gvpgvLDrfgqIE-P--KVLfavdaYTYNGKRHDVREKVAELVKGLPsllavvvVPYTVAAGQPDLSKIakaltLEDFLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPEVALH-----GDNLAYVIYTSGSTGMPKGVAVSH-GPLIAHIVATGERYEMTPEDcELHFMSFAfdgsheGWM--HP 4742
Cdd:cd05943 235 TGAAGELEfeplpFDHPLYILYSSGTTGLPKCIVHGAgGTLLQHLKEHILHCDLRPGD-RLFYYTTC------GWMmwNW 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 LIN----GARVLIRDDSLWLP--ERTYAEMHRHGVTVGVFPPVYLQQLaehaERDGNPPP-------VRVYCFGGDAVAQ 4809
Cdd:cd05943 308 LVSglavGATIVLYDGSPFYPdtNALWDLADEEGITVFGTSAKYLDAL----EKAGLKPAethdlssLRTILSTGSPLKP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4810 ASYDLAWRALKPKYLFNGY-GPTetvvtpllwkaragDACGAaympigTLLGNRSGYILDGQLNLLPVGVAGELYLG--- 4885
Cdd:cd05943 384 ESFDYVYDHIKPDVLLASIsGGT--------------DIISC------FVGGNPLLPVYRGEIQCRGLGMAVEAFDEegk 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4886 ------GEGV-ARGYLERPAltaeRFVPDPFGA----------PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd05943 444 pvwgekGELVcTKPFPSMPV----GFWNDPDGSryraayfakyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRI 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaECRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd05943 518 GTAEIYRVVEKIPEVEDSLVVGQEWKDGdERVILFVKLREGVELDD-----ELRKRIRSTIRSALSPRHVPAKIIAVPDI 592
|
....*..
gi 2310915810 5028 PLTPNGK 5034
Cdd:cd05943 593 PRTLSGK 599
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
4089-4503 |
3.39e-11 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 69.20 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQgMLFHslYEQASSDYINQ---MRVDvSGLDIPRFRAAWQSALDRHAILRSGFAW-QGELQQPLQIvYRQRQLP 4164
Cdd:cd19534 3 PLTPIQR-WFFE--QNLAGRHHFNQsvlLRVP-QGLDPDALRQALRALVEHHDALRMRFRReDGGWQQRIRG-DVEELFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4165 FAEEDLSQAANRDAALLALAAAERerGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSnAQLLSEVLES-----Y 4239
Cdd:cd19534 78 LEVVDLSSLAQAAAIEALAAEAQS--SLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVS-WRILLEDLEAayeqaL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4240 AGRSPEQPRDGRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRlvealAQPGLTSANGVGEHLrEVDATATARL- 4314
Cdd:cd19534 155 AGEPIPLPSKTSFQTWAELLAEYaqspALLEELAYWRELPAADYWGLP-----KDPEQTYGDARTVSF-TLDEEETEALl 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4315 RDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVfgatVS----GRPADLPGVE--NQVGLFINTLPVVVTLAPQmtlDEL 4388
Cdd:cd19534 229 QEANAAYRTEINDLLLAALALAFQDWTGRAPPA----IFleghGREEIDPGLDlsRTVGWFTSMYPVVLDLEAS---EDL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4389 LQGLQRQNLALR----------------EQEHTPLFEL-----------QRWAGFGGEAVFDnllvfenYPVDEVLERSS 4441
Cdd:cd19534 302 GDTLKRVKEQLRripnkgigygilryltPEGTKRLAFHpqpeisfnylgQFDQGERDDALFV-------SAVGGGGSDIG 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4442 AGGVRFGAVAMHeqtnyplALALGGgdSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEH 4503
Cdd:cd19534 375 PDTPRFALLDIN-------AVVEGG--QLVITVSYSRNMYHEETIQQLADSYKEALEALIEH 427
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
2311-2479 |
3.62e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 69.79 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2311 ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRG 2390
Cdd:PRK05677 391 VIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2391 FRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:PRK05677 464 FNVYPNELEDVLAALPGVLQCAAIGVpDEKSGEAIKVFVVVKP---GETLTKEqVMEHMRANLTGYKVPKAVEFRDELPT 540
|
170
....*....|.
gi 2310915810 2469 NANGKLDRKAL 2479
Cdd:PRK05677 541 TNVGKILRREL 551
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
3038-3467 |
4.24e-11 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 69.52 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPAL-AFGEErLDYAELNRRANRLAHALI-----ERGvgaDRlVGVAMERSIEMVVALMAILKA 3111
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYhSFGKT-ITYREADQLVEQFAAYLLgelqlKKG---DR-VALMMPNCLQYPIATFGVLRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3112 GGAYVPVDPEYPEERQAYMLEDSG-------------VELLLSQSHLKLPLAQGV-QRIDLDRGA----------PWFED 3167
Cdd:PRK08751 100 GLTVVNVNPLYTPRELKHQLIDSGasvlvvidnfgttVQQVIADTPVKQVITTGLgDMLGFPKAAlvnfvvkyvkKLVPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3168 YSEAN----------------PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG--------DT 3223
Cdd:PRK08751 180 YRINGairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQWLAGtgkleegcEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3224 VLQKTPFS--FDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKR 3299
Cdd:PRK08751 257 VITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQIDFSSLKM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3300 IVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEA--AIDVTHWTCVEEGKDavpIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:PRK08751 334 TLGGGMAVQRSVAER-WKQVTGLTLVEAYGLTETspAACINPLTLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:PRK08751 410 ELCIKGPQVMKGYWKRPEETAKVMDA------DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMP 483
|
490
....*....|
gi 2310915810 3458 WVREAAVLAV 3467
Cdd:PRK08751 484 GVLEVAAVGV 493
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
4117-4395 |
4.42e-11 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 68.67 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4117 DVSGLDIPRFRAAWQSALDRHAILRSGFAWQGElQQPLQIVYRQRqlpFAEEDLSQAANRDAALLALAAAERE--RGFEL 4194
Cdd:cd19535 33 DGEDLDPDRLERAWNKLIARHPMLRAVFLDDGT-QQILPEVPWYG---ITVHDLRGLSEEEAEAALEELRERLshRVLDV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4195 QRAPLLRLLLVKTAEGEHHLiythhHI-----LLDGWSNAQLLSEVLESYAGR-SPEQPRDGRYSDYIAWLQRQDAAATE 4268
Cdd:cd19535 109 ERGPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPgEPLPPLELSFRDYLLAEQALRETAYE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4269 ---AFWREQMAALDEPTRL-----VEALAQPGLTSangvgeHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRY 4340
Cdd:cd19535 184 rarAYWQERLPTLPPAPQLplakdPEEIKEPRFTR------REHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4341 TGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQ 4395
Cdd:cd19535 258 SGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQ 312
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
3180-3527 |
4.84e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.15 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGlGVGDTVLQKTPF---SFDVSVWEffwpLMSGARLVVAAPGD 3256
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPAHhiaGLQVLVRS----VIAGSEPVELDVSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3257 HRDPAKLVALINREGVDTLH--FVPSMLQAFLQD-EDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL--YNLYGPT 3331
Cdd:PRK07824 110 GFDPTALPRAVAELGGGRRYtsLVPMQLAKALDDpAATAALAELDAVLVGGGPAPA----PVLDAAAAAGInvVRTYGMS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3332 EaaidvTHWTCVEEGkdavpigRPIANLACYILDGnlepvpvgvlgELYLAGQGLARGYHQRPgltaerfvASPFVAGER 3411
Cdd:PRK07824 186 E-----TSGGCVYDG-------VPLDGVRVRVEDG-----------RIALGGPTLAKGYRNPV--------DPDPFAEPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 MYRTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWRE 3487
Cdd:PRK07824 235 WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPddrlGQRVVAAVVGDGGPAPTLE 313
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
4561-5042 |
5.21e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 69.04 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD-----------IEY------- 4621
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNkqlmndqivhiINHaedeviv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 --PR--ERLLYMMQDS---RAHLLL-THSHLLERLPIPEGLSCLSVdrEEEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:PRK05620 117 adPRlaEQLGEILKECpcvRAVVFIgPSDADSAAAHMPEGIKVYSY--EALLDGRSTVYDWPELDETTAAAICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIAHIVA--TGERYEMTPEDCEL------HFMSfafdgshegWMHPL---INGARVLIRDDSLWLPERT 4762
Cdd:PRK05620 195 APKGVVYSHRSLYLQSLSlrTTDSLAVTHGESFLccvpiyHVLS---------WGVPLaafMSGTPLVFPGPDLSAPTLA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 Y---AEMHR--HGVtvgvfPPVYLQqLAEHAERdgNPP---PVRVYCFGGDAVAQASYDLaWRALKPKYLFNGYGPTETV 4834
Cdd:PRK05620 266 KiiaTAMPRvaHGV-----PTLWIQ-LMVHYLK--NPPermSLQEIYVGGSAVPPILIKA-WEERYGVDVVHVWGMTETS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 VTPLLWKARAGdACGAAympigtllgnRSGY-ILDGQLnllPVGV-----------------AGELYLGGEGVARGYLER 4896
Cdd:PRK05620 337 PVGTVARPPSG-VSGEA----------RWAYrVSQGRF---PASLeyrivndgqvmestdrnEGEIQVRGNWVTASYYHS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4897 PALT----AERF-------VPDPFGAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4965
Cdd:PRK05620 403 PTEEgggaASTFrgedvedANDRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4966 AVVVAQPGAV-GQQLVGYVVaqepaVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK05620 481 CAVIGYPDDKwGERPLAVTV-----LAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
651-942 |
5.38e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.07 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 651 NGENLAYVIYTSGSTGKPKGAGNRHSAL--SNRLCWmqQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVV 724
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLlaNQRACL--KFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 725 AApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 802
Cdd:PRK06334 256 AY--NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 803 PTEAAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLE-PVPVGVLGELYLAGRGLARGY-HQRPGltaERFVAspfV 880
Cdd:PRK06334 334 TTECS-PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYlGEDFG---QGFVE---L 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH---PWVREAAVLAVDG 942
Cdd:PRK06334 407 GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPLVVCG 471
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
661-941 |
6.70e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 68.25 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 661 TSGSTGKPKGAG-NRHSALSNRLCWMQ--QAYGLGVGDTVLqkTPFSFDVSVWefFWPLMSGAR-----LVVAAPGDhrd 732
Cdd:COG1541 91 SSGTTGKPTVVGyTRKDLDRWAELFARslRAAGVRPGDRVQ--NAFGYGLFTG--GLGLHYGAErlgatVIPAGGGN--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 733 PAKLVELINREGVDTLHFVPSMLQAFLqdeDVA-------SCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTE 805
Cdd:COG1541 164 TERQLRLMQDFGPTVLVGTPSYLLYLA---EVAeeegidpRDLSLKKGIFGGEPWS-EEMRKEIEERWGIKAYDIYGLTE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 806 aaidVTHWTCVE-EGKDtvpigrpignlGCY---------ILD-GNLEPVPVGVLGELYLAGrglargyhqrpgLTAErf 874
Cdd:COG1541 240 ----VGPGVAYEcEAQD-----------GLHiwedhflveIIDpETGEPVPEGEEGELVVTT------------LTKE-- 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 875 vASPFVageRmYRTGDLARY------------RADGVIeyaGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD 941
Cdd:COG1541 291 -AMPLI---R-YRTGDLTRLlpepcpcgrthpRIGRIL---GRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVD 361
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
511-940 |
6.91e-11 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 68.75 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 511 RGVHRLFEEQVERTPTAPAL-AFGEErLDYAELNRRANRLAHALI-----ERGigaDRlVGVAMERSIEMVVALMAILKA 584
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYhSFGKT-ITYREADQLVEQFAAYLLgelqlKKG---DR-VALMMPNCLQYPIATFGVLRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 585 GGAYVPVDPEYPEERQAYMLEDSG-------------VQLLLSQSHLKLPLAQGVQRIdLDQADAWLENHAENN------ 645
Cdd:PRK08751 100 GLTVVNVNPLYTPRELKHQLIDSGasvlvvidnfgttVQQVIADTPVKQVITTGLGDM-LGFPKAALVNFVVKYvkklvp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 646 ----------------------PGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG--------D 695
Cdd:PRK08751 179 eyringairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQWLAGtgkleegcE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 696 TVLQKTPFS--FDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DVASCTSLK 771
Cdd:PRK08751 256 VVITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQIDFSSLK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 772 RIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEA--AIDVTHWTCVEEGKDtvpIGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:PRK08751 333 MTLGGGMAVQRSVAER-WKQVTGLTLVEAYGLTETspAACINPLTLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 850 GELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:PRK08751 409 GELCIKGPQVMKGYWKRPEETAKVMDA------DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490
....*....|.
gi 2310915810 930 PWVREAAVLAV 940
Cdd:PRK08751 483 PGVLEVAAVGV 493
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
3061-3470 |
7.21e-11 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 68.15 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 sqshlklplaqgvqrIDLdrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05940 81 ---------------VDA------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAFL----QDEDVASct 3295
Cdd:cd05940 122 SDVLYTCLPlYHSTALIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLnqppKPTERKH-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3296 SLKRIvcSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWtcveEGKDAV-----PIGRPIANLACYILD----- 3365
Cdd:cd05940 197 KVRMI--FGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF----FGKPGAigrnpSLLRKVAPLALVKYDlesge 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3366 ------GNLEPVPVGVLGELYLAGQGLAR--GYhQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 3437
Cdd:cd05940 271 pirdaeGRCIKVPRGEPGLLISRINPLEPfdGY-TDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTF 349
|
410 420 430
....*....|....*....|....*....|....*...
gi 2310915810 3438 KLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGR 3470
Cdd:cd05940 350 RWKGENVSTTEVAAVLGAFPGVEEANVYGVqvpgtDGR 387
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
4880-5040 |
7.43e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 67.38 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4880 GELYLGGEGVARGYLERPaltaerfVPDPFGAPG-SRLYRSGDLTrgraDGVVDYLGRVDHQVKIRGFRIELGEIEARLR 4958
Cdd:PRK07824 208 GRIALGGPTLAKGYRNPV-------DPDPFAEPGwFRTDDLGALD----DGVLTVLGRADDAISTGGLTVLPQVVEAALA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4959 EHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PRK07824 277 THPAVADCAVFGLPDDrLGQRVVAAVVGD--------GGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDR 348
|
...
gi 2310915810 5038 KGL 5040
Cdd:PRK07824 349 RAL 351
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
2053-2479 |
7.52e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 68.54 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2053 VGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLA---ERLPCPAEVERLPLETAAWPASADTRPL----- 2124
Cdd:PRK08974 89 IALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAhtlEKVVFKTPVKHVILTRMGDQLSTAKGTLvnfvv 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 --------------------------------PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--VGP 2170
Cdd:PRK08974 169 kyikrlvpkyhlpdaisfrsalhkgrrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 GDcqlQFASIS------FDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTILD----LPPAYLQ-QQAEELR 2239
Cdd:PRK08974 249 GK---ELVVTAlplyhiFALTVNCLLFIELGGQNLLITNPRDIPG--FVKELKKYPFTAITgvntLFNALLNnEEFQELD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2240 HAGRRIAVRtcilGGEAwdasllTQQAVqAEAWFNA--------YGPTEAviTPLAWHCRAQ-EGGAPAIGRALGARRAC 2310
Cdd:PRK08974 324 FSSLKLSVG----GGMA------VQQAV-AERWVKLtgqyllegYGLTEC--SPLVSVNPYDlDYYSGSIGLPVPSTEIK 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2311 ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRG 2390
Cdd:PRK08974 391 LVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW-------LATGDIAVMDEEGFLRIVDRKKDMILVSG 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2391 FRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDA-MRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPL 2468
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEVAAVGVpSEVSGEAVKIFVVKKDPsLTEEELITHCRRHLTG----YKVPKLVEFRDELPK 538
|
490
....*....|.
gi 2310915810 2469 NANGKLDRKAL 2479
Cdd:PRK08974 539 SNVGKILRREL 549
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
3185-3478 |
7.73e-11 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 68.26 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALSNRLC-----WMqqayGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVaapgdHR 3258
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSSLGLGLKvngryWL----DLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFV-----HH 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 ----DPAKLVALINREGVDTLHFVPSMLQAFLQdEDVASCT--SLKRIVCSGEALPADAQQQVFAklpQAGL--YNLYGP 3330
Cdd:cd05928 250 lprfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKfpSLQHCVTGGEPLNPEVLEKWKA---QTGLdiYEGYGQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAIdvthwTC-VEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ-----GLARGYHQRPGLTAERFV 3402
Cdd:cd05928 326 TETGL-----ICaNFKGMKIKPgsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3403 ASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGRQLVGYVVL 3478
Cdd:cd05928 401 GD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspdpIRGEVVKAFVVL 473
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1127-1515 |
8.25e-11 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 67.71 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1127 RQPLDGDRLGRALERLQAQHDALRLRFREERGawHQAYaeQA---GEPLWRRQAGSEEALLALCEeaQRSLDLEQgPLLR 1203
Cdd:cd19545 31 PPDIDLARLQAAWEQVVQANPILRTRIVQSDS--GGLL--QVvvkESPISWTESTSLDEYLEEDR--AAPMGLGG-PLVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1204 ALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAdlgPRSSSYQTWSRHLHEQagaRLDEL-DYWQAQLHD 1282
Cdd:cd19545 104 LALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPV---PQPPPFSRFVKYLRQL---DDEAAaEFWRSYLAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1283 APHALPCENPHGALENRHERKLvltldaERTRQLLQEAPAAYRTQVndLLLTALARATCRWSGDASVLVQLEGHGREDLG 1362
Cdd:cd19545 178 LDPAVFPPLPSSRYQPRPDATL------EHSISLPSSASSGVTLAT--VLRAAWALVLSRYTGSDDVVFGVTLSGRNAPV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1363 EAIDlsRTVG-WFTSL-FPVRLTPAADLGESLKAIKEQL-RGVPDKGVGYGLLRYLAGEeaaTRLAALPQPRITFNYlgr 1439
Cdd:cd19545 250 PGIE--QIVGpTIATVpLRVRIDPEQSVEDFLQTVQKDLlDMIPFEHTGLQNIRRLGPD---ARAACNFQTLLVVQP--- 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 1440 fDRQFDGAALLVPATESAGAAQDPCAPLAnwLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19545 322 -ALPSSTSESLELGIEEESEDLEDFSSYG--LTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
4563-5038 |
8.36e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 68.61 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAhALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-DIEYP--RERLLYMMQDSRAHLLL 4639
Cdd:PRK12476 69 LTWTQLGVRLRAVG-ARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 THSHLLE-------RLPIPEGLSCLSVDR--EEEWAGFPAhdpeVALHGDNLAYVIYTSGSTGMPKGVAVSH---GPLIA 4707
Cdd:PRK12476 148 TTTAAAEavegflrNLPRLRRPRVIAIDAipDSAGESFVP----VELDTDDVSHLQYTSGSTRPPVGVEITHravGTNLV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4708 HIVATGERYEMTPEDCE----LHFMSF------AFDGSHEGWMHPLingarVLIRDDSLWLpeRTYAEMHRHGVTVGVfP 4777
Cdd:PRK12476 224 QMILSIDLLDRNTHGVSwlplYHDMGLsmigfpAVYGGHSTLMSPT-----AFVRRPQRWI--KALSEGSRTGRVVTA-A 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAehAERdGNPP-----------------PVRVycfggDAV-----AQASYDLAWRALKPKY------LF-NGY 4828
Cdd:PRK12476 296 PNFAYEWA--AQR-GLPAegddidlsnvvliigsePVSI-----DAVttfnkAFAPYGLPRTAFKPSYgiaeatLFvATI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GP-TETVVTPL----LWKARA----GDACGA-AYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERP 4897
Cdd:PRK12476 368 APdAEPSVVYLdreqLGAGRAvrvaADAPNAvAHVSCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRP 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4898 ALTAERF-----VPDPFG------APGSRLYRSGDLTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HPAVRE 4965
Cdd:PRK12476 448 EETERTFgaklqSRLAEGshadgaADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRR 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4966 AVVVA--QPGAVGQQLVgyVVAQEPAVADSPEAQAECRAqLKTALRERlpeYMVPSH-LLFLAR--MPLTPNGKLDRK 5038
Cdd:PRK12476 527 GYVTAftVPAEDNERLV--IVAERAAGTSRADPAPAIDA-IRAAVSRR---HGLAVAdVRLVPAgaIPRTTSGKLARR 598
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2500-2559 |
1.05e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 59.88 E-value: 1.05e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2500 RSVAAIWEALLGV--EGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLAD 2559
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
3166-3468 |
1.05e-10 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 67.48 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3166 EDYSEANPD--IHLDGENLAYVIYTSGSTGKPKGAG-NRHSALSNRLCWMQ--QAYGLGVGDTVLqkTPFSFDVSVWefF 3240
Cdd:COG1541 67 EDLRDNYPFglFAVPLEEIVRIHASSGTTGKPTVVGyTRKDLDRWAELFARslRAAGVRPGDRVQ--NAFGYGLFTG--G 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3241 WPLMSGAR-----LVVAAPGDhrdPAKLVALINREGVDTLHFVPSMLQAFLqdeDVA-------SCTSLKRIVCSGEALP 3308
Cdd:COG1541 143 LGLHYGAErlgatVIPAGGGN---TERQLRLMQDFGPTVLVGTPSYLLYLA---EVAeeegidpRDLSLKKGIFGGEPWS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3309 aDAQQQVFAKLPQAGLYNLYGPTEaaidVTHWTCVE-EGKDavpiGRPIANLACY--ILD-GNLEPVPVGVLGELYLAGq 3384
Cdd:COG1541 217 -EEMRKEIEERWGIKAYDIYGLTE----VGPGVAYEcEAQD----GLHIWEDHFLveIIDpETGEPVPEGEEGELVVTT- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3385 glargyhqrpgLTAErfvASPFVageRmYRTGDLARY------------RADGVIeyaGRIDHQVKLRGLRIELGEIEAR 3452
Cdd:COG1541 287 -----------LTKE---AMPLI---R-YRTGDLTRLlpepcpcgrthpRIGRIL---GRADDMLIIRGVNVFPSQIEEV 345
|
330
....*....|....*.
gi 2310915810 3453 LLEHPWVREAAVLAVD 3468
Cdd:COG1541 346 LLRIPEVGPEYQIVVD 361
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
534-943 |
1.21e-10 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 67.38 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 614 sqshlklplaqgvqridldqADAwlenhaennpgielngenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05940 81 --------------------VDA-------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 694 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAFL----QDEDVASct 768
Cdd:cd05940 122 SDVLYTCLPlYHSTALIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLnqppKPTERKH-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 769 SLKRIvcSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWtcveEGKDTVpIGRpIGNLGCYIL----------- 837
Cdd:cd05940 197 KVRMI--FGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF----FGKPGA-IGR-NPSLLRKVAplalvkydles 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 838 -------DGNLEPVPVGVLGELYLAGRGLAR--GYhQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDH 908
Cdd:cd05940 269 gepirdaEGRCIKVPRGEPGLLISRINPLEPfdGY-TDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2310915810 909 QVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGR 943
Cdd:cd05940 348 TFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvpgtDGR 387
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
516-940 |
1.44e-10 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 67.77 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAhALIERGIG---ADRlVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFA-AYLQNGLGlkkGDR-VALMMPNLLQYPIALFGILRAGMIVVNVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PEY-PEERQaYMLEDSGVQLLLSQSHL-----------------------KLPLAQG-------------VQRIDLDQAD 635
Cdd:PRK08974 106 PLYtPRELE-HQLNDSGAKAIVIVSNFahtlekvvfktpvkhviltrmgdQLSTAKGtlvnfvvkyikrlVPKYHLPDAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 636 AWLENHAEN------NPgiELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG--LGVG-DTVLQKTP---- 702
Cdd:PRK08974 185 SFRSALHKGrrmqyvKP--ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGkELVVTALPlyhi 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 703 FSFDVSVWEFFWplMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEAL 780
Cdd:PRK08974 263 FALTVNCLLFIE--LGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGGMAV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 781 padaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTcveeGKdtvpIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:PRK08974 338 ----QQAVaerWVKLTGQYLLEGYGLTECSplvsvnpYDLDYYS----GS----IGLPVPSTEIKLVDDDGNEVPPGEPG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 851 ELYLAGRGLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:PRK08974 406 ELWVKGPQVMLGYWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
|
490
....*....|
gi 2310915810 931 WVREAAVLAV 940
Cdd:PRK08974 479 KVLEVAAVGV 488
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
3178-3469 |
1.67e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 67.53 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAGNRHSAL--SNRLCWmqQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVV 3251
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLlaNQRACL--KFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3252 AApgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 3329
Cdd:PRK06334 256 AY--NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3330 PTEAAiDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLE-PVPVGVLGELYLAGQGLARGY-HQRPGltaERFVAspfV 3407
Cdd:PRK06334 334 TTECS-PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYlGEDFG---QGFVE---L 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3408 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH---PWVREAAVLAVDG 3469
Cdd:PRK06334 407 GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPLVVCG 471
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
535-955 |
1.82e-10 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 67.11 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL- 613
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 614 ----SQSHLKLPLAQGVQRIDLDQADA------WLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAGNRHSALSn 680
Cdd:cd05932 85 gkldDWKAMAPGVPEGLISISLPPPSAancqyqWDDLIAQHPPLEERptrFPEQLATLIYTSGTTGQPKGVMLTFGSFA- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 681 rlcWMQQA----YGLGVGDTVLQKTPFSfdvsvweffwplmsgarlvvaapgdHRDPAKLVELINREGVDTLHFVPSmLQ 756
Cdd:cd05932 164 ---WAAQAgiehIGTEENDRMLSYLPLA-------------------------HVTERVFVEGGSLYGGVLVAFAES-LD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 757 AFLQDEDVASCTslkrIVCSGEALPADAQQQVFAKLPQAGL---------------------------YNLYGPTEAAID 809
Cdd:cd05932 215 TFVEDVQRARPT----LFFSVPRLWTKFQQGVQDKIPQQKLnlllkipvvnslvkrkvlkglgldqcrLAGCGSAPVPPA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 810 VTHW-----TCVEEGKD----------TVPIGRPIGNLGcyildgnlEPVP-----VGVLGELYLAGRGLARGYHQRPGL 869
Cdd:cd05932 291 LLEWyrslgLNILEAYGmtenfayshlNYPGRDKIGTVG--------NAGPgvevrISEDGEILVRSPALMMGYYKDPEA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 870 TAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGY 948
Cdd:cd05932 363 TAEAFTADGFL------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLAL 436
|
....*..
gi 2310915810 949 VVLESEG 955
Cdd:cd05932 437 VVLSEEA 443
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
4560-4711 |
2.12e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.34 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP---RE----RLLYMMQD 4632
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggREsyiaQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4633 SRAHLLLTHSHLLE-------RLPIPEGLSCLSVD-REEEWAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGP 4704
Cdd:PRK09192 127 AQPAAIITPDELLPwvneathGNPLLHVLSHAWFKaLPEADVALPRPTP------DDIAYLQYSSGSTRFPRGVIITHRA 200
|
....*..
gi 2310915810 4705 LIAHIVA 4711
Cdd:PRK09192 201 LMANLRA 207
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2494-2569 |
2.39e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 59.48 E-value: 2.39e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2494 PREGLERSVAAIWEALLGV--EGIARDEHFF-ELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASLESQAA 2569
Cdd:COG0236 2 PREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
2016-2476 |
2.96e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 66.71 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2016 YAELDMRAERLARGLRARGvvAEALVAIAAERSFDLVVGLLGILKAGAGY--LP-----LDPNYPAERLAYMLRDSGARW 2088
Cdd:PRK05851 34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVsiLPgpvrgADDGRWADATLTRFAGIGVRT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LICQETLAERLPcpAEVERLPLETAAWPASADTR-PLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG 2167
Cdd:PRK05851 112 VLSHGSHLERLR--AVDSSVTVHDLATAAHTNRSaSLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2168 VGPG-DCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHL--ADEVERHAVTILDLPP-AYlqqqaEELRHAGR 2243
Cdd:PRK05851 190 LDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASPFrwLSWLSDSRATLTAAPNfAY-----NLIGKYAR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2244 RI------AVRTCILGGEAWDASLLTQQAVQ-------AEAWFNAYGPTE---AVITP-LAWHCRAQEGGAPAIGralGA 2306
Cdd:PRK05851 265 RVsdvdlgALRVALNGGEPVDCDGFERFATAmapfgfdAGAAAPSYGLAEstcAVTVPvPGIGLRVDEVTTDDGS---GA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRACILDAALqpcaPGM-----------------IGELYIGGQCLARGYLGR-PGQTAERFvadpfsgsgerlyRTGDLA 2368
Cdd:PRK05851 342 RRHAVLGNPI----PGMevrispgdgaagvagreIGEIEIRGASMMSGYLGQaPIDPDDWF-------------PTGDLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 rYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALdGVG------GPLLAAYLVGRDAMRGEDLLAE 2442
Cdd:PRK05851 405 -YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV-GTGegsarpGLVIAAEFRGPDEAGARSEVVQ 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 2310915810 2443 LRTWLAGRLPA---YMQPtawqvlSSLPLNANGKLDR 2476
Cdd:PRK05851 483 RVASECGVVPSdvvFVAP------GSLPRTSSGKLRR 513
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
2137-2479 |
3.24e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 66.58 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVAVSQAAlvAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLF---VPLLAGARVLLGDAgqwSAQHLA 2213
Cdd:PLN03102 193 YTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFtwgTAARGGTSVCMRHV---TAPEIY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2214 DEVERHAVTILDLPPA----YLQQQAEELRHAGRRIAVRTcilGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPL--- 2286
Cdd:PLN03102 268 KNIEMHNVTHMCCVPTvfniLLKGNSLDLSPRSGPVHVLT---GGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLfce 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 ---AWHcRAQEGGAPAIGRALGARRACILDAAL-----QPCAP---GMIGELYIGGQCLARGYLGRPGQTAERFvadpfs 2355
Cdd:PLN03102 345 wqdEWN-RLPENQQMELKARQGVSILGLADVDVknketQESVPrdgKTMGEIVIKGSSIMKGYLKNPKATSEAF------ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 gsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRdam 2434
Cdd:PLN03102 418 --KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMpHPTWGETPCAFVVLE--- 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2435 RGEDLLAELRTWLAGR-----------LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN03102 493 KGETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
3545-3602 |
3.62e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 58.73 E-value: 3.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3545 RRIAAVWADVLKL--EEVGATDNFFALGGDSIVSIQVVSRCRAA-GIQFTPKDLFQQQTVQ 3602
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
4680-4931 |
3.72e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 65.97 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGA-------RVLI 4751
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDmGLIAFHLAPLIAGMnqylmptRLFI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 RDDSLWLpertyAEMHRHGVTVGVFP----PVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYD-----LAWRALKPK 4822
Cdd:cd05908 186 RRPILWL-----KKASEHKATIVSSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHefldhMSKYGLKRN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 YLFNGYGPTETVVTPLLWKARA-----------------------GDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVA 4879
Cdd:cd05908 261 AILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKILPDGYI 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4880 GELYLGGEGVARGYLERPALTAERFVPDPFGAPGSR-LYRSGDLT-RGRADGVV 4931
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLgFIRNGRLViTGREKDII 394
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
4543-5010 |
4.09e-10 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 66.30 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDE-----EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL 4617
Cdd:cd05921 1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 D------------IEYPRERL---LYMMQDSRAHLLLTHSHLLERLPI------PEGLSCLSVDREEEWAGFPAHDPEVA 4676
Cdd:cd05921 81 SpayslmsqdlakLKHLFELLkpgLVFAQDAAPFARALAAIFPLGTPLvvsrnaVAGRGAISFAELAATPPTAAVDAAFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4677 LHG-DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED--CELHFM--SFAFDGSHEgwMHPLINGARVLI 4751
Cdd:cd05921 161 AVGpDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLpwNHTFGGNHN--FNLVLYNGGTLY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 RDDSLWLP---ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-----PPVRVYCFGGDAVAQASYD----LAWRAL 4819
Cdd:cd05921 239 IDDGKPMPggfEETLRNLREISPTVYFNVPAGWEMLVAALEKDEALrrrffKRLKLMFYAGAGLSQDVWDrlqaLAVATV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4820 KPKYLF-NGYGPTETvvtpllwkarAGDACGAaympigTLLGNRSGYI---LDG-QLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:cd05921 319 GERIPMmAGLGATET----------APTATFT------HWPTERSGLIglpAPGtELKLVPSGGKYEVRVKGPNVTPGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4895 ERPALTAERFVPDPFgapgsrlYRSGDLTRgRAD------GVVdYLGRVDHQVKIR-GFRIELGEIEARLREH--PAVRE 4965
Cdd:cd05921 383 RQPELTAQAFDEEGF-------YCLGDAAK-LADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4966 AVVVAQPGA-VG----------QQLVGYVVAQEPAVADSPEAQAECRAQLKTALRE 5010
Cdd:cd05921 454 AVVAGEDRAeVGalvfpdllacRRLVGLQEASDAEVLRHAKVRAAFRDRLAALNGE 509
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
2103-2406 |
4.28e-10 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 65.72 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2103 AEVERLPLETAAwpasaDTR-----PLPEVAGETLAYVIYTSGSTGQPKGVAVSQ------AALVAHCQAAArtyGVGPG 2171
Cdd:cd05913 51 DDLRKLPFTTKE-----DLRdnypfGLFAVPREKVVRIHASSGTTGKPTVVGYTKndldvwAELVARCLDAA---GVTPG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2172 DCQ-------LQFASISFDAAAEQLfvpllaGARVLLGDAGQwsaqhladeVERHAVTILDL-------PPAYLQQQAEE 2237
Cdd:cd05913 123 DRVqnaygygLFTGGLGFHYGAERL------GALVIPAGGGN---------TERQLQLIKDFgptvlccTPSYALYLAEE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2238 LRHAG---RRIAVRTCILGGEAWDASLLTQQAVQAEAW-FNAYGPTEaVITP-LAWHCRAQEGG-------APAIgralg 2305
Cdd:cd05913 188 AEEEGidpRELSLKVGIFGAEPWTEEMRKRIERRLGIKaYDIYGLTE-IIGPgVAFECEEKDGLhiwedhfIPEI----- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 arracILDAALQPCAPGMIGELYIGGqclargyLGRPGQTAERfvadpfsgsgerlYRTGDLARY------------RVD 2373
Cdd:cd05913 262 -----IDPETGEPVPPGEVGELVFTT-------LTKEAMPLIR-------------YRTRDITRLlpgpcpcgrthrRID 316
|
330 340 350
....*....|....*....|....*....|...
gi 2310915810 2374 GqveYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:cd05913 317 R---ITGRSDDMLIIRGVNVFPSQIEDVLLKIP 346
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
3035-3477 |
6.24e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 65.67 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3035 PLQRGVHRLFEEQVERTPTAPALA-----FGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAIL 3109
Cdd:PRK08180 36 DYPRRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3110 KAGGAYVPVDPEY------------------P-----EERQAY-----MLEDSGVELLLSQshlklPLAQGVQRIDLDR- 3160
Cdd:PRK08180 116 YAGVPYAPVSPAYslvsqdfgklrhvlelltPglvfaDDGAAFaralaAVVPADVEVVAVR-----GAVPGRAATPFAAl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3161 -GAPWFEDYSEANPDIHLDgeNLAYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGlgvgdtvlqktpfsfdvSVWEF 3239
Cdd:PRK08180 191 lATPPTAAVDAAHAAVGPD--TIAKFLFTSGSTGLPKAVINTHRM----LCANQQMLA-----------------QTFPF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3240 FwpLMSGARLVVAAPGDHR-------------------DPAK-LVALI------NREGVDTLHF-VP----SMLQAFLQD 3288
Cdd:PRK08180 248 L--AEEPPVLVDWLPWNHTfggnhnlgivlynggtlyiDDGKpTPGGFdetlrnLREISPTVYFnVPkgweMLVPALERD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVAScTSLKRIVC---SGEALPAD--------AQQQVFAKLP-QAGLynlyGPTEAAIDVT--HWTCVEEGkdavPIGR 3354
Cdd:PRK08180 326 AALRR-RFFSRLKLlfyAGAALSQDvwdrldrvAEATCGERIRmMTGL----GMTETAPSATftTGPLSRAG----NIGL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLAcyildgnLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYrAD------GVIe 3428
Cdd:PRK08180 397 PAPGCE-------VKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF-VDpadperGLM- 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3429 YAGRIDHQVKL-RGLRIELGEIEARLLEH--PWVREaAVLAVDGRQLVGYVV 3477
Cdd:PRK08180 462 FDGRIAEDFKLsSGTWVSVGPLRARAVSAgaPLVQD-VVITGHDRDEIGLLV 512
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
4547-5042 |
6.43e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 65.28 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP---R 4623
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPqplL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAhlllthsHLLERLPIPEGLSCLSVDReeewagfPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:PRK09029 93 EELLPSLTLDFA-------LVLEGENTFSALTSLHLQL-------VEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 pliAHIV-ATGERYEM--TPEDCELhfMSFA-FDGSHEG----WmhpLINGARVLIRDDslwlpERTYAEMhrHGVTVGV 4775
Cdd:PRK09029 159 ---AHLAsAEGVLSLMpfTAQDSWL--LSLPlFHVSGQGivwrW---LYAGATLVVRDK-----QPLEQAL--AGCTHAS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4776 FPPVYLQQLAEHaerDGNPPPVRVYCFGGDAVAQAsydLAWRALK---PKYLfnGYGPTE---TVVTpllwkARAGDACG 4849
Cdd:PRK09029 224 LVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVE---LTEQAEQqgiRCWC--GYGLTEmasTVCA-----KRADGLAG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4850 AaympiGTLLGNRsgyildgQLNLlpvgVAGELYLGGEGVARGYlerpaltaerfvpdpfgapgsrlYRSGDLT------ 4923
Cdd:PRK09029 291 V-----GSPLPGR-------EVKL----VDGEIWLRGASLALGY-----------------------WRQGQLVplvnde 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4924 -------RGR-ADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVgyvvaqepAVADSP 4994
Cdd:PRK09029 332 gwfatrdRGEwQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAeFGQRPV--------AVVESD 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4995 EAQAecRAQLKTALRERLPEYMVPSHLLflaRMPLT-PNG--KLDRKGLPQ 5042
Cdd:PRK09029 404 SEAA--VVNLAEWLQDKLARFQQPVAYY---LLPPElKNGgiKISRQALKE 449
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
653-998 |
7.22e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 64.30 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGlGVGDTVLQKTPF---SFDVSVWEffwpLMSGARLVVAAPGD 729
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPAHhiaGLQVLVRS----VIAGSEPVELDVSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 730 HRDPAKLVELINREGVDTLH--FVPSMLQAFLQD-EDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL--YNLYGPT 804
Cdd:PRK07824 110 GFDPTALPRAVAELGGGRRYtsLVPMQLAKALDDpAATAALAELDAVLVGGGPAPA----PVLDAAAAAGInvVRTYGMS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 805 EaaidvTHWTCVEEGkdtvpigRPIGNLGCYILDGnlepvpvgvlgELYLAGRGLARGYHQRPgltaerfvASPFVAGER 884
Cdd:PRK07824 186 E-----TSGGCVYDG-------VPLDGVRVRVEDG-----------RIALGGPTLAKGYRNPV--------DPDPFAEPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 885 MYRTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWRE 960
Cdd:PRK07824 235 WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPddrlGQRVVAAVVGDGGPAPTLE 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 2310915810 961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
4544-4922 |
7.57e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 65.35 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDE---------EKLTYAELDSRANRLAHALIARGVgPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:PRK05850 8 RERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPLDIEYPR---ERLLYMMQDSRAH------------LLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVAlhg 4679
Cdd:PRK05850 87 VPLSVPQGGahdERVSAVLRDTSPSvvlttsavvddvTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLPSTA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 dnlaYVIYTSGSTGMPKGVAVSHGPLIAHIVatgeryemtpedcelHFMSFAFdgSHEGWMHPLingarvlirDDSL--W 4757
Cdd:PRK05850 164 ----YLQYTSGSTRTPAGVMVSHRNVIANFE---------------QLMSDYF--GDTGGVPPP---------DTTVvsW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 LPerTYAEMhrhGVTVGVFPPVY--------------------LQQLAEH------------------------AERD-G 4792
Cdd:PRK05850 214 LP--FYHDM---GLVLGVCAPILggcpavltspvaflqrparwMQLLASNphafsaapnfafelavrktsdddmAGLDlG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4793 NpppVRVYCFGGDAVAQAS----------YDLAWRALKPkylfnGYGPTETVVtpLLWKARAGDACGAAY-----MPIGT 4857
Cdd:PRK05850 289 G---VLGIISGSERVHPATlkrfadrfapFNLRETAIRP-----SYGLAEATV--YVATREPGQPPESVRfdyekLSAGH 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4858 --LLGNRSG-----Y---------ILDGQLNL-LPVGVAGELYLGGEGVARGYLERPALTAERF-----VPDPfGAPGSR 4915
Cdd:PRK05850 359 akRCETGGGtplvsYgsprsptvrIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvDPSP-GTPEGP 437
|
....*..
gi 2310915810 4916 LYRSGDL 4922
Cdd:PRK05850 438 WLRTGDL 444
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1997-2489 |
7.69e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.41 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1997 QVASAPEAIAL--VCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPA 2074
Cdd:PRK05857 23 QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2075 E---------RLAYMLRDSGARwlICQETLAERLPC-PAEVERLPLETAAWPASADT-RPLPEV---AGETLAyVIYTSG 2140
Cdd:PRK05857 103 AaierfcqitDPAAALVAPGSK--MASSAVPEALHSiPVIAVDIAAVTRESEHSLDAaSLAGNAdqgSEDPLA-MIFTSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2141 STGQPKGVAVsqaalvahcqaAARTYGVGPGDCQLQ-FASISFdAAAEQLFVPLLA---------------GARVLLGda 2204
Cdd:PRK05857 180 TTGEPKAVLL-----------ANRTFFAVPDILQKEgLNWVTW-VVGETTYSPLPAthigglwwiltclmhGGLCVTG-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQWSAQhLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGE---AWDASLLTQQAVQAEawfNAYGPTE 2280
Cdd:PRK05857 246 GENTTS-LLEILTTNAVATTCLVPTLLSKLVSELKSANATVpSLRLVGYGGSraiAADVRFIEATGVRTA---QVYGLSE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2281 AVITPLawhCRAQEGG------APAIGRALGARRACILDA-ALQPCAPGM-----IGELYIGGQCLARGYLGRPGQTAER 2348
Cdd:PRK05857 322 TGCTAL---CLPTDDGsivkieAGAVGRPYPGVDVYLAATdGIGPTAPGAgpsasFGTLWIKSPANMLGYWNNPERTAEV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2349 FVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAY 2427
Cdd:PRK05857 399 LI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIpDEEFGALVGLA 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2428 LVGRDAMRGEDlLAELRTWLAGRL----PAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQ 2489
Cdd:PRK05857 471 VVASAELDESA-ARALKHTIAARFrresEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKAR 535
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
2008-2474 |
1.02e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 64.73 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2008 VCGDEH-LSYAELDMRAERLARGLRARGVVAEALVAIAA---ERSFDLVVGLLGilkAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:PRK07008 33 VEGDIHrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQ-------ETLAERLPcpaEVERLPLETAAWPASADTRPL----------------PEVAGETLAYVIYTSG 2140
Cdd:PRK07008 110 AEDRYVLFDltflplvDALAPQCP---NVKGWVAMTDAAHLPAGSTPLlcyetlvgaqdgdydwPRFDENQASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2141 STGQPKGVAVSQAALVAHCQAAA--RTYGVGPGDCQLQFASIsFDAAAEQL--FVPLLAGARVLLGDAgqWSAQHLADEV 2216
Cdd:PRK07008 187 TTGNPKGALYSHRSTVLHAYGAAlpDAMGLSARDAVLPVVPM-FHVNAWGLpySAPLTGAKLVLPGPD--LDGKSLYELI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLT--QQAVQAEAwFNAYGPTEavITPLAWHCR-- 2291
Cdd:PRK07008 264 EAERVTFSAGVPTVWLGLLNHMREAGLRFStLRRTVIGGSACPPAMIRtfEDEYGVEV-IHAWGMTE--MSPLGTLCKlk 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 -AQEGGAPAI--------GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGqtaerfvaDPFSgsgER 2360
Cdd:PRK07008 341 wKHSQLPLDEqrkllekqGRVIYGVDMKIVGDDgrELPWDGKAFGDLQVRGPWVIDRYFRGDA--------SPLV---DG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2361 LYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL---DGVGGPLLAAYL-VGRDAMRg 2436
Cdd:PRK07008 410 WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpKWDERPLLVVVKrPGAEVTR- 488
|
490 500 510
....*....|....*....|....*....|....*...
gi 2310915810 2437 EDLLAelrtWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK07008 489 EELLA----FYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1995-2456 |
1.05e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 64.76 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1995 AHQVASAPEAIALVCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:cd05921 2 AHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPA-----ERLAYML-----------------RDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPL-PE 2126
Cdd:cd05921 82 PAYSLmsqdlAKLKHLFellkpglvfaqdaapfaRALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAfAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2127 VAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD--CQLQFASISFDAAAEQLFVPLLAGARVLLGDA 2204
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQWSAQHLADeverhavTILDL----PPAYLQQQA--EELRHAGRRIA---------VRTCILGGEA-----WDAslLTQ 2264
Cdd:cd05921 242 GKPMPGGFEE-------TLRNLreisPTVYFNVPAgwEMLVAALEKDEalrrrffkrLKLMFYAGAGlsqdvWDR--LQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2265 QAVQAEA----WFNAYGPTEAviTPLAWHC-----RAQEGGAPAIGralgarraciLDAALQPCapGMIGELYIGGQCLA 2335
Cdd:cd05921 313 LAVATVGeripMMAGLGATET--APTATFThwpteRSGLIGLPAPG----------TELKLVPS--GGKYEVRVKGPNVT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVE----YLGRADQQIKIR-GFRIEIGEIESQLLAH--PYV 2408
Cdd:cd05921 379 PGYWRQPELTAQAFDEEGF-------YCLGDAAKLADPDDPAkglvFDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2409 AEAAVVALDGVGGPLLA-------AYLVGRDAMRGEDLL--AELRTWLAGRLPAYMQ 2456
Cdd:cd05921 452 HDAVVAGEDRAEVGALVfpdllacRRLVGLQEASDAEVLrhAKVRAAFRDRLAALNG 508
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
508-950 |
1.36e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 64.51 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 508 PLQRGVHRLFEEQVERTPTAPALA-----FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAIL 582
Cdd:PRK08180 36 DYPRRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 583 KAGGAYVPVDPEY------------------P-----EERQAY-----MLEDSGVQLLLSQSHLK----LPLAQGVQRID 630
Cdd:PRK08180 116 YAGVPYAPVSPAYslvsqdfgklrhvlelltPglvfaDDGAAFaralaAVVPADVEVVAVRGAVPgraaTPFAALLATPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 631 LDQADAwleNHAENNPgielngENLAYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGlgvgdtvlqktpfsfdvSVW 710
Cdd:PRK08180 196 TAAVDA---AHAAVGP------DTIAKFLFTSGSTGLPKAVINTHRM----LCANQQMLA-----------------QTF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 711 EFFwpLMSGARLVVAAPGDHR-------------------D-----PAKLVELI--NREGVDTLHF-VP----SMLQAFL 759
Cdd:PRK08180 246 PFL--AEEPPVLVDWLPWNHTfggnhnlgivlynggtlyiDdgkptPGGFDETLrnLREISPTVYFnVPkgweMLVPALE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 760 QDEDVAScTSLKRIVC---SGEALPAD--------AQQQVFAKLP-QAGLynlyGPTEAAIDVT--HWTCVEEGkdtvPI 825
Cdd:PRK08180 324 RDAALRR-RFFSRLKLlfyAGAALSQDvwdrldrvAEATCGERIRmMTGL----GMTETAPSATftTGPLSRAG----NI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 826 GRPIGnlGCyildgNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYrAD------GV 899
Cdd:PRK08180 395 GLPAP--GC-----EVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF-VDpadperGL 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 900 IeYAGRIDHQVKL-RGLRIELGEIEARLLEH--PWVREaAVLAVDGRQLVGYVV 950
Cdd:PRK08180 461 M-FDGRIAEDFKLsSGTWVSVGPLRARAVSAgaPLVQD-VVITGHDRDEIGLLV 512
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
4668-5036 |
1.56e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 64.73 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4668 FPaHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDcelHFMS----FAFDGSHEGWMHPL 4743
Cdd:PRK08043 354 MP-RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPND---RFMSalplFHSFGLTVGLFTPL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDSLW---LPERTYAEmhrhGVTVGVFPPVYLQQLAEHAerdgNP---PPVRvYCFGGDAVAQASYDLAWr 4817
Cdd:PRK08043 430 LTGAEVFLYPSPLHyriVPELVYDR----NCTVLFGTSTFLGNYARFA----NPydfARLR-YVVAGAEKLQESTKQLW- 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 alKPKY---LFNGYGPTET--VVtpllwkaragdacgAAYMPIGTLLGNrSGYILDG-QLNLLPV-GVA--GELYLGGEG 4888
Cdd:PRK08043 500 --QDKFglrILEGYGVTECapVV--------------SINVPMAAKPGT-VGRILPGmDARLLSVpGIEqgGRLQLKGPN 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4889 VARGYL--ERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEA-RLREHPAVRE 4965
Cdd:PRK08043 563 IMNGYLrvEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQH 642
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4966 AVVVAQPGAVGQQLVGYVVAQEPAvadspeaqaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK08043 643 ATAIKSDASKGEALVLFTTDSELT-----------REKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
2015-2479 |
1.71e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 64.00 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAA---ERSFDLVVGLLGIlkaGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAwntWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 Q-------ETLAERLPcpaEVERLPLETAAWPASADTRP--------LPEVAGE---------TLAYVIYTSGSTGQPKG 2147
Cdd:PRK06018 118 DltfvpilEKIADKLP---SVERYVVLTDAAHMPQTTLKnavayeewIAEADGDfawktfdenTAAGMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAHCQAA--ARTYGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGARVLLGDAgQWSAQHLADEVERHAVTIL 2224
Cdd:PRK06018 195 VLYSHRSNVLHALMAnnGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPGA-KLDGASVYELLDTEKVTFT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPA-------YLQQQAEELRHagrriaVRTCILGGEAWDASLLTQ-QAVQAEAwFNAYGPTEavITPLAWHCRAQEGG 2296
Cdd:PRK06018 273 AGVPTvwlmllqYMEKEGLKLPH------LKMVVCGGSAMPRSMIKAfEDMGVEV-RHAWGMTE--MSPLGTLAALKPPF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APAI-----------GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGqtaERFVADPFsgsgerlYR 2363
Cdd:PRK06018 344 SKLPgdarldvlqkqGYPPFGVEMKITDDAgkELPWDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGF-------FD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2364 TGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP-------LLAAYLVGRDAMRg 2436
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI---GVYHPkwderplLIVQLKPGETATR- 489
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 2437 EDLLAelrtWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06018 490 EEILK----YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
3645-3872 |
2.07e-09 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 63.36 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGtwhaehaeatlGGALLWRAEAVDRQALESL--CEESQRS 3722
Cdd:cd19537 24 FNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDG-----------GLRRSYSSSPPRVQRVDTLdvWKEINRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3723 LDLTDGPLLRSLLVDmadggQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrGEAPRLPGKTSPFKAWAGRVSEHarge 3802
Cdd:cd19537 93 FDLEREDPIRVFISP-----DTLLVVMSHIICDLTTLQLLLREVSAAYNG---KLLPPVRREYLDSTAWSRPASPE---- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3803 smkaQLQFWRELLEGAPaeLPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRT--QvndLLLTALA 3872
Cdd:cd19537 161 ----DLDFWSEYLSGLP--LLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITlhQ---LALAAVA 223
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
77-361 |
2.52e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.41 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 77 AVRLNGPLDRQALERAFASLVQRHETLRTVFprgaddslaqaplqrplevafedcsglpeaeqearlreeaqreslqpfd 156
Cdd:PRK12467 3676 DVPVNLLLDLNRLETGFPALFCRHEGLGTVF------------------------------------------------- 3706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 157 lCEGPLLRVrlirLGEERHVLLLTLHHIVSDGWsmnvlieefsrfysayatgAEPGLPALPIQYADYALWQRSWLEAGEq 236
Cdd:PRK12467 3707 -DYEPLAVI----LEGDRHVLGLTCRHLLDDGW-------------------QDTSLQAMAVQYADYILWQQAKGPYGL- 3761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 237 erqleywrgkLGerhpvlelptdhprpvvpsyrgsryeFSIEPALAEALRGTARRQGltlfmlllggfnillqrysgqtd 316
Cdd:PRK12467 3762 ----------LG--------------------------WSLGGTLARLVAELLEREG----------------------- 3782
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2310915810 317 lrvgvpianrnraEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:PRK12467 3783 -------------ESEAFLGLFDNTLPLPDEFVPQAEFLELLRQL 3814
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1583-1879 |
3.52e-09 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 62.66 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDgwPQPLQVVFEQATLELRL------APPGSDPQRQAEAEREAGFDPARAP 1656
Cdd:cd20483 34 GKPDVNLLQKALSELVRRHEVLRTAYFEGD--DFGEQQVLDDPSFHLIVidlseaADPEAALDQLVRNLRRQELDIEEGE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1657 LQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY----AGQEVaATVGR----YRDYIGW----LQGRDAMAT 1724
Cdd:cd20483 112 VIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDL-ATVPPppvqYIDFTLWhnalLQSPLVQPL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1725 EFFWRDRLASLEMPTRL---ARQARTE--QPGQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETV 1799
Cdd:cd20483 191 LDFWKEKLEGIPDASKLlpfAKAERPPvkDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1800 AFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPlydiqrwaghggealFDSIL 1879
Cdd:cd20483 271 TIGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVP---------------FDYIV 333
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
4913-5041 |
4.02e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 62.36 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4913 GSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPavA 4991
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVaGERVKAKVISHEE--I 366
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4992 DSPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:PRK08308 367 DPVQLREWC--------IQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
3063-3477 |
5.24e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 62.45 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS- 3141
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAKLKHLFELLKPg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 ----------QSHLKLPLAQGVQRIDL-----DRGAPWFEDYSEANPDIHLDG-------ENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd05921 105 lvfaqdaapfARALAAIFPLGTPLVVSrnavaGRGAISFAELAATPPTAAVDAafaavgpDTVAKFLFTSGSTGLPKAVI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTvlqktPFSFDVSVWEFFWPLMSGARLVVAAPGD-HRDPAKLVA------LIN-REG 3271
Cdd:cd05921 185 NTQRMLCANQAMLEQTYPFFGEEP-----PVLVDWLPWNHTFGGNHNFNLVLYNGGTlYIDDGKPMPggfeetLRNlREI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3272 VDTLHF-VP---SMLQAFLQDeDVASCTS----LKRIVCSGEALPAD--------AQQQVFAKLPqagLYNLYGPTEAA- 3334
Cdd:cd05921 260 SPTVYFnVPagwEMLVAALEK-DEALRRRffkrLKLMFYAGAGLSQDvwdrlqalAVATVGERIP---MMAGLGATETAp 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3335 -IDVTHWTCVEEGKdavpIGRPIANLAcyildgnLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermY 3413
Cdd:cd05921 336 tATFTHWPTERSGL----IGLPAPGTE-------LKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF------Y 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3414 RTGDLARYrAD------GVIeYAGRIDHQVKLR-GLRIELGEIEARLLEH--PWVREaAVLAVDGRQLVGYVV 3477
Cdd:cd05921 399 CLGDAAKL-ADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD-AVVAGEDRAEVGALV 468
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
4561-4969 |
5.52e-09 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 62.44 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLT 4640
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4641 H--------SHLLERLPI--------PEGLSCLSVDR-------EEEWAGFPAHDPEV------ALHGDNLAYVIYTSGS 4691
Cdd:cd17641 90 EdeeqvdklLEIADRIPSvryviycdPRGMRKYDDPRlisfedvVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGshEGWM---HPLINGARVLIRDDslwlPERTYAEMHR 4768
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIG--EQMYsvgQALVCGFIVNFPEE----PETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 HGVTVGVFPP-VYLQQLAEHAERDGNPPPVRVYCFggDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKA----- 4842
Cdd:cd17641 244 IGPTFVLLPPrVWEGIAADVRARMMDATPFKRFMF--ELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPlrdrl 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4843 -----RAGDACGAAY------------MPIGTLLGNR--SGYIL---DGQLNLLPVGV-----------AGELYLGGEGV 4889
Cdd:cd17641 322 gfsrlRSAATGGAALgpdtfrffhaigVPLKQLYGQTelAGAYTvhrDGDVDPDTVGVpfpgtevrideVGEILVRSPGV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4890 ARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVV 4968
Cdd:cd17641 402 FVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAVV 474
|
.
gi 2310915810 4969 V 4969
Cdd:cd17641 475 L 475
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2012-2408 |
6.26e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 62.44 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:PLN02387 105 EWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 -------------QETLAERLPCP----------------------AEVERLPLETaawPASADTrPLPEvageTLAYVI 2136
Cdd:PLN02387 185 dskqlkklidissQLETVKRVIYMddegvdsdsslsgssnwtvssfSEVEKLGKEN---PVDPDL-PSPN----DIAVIM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVAVSQAALVAHCqAAARTY--GVGPGDCQLQFASIS--FDAAAEQlfVPLLAGARVllgdaGQWSAQHL 2212
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATV-AGVMTVvpKLGKNDVYLAYLPLAhiLELAAES--VMAAVGAAI-----GYGSPLTL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2213 AD-----------EVERHAVTILDLPPAYLQQQAEelrhaGRRIAVRTciLGGEA---WDASLLTQQAVQAEAWFNAYGP 2278
Cdd:PLN02387 329 TDtsnkikkgtkgDASALKPTLMTAVPAILDRVRD-----GVRKKVDA--KGGLAkklFDIAYKRRLAAIEGSWFGAWGL 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 tEAVI----------TPLAWHCRAQ-EGGAP---------------AIGRALGARRACIlDAALQ--------------P 2318
Cdd:PLN02387 402 -EKLLwdalvfkkirAVLGGRIRFMlSGGAPlsgdtqrfiniclgaPIGQGYGLTETCA-GATFSewddtsvgrvgpplP 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CA-----------------PGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGR 2381
Cdd:PLN02387 480 CCyvklvsweeggylisdkPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDE---RGMRWFYTGDIGQFHPDGCLEIIDR 556
|
490 500
....*....|....*....|....*...
gi 2310915810 2382 ADQQIKIR-GFRIEIGEIESQLLAHPYV 2408
Cdd:PLN02387 557 KKDIVKLQhGEYVSLGKVEAALSVSPYV 584
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1099-1381 |
8.58e-09 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 61.56 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1099 ALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYaeQAGEPLWRRQ 1176
Cdd:cd20484 3 PLSEGQKglWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKI--EPSKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AG-----SEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPR 1251
Cdd:cd20484 81 EDisslkESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1252 SSS-------YQTWsrhlhEQ---AGARLDE-LDYWQAQLHDA-PH-ALPCENPHGALENRHERKLVLTLDAERTRQLLQ 1318
Cdd:cd20484 161 LASspasyydFVAW-----EQdmlAGAEGEEhRAYWKQQLSGTlPIlELPADRPRSSAPSFEGQTYTRRLPSELSNQIKS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 1319 EApAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGR-EDLGEAIdlsrtVGWFTSLFPVR 1381
Cdd:cd20484 236 FA-RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRpEERFDSL-----IGYFINMLPIR 293
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1977-2511 |
9.58e-09 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 62.20 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1977 DWQAPLEALPRGGVAA---AFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVV 2053
Cdd:COG3321 848 DWSALYPGRGRRRVPLptyPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2054 GLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLA 2133
Cdd:COG3321 928 ALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAA 1007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 yviytSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLA 2213
Cdd:COG3321 1008 -----AALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAA 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2214 DEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQ 2293
Cdd:COG3321 1083 ALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAA 1162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2294 EGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVD 2373
Cdd:COG3321 1163 LAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAA 1242
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2374 GQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPA 2453
Cdd:COG3321 1243 AAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALA 1322
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2454 YMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLG 2511
Cdd:COG3321 1323 AALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAA 1380
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
2015-2428 |
1.46e-08 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 61.28 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE- 2093
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 -------TLAERLPC----------------------PAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQ 2144
Cdd:cd17641 93 eqvdkllEIADRIPSvryviycdprgmrkyddprlisFEDVVALGRALDRRDPGLYEREVAAGKGEDVAVLCTTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2145 PKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFdaAAEQLFV---PLLAGARVLLGDagqwSAQHLADEVERHAV 2221
Cdd:cd17641 173 PKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW--IGEQMYSvgqALVCGFIVNFPE----EPETMMEDLREIGP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2222 TILDLPPAYLQQQAEELR----HAGR------RIAVRtciLGGEAWDASLltqQAVQAEAWFN-AYGPTEAVI-TPLAWH 2289
Cdd:cd17641 247 TFVLLPPRVWEGIAADVRarmmDATPfkrfmfELGMK---LGLRALDRGK---RGRPVSLWLRlASWLADALLfRPLRDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2290 C------RAQEGGAP----------AIGRAL----GARRACIL-----DAALQPCAPGM-----------IGELYIGGQC 2333
Cdd:cd17641 321 LgfsrlrSAATGGAAlgpdtfrffhAIGVPLkqlyGQTELAGAytvhrDGDVDPDTVGVpfpgtevrideVGEILVRSPG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2334 LARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRA-DQQIKIRGFRIEIGEIESQLLAHPYVAEAA 2412
Cdd:cd17641 401 VFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAV 473
|
490
....*....|....*.
gi 2310915810 2413 VValdGVGGPLLAAYL 2428
Cdd:cd17641 474 VL---GAGRPYLTAFI 486
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
4531-5035 |
1.63e-08 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 60.93 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPLVHQRVAERARMAPD---AVAVIFDEEKLTYAELDSRANRLAHALIA-RGVGPEVRVAIAMQRSAEIMVAFLA 4606
Cdd:cd17632 33 TGYADRPALGQRATELVTDPATgrtTLRLLPRFETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4607 VLKAGGAYVPLDIEYPRERLLYMMQDSR-------------AHLLLTHSHLLERL------------------------P 4649
Cdd:cd17632 113 LTRLGAVSVPLQAGASAAQLAPILAETEprllavsaehldlAVEAVLEGGTPPRLvvfdhrpevdahraalesarerlaA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4650 IPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGpLIAH----IVATGERYEmtPEDCEL 4725
Cdd:cd17632 193 VGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTER-LVATfwlkVSSIQDIRP--PASITL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4726 HFMSFafdgSHEGWMHPLING-AR-------------------VLIRDDSLWLPERTYAEMHRHgvtvgvfppvYLQQLA 4785
Cdd:cd17632 270 NFMPM----SHIAGRISLYGTlARggtayfaaasdmstlfddlALVRPTELFLVPRVCDMLFQR----------YQAELD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4786 ehaerdgnpppvRVYCFGGDAVAQAsyDLAWRALKPKYLFNGYGPTETVVTPLLWKARAG-DACGAAYMPIGTLLGNRSG 4864
Cdd:cd17632 336 ------------RRSVAGADAETLA--ERVKAELRERVLGGRLLAAVCGSAPLSAEMKAFmESLLDLDLHDGYGSTEAGA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4865 YILDGQLNLLPV------GVA-------------GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRG 4925
Cdd:cd17632 402 VILDGVIVRPPVldyklvDVPelgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDVMAE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4926 RADGVVDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVVAQpgAVGQQLVGYVVAQEPAVADSPEAQAecRAQL 5004
Cdd:cd17632 475 LGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGN--SERAYLLAVVVPTQDALAGEDTARL--RAAL 550
|
570 580 590
....*....|....*....|....*....|....*..
gi 2310915810 5005 KTALRE-----RLPEYMVPSHLLfLARMPLTP-NGKL 5035
Cdd:cd17632 551 AESLQRiareaGLQSYEIPRDFL-IETEPFTIaNGLL 586
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1583-1828 |
1.74e-08 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 60.57 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFlwkdgwPQPLQVVF------EQATLELRLAPPGSD--PQRQAE-AEREagFDPA 1653
Cdd:cd19546 37 GRLDRDALEAALGDVAARHEILRTTF------PGDGGDVHqrildaDAARPELPVVPATEEelPALLADrAAHL--FDLT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1654 RAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ------EVAATVGRYRDYIGW-------LQGRD 1720
Cdd:cd19546 109 RETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrapERAPLPLQFADYALWerellagEDDRD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1721 AMATE--FFWRDRLA----SLEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHC 1794
Cdd:cd19546 189 SLIGDqiAYWRDALAgapdELELPTDRPRPVLPSRRAGAVPLR-LDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLG 267
|
250 260 270
....*....|....*....|....*....|....
gi 2310915810 1795 GQETVAFGaTVAGRPAELPGIEAQIGLFINTLPV 1828
Cdd:cd19546 268 AGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLAL 300
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4531-5040 |
1.95e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 60.76 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPL-----VHQRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVA 4603
Cdd:PLN02330 17 SRYPSVPVpdkltLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4604 FLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER-----LPIPEgLSCLSVDREEEW-----AGFPAHDP 4673
Cdd:PLN02330 97 ALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKvkglgLPVIV-LGEEKIEGAVNWkelleAADRAGDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4674 EV--ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT--GERYEMTPEDCELHFMSFAFDGSHEG-WMHPLINGAR 4748
Cdd:PLN02330 176 SDneEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSlfSVGPEMIGQVVTLGLIPFFHIYGITGiCCATLRNKGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4749 VLIRD--------DSLWLPERTYAEmhrhgvtvgVFPPVYLQQLAEHAERDGNPPPVRVycfggDAVAQASYDLA---WR 4817
Cdd:PLN02330 256 VVVMSrfelrtflNALITQEVSFAP---------IVPPIILNLVKNPIVEEFDLSKLKL-----QAIMTAAAPLApelLT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 ALKPKY----LFNGYGPTE-TVVTPLLWKARAGDACgAAYMPIGTLLGNRSGYILDGQLNL-LPVGVAGELYLGGEGVAR 4891
Cdd:PLN02330 322 AFEAKFpgvqVQEAYGLTEhSCITLTHGDPEKGHGI-AKKNSVGFILPNLEVKFIDPDTGRsLPKNTPGELCVRSQCVMQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4892 GYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:PLN02330 401 GYYNNKEETDRTIDEDGW-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 4972 PGAVGQQLVGYVVAQEPAVADSPEAQAECRAqlktalrERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN02330 474 PDEEAGEIPAACVVINPKAKESEEDILNFVA-------ANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
3062-3481 |
2.07e-08 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 60.56 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL- 3140
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 ----SQSHLKLPLAQGVQRIDLDRGAP------WFEDYSEANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSALSn 3207
Cdd:cd05932 85 gkldDWKAMAPGVPEGLISISLPPPSAancqyqWDDLIAQHPPLEERptrFPEQLATLIYTSGTTGQPKGVMLTFGSFA- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 rlcWMQQA----YGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgdhrdpaklvalinrEGVDTlhfvpsml 3282
Cdd:cd05932 164 ---WAAQAgiehIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVAFA-----------------ESLDT-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3283 qaFLQDEDVASCTslkrIVCSGEALPADAQQQVFAKLPQAGLYNLYG----------PTEAAIDVTHWTCVEEGKDAVP- 3351
Cdd:cd05932 216 --FVEDVQRARPT----LFFSVPRLWTKFQQGVQDKIPQQKLNLLLKipvvnslvkrKVLKGLGLDQCRLAGCGSAPVPp 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 --------IGRPI-------ANLACYILD----------GNLEP---VPVGVLGELYLAGQGLARGYHQRPGLTAERFVA 3403
Cdd:cd05932 290 allewyrsLGLNIleaygmtENFAYSHLNypgrdkigtvGNAGPgveVRISEDGEILVRSPALMMGYYKDPEATAEAFTA 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3404 SPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESE 3481
Cdd:cd05932 370 DGFL------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEE 442
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
3448-3519 |
2.07e-08 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 54.09 E-value: 2.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3448 EIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPdelkGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
4561-5040 |
2.27e-08 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 60.13 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllt 4640
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4641 hshlleRLPIPEGLSCLSVDREEEwagfPAHDPEVALHgDNLAYvIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05939 77 ------KALIFNLLDPLLTQSSTE----PPSQDDVNFR-DKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDceLHFMSFAFDGSHEGWM---HPLINGARVLIRDDslWLPERTYAEMHRHGVTVGvfppvylQQLAEHAERDGNPPPV 4797
Cdd:cd05939 145 ED--VVYDCLPLYHSAGGIMgvgQALLHGSTVVIRKK--FSASNFWDDCVKYNCTIV-------QYIGEICRYLLAQPPS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4798 ------RVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGdACGaaYMPIgtllgnrsgyILdgqL 4871
Cdd:cd05939 214 eeeqkhNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVG-ACG--FNSR----------IL---P 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4872 NLLPVGV------AGELYLGGEGVA------------------------RGYLERPAlTAERFVPDPFgAPGSRLYRSGD 4921
Cdd:cd05939 278 SVYPIRLikvdedTGELIRDSDGLCipcqpgepgllvgkiiqndplrrfDGYVNEGA-TNKKIARDVF-KKGDSAFLSGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4922 LTrgradgVVDYLG------RVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADs 4993
Cdd:cd05939 356 VL------VMDELGylyfkdRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGR-------AGMAAIVD- 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2310915810 4994 PEAQAECrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05939 422 PERKVDL-DRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
4552-5037 |
2.46e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 60.54 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4552 DAVAVIF------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG-------GAYVPld 4618
Cdd:PRK00174 82 DKVAIIWegddpgDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGFSA-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 iEYPRERLlymmQDSRAhlllthshlleRL------------PIP------EGLS-CLSVDR------------------ 4661
Cdd:PRK00174 160 -EALADRI----IDAGA-----------KLvitadegvrggkPIPlkanvdEALAnCPSVEKvivvrrtggdvdwvegrd 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4662 ---EEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeryemtpedcelhfMSFAFDgSHE- 4737
Cdd:PRK00174 224 lwwHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMT---------------MKYVFD-YKDg 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4738 ---------GWM--H------PLINGARVLIRD--------DSLWlpertyaEM-HRHGVTVGVFPPVYLQQLAehaeRD 4791
Cdd:PRK00174 288 dvywctadvGWVtgHsyivygPLANGATTLMFEgvpnypdpGRFW-------EViDKHKVTIFYTAPTAIRALM----KE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4792 GNPPPvrvycfggdavaqASYDL----------------AWRalkpkYLFNGYG----P-------TET---VVTPLlwk 4841
Cdd:PRK00174 357 GDEHP-------------KKYDLsslrllgsvgepinpeAWE-----WYYKVVGgercPivdtwwqTETggiMITPL--- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 aragdaCGAAYMPIGT----LLGnRSGYILDGQLNLLPvgvagelylGGEGvarGYL--ERP----ALTA----ERFVPD 4907
Cdd:PRK00174 416 ------PGATPLKPGSatrpLPG-IQPAVVDEEGNPLE---------GGEG---GNLviKDPwpgmMRTIygdhERFVKT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4908 PFGA-PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVA 4985
Cdd:PRK00174 477 YFSTfKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIkGQGIYAFVTL 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4986 QEPAvadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PRK00174 555 KGGE-----EPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
4563-4731 |
2.65e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 60.31 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGV--GPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLdieYPR---ERLLYMMQDSRAhl 4637
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPL---YDTlgpEAIEYILNHAEI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 llthshllERLPIPEGLSCLSVDREEEWAGFPAHDPEVAlHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVA----TG 4713
Cdd:cd05927 81 --------SIVFCDAGVKVYSLEEFEKLGKKNKVPPPPP-KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvfkiLE 151
|
170
....*....|....*...
gi 2310915810 4714 ERYEMTPEDCELHFMSFA 4731
Cdd:cd05927 152 ILNKINPTDVYISYLPLA 169
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
921-992 |
3.68e-08 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 53.32 E-value: 3.68e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 921 EIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPdelkGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
2011-2481 |
4.34e-08 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 59.36 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CQetlaerlpcpaEVERLPLETAAWPASADTRPLPEVagetLAYvIYTSGSTGQPKgvavsqAALVAHCQ------AAAR 2164
Cdd:cd05939 81 FN-----------LLDPLLTQSSTEPPSQDDVNFRDK----LFY-IYTSGTTGLPK------AAVIVHSRyyriaaGAYY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2165 TYGVGPGDcqlqfasISFDAaaeqlfVPLL--AGARVLLGDA----------GQWSAQHLADEVERHAVTI--------- 2223
Cdd:cd05939 139 AFGMRPED-------VVYDC------LPLYhsAGGIMGVGQAllhgstvvirKKFSASNFWDDCVKYNCTIvqyigeicr 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2224 --LDLPPAylqqqAEELRHagrriAVRTCI---LGGEAWdaslltQQAVQAeawFNA------YGPTE--AVITPLAWHC 2290
Cdd:cd05939 206 ylLAQPPS-----EEEQKH-----NVRLAVgngLRPQIW------EQFVRR---FGIpqigefYGATEgnSSLVNIDNHV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2291 RAQeGGAPAIGRALGARRACILDAAL-----------QPCAPGMIGELY---IGGQCLAR--GYLGRpGQTAERFVADPF 2354
Cdd:cd05939 267 GAC-GFNSRILPSVYPIRLIKVDEDTgelirdsdglcIPCQPGEPGLLVgkiIQNDPLRRfdGYVNE-GATNKKIARDVF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2355 SgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAYLVgrD 2432
Cdd:cd05939 345 K-KGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIV--D 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2310915810 2433 AMRGEDlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:cd05939 422 PERKVD-LDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
2010-2457 |
4.84e-08 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 59.61 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRA-RGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARW 2088
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LIC----QETLAERLPC----------------PAEVERLPLETAAWPASADTRPLP-EVAGETLAYVIYTSGSTGQPKG 2147
Cdd:cd05938 82 LVVapelQEAVEEVLPAlradgvsvwylshtsnTEGVISLLDKVDAASDEPVPASLRaHVTIKSPALYIYTSGTTGLPKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAhCQAAARTYGVGPGDcqlqfasISFDAaaeqlfVPLLAGARVLLGDAG------------QWSAQHLADE 2215
Cdd:cd05938 162 ARISHLRVLQ-CSGFLSLCGVTADD-------VIYIT------LPLYHSSGFLLGIGGcielgatcvlkpKFSASQFWDD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVTIL-----------DLPpaylqQQAEELRHagrriAVRTCILGGeawdaslltqqaVQAEAW------------ 2272
Cdd:cd05938 228 CRKHNVTVIqyigellrylcNQP-----QSPNDRDH-----KVRLAIGNG------------LRADVWreflrrfgpiri 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 FNAYGPTEAVITPLAWhcraqEGGAPAIGRA-----------------------LGARRACIldaalqPCAPGMIGELY- 2328
Cdd:cd05938 286 REFYGSTEGNIGFFNY-----TGKIGAVGRVsylykllfpfelikfdvekeepvRDAQGFCI------PVAKGEPGLLVa 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 -IGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:cd05938 355 kITQQSPFLGYAGDKEQTEKKLLRDVFK-KGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDF 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2408 VAEAAV--VALDGVGGPLLAAYLVGRD--AMRGEDLLAELRTWlagrLPAYMQP 2457
Cdd:cd05938 434 LQEVNVygVTVPGHEGRIGMAAVKLKPghEFDGKKLYQHVREY----LPAYARP 483
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
3059-3484 |
5.06e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 59.37 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3059 FGEERLDYAELNRRANRLAHALI-ERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDpeypeerqaYMLEDSGVE 3137
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3138 LLLSQSHLKLPLAqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW-----M 3212
Cdd:cd05937 72 HCLKLSGSRFVIV---------------------------DPDDPAILIYTSGTTGLPKAA-----AISWRRTLvtsnlL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3213 QQAYGLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHR--------DPAKLVALINREGVDTLHFVPSmlq 3283
Cdd:cd05937 120 SHDLNLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRKFSASqfwkdvrdSGATIIQYVGELCRYLLSTPPS--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3284 aflQDEDVASCtslkrIVCSGEALPAD---AQQQVFAkLPQAGlyNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLa 3360
Cdd:cd05937 197 ---PYDRDHKV-----RVAWGNGLRPDiweRFRERFN-VPEIG--EFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRW- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3361 cyILDGNLEPV---------------------PVG----VLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRT 3415
Cdd:cd05937 265 --KFENQVVLVkmdpetddpirdpktgfcvraPVGepgeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRT 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3416 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGD 3484
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGRAGCAAITLEESSAV 416
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
651-939 |
5.96e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 59.15 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 651 NGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTP----FSFDVSVWEFFWplmsGARLVV 724
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGpdDRYLAYLPlahiFELAAENVCLYR----GGTIGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 725 AAP---------GDHRD-----PAKLV------ELInREGV-DTLHFVPSMLQ-------------------AFLQDEDV 764
Cdd:cd17639 162 GSPrtltdkskrGCKGDltefkPTLMVgvpaiwDTI-RKGVlAKLNPMGGLKRtlfwtayqsklkalkegpgTPLLDELV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 765 ------ASCTSLKRIVCSGEALPADAQQQ---VFAKLPQAglynlYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGnlG 833
Cdd:cd17639 241 fkkvraALGGRLRYMLSGGAPLSADTQEFlniVLCPVIQG-----YGLTEtcAGGTVQDPGDLETGR----VGPPLP--C 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 834 CYIL-----DGNLE---PVPvgvLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGVIEYAGR 905
Cdd:cd17639 310 CEIKlvdweEGGYStdkPPP---RGEILIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDR 380
|
330 340 350
....*....|....*....|....*....|....*
gi 2310915810 906 IDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:cd17639 381 KKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
3654-3782 |
6.70e-08 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 58.60 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3654 REALNAkaLEAALQALVEHHDALRLRFHetdgtW------------HAE--HAEATLGGallwrAEAVDRQaLESLCEES 3719
Cdd:cd19544 35 RARLDA--FLAALQQVIDRHDILRTAIL-----WeglsepvqvvwrQAElpVEELTLDP-----GDDALAQ-LRARFDPR 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3720 QRSLDLTDGPLLRSLLVDMADGGQRLLLV-IHHLVVDGVSWRILLEDLQrAYqqsLRGEAPRLP 3782
Cdd:cd19544 102 RYRLDLRQAPLLRAHVAEDPANGRWLLLLlFHHLISDHTSLELLLEEIQ-AI---LAGRAAALP 161
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1133-1320 |
8.40e-08 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 58.22 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1133 DRLGRALERLQAQHDALRLRFreergAWhqayaEQAGEPL---WRR------------QAGSEEALLALCEEAQRSLDLE 1197
Cdd:cd19544 39 DAFLAALQQVIDRHDILRTAI-----LW-----EGLSEPVqvvWRQaelpveeltldpGDDALAQLRARFDPRRYRLDLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1198 QGPLLRALLV-DMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLgPRSSSYqtwsRHLHEQAGARLDELD-- 1274
Cdd:cd19544 109 QAPLLRAHVAeDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRAAAL-PPPVPY----RNFVAQARLGASQAEhe 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1275 -YWQAQLHD-----APHALpcENPHGALENRHErkLVLTLDAERTRQLLQEA 1320
Cdd:cd19544 184 aFFREMLGDvdeptAPFGL--LDVQGDGSDITE--ARLALDAELAQRLRAQA 231
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
536-950 |
8.94e-08 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 58.60 E-value: 8.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvqlLLSQ 615
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYS---------------LMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 616 SHLKL------------------PLAQGVQRI-DLDQADAWLENHAENNPGIELNG-------------------ENLAY 657
Cdd:cd05921 90 DLAKLkhlfellkpglvfaqdaaPFARALAAIfPLGTPLVVSRNAVAGRGAISFAElaatpptaavdaafaavgpDTVAK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTvlqktPFSFDVSVWEFFWPLMSGARLVVAAPGD-HRD---- 732
Cdd:cd05921 170 FLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP-----PVLVDWLPWNHTFGGNHNFNLVLYNGGTlYIDdgkp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 733 -PAKLVELIN--REGVDTLHF-VP---SMLQAFLQDeDVASCTS----LKRIVCSGEALPAD--------AQQQVFAKLP 793
Cdd:cd05921 245 mPGGFEETLRnlREISPTVYFnVPagwEMLVAALEK-DEALRRRffkrLKLMFYAGAGLSQDvwdrlqalAVATVGERIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 794 qagLYNLYGPTEAA--IDVTHWtcveegkdtvPIGRPiGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTA 871
Cdd:cd05921 324 ---MMAGLGATETAptATFTHW----------PTERS-GLIGLPAPGTELKLVPSGGKYEVRVKGPNVTPGYWRQPELTA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 872 ERFVASPFvagermYRTGDLARYrAD------GVIeYAGRIDHQVKLR-GLRIELGEIEARLLEH--PWVREaAVLAVDG 942
Cdd:cd05921 390 QAFDEEGF------YCLGDAAKL-ADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD-AVVAGED 460
|
....*...
gi 2310915810 943 RQLVGYVV 950
Cdd:cd05921 461 RAEVGALV 468
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
2006-2419 |
9.31e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.47 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07768 18 GMVTGEPDapvrHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDS-------GARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPlPEVAGETLAYVIYTSGSTGQPKGVAVSQAA 2154
Cdd:PRK07768 98 EDTlrvigmiGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAADPIDP-VETGEDDLALMQLTSGSTGSPKAVQITHGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2155 LVAHCQAaartygvgpgdcqlQFASISFDAAAEQ----------------LFVPLLAGARVL-------LGDAGQWsaqh 2211
Cdd:PRK07768 177 LYANAEA--------------MFVAAEFDVETDVmvswlplfhdmgmvgfLTVPMYFGAELVkvtpmdfLRDPLLW---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 lADEVERHAVTILDLPP-AY------LQQQAEELRH--AGRRIAVRtcilGGEAWD----ASLLTQQA---VQAEAWFNA 2275
Cdd:PRK07768 239 -AELISKYRGTMTAAPNfAYallarrLRRQAKPGAFdlSSLRFALN----GAEPIDpadvEDLLDAGArfgLRPEAILPA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTEAVIT------------------PLAWHCRA---QEGGA---PAIGRALGARRACILDAALQPCAPGMIGELYIGG 2331
Cdd:PRK07768 314 YGMAEATLAvsfspcgaglvvdevdadLLAALRRAvpaTKGNTrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2332 QCLARGYLgrpgqTAERFVA--DPfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIeigeiesqllaHPYVA 2409
Cdd:PRK07768 394 ESVTPGYL-----TMDGFIPaqDA-----DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNI-----------YPTDI 452
|
490
....*....|
gi 2310915810 2410 EAAVVALDGV 2419
Cdd:PRK07768 453 ERAAARVEGV 462
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
532-943 |
1.01e-07 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 58.21 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 532 FGEERLDYAELNRRANRLAHALI-ERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDpeypeerqaYMLEDSGVQ 610
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 611 LLLSQSHLKLPLAqgvqridlDQADawlenhaennpgielngenLAYVIYTSGSTGKPKGAgnrhsALSNRLCW-----M 685
Cdd:cd05937 72 HCLKLSGSRFVIV--------DPDD-------------------PAILIYTSGTTGLPKAA-----AISWRRTLvtsnlL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 686 QQAYGLGVGDTVLQKTPF------------------------SFDVSVwefFWP--LMSGA----------RLVVAAPGD 729
Cdd:cd05937 120 SHDLNLKNGDRTYTCMPLyhgtaaflgacnclmsggtlalsrKFSASQ---FWKdvRDSGAtiiqyvgelcRYLLSTPPS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 730 HRDPAKLVELINREGVDtlhfvPSMLQAFLQDEDVASCTSLKRivcSGEALPADAQQQV--FAklpqAGLYNLYGPteaa 807
Cdd:cd05937 197 PYDRDHKVRVAWGNGLR-----PDIWERFRERFNVPEIGEFYA---ATEGVFALTNHNVgdFG----AGAIGHHGL---- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 808 idVTHWTCveeGKDTVPIgRPIGNLGCYILD---GNLEPVPVG----VLGELYLAGRGLARGYHQRPGLTAERFVASPFV 880
Cdd:cd05937 261 --IRRWKF---ENQVVLV-KMDPETDDPIRDpktGFCVRAPVGepgeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFR 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGR 943
Cdd:cd05937 335 KGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGR 402
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
3299-3466 |
1.31e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 58.00 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEA-LPADAQQQ---VFAKLPQAglynlYGPTE--AAIDVTHWTCVEEGKdavpIGRPIAnlACYIL-----DGN 3367
Cdd:cd17639 253 RYMLSGGApLSADTQEFlniVLCPVIQG-----YGLTEtcAGGTVQDPGDLETGR----VGPPLP--CCEIKlvdweEGG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3368 LE---PVPvgvLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLR 3443
Cdd:cd17639 322 YStdkPPP---RGEILIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEY 392
|
170 180
....*....|....*....|...
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLA 3466
Cdd:cd17639 393 IALEKLESIYRSNPLVNNICVYA 415
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
881-1005 |
1.51e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 57.35 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEGG 956
Cdd:PRK08308 288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEID 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 957 -----DWrealaahLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSV 1005
Cdd:PRK08308 368 pvqlrEW-------CIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
2122-2496 |
1.68e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.05 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2122 RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAARTyGVGPGD----CQLQFASISFDAAaeqLFVPLLAG 2196
Cdd:PRK06814 785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRaQVAARI-DFSPEDkvfnALPVFHSFGLTGG---LVLPLLSG 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2197 ARVLLGDagqwSAQH---LADEVERHAVTILDLPPAYLQQQAeELRHAGRRIAVRTCILGGEAWDASllTQQaVQAEAW- 2272
Cdd:PRK06814 861 VKVFLYP----SPLHyriIPELIYDTNATILFGTDTFLNGYA-RYAHPYDFRSLRYVFAGAEKVKEE--TRQ-TWMEKFg 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 ---FNAYGPTE-----AVITPLawHCRAQeggapAIGRALGArraciLDAALQPcAPG--MIGELYIGGQCLARGYL--G 2340
Cdd:PRK06814 933 iriLEGYGVTEtapviALNTPM--HNKAG-----TVGRLLPG-----IEYRLEP-VPGidEGGRLFVRGPNVMLGYLraE 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGqtaerfVADPFSgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESqlLAHPY--VAEAAVVAL-D 2417
Cdd:PRK06814 1000 NPG------VLEPPA---DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAELwpDALHAAVSIpD 1068
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2418 GVGGPLLAAYLVGRDAMRgEDLLAELRTWLAGRLpayMQPTAWQVLSSLPLNANGKLDrkaLPKVDAAARRQAGEPPRE 2496
Cdd:PRK06814 1069 ARKGERIILLTTASDATR-AAFLAHAKAAGASEL---MVPAEIITIDEIPLLGTGKID---YVAVTKLAEEAAAKPEAA 1140
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
4555-4973 |
1.71e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 57.52 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4555 AVIFDEE--KLTYaeldsraNRLAHALIARGVG----PEVRVAIAMQRSAEIMVAFLAVLKAGGAYV------------- 4615
Cdd:PRK06334 36 TVCWDEQlgKLSY-------NQVRKAVIALATKvskyPDQHIGIMMPASAGAYIAYFATLLSGKIPVminwsqglrevta 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 --------------PL----------DIEYPRErLLYMmQDSRAHLLLThshllERLPIPEGLSClSVDREEEWAGFPAH 4671
Cdd:PRK06334 109 canlvgvthvltskQLmqhlaqthgeDAEYPFS-LIYM-EEVRKELSFW-----EKCRIGIYMSI-PFEWLMRWFGVSDK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4672 DPEvalhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM-SFAFDGSHEGWMHPLINGARVL 4750
Cdd:PRK06334 181 DPE------DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLpPFHAYGFNSCTLFPLLSGVPVV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IRDDSLWlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYG 4829
Cdd:PRK06334 255 FAYNPLY-PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESClPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4830 PTET--VVTPLLWKARAGDACGAayMPI---GTLLGNRSGYIldgqlnLLPVGVAGELYLGGEGVARGYLErpALTAERF 4904
Cdd:PRK06334 334 TTECspVITINTVNSPKHESCVG--MPIrgmDVLIVSEETKV------PVSSGETGLVLTRGTSLFSGYLG--EDFGQGF 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4905 VPdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH---PAVREA---VVVAQPG 4973
Cdd:PRK06334 404 VE----LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAgplVVCGLPG 474
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
3066-3465 |
1.93e-07 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 57.43 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS---- 3141
Cdd:cd17641 14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAedee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 QSHLKLPLAQGVQRIDL-----DRGAP--------WFEDYSEANPDIH-------------LDGENLAYVIYTSGSTGKP 3195
Cdd:cd17641 94 QVDKLLEIADRIPSVRYviycdPRGMRkyddprliSFEDVVALGRALDrrdpglyerevaaGKGEDVAVLCTTSGTTGKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3196 KGA----GN--RHSALSNR---------------LCW-MQQAYGLGVG-------------DTVLQK------TPFSFDV 3234
Cdd:cd17641 174 KLAmlshGNflGHCAAYLAadplgpgdeyvsvlpLPWiGEQMYSVGQAlvcgfivnfpeepETMMEDlreigpTFVLLPP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3235 SVWE------------------FFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPsmlqafLQDEdvASCTS 3296
Cdd:cd17641 254 RVWEgiaadvrarmmdatpfkrFMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRP------LRDR--LGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3297 LKRIVCSGEALPADaqqqVFAKLPQAG--LYNLYGPTEAAIDVThwtcVEEGKDAVP--IGRPIANLACYILDgnlepvp 3372
Cdd:cd17641 326 LRSAATGGAALGPD----TFRFFHAIGvpLKQLYGQTELAGAYT----VHRDGDVDPdtVGVPFPGTEVRIDE------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3373 vgvLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEA 3451
Cdd:cd17641 391 ---VGEILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIEN 461
|
490
....*....|....
gi 2310915810 3452 RLLEHPWVREAAVL 3465
Cdd:cd17641 462 KLKFSPYIAEAVVL 475
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1100-1399 |
2.38e-07 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 56.94 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQRWFFEQSI--PNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR--- 1174
Cdd:cd19547 4 LAPMQEGMLFRGLfwPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWAlld 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1175 -------RQAGSEEALLAlcEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD 1247
Cdd:cd19547 84 wsgedpdRRAELLERLLA--DDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1248 LGPRSS---SYQTWSRHLHEQAgARLDELD-YWQAQLHDAPHALPCENPHgalENRHERKLVLTLDAERTRQLLQEAPAA 1323
Cdd:cd19547 162 REPQLSpcrPYRDYVRWIRART-AQSEESErFWREYLRDLTPSPFSTAPA---DREGEFDTVVHEFPEQLTRLVNEAARG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 1324 YRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLsrTVGWFTSLFP--VRLTPAADLGESLKAIKEQL 1399
Cdd:cd19547 238 YGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPlrIRLDPDQTVTGLLETIHRDL 313
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1118-1286 |
2.52e-07 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 56.81 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAgePlwRRQagsEEALLALCEEAQRSLDLE 1197
Cdd:cd19537 24 FNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSP--P--RVQ---RVDTLDVWKEINRPFDLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1198 QGPLLRALLvdmadgSQR-LLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQT-WSRHlheqagARLDELDY 1275
Cdd:cd19537 97 REDPIRVFI------SPDtLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTaWSRP------ASPEDLDF 164
|
170
....*....|.
gi 2310915810 1276 WQAQLHDAPHA 1286
Cdd:cd19537 165 WSEYLSGLPLL 175
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
2003-2155 |
3.24e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 57.05 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2003 EAIALVCGDEhLSYAELDMRAER--LAR-------GLRARGVVA--------EALVAIAAERSFDLVVGLLGILKAGAGY 2065
Cdd:PRK07769 28 ERWAKVRGDK-LAYRFLDFSTERdgVARdltwsqfGARNRAVGArlqqvtkpGDRVAILAPQNLDYLIAFFGALYAGRIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2066 LPL-DPNYP--AERLAYMLRD-------------SGARWLICQETLAERlPCPAEVERLPLETAAwpasadTRPLPEVAG 2129
Cdd:PRK07769 107 VPLfDPAEPghVGRLHAVLDDctpsailtttdsaEGVRKFFRARPAKER-PRVIAVDAVPDEVGA------TWVPPEANE 179
|
170 180
....*....|....*....|....*.
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:PRK07769 180 DTIAYLQYTSGSTRIPAGVQITHLNL 205
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
4684-5037 |
3.49e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 56.67 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4684 YVIYTSGSTGMPKGVAVSHGPliaHIVATGERYE-MTPEDCELHFMSFafdgSHEGWM--HPLINGARVL---------- 4750
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRsIIEKDIPTVVFSH----SSIGWVsfHGFLYGSLSLgntfvmfegg 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 ------IRDDsLWlpertyAEMHRHGVTVGVFPPVYLQQL------AEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRA 4818
Cdd:PTZ00237 331 iiknkhIEDD-LW------NTIEKHKVTHTLTLPKTIRYLiktdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4819 LKPKYLfNGYGPTETVVTPLLwkaragdACGAAYMPIGTLlGNRSGYIL------DGQLnlLPVGVAGELYLGgegvarg 4892
Cdd:PTZ00237 404 LKIKSS-RGYGQTEIGITYLY-------CYGHINIPYNAT-GVPSIFIKpsilseDGKE--LNVNEIGEVAFK------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4893 yLERPALTAERFVP--DPFGAPGSRL---YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PTZ00237 466 -LPMPPSFATTFYKndEKFKQLFSKFpgyYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4968 VVA-QPGAVGQQLVGYVVAQEPAvADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PTZ00237 545 SIGiYDPDCYNVPIGLLVLKQDQ-SNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
4550-5035 |
3.67e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 56.73 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4550 APDAVAVIFDEEK-----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG----------GAY 4614
Cdd:PRK03584 97 RDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiwsscspdfGVQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPLD----IEyPreRLL-----YMMQDSRAHLLLTHSHLLERLP----------IPEGLSCLSVDREEEWAGFPAHDPEV 4675
Cdd:PRK03584 177 GVLDrfgqIE-P--KVLiavdgYRYGGKAFDRRAKVAELRAALPslehvvvvpyLGPAAAAAALPGALLWEDFLAPAEAA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4676 ALHGDNLA-----YVIYTSGSTGMPKGVAVSH-GPLIAHIVATGERYEMTPEDCELHFMSfafdgshEGWM------HPL 4743
Cdd:PRK03584 254 ELEFEPVPfdhplWILYSSGTTGLPKCIVHGHgGILLEHLKELGLHCDLGPGDRFFWYTT-------CGWMmwnwlvSGL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDS--------LWlperTYAEmhRHGVTV-GVFPPvYLQQLAE---HAERDGNPPPVRVYCFGGDAVAQAS 4811
Cdd:PRK03584 327 LVGATLVLYDGSpfypdpnvLW----DLAA--EEGVTVfGTSAK-YLDACEKaglVPGETHDLSALRTIGSTGSPLPPEG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 YDLAWRALKPK-YLFNGYGPTetvvtpllwkaragDACGAaympigTLLGNRsgyildgqlnLLPVgVAGEL---YLG-- 4885
Cdd:PRK03584 400 FDWVYEHVKADvWLASISGGT--------------DICSC------FVGGNP----------LLPV-YRGEIqcrGLGma 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4886 -------GEGVARgylERPALTAERFVP--------DPFGA----------PGsrLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:PRK03584 449 veawdedGRPVVG---EVGELVCTKPFPsmplgfwnDPDGSryrdayfdtfPG--VWRHGDWIEITEHGGVVIYGRSDAT 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADspeaqAECRAQLKTALRERLPEYMVPS 5019
Cdd:PRK03584 524 LNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDvRMPLFVVLAEGVTLD-----DALRARIRTTIRTNLSPRHVPD 598
|
570
....*....|....*.
gi 2310915810 5020 HLLFLARMPLTPNGKL 5035
Cdd:PRK03584 599 KIIAVPDIPRTLSGKK 614
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
2014-2413 |
5.81e-07 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 55.82 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQ 2092
Cdd:cd05905 15 LTWGKLLSRAEKIAAVLQKKVGLkPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2093 ETLAERLPCPAEVERLPLETA---AWPASADT--------------RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:cd05905 95 EACLKGLPKKLLKSKTAAEIAkkkGWPKILDFvkipkskrsklkkwGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2156 VAHCQAAARTYGVGPGD---CQLQFAS-ISFDAAAeqlFVPLLAGARVLLGD-----AGQWSAQHLadeVERHAVTILDL 2226
Cdd:cd05905 175 LAHCRALKEACELYESRplvTVLDFKSgLGLWHGC---LLSVYSGHHTILIPpelmkTNPLLWLQT---LSQYKVRDAYV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 P----PAYLQQQAEELRHAGRRI----AVRTCIL-GGEAWDASlLTQQAVQAeawFNAYGPTEAVITPLAWHC------- 2290
Cdd:cd05905 249 KlrtlHWCLKDLSSTLASLKNRDvnlsSLRMCMVpCENRPRIS-SCDSFLKL---FQTLGLSPRAVSTEFGTRvnpficw 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2291 RAQEGGAPAIG----RAL----------GARRA-CILDAA---------------LQPCAPGMIGELYIGGQCLARGYLG 2340
Cdd:cd05905 325 QGTSGPEPSRVyldmRALrhgvvrlderDKPNSlPLQDSGkvlpgaqvaivnpetKGLCKDGEIGEIWVNSPANASGYFL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQT-AERFVADPFSGS---GERLY-RTGDLARYR---------VDGQVEY-LGRADQQIKIRGFRIEIGEIESQ-LLA 2404
Cdd:cd05905 405 LDGETnDTFKVFPSTRLStgiTNNSYaRTGLLGFLRptkctdlnvEEHDLLFvVGSIDETLEVRGLRHHPSDIEATvMRV 484
|
....*....
gi 2310915810 2405 HPYVAEAAV 2413
Cdd:cd05905 485 HPYRGRCAV 493
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
515-940 |
6.48e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 55.77 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 515 RLFEEQVERTPTAP-ALAFGE----ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA-- 587
Cdd:PRK07768 3 RFTEKMYANARTSPrGMVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 588 --YVP---VD-PEYPEE--RQAYMLEDSGVqlLLSQSHLKL-PL--AQGVQRIDLDQADAwlenhAENNPGIELNGENLA 656
Cdd:PRK07768 83 mlHQPtprTDlAVWAEDtlRVIGMIGAKAV--VVGEPFLAAaPVleEKGIRVLTVADLLA-----ADPIDPVETGEDDLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 657 YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG-DTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAAPGDH-RDP 733
Cdd:PRK07768 156 LMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPMDFlRDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 734 AKLVELINR-EGVDTL--HFVPSMLQAFL--QDEDVA-SCTSLKRIVCSGEAL-PADAQQQVFA----KLPQAGLYNLYG 802
Cdd:PRK07768 236 LLWAELISKyRGTMTAapNFAYALLARRLrrQAKPGAfDLSSLRFALNGAEPIdPADVEDLLDAgarfGLRPEAILPAYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 803 PTEAAIDVTHWTC-------------VEEGKDTVP-----------IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRG 858
Cdd:PRK07768 316 MAEATLAVSFSPCgaglvvdevdadlLAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 859 LARGYhqrpgLTAERFVasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 938
Cdd:PRK07768 396 VTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
..
gi 2310915810 939 AV 940
Cdd:PRK07768 469 AV 470
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
3042-3467 |
6.54e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 55.77 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAP-ALAFGE----ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA-- 3114
Cdd:PRK07768 3 RFTEKMYANARTSPrGMVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 --YVP---VD-PEYPEE--RQAYMLEDSGVEL---------LLSQSHLKlplaqgVQRI-DLDRGAPwfEDYSEANPDih 3176
Cdd:PRK07768 83 mlHQPtprTDlAVWAEDtlRVIGMIGAKAVVVgepflaaapVLEEKGIR------VLTVaDLLAADP--IDPVETGED-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3177 ldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG-DTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAAP 3254
Cdd:PRK07768 153 ----DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3255 GDH-RDPAKLVALINR-EGVDTL--HFVPSMLQAFL--QDEDVA-SCTSLKRIVCSGEAL-PADAQQQVFA----KLPQA 3322
Cdd:PRK07768 229 MDFlRDPLLWAELISKyRGTMTAapNFAYALLARRLrrQAKPGAfDLSSLRFALNGAEPIdPADVEDLLDAgarfGLRPE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3323 GLYNLYGPTEAAIDVTHWTC-------------VEEGKDAVP-----------IGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:PRK07768 309 AILPAYGMAEATLAVSFSPCgaglvvdevdadlLAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYLAGQGLARGYhqrpgLTAERFVasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:PRK07768 389 IELRGESVTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEG 461
|
....*....
gi 2310915810 3459 VREAAVLAV 3467
Cdd:PRK07768 462 VRPGNAVAV 470
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
3408-3532 |
7.06e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 55.43 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3408 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESE-- 3481
Cdd:PRK08308 288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEid 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3482 SGDWREalaaHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAA 3532
Cdd:PRK08308 368 PVQLRE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
533-998 |
7.59e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 55.56 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 533 GEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK05620 35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 612 LLSQSHLKLPLAQ------GVQRI------DLDQA-------------DAWLENHAENNPGIELNGENLAYVIYTSGSTG 666
Cdd:PRK05620 115 IVADPRLAEQLGEilkecpCVRAVvfigpsDADSAaahmpegikvysyEALLDGRSTVYDWPELDETTAAAICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 667 KPKGAGNRHSALsnrlcWMQqAYGLGVGDT--VLQKTPFSFDVSVWEFF-W--PL---MSGARLVVaaPGDHRDPAKLVE 738
Cdd:PRK05620 195 APKGVVYSHRSL-----YLQ-SLSLRTTDSlaVTHGESFLCCVPIYHVLsWgvPLaafMSGTPLVF--PGPDLSAPTLAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 739 LINREGVDTLHFVP----SMLQAFLQDEdvASCTSLKRIVCSGEALPAdaqqqVFAKLPQAGlynlYGpteaaIDVTH-W 813
Cdd:PRK05620 267 IIATAMPRVAHGVPtlwiQLMVHYLKNP--PERMSLQEIYVGGSAVPP-----ILIKAWEER----YG-----VDVVHvW 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 814 TCVEegkdTVPIGR----PIGNLG----CY---------------ILDGNLEPVPVGVLGELYLAGRGLARGYHQRP--- 867
Cdd:PRK05620 331 GMTE----TSPVGTvarpPSGVSGearwAYrvsqgrfpasleyriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPtee 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 868 -GLTAERFVASPFVAGERMY------RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK05620 407 gGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 941 DGRQLVGY---VVLESEGGDWR----EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK05620 487 PDDKWGERplaVTVLAPGIEPTretaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
4558-4702 |
8.87e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 55.38 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4558 FDEEKLTYAELDSRANRLAHALIA-RGVGPEVRVAIAMQRSAEIMVAFLAVLKAG--GAYVPLDIEypRERLLYMMQDSR 4634
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNTNIR--SKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4635 A----HLLLTHSHLLERLP----------------IPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGM 4694
Cdd:cd05938 79 AkvlvVAPELQEAVEEVLPalradgvsvwylshtsNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGL 158
|
....*...
gi 2310915810 4695 PKGVAVSH 4702
Cdd:cd05938 159 PKAARISH 166
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
3060-3433 |
1.30e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 55.12 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEER-LDYAELNRRANRLAHALIERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSG 3135
Cdd:PRK07769 51 GVARdLTWSQFGARNRAVGARLQQVTKPGDR-VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3136 VELLLSQSHL---------KLPLAQGVQRIDLDR-----GAPWfedyseANPDIHLDgeNLAYVIYTSGSTGKPKGAGNR 3201
Cdd:PRK07769 130 PSAILTTTDSaegvrkffrARPAKERPRVIAVDAvpdevGATW------VPPEANED--TIAYLQYTSGSTRIPAGVQIT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH-RDPAKLVALINREGVD---TLHF 3277
Cdd:PRK07769 202 HLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFvRRPGRWIRELARKPGGtggTFSA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 VPSMlqAF---------LQDEDVASCTSLKRIVCSGEALPADAQQQ---VFAK--LPQAGLYNLYGPTEAAIDVTHWTCV 3343
Cdd:PRK07769 282 APNF--AFehaaarglpKDGEPPLDLSNVKGLLNGSEPVSPASMRKfneAFAPygLPPTAIKPSYGMAEATLFVSTTPMD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3344 EEGK------DAVPIGR----------PIANLAC---------YILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLT 3397
Cdd:PRK07769 360 EEPTviyvdrDELNAGRfvevpadapnAVAQVSAgkvgvsewaVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEET 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2310915810 3398 AERF---VASPFV--------AGERMYRTGDLARYrADGVIEYAGRI 3433
Cdd:PRK07769 440 AATFqniLKSRLSeshaegapDDALWVRTGDYGVY-FDGELYITGRV 485
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
3066-3198 |
1.63e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 54.53 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGV--GADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS 3143
Cdd:cd05927 8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3144 hlklplaqGVQRIDLDRgapwFEDYSEANPDIHL--DGENLAYVIYTSGSTGKPKGA 3198
Cdd:cd05927 88 --------GVKVYSLEE----FEKLGKKNKVPPPppKPEDLATICYTSGTTGNPKGV 132
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
2012-2451 |
2.17e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 54.00 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL- 2089
Cdd:cd17632 66 ETITYAELWERVGAVAAAHDPEQPVrPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLa 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETLAERLPCPAEV-----------------ERLPLETAAWPASA----------------DTRPLPEVAGET----L 2132
Cdd:cd17632 146 VSAEHLDLAVEAVLEGgtpprlvvfdhrpevdaHRAALESARERLAAvgipvttltliavrgrDLPPAPLFRPEPdddpL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2133 AYVIYTSGSTGQPKGvAVSQAALVAHC--QAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSA- 2209
Cdd:cd17632 226 ALLIYTSGSTGTPKG-AMYTERLVATFwlKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTl 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 -----------------------QHLADEVERHAVTILDlPPAYLQQQAEELRHA--GRRIAVRTC---ILGGE--AWDA 2259
Cdd:cd17632 305 fddlalvrptelflvprvcdmlfQRYQAELDRRSVAGAD-AETLAERVKAELRERvlGGRLLAAVCgsaPLSAEmkAFME 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2260 SLLTQQAVqaeawfNAYGPTEAvitplawhcraqeGGAPAIGRALgarRACILDAALQPCA---------PGMIGELYIG 2330
Cdd:cd17632 384 SLLDLDLH------DGYGSTEA-------------GAVILDGVIV---RPPVLDYKLVDVPelgyfrtdrPHPRGELLVK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2331 GQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGD-LARYRVDgQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYV 2408
Cdd:cd17632 442 TDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2310915810 2409 AEAAVVAlDGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRL 2451
Cdd:cd17632 514 RQIFVYG-NSERAYLLAVVVPTQDALAGED-TARLRAALAESL 554
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
2014-2199 |
2.94e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 53.76 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGV--VAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 QETLaeRLPCPAEVERLpletaawpASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAA----ARTYG 2167
Cdd:cd05927 86 DAGV--KVYSLEEFEKL--------GKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNK 155
|
170 180 190
....*....|....*....|....*....|....
gi 2310915810 2168 VGPGDCQLQFASIS--FDAAAEQLFvpLLAGARV 2199
Cdd:cd05927 156 INPTDVYISYLPLAhiFERVVEALF--LYHGAKI 187
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
3060-3525 |
3.32e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 53.63 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVEL 3138
Cdd:PRK05620 35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3139 LLSQSHLKLPLAQ------GVQRIDLDRGAPWFEDYSEANPDIH-------LDGENLAY------------VIYTSGSTG 3193
Cdd:PRK05620 115 IVADPRLAEQLGEilkecpCVRAVVFIGPSDADSAAAHMPEGIKvysyealLDGRSTVYdwpeldettaaaICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3194 KPKGAGNRHSALsnrlcWMqQAYGLGVGDT--VLQKTPFSFDVSVWEFF-W--PL---MSGARLVVaaPGDHRDPAKLVA 3265
Cdd:PRK05620 195 APKGVVYSHRSL-----YL-QSLSLRTTDSlaVTHGESFLCCVPIYHVLsWgvPLaafMSGTPLVF--PGPDLSAPTLAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3266 LINREGVDTLHFVP----SMLQAFLQDEdvASCTSLKRIVCSGEALPAdaqqqVFAKLPQAGlynlYGpteaaIDVTH-W 3340
Cdd:PRK05620 267 IIATAMPRVAHGVPtlwiQLMVHYLKNP--PERMSLQEIYVGGSAVPP-----ILIKAWEER----YG-----VDVVHvW 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3341 TCVEEGkdavPIG---RPIANLA-----CY---------------ILDGNLEPVPVGVLGELYLAGQGLARGYHQRP--- 3394
Cdd:PRK05620 331 GMTETS----PVGtvaRPPSGVSgearwAYrvsqgrfpasleyriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPtee 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3395 -GLTAERFVASPFVAGERMY------RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK05620 407 gGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3468 DGRQLVGY---VVLESESGDWR----EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK05620 487 PDDKWGERplaVTVLAPGIEPTretaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
539-671 |
4.04e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 53.37 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 539 YAELNRRANRLAHALIERGI--GADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS 616
Cdd:cd05927 8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 617 hlklplaqGVQRIDLDQadawLENHAENNPG--IELNGENLAYVIYTSGSTGKPKGA 671
Cdd:cd05927 88 --------GVKVYSLEE----FEKLGKKNKVppPPPKPEDLATICYTSGTTGNPKGV 132
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
2487-2567 |
4.57e-06 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 47.63 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2487 RRQAGEPPREGLERSVAAIWEALLGV---EGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAAS 2563
Cdd:smart00823 2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
|
....
gi 2310915810 2564 LESQ 2567
Cdd:smart00823 82 LAAE 85
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
4559-5052 |
4.89e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 53.20 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLL 4638
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 LTHSHLLERLP-IPEGL---------------SCLSVDREEEWAGFP-----------AHDPEVALHGDnLAYVIYTSGS 4691
Cdd:PLN02387 183 ICDSKQLKKLIdISSQLetvkrviymddegvdSDSSLSGSSNWTVSSfseveklgkenPVDPDLPSPND-IAVIMYTSGS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIAHIVATgeryeMT------PEDCEL------HFMSFAFD------GSHEGWMHPLIngarvlIRD 4753
Cdd:PLN02387 262 TGLPKGVMMTHGNIVATVAGV-----MTvvpklgKNDVYLaylplaHILELAAEsvmaavGAAIGYGSPLT------LTD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4754 DSLWLPERTYAEMHRHGVTVGVFPPVYLQQLaehaeRDGnpppVR--VYCFGGdaVAQASYDLAWR----ALKPKYlFNG 4827
Cdd:PLN02387 331 TSNKIKKGTKGDASALKPTLMTAVPAILDRV-----RDG----VRkkVDAKGG--LAKKLFDIAYKrrlaAIEGSW-FGA 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4828 YGPTEtvvtpLLWKAragdacgAAYMPIGTLLGNRSGYILDGQLNL-------------LPVGVA--------------- 4879
Cdd:PLN02387 399 WGLEK-----LLWDA-------LVFKKIRAVLGGRIRFMLSGGAPLsgdtqrfiniclgAPIGQGygltetcagatfsew 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4880 ------------------------------------GELYLGGEGVARGYLERPALTAERFVPDpfgAPGSRLYRSGDLT 4923
Cdd:PLN02387 467 ddtsvgrvgpplpccyvklvsweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVD---ERGMRWFYTGDIG 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4924 RGRADGVVDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREAVVVAQPgaVGQQLVGYVVAQEPAVAD---------- 4992
Cdd:PLN02387 544 QFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHADP--FHSYCVALVVPSQQALEKwakkagidys 621
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4993 -------SPEAQAECRAQL-KTALRERLPEYMVPSHLLFLARmPLTPNG-------KLDRKGLPQPDASLLQQVY 5052
Cdd:PLN02387 622 nfaelceKEEAVKEVQQSLsKAAKAARLEKFEIPAKIKLLPE-PWTPESglvtaalKLKREQIRKKFKDDLKKLY 695
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
4858-5042 |
6.32e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 52.30 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4858 LLGNRS-GYILDG-QLNLLPvGVAGELYLGGEGVARGYlerpaltaerfVPDPFGAPgsRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK07445 279 LAGNNSsGQVLPHaQITIPA-NQTGNITIQAQSLALGY-----------YPQILDSQ--GIFETDDLGYLDAQGYLHILG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVaqepavadsPEAQAECRAQLKTALRERLPE 5014
Cdd:PRK07445 345 RNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwGEVVTAIYV---------PKDPSISLEELKTAIKDQLSP 415
|
170 180
....*....|....*....|....*...
gi 2310915810 5015 YMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK07445 416 FKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
4563-4970 |
7.78e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 52.42 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRaNRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-DIEYP--RERLLYMMQDSRAHLLL 4639
Cdd:PRK07769 56 LTWSQFGAR-NRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAIL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 THSHLLER-------LPIPEGLSCLSVDREEEWAGFPAHDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT 4712
Cdd:PRK07769 135 TTTDSAEGvrkffraRPAKERPRVIAVDAVPDEVGATWVPPEANE--DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4713 GERYEMTPEDCELHFMSFAFD------------GSHEGWMHPlingaRVLIRDDSLWLPERTyAEMHRHGVTVGVFPPVY 4780
Cdd:PRK07769 213 IDALEGQEGDRGVSWLPFFHDmglitvllpallGHYITFMSP-----AAFVRRPGRWIRELA-RKPGGTGGTFSAAPNFA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 LQQLAEHA-ERDGNPP--------------PVRVYCFGGDAVAQASYDLAWRALKPKY------LFNGYGPTETVVTPL- 4838
Cdd:PRK07769 287 FEHAAARGlPKDGEPPldlsnvkgllngsePVSPASMRKFNEAFAPYGLPPTAIKPSYgmaeatLFVSTTPMDEEPTVIy 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 -----LWKARA----GDACGA-AYMPIGTLLGNRSGYILDG-QLNLLPVGVAGELYLGGEGVARGYLERPALTAERF--- 4904
Cdd:PRK07769 367 vdrdeLNAGRFvevpADAPNAvAQVSAGKVGVSEWAVIVDPeTASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqni 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4905 ----VPDPF--GAP-GSRLYRSGDLTrGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HPAVREAVVVA 4970
Cdd:PRK07769 447 lksrLSESHaeGAPdDALWVRTGDYG-VYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEaTKALRTGYVAA 519
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
5056-5128 |
8.22e-06 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.86 E-value: 8.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 5056 RSDLEQQVAGIWAEVLQL---QQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQ 5128
Cdd:smart00823 10 RRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
515-765 |
9.22e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 52.41 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYV--PVD 592
Cdd:PRK07868 451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVlmPPD 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 593 PEY---------------PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQAD-------AWLenhaENNPGIel 650
Cdd:PRK07868 531 TDLaaavrlggvteiitdPTNLEAARQLPGRVLVLGGGESRDLDLPDDADVIDMEKIDpdavelpGWY----RPNPGL-- 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 651 nGENLAYVIY-TSGSTGKPKGAGNRHSALSnrlcwmqqAYG------LGVGDTVLQKTPFSFDVSVweffwpLMS----- 718
Cdd:PRK07868 605 -ARDLAFIAFsTAGGELVAKQITNYRWALS--------AFGtasaaaLDRRDTVYCLTPLHHESGL------LVSlggav 669
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2310915810 719 --GARLvvaAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA 765
Cdd:PRK07868 670 vgGSRI---ALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFV 715
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
3062-3198 |
1.02e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYP---EERQAYMLEDSGVEL 3138
Cdd:PRK05850 34 ETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSV 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3139 LLSQS--------HLKLPLAQG------VQRIDLDRGAPwfedySEANPDihlDGENLAYVIYTSGSTGKPKGA 3198
Cdd:PRK05850 113 VLTTSavvddvteYVAPQPGQSappvieVDLLDLDSPRG-----SDARPR---DLPSTAYLQYTSGSTRTPAGV 178
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
2134-2410 |
1.23e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 51.67 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAA-LVahCQAAARTYGVGPGDCQLQFAS-----ISFDAAaeqLFVPLLAGARVLLGDAGQW 2207
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGPhLV--GLKYYWRSIIEKDIPTVVFSHssigwVSFHGF---LYGSLSLGNTFVMFEGGII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2208 SAQHLADE----VERHAVTI-LDLPPA--YLQQ---QAEELRHAGRRIAVRTCILGGEAWDASL--LTQQAVQAEAwFNA 2275
Cdd:PTZ00237 333 KNKHIEDDlwntIEKHKVTHtLTLPKTirYLIKtdpEATIIRSKYDLSNLKEIWCGGEVIEESIpeYIENKLKIKS-SRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTEAVITPL----AWHCRAQEGGAPAI----------GRALGARRacILDAALQ-PCAPGMIGELYiggqclargylg 2340
Cdd:PTZ00237 412 YGQTEIGITYLycygHINIPYNATGVPSIfikpsilsedGKELNVNE--IGEVAFKlPMPPSFATTFY------------ 477
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2341 rpgQTAERF--VADPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE 2410
Cdd:PTZ00237 478 ---KNDEKFkqLFSKFPG----YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
930-1453 |
1.38e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 51.80 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 930 PWVREAAVLAVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAG 1009
Cdd:COG3321 867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1010 YSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAAKAGAATA 1089
Cdd:COG3321 947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1090 EQGPASGEVALAPVQRWFFEQSipnRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAG 1169
Cdd:COG3321 1027 LLAAAAAALAAAAAAAAAAAAL---AALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1170 EPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLG 1249
Cdd:COG3321 1104 AALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAA 1183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPcenPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVN 1329
Cdd:COG3321 1184 ALAAALAGLAALLLAALLAALLAALLALALAALAAAAAA---LLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1330 DLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGY 1409
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2310915810 1410 GLLRYLAGEEAATRLAALPQPRITFNYLGRFDRQFDGAALLVPA 1453
Cdd:COG3321 1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
3275-3536 |
1.54e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.15 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3275 LHFVPSMLQAFLQdEDVASCTSLKRIVCSG-EALPADAQQQVFAKLPqagLYNLYGPTEAAIDVTHWTCVE--EGKDAVp 3351
Cdd:PRK07445 211 LSLVPTQLQRLLQ-LRPQWLAQFRTILLGGaPAWPSLLEQARQLQLR---LAPTYGMTETASQIATLKPDDflAGNNSS- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 iGRPI--ANLAcyildgnlepVPVGVLGELYLAGQGLARGYHQrpgltaerfvasPFVAGERMYRTGDLARYRADGVIEY 3429
Cdd:PRK07445 286 -GQVLphAQIT----------IPANQTGNITIQAQSLALGYYP------------QILDSQGIFETDDLGYLDAQGYLHI 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3430 AGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPeYMVPAQ 3505
Cdd:PRK07445 343 LGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPdphwGEVVTAIYVPKDPSISLEELKTAIKDQLSP-FKQPKH 421
|
250 260 270
....*....|....*....|....*....|.
gi 2310915810 3506 WLALERMPLSPNGKLDRKALprpQAAAGQTH 3536
Cdd:PRK07445 422 WIPVPQLPRNPQGKINRQQL---QQIAVQRL 449
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
4670-4937 |
1.59e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 51.52 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4670 AHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY-----EMTPEDCEL------HFMSFA------F 4732
Cdd:PTZ00216 254 HHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndligPPEEDETYCsylplaHIMEFGvtniflA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4733 DGSHEGWMHPlingaRVLIrddslwlpeRTYAEMH------RHGVTVGV--------------FPPV-----------YL 4781
Cdd:PTZ00216 334 RGALIGFGSP-----RTLT---------DTFARPHgdltefRPVFLIGVprifdtikkaveakLPPVgslkrrvfdhaYQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAehAERDGNPPP-----------------VRVYCFGGDAVAQASYDLAWRALKPkyLFNGYGPTETVvtpllwkara 4844
Cdd:PTZ00216 400 SRLR--ALKEGKDTPywnekvfsapravlggrVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETV---------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 gdACGAAYMPiGTLLGNRSGYILDGQ-LNLLPVG---------VAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:PTZ00216 466 --CCGGIQRT-GDLEPNAVGQLLKGVeMKLLDTEeykhtdtpePRGEILLRGPFLFKGYYKQEELTREVLDEDGW----- 537
|
330 340
....*....|....*....|...
gi 2310915810 4915 rlYRSGDLTRGRADGVVDYLGRV 4937
Cdd:PTZ00216 538 --FHTGDVGSIAANGTLRIIGRV 558
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3983-4339 |
2.07e-05 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 51.40 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3983 ALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPS 4062
Cdd:COG1020 970 APAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAA 1049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4063 DFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRS 4142
Cdd:COG1020 1050 AAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARR 1129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4143 GFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHIL 4222
Cdd:COG1020 1130 AVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 1209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4223 LDGWSNAQLLSEVLESYAGRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLV---EALAQPGLTSANGV 4299
Cdd:COG1020 1210 LLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLllaLALLLPALARARAA 1289
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2310915810 4300 GEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQR 4339
Cdd:COG1020 1290 RTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
2014-2154 |
2.79e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.51 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAErlARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL-DPNYP--AERLAYMLRDsgARWL 2089
Cdd:PRK12476 69 LTWTQLGVRLR--AVGARLQQVAGPGdRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRD--AEPT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETLAERLPCPAEVERLPletaawpasADTRP-------LPEVAGET----------LAYVIYTSGSTGQPKGVAVSQ 2152
Cdd:PRK12476 145 VVLTTTAAAEAVEGFLRNLP---------RLRRPrviaidaIPDSAGESfvpveldtddVSHLQYTSGSTRPPVGVEITH 215
|
..
gi 2310915810 2153 AA 2154
Cdd:PRK12476 216 RA 217
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
4687-5040 |
5.65e-05 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 49.35 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4687 YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS---FAFDGSHEGWMHPLINGARVLIRDdsLWLPERTY 4763
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVvpmFHVNAWCLPYAATLVGAKQVLPGP--RLDPASLV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVT-VGVFPPVyLQQLAEHAERDGNPPPVRVYCFGGDAvAQASYDLAWRALKPKYLFNGYGPTET--VVTPLLW 4840
Cdd:cd05915 238 ELFDGEGVTfTAGVPTV-WLALADYLESTGHRLKTLRRLVVGGS-AAPRSLIARFERMGVEVRQGYGLTETspVVVQNFV 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 -------------KARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLpvgvageLYLGGEGVARGYL-ERPALTAERFvp 4906
Cdd:cd05915 316 kshleslseeeklTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGE-------VQLKGPWITGGYYgNEEATRSALT-- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 dpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVA 4985
Cdd:cd05915 387 ------PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHpKWQERPLAVVVP 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4986 QEpAVADSPEAQAECRAQLKTAlrerlpeYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05915 461 RG-EKPTPEELNEHLLKAGFAK-------WQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
3042-3292 |
9.13e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 48.95 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYV--PVD 3119
Cdd:PRK07868 451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVlmPPD 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYpeerqAYMLEDSGV-ELLLSQSHLK-------------------LPLAQGVQRIDLDRGAP-------WFEdysean 3172
Cdd:PRK07868 531 TDL-----AAAVRLGGVtEIITDPTNLEaarqlpgrvlvlgggesrdLDLPDDADVIDMEKIDPdavelpgWYR------ 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 PDIHLDGEnLAYVIY-TSGSTGKPKGAGNRHSALSnrlcwmqqAYG------LGVGDTVLQKTPFSFDVSVweffwpLMS 3245
Cdd:PRK07868 600 PNPGLARD-LAFIAFsTAGGELVAKQITNYRWALS--------AFGtasaaaLDRRDTVYCLTPLHHESGL------LVS 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3246 -------GARLvvaAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA 3292
Cdd:PRK07868 665 lggavvgGSRI---ALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFV 715
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
534-678 |
9.46e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 48.85 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD-PEYPEERQAY------MLED 606
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLAS 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 607 SGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAGNRHSAL 678
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALprpTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
4563-4732 |
1.06e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 48.68 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-------DIEY---PRERLLYMMQD 4632
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLydtlganAVEFiinHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4633 SR---------------------AHLLLTHSHLLERLpipeGLSCLSVdreEEWAGFPAHDPEV-ALHGDNLAYVIYTSG 4690
Cdd:PLN02861 158 SKissilsclpkcssnlktivsfGDVSSEQKEEAEEL----GVSCFSW---EEFSLMGSLDCELpPKQKTDICTIMYTSG 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2310915810 4691 STGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAF 4732
Cdd:PLN02861 231 TTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEEDSYFSY 272
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2168-2713 |
1.14e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.10 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2168 VGPGDCQLQFASISFDAAAEQLFVPLL----AGARVLLGDAGQ---------WSAQHLADEVERhavtiLDLPPAYLQQQ 2234
Cdd:COG3321 797 VGPGPVLTGLVRQCLAAAGDAVVLPSLrrgeDELAQLLTALAQlwvagvpvdWSALYPGRGRRR-----VPLPTYPFQRE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 AEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDA 2314
Cdd:COG3321 872 DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAA 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2315 ALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIE 2394
Cdd:COG3321 952 AAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAA 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2395 IGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:COG3321 1032 AAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLAL 1111
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2475 DRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFER 2554
Cdd:COG3321 1112 LAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAG 1191
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2555 PVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRH 2634
Cdd:COG3321 1192 LAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGL 1271
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2635 ETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHH 2713
Cdd:COG3321 1272 AALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAA 1350
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1994-2495 |
1.18e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 48.42 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQV---ASAPEAIALVCGDEH----LSYAELDMRAERLARGLRARGVvaealvaiaaeRSFDLVVGLLgilkagagyl 2066
Cdd:cd05943 72 YAENLlrhADADDPAAIYAAEDGerteVTWAELRRRVARLAAALRALGV-----------KPGDRVAGYL---------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2067 pldPNYPaERLAYMLRDS--GARWLIC------------------------------------QETLAE---RLPCPAEV 2105
Cdd:cd05943 131 ---PNIP-EAVVAMLATAsiGAIWSSCspdfgvpgvldrfgqiepkvlfavdaytyngkrhdvREKVAElvkGLPSLLAV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2106 ERLPLETAAwpASADTRPLPEVAG--ETLA------------------YVIYTSGSTGQPKGVAVSQAA-LVAHCQAAAR 2164
Cdd:cd05943 207 VVVPYTVAA--GQPDLSKIAKALTleDFLAtgaagelefeplpfdhplYILYSSGTTGLPKCIVHGAGGtLLQHLKEHIL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2165 TYGVGPGDCQLQFAS---------ISFdaaaeqlfvpLLAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:cd05943 285 HCDLRPGDRLFYYTTcgwmmwnwlVSG----------LAVGATIVLydGSPFYPDTNALWDLADEEGITVFGTSAKYLDA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 QAE---ELRHAGRRIAVRTCILGGeawdASLLTQ------QAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAI-GRA 2303
Cdd:cd05943 355 LEKaglKPAETHDLSSLRTILSTG----SPLKPEsfdyvyDHIKPDVLLASISGGTDIISCFVGGNPLLPVYRGEIqCRG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2304 LGARrACILDAALQPcAPGMIGELYIggqclARGYLGRPGQtaerFVADPfsgSGER-----------LYRTGDLARYRV 2372
Cdd:cd05943 431 LGMA-VEAFDEEGKP-VWGEKGELVC-----TKPFPSMPVG----FWNDP---DGSRyraayfakypgVWAHGDWIEITP 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2373 DGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGG----PLlaaYLVGRDAMR-GEDLLAELRTWL 2447
Cdd:cd05943 497 RGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGdervIL---FVKLREGVElDDELRKRIRSTI 573
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2310915810 2448 AGRLPAYMQPTAWQVLSSLPLNANGKldrkalpKVDAAARRQ-AGEPPR 2495
Cdd:cd05943 574 RSALSPRHVPAKIIAVPDIPRTLSGK-------KVEVAVKKIiAGRPVK 615
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
535-693 |
1.29e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 48.19 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG------ 608
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKakalif 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 609 --VQLLLSQSHLKLPLAQGVQRIDLdqadawlenhaennpgielngenLAYvIYTSGSTGKPKGAGNRHSalsnRLCWMQ 686
Cdd:cd05939 82 nlLDPLLTQSSTEPPSQDDVNFRDK-----------------------LFY-IYTSGTTGLPKAAVIVHS----RYYRIA 133
|
....*....
gi 2310915810 687 Q--AYGLGV 693
Cdd:cd05939 134 AgaYYAFGM 142
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
3064-3485 |
1.64e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 48.11 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGV--GADRLVGVaMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV----- 3136
Cdd:cd05905 15 LTWGKLLSRAEKIAAVLQKKVGlkPGDRVALM-YPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVrvalt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 -ELLLSQSHLKLPLAQGVQRIDLDRGAP---WFEDYSEAN--------PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:cd05905 94 vEACLKGLPKKLLKSKTAAEIAKKKGWPkilDFVKIPKSKrsklkkwgPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWefFWPLMS---GARLVVAAPGDHR-DPAKLVALINREGVDTLhFVPS 3280
Cdd:cd05905 174 LLAHCRALKEACELYESRPLVTVLDFKSGLGLW--HGCLLSvysGHHTILIPPELMKtNPLLWLQTLSQYKVRDA-YVKL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVASCTSLKR------------IVCSGE--ALPADAQQQVFAKL---PQAGLYNLYGPTEAAIDVTHWT-- 3341
Cdd:cd05905 251 RTLHWCLKDLSSTLASLKNrdvnlsslrmcmVPCENRprISSCDSFLKLFQTLglsPRAVSTEFGTRVNPFICWQGTSgp 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3342 ------------------CVEEGK-DAVPI----GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLT- 3397
Cdd:cd05905 331 epsrvyldmralrhgvvrLDERDKpNSLPLqdsgKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYFLLDGETn 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3398 AERFVA-----SPFVAGERMYRTGDL----------ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE 3461
Cdd:cd05905 411 DTFKVFpstrlSTGITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRvHPYRGR 490
|
490 500 510
....*....|....*....|....*....|
gi 2310915810 3462 AAVLAVDGRqLVgyVVLES------ESGDW 3485
Cdd:cd05905 491 CAVFSITGL-VV--VVAEQppgseeEALDL 517
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
4680-4731 |
1.65e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 48.17 E-value: 1.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA 4731
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLA 272
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
2611-2825 |
1.84e-04 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 47.40 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2611 VLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQArqtilanmpLRIVLEDCAGASEATLRQRVAEEIRqPFDLARG 2690
Cdd:PRK09294 27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGG---------WELVADDLLHPGIVVVDGDAARPLP-ELQLDQG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2691 PLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAY-------AAARRGEQPTLAPLKlqyaDYAAwhrawlDS 2763
Cdd:PRK09294 97 VSLLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYtdvvttgDPGPIRPQPAPQSLE----AVLA------QR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2764 GEGARQLDyWRERLGAEQPVLELP-ADRVRPAQASGRGQRLDMA---LPVPLSEELLACARREGVT 2825
Cdd:PRK09294 167 GIRRQALS-GAERFMPAMYAYELPpTPTAAVLAKPGLPQAVPVTrcrLSKAQTSSLAAFGRRHRLT 231
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
535-671 |
1.87e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.01 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYP---EERQAYMLEDSGVQL 611
Cdd:PRK05850 34 ETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSV 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 612 LLSQSHLKLPLAQGVQRIDLDQA------DAwLENHAENNPGIEL-NGENLAYVIYTSGSTGKPKGA 671
Cdd:PRK05850 113 VLTTSAVVDDVTEYVAPQPGQSAppvievDL-LDLDSPRGSDARPrDLPSTAYLQYTSGSTRTPAGV 178
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1052-1536 |
2.08e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 47.94 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1052 QVVSRARQAGLQLSPRDL---------------FQHQNIRSLALAAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQ 1116
Cdd:COG3321 835 TALAQLWVAGVPVDWSALypgrgrrrvplptypFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAA 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1117 HWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:COG3321 915 AAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAA 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:COG3321 995 ALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAAL 1074
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:COG3321 1075 AELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAA 1154
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1357 GREDLGEAIDLSRTVGWFTSLFPV----RLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRI 1432
Cdd:COG3321 1155 AAAALAAALAAALLAAAALLLALAlalaAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALA 1234
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1433 TFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHAL 1512
Cdd:COG3321 1235 LLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAA 1314
|
490 500
....*....|....*....|....
gi 2310915810 1513 IEHCLDPRHRGVTPSDFPLAGLSQ 1536
Cdd:COG3321 1315 AAAAAALAAALLAAALAALAAAVA 1338
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
3083-3486 |
2.44e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.43 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3083 RGVGA---------DRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSGVELLLSQ-------- 3142
Cdd:PRK12476 79 RAVGArlqqvagpgDR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTtaaaeave 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 ------SHLKLPLAQGVQRIDLDRGapwfEDYSEANPDIhldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAY 3216
Cdd:PRK12476 158 gflrnlPRLRRPRVIAIDAIPDSAG----ESFVPVELDT----DDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3217 GL------GV--------------------GDTVLQKTPFSFDVSVWEFFWPLMSGA---RLVVAAP------------- 3254
Cdd:PRK12476 230 DLldrnthGVswlplyhdmglsmigfpavyGGHSTLMSPTAFVRRPQRWIKALSEGSrtgRVVTAAPnfayewaaqrglp 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3255 --GDHRDPAKLVALINRE-----------------GVDTLHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQ 3313
Cdd:PRK12476 310 aeGDDIDLSNVVLIIGSEpvsidavttfnkafapyGLPRTAFKPSygIAEATLFVATIAPDAEPSVVYLDREQLGAGRAV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3314 QVFAKLPQAglynlygpteaaidVTHWTCveegkdavpiGRPIANLACYILDGNLE-PVPVGVLGELYLAGQGLARGYHQ 3392
Cdd:PRK12476 390 RVAADAPNA--------------VAHVSC----------GQVARSQWAVIVDPDTGaELPDGEVGEIWLHGDNIGRGYWG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3393 RPGLTAERFVA---SPFVAGE---------RMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWV 3459
Cdd:PRK12476 446 RPEETERTFGAklqSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMV 524
|
490 500 510
....*....|....*....|....*....|..
gi 2310915810 3460 REA-----AVLAVDGRQLVgyVVLESESGDWR 3486
Cdd:PRK12476 525 RRGyvtafTVPAEDNERLV--IVAERAAGTSR 554
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2099-2172 |
2.50e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.40 E-value: 2.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2099 LPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD 2172
Cdd:PLN02736 190 LPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSD 263
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
77-296 |
2.57e-04 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 47.01 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 77 AVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDS--LAQAPLQRPLEVAFEDCSGLPEAeqEARLREEAQreslqp 154
Cdd:PRK09294 27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGweLVADDLLHPGIVVVDGDAARPLP--ELQLDQGVS------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 155 fdlcegpLLRVRLIRLGEERHVLLLTlHHIVSDGWSMNVLIEE-FSRFYSAYATGAEPGLPALPI-QYADYALWQR---- 228
Cdd:PRK09294 99 -------LLALDVVPDDGGARVTLYI-HHSIADAHHSASLLDElWSRYTDVVTTGDPGPIRPQPApQSLEAVLAQRgirr 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 229 SWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVvpsyRGSRYEFSiePALAEALRGTARRQGLTL 296
Cdd:PRK09294 171 QALSGAERFMPAMYAYELPPTPTAAVLAKPGLPQAV----PVTRCRLS--KAQTSSLAAFGRRHRLTV 232
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
4543-4621 |
2.97e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 47.40 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQR--SAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK07868 453 IAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETrpSALVAIAALSRLGAVAVLMPPDTD 532
|
.
gi 2310915810 4621 Y 4621
Cdd:PRK07868 533 L 533
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
2050-2479 |
3.06e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 47.12 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2050 DLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLA---ERLP--------CPAEVERLPL-------- 2110
Cdd:PLN03051 6 DAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggRALPlyskvveaAPAKAIVLPAagepvavp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2111 -------------ETAAWPASADTRPLPEVA-GETLAYVIYTSGSTGQPKGVAVSQAALVaHCQAAARTY-GVGPGDCQL 2175
Cdd:PLN03051 86 lreqdlswcdflgVAAAQGSVGGNEYSPVYApVESVTNILFSSGTTGEPKAIPWTHLSPL-RCASDGWAHmDIQPGDVVC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2176 QFASISFDAAAEQLFVPLLAGARVLLGdAGQWSAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGRRIA-------VR 2248
Cdd:PLN03051 165 WPTNLGWMMGPWLLYSAFLNGATLALY-GGAPLGRGFGKFVQDAGVTVLGLVPSIVKA----WRHTGAFAMegldwskLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 TCILGGEAwdaslltqQAVQAEAWFNAygpTEAVITPLAWHCRAQEGGApaigralgarrACILDAALQPCAPGMIGELY 2328
Cdd:PLN03051 240 VFASTGEA--------SAVDDVLWLSS---VRGYYKPVIEYCGGTELAS-----------GYISSTLLQPQAPGAFSTAS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 IGGQ--CLARGYLGRPGQ---TAERFVADPFSGSGERLY-----------------------RTGDLARYRVDGQVEYLG 2380
Cdd:PLN03051 298 LGTRfvLLNDNGVPYPDDqpcVGEVALAPPMLGASDRLLnadhdkvyykgmpmygskgmplrRHGDIMKRTPGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2381 RADQQIKIRGFRIEIGEIESQLL-AHPYVAEAAVVALDGV-GGP-LLAAYLV------GRDAMRGEDLLAELRTWLAGRL 2451
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPdGGPeLLVIFLVlgeekkGFDQARPEALQKKFQEAIQTNL 457
|
490 500
....*....|....*....|....*...
gi 2310915810 2452 PAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVL 485
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
3061-3205 |
3.69e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 46.92 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD-PEYPEERQAY------MLED 3133
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLAS 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3134 SGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSAL 3205
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALprpTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1006-1078 |
3.84e-04 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 42.24 E-value: 3.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 1006 AQAGYSAPRNAVERTLAEIWQDLLGV---ERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRSL 1078
Cdd:smart00823 2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAAL 78
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
3049-3478 |
5.14e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 46.48 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAF-----GEER-LDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMA-------------- 3107
Cdd:PRK10524 64 AKRPEQLALIAvstetDEERtYTFRQLHDEVNRMAAMLRSLGVQrGDRVL-IYMPMIAEAAFAMLAcarigaihsvvfgg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 -----------------ILKA-----GGAYVPVDPeypeerqaymLEDSGVE---------LLLSQSHLKLPLAQGvqrI 3156
Cdd:PRK10524 143 fashslaariddakpvlIVSAdagsrGGKVVPYKP----------LLDEAIAlaqhkprhvLLVDRGLAPMARVAG---R 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3157 DLDRgAPWFEDYSEAN-PDIHLDGENLAYVIYTSGSTGKPKGA----GNRHSALSNRlcwMQQAYGLGVGDTvlqktpfs 3231
Cdd:PRK10524 210 DVDY-ATLRAQHLGARvPVEWLESNEPSYILYTSGTTGKPKGVqrdtGGYAVALATS---MDTIFGGKAGET-------- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 fdvsvweFF------W----------PLMSGARLVVAAPGDHR-DPAKLVALINREGVDTLHFVPS---MLQ----AFLQ 3287
Cdd:PRK10524 278 -------FFcasdigWvvghsyivyaPLLAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTairVLKkqdpALLR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3288 DEDVascTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNlYGPTEaaidvTHW--TCVEEGKDAVPI-----GRPIANLA 3360
Cdd:PRK10524 351 KHDL---SSLRALFLAGEPLDEPTASWISEALGVPVIDN-YWQTE-----TGWpiLAIARGVEDRPTrlgspGVPMYGYN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3361 CYILDGNL-EPVPVGVLGELYLAGQgLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:PRK10524 422 VKLLNEVTgEPCGPNEKGVLVIEGP-LPPGCMQTVWGDDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVIN 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2310915810 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL 3478
Cdd:PRK10524 501 VAGHRLGTREIEESISSHPAVAEVAVVGVKdalkGQVAVAFVVP 544
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
4195-4337 |
5.83e-04 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 45.86 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4195 QRAPLLRLLLVKTAEGEHHLIYTHHHILlDGWSNAQLLSEVLESY--------AGRSPEQPRDGRYSDYIAWLQRQDAAA 4266
Cdd:PRK09294 95 QGVSLLALDVVPDDGGARVTLYIHHSIA-DAHHSASLLDELWSRYtdvvttgdPGPIRPQPAPQSLEAVLAQRGIRRQAL 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4267 TEAFW-REQMAALDEPTRLVEALAQ-PGLTSANGVGEHlrEVDATATARLRDFARRHQVTLNTLVQAgwALLL 4337
Cdd:PRK09294 174 SGAERfMPAMYAYELPPTPTAAVLAkPGLPQAVPVTRC--RLSKAQTSSLAAFGRRHRLTVNALVSA--AILL 242
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
850-999 |
5.99e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 46.14 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 850 GELYLAGRGLARGYHQrpgltaerfvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:PRK07445 302 GNITIQAQSLALGYYP------------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 930 PWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKALP 999
Cdd:PRK07445 370 GLVQDVCVLGLPdphwGEVVTAIYVPKDPSISLEELKTAIKDQLSP-FKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
653-994 |
6.18e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 46.24 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVV-AAPGD 729
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLyPSPLH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 730 HRDPAKLVELINRegvdTLHFVPSMLQA----FLQDEDVASctsLKRIVCSGEALPADAQQQVFAKLpqaGLYNL--YGP 803
Cdd:PRK08043 444 YRIVPELVYDRNC----TVLFGTSTFLGnyarFANPYDFAR---LRYVVAGAEKLQESTKQLWQDKF---GLRILegYGV 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 804 TEAAIDVThwtcveegkDTVPIGRPIGNLGCYI--LDGNLEPVPvGVL--GELYLAGRGLARGYH--QRPGL----TAER 873
Cdd:PRK08043 514 TECAPVVS---------INVPMAAKPGTVGRILpgMDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVlevpTAEN 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 874 fvaspfVAGER---MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA-RLLEHPWVREAAVLAVDGRQLVGYV 949
Cdd:PRK08043 584 ------ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKGEALV 657
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2310915810 950 VLESEGGDWREALAAHLAAS-LPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK08043 658 LFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
3044-3316 |
6.77e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.94 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQV--ERTPTAPALAF-----GEERLDYAELNRRANRLAHALIERGVGA-DRLVGVaMERSIEMVVALMA-------- 3107
Cdd:PRK03584 88 YAENLlrHRRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-LPNIPETVVAMLAtaslgaiw 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 ----------------------ILKA------GGAYVPVDPEYPEERQAYmledSGVELLLSQSHLKLPLAQGvqriDLD 3159
Cdd:PRK03584 167 sscspdfgvqgvldrfgqiepkVLIAvdgyryGGKAFDRRAKVAELRAAL----PSLEHVVVVPYLGPAAAAA----ALP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3160 RGAPWfEDYSEANPDIHLDGENLA-----YVIYTSGSTGKPK----GAGnrhSALSNRLCWMQQAYGLGVGDTVLQKTPF 3230
Cdd:PRK03584 239 GALLW-EDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhGHG---GILLEHLKELGLHCDLGPGDRFFWYTTC 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3231 S-----FDVSVweffwpLMSGARLVV--AAPGdHRDPAKLVALINREGVdTL-----HFVPSMLQAFLQDEDVASCTSLK 3298
Cdd:PRK03584 315 GwmmwnWLVSG------LLVGATLVLydGSPF-YPDPNVLWDLAAEEGV-TVfgtsaKYLDACEKAGLVPGETHDLSALR 386
|
330
....*....|....*...
gi 2310915810 3299 RIVCSGEALPADAQQQVF 3316
Cdd:PRK03584 387 TIGSTGSPLPPEGFDWVY 404
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
561-959 |
1.31e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 45.12 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 561 DRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQA--- 634
Cdd:PRK12476 93 DR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRprv 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 635 ---DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL------GV------------ 693
Cdd:PRK12476 172 iaiDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLldrnthGVswlplyhdmgls 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 694 --------GDTVLQKTPFSFDVSVWEFFWPLMSGA---RLVVAAP---------------GDHRDPAKLVELINRE---- 743
Cdd:PRK12476 252 migfpavyGGHSTLMSPTAFVRRPQRWIKALSEGSrtgRVVTAAPnfayewaaqrglpaeGDDIDLSNVVLIIGSEpvsi 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 744 -------------GVDTLHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAglynlygpteaai 808
Cdd:PRK12476 332 davttfnkafapyGLPRTAFKPSygIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNA------------- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 809 dVTHWTCveegkdtvpiGRPIGNLGCYILDGNLE-PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVA---SPFVAGE- 883
Cdd:PRK12476 399 -VAHVSC----------GQVARSQWAVIVDPDTGaELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqSRLAEGSh 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 884 --------RMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREA-----AVLAVDGRQLVgyV 949
Cdd:PRK12476 468 adgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRRGyvtafTVPAEDNERLV--I 544
|
490
....*....|
gi 2310915810 950 VLESEGGDWR 959
Cdd:PRK12476 545 VAERAAGTSR 554
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1656-1897 |
3.52e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 44.00 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1656 PLQRLvlvpLANGRMHLIYTYHHILMDGWSNAQLLAEVLQryagqevaatvgrYRDYIGWLQGRDAmateffwrdrlasl 1735
Cdd:PRK12467 3710 PLAVI----LEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQ-------------YADYILWQQAKGP-------------- 3758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1736 emptrlarqarteqpgQGEHLRELDPQTTRQLASFAQGQKvtlntlvqaawalllqrhcgqETVAFgatvagrpaelpgi 1815
Cdd:PRK12467 3759 ----------------YGLLGWSLGGTLARLVAELLEREG---------------------ESEAF-------------- 3787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1816 eaqIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYD-----------IQRW----AGHGGEALFDSILV 1880
Cdd:PRK12467 3788 ---LGLFDNTLPLPDEFVPQAEFLELLRQLGELIGRANRLLRGLEEGgvgpdvlvgiaIQRCfdiaPLELYTPLLDAGEL 3864
|
250
....*....|....*..
gi 2310915810 1881 FENFPVAEALRQAPADL 1897
Cdd:PRK12467 3865 AHIFDVAMRLKLLSLQL 3881
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
657-951 |
4.47e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 43.40 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 657 YVIYTSGSTGKPKGA----GNRHSALSNRlcwMQQAYGLGVGDTvlqktpfsfdvsvweFF------W----------PL 716
Cdd:PRK10524 237 YILYTSGTTGKPKGVqrdtGGYAVALATS---MDTIFGGKAGET---------------FFcasdigWvvghsyivyaPL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 717 MSGARLVVAAPGDHR-DPAKLVELINREGVDTLHFVPS---MLQ----AFLQDEDVascTSLKRIVCSGEALPADAQQQV 788
Cdd:PRK10524 299 LAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTairVLKkqdpALLRKHDL---SSLRALFLAGEPLDEPTASWI 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 789 FAKLPQAGLYNlYGPTEaaidvTHW--TCVEEGKDTVPI-----GRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRgLA 860
Cdd:PRK10524 376 SEALGVPVIDN-YWQTE-----TGWpiLAIARGVEDRPTrlgspGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGP-LP 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 861 RGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PRK10524 449 PGCMQTVWGDDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVG 528
|
330
....*....|....*.
gi 2310915810 940 VD----GRQLVGYVVL 951
Cdd:PRK10524 529 VKdalkGQVAVAFVVP 544
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
3178-3538 |
4.53e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 43.42 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAgnrhsALSNR--LCWMQQAYG---LGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLV 3250
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGV-----VLSHRnlLANRAQVAAridFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVF 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3251 V-AAPGDHRDPAKLVALINRE---GVDTLhfvpsmLQAFLQDEDVASCTSLKRIVCSGEALpADAQQQVFAKLPQAGLYN 3326
Cdd:PRK06814 865 LyPSPLHYRIIPELIYDTNATilfGTDTF------LNGYARYAHPYDFRSLRYVFAGAEKV-KEETRQTWMEKFGIRILE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3327 LYGPTEAAidvthwtcveegkDAVPIGRPIANLACYI------LDGNLEPVPvGVL--GELYLAGQGLARGY--HQRPGl 3396
Cdd:PRK06814 938 GYGVTETA-------------PVIALNTPMHNKAGTVgrllpgIEYRLEPVP-GIDegGRLFVRGPNVMLGYlrAENPG- 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3397 taerfVASPFVAGErmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGR---QL 3472
Cdd:PRK06814 1003 -----VLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVSIPDARkgeRI 1075
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3473 VgyVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVA 3538
Cdd:PRK06814 1076 I--LLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
517-789 |
4.56e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 43.25 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 517 FEEQV--ERTPTAPALAF-----GEERLDYAELNRRANRLAHALIERGIGA-DRLVGVaMERSIEMVVALMA-------- 580
Cdd:PRK03584 88 YAENLlrHRRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-LPNIPETVVAMLAtaslgaiw 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 581 ----------------------ILKA------GGAYVPVDPEYPEERQAYmledSGVQLLLSQSHLKLPLAQGvqriDLD 632
Cdd:PRK03584 167 sscspdfgvqgvldrfgqiepkVLIAvdgyryGGKAFDRRAKVAELRAAL----PSLEHVVVVPYLGPAAAAA----ALP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 633 QADAWlENHAENNPGIELNGENLA-----YVIYTSGSTGKPK----GAGnrhSALSNRLCWMQQAYGLGVGDTVLQKTPF 703
Cdd:PRK03584 239 GALLW-EDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhGHG---GILLEHLKELGLHCDLGPGDRFFWYTTC 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 704 S-----FDVSVweffwpLMSGARLVV--AAPGdHRDPAKLVELINREGVdTL-----HFVPSMLQAFLQDEDVASCTSLK 771
Cdd:PRK03584 315 GwmmwnWLVSG------LLVGATLVLydGSPF-YPDPNVLWDLAAEEGV-TVfgtsaKYLDACEKAGLVPGETHDLSALR 386
|
330
....*....|....*...
gi 2310915810 772 RIVCSGEALPADAQQQVF 789
Cdd:PRK03584 387 TIGSTGSPLPPEGFDWVY 404
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1097-1468 |
7.87e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 42.70 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRRQ 1176
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AGSEEALLALCEEAQRSLDLeqgpLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQ 1256
Cdd:COG3903 626 LAALAAAAAAAAAAAAAAAA----AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAA 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1257 TWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTAL 1336
Cdd:COG3903 702 ALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAA 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1337 ARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLA 1416
Cdd:COG3903 782 AAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAA 861
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1417 GEEAATRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLA 1468
Cdd:COG3903 862 AAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAA 913
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
651-994 |
8.60e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 42.65 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 651 NGENLAYVIYTSGSTGKPKGAgnrhsALSNR--LCWMQQAYG---LGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLV 723
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGV-----VLSHRnlLANRAQVAAridFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVF 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 724 V-AAPGDHRDPAKLVELINRE---GVDTLhfvpsmLQAFLQDEDVASCTSLKRIVCSGEALpADAQQQVFAKLPQAGLYN 799
Cdd:PRK06814 865 LyPSPLHYRIIPELIYDTNATilfGTDTF------LNGYARYAHPYDFRSLRYVFAGAEKV-KEETRQTWMEKFGIRILE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 800 LYGPTEAAIDVTHWTCVEEGKDTVpiGRpignlgcyILDG---NLEPVPvGVL--GELYLAGRGLARGY--HQRPGltae 872
Cdd:PRK06814 938 GYGVTETAPVIALNTPMHNKAGTV--GR--------LLPGieyRLEPVP-GIDegGRLFVRGPNVMLGYlrAENPG---- 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 873 rfVASPFVAGErmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGR---QLVgy 948
Cdd:PRK06814 1003 --VLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVSIPDARkgeRII-- 1076
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2310915810 949 VVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK06814 1077 LLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
3180-3521 |
9.84e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.39 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVV-AAPGD 3256
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLyPSPLH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3257 HRDPAKLVALINRegvdTLHFVPSMLQA----FLQDEDVASctsLKRIVCSGEALPADAQQQVFAKLpqaGLYNL--YGP 3330
Cdd:PRK08043 444 YRIVPELVYDRNC----TVLFGTSTFLGnyarFANPYDFAR---LRYVVAGAEKLQESTKQLWQDKF---GLRILegYGV 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAidvthwtcveegkDAVPIGRPIA---NLACYIL---DGNLEPVPvGVL--GELYLAGQGLARGYH--QRPGL---- 3396
Cdd:PRK08043 514 TECA-------------PVVSINVPMAakpGTVGRILpgmDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVlevp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3397 TAERfvaspfVAGER---MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA-RLLEHPWVREAAVLAVDGRQL 3472
Cdd:PRK08043 580 TAEN------ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKG 653
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3473 VGYVVLESESGDWREALAAHLAAS-LPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK08043 654 EALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
|