|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
252-1890 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 949.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 252 LDALLADPADPIAAPIVTQPHTLHRLSQFNATDDAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEIDRASDQFAC 331
Cdd:PRK12467 473 LEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAH 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 332 WLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSplhSGDAPCIAPSSI 411
Cdd:PRK12467 553 VLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS---HLLAQLPVPAGL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 412 DYRSLNIHAEQL----------PQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFD 481
Cdd:PRK12467 630 RSLCLDEPADLLcgysghnpevALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFD 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 482 AFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELL---PREMWP-GLRTMIVMGDAPPADVVA 557
Cdd:PRK12467 710 LGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALlqaSRVALPrPQRALVCGGEALQVDLLA 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 558 WWAE---RTRLCNGYGPTEASIATSLCEYR------PGVPwncIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAH 628
Cdd:PRK12467 790 RVRAlgpGARLINHYGPTETTVGVSTYELSdeerdfGNVP---IGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLAR 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 629 GYLHQEALSAEKFIICrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVV 708
Cdd:PRK12467 867 GYHRRPALTAERFVPD--PFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVL 944
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 709 ARSQPSGKILAAFVQP------ASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDERNERL 782
Cdd:PRK12467 945 AQPGDAGLQLVAYLVPaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATF 1024
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 783 TPPETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYIENKAVAA 862
Cdd:PRK12467 1025 VAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGA 1104
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 863 ERAIAICDEHRA-PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQL 941
Cdd:PRK12467 1105 QPALPDVDRDQPlPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQV 1184
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 942 AEPHTPIRLADHWVDGQTLSAEK---WVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLW 1018
Cdd:PRK12467 1185 IHPVGSLTLEEPLLLAADKDEAQlkvYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELV 1264
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1019 QRYNELDDHHGLDAPQPQIQTidivnsgiaspapADVAYWQQQLQDCRE------------------LDFPLDKPRPLMP 1080
Cdd:PRK12467 1265 ALYAAYSQGQSLQLPALPIQY-------------ADYAVWQRQWMDAGErarqlaywkaqlggeqpvLELPTDRPRPAVQ 1331
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1081 THAGERIHYQLQPDVAGLLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRI 1160
Cdd:PRK12467 1332 SHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRA 1411
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1161 QLSEQDTLAGLIGNMMETCIGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAGDVCQQNLRDCTLHRLPLSSGF 1240
Cdd:PRK12467 1412 EVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGLSVESLSWESQT 1491
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1241 SMFDMTWNFSVEQDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLP-ANTAQLALNPLCEREQQWLQQLAVNADAG 1319
Cdd:PRK12467 1492 AQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPeRRLGELDLLDEAERRQILEGWNATHTGYP 1571
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1320 SRDSLLMHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHY 1398
Cdd:PRK12467 1572 LARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVlVGIAVERSLEMVVGLLAILKAGGAY 1651
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1399 VPIDVHYPADRVSYMIENAQARLLVTDGEPEQGWASPAvGFDSLVSHPAAA------DALPI--PADDTLAYIMYTSGST 1470
Cdd:PRK12467 1652 VPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPD-GLRSLVLDQEDDwlegysDSNPAvnLAPQNLAYVIYTSGST 1730
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1471 GNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQP 1550
Cdd:PRK12467 1731 GRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQV 1810
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1551 SVIQATPTVWSTIVHHlPAASQRPLT---VLCGGEKMPAALLTQ-LRRI-ATRVLQVYGPTETTI----WsTCADLTHEG 1621
Cdd:PRK12467 1811 TTLHFVPSMLQQLLQM-DEQVEHPLSlrrVVCGGEALEVEALRPwLERLpDTGLFNLYGPTETAVdvthW-TCRRKDLEG 1888
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1622 -ASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQ-AFGAERyMYRTGDIVRFNRQ 1699
Cdd:PRK12467 1889 rDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPfGTVGSR-LYRTGDLARYRAD 1967
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1700 GQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIeRSLSLIVGEGQQAR-IVSYLqLTSGEELNEKAV---------RT 1769
Cdd:PRK12467 1968 GVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV-REAVVIAQDGANGKqLVAYV-VPTDPGLVDDDEaqvalrailKN 2045
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1770 ALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPETrySASEADYTPAANEAESAMQHIWQQVLSQTQISVCDSFFS 1849
Cdd:PRK12467 2046 HLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDA--SELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFE 2123
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|.
gi 1725075560 1850 LGGNSLQIPQLLHAIRQQmGVSLTIREFIMHSQIRELTALA 1890
Cdd:PRK12467 2124 LGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVA 2163
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
188-1900 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 868.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 188 FHTVPVADITSPAQLQHFFFNETGALKQGRYAQprvmvdVAACGDGTQLTL-YG-DDMRFNA---------FTDYLDALL 256
Cdd:PRK12316 1894 FENYPVAEALKQGAPAGLVFGRVSNHEQTNYPL------TLAVTLGETLSLqYSyDRGHFDAaaierldrhLLHLLEQMA 1967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 257 ADPADPIAAPIVTQPHTLHR-LSQFNATDDAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEIDRASDQFACWLLE 335
Cdd:PRK12316 1968 EDAQAALGELALLDAGERQRiLADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA 2047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 336 HSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADS------PLHSGDAPCIAPS 409
Cdd:PRK12316 2048 RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRhllerlPLPAGVARLPLDR 2127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 410 SIDYRSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYG 489
Cdd:PRK12316 2128 DAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFH 2207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 490 ALVSGATLYLAPSElHTDVGALHDYLTQHDIGHITITPAILELLPREMW-----PGLRTMIVMGDAPPADVVAWWAERTR 564
Cdd:PRK12316 2208 PLLNGARVLIRDDE-LWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAErdgrpPAVRVYCFGGEAVPAASLRLAWEALR 2286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 565 ---LCNGYGPTEASIATSLCEYRPGVPWNC----IGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALS 637
Cdd:PRK12316 2287 pvyLFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLT 2366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 638 AEKFIicRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSGKI 717
Cdd:PRK12316 2367 AERFV--PDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQ 2444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 718 LAAFVQPASP-ELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDERNERLTPPETETEAILERI 796
Cdd:PRK12316 2445 LVAYVVPDDAaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAI 2524
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 797 VANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYIENKAVAaeRAIAICDEHRA-- 874
Cdd:PRK12316 2525 WQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTS--RAPVLQKVTRVqp 2602
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 -PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLADH 953
Cdd:PRK12316 2603 lPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLE 2682
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 954 W-VDGQTLSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDHHGLDA 1032
Cdd:PRK12316 2683 DcAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTL 2762
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1033 PQPQIQTIDIV----NSGIASPAPADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRGKALG 1107
Cdd:PRK12316 2763 PPLPLQYADYAawqrAWMDSGEGARQLDYWRERLGGEQPvLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREG 2842
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1108 ATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGAYQHQQ 1187
Cdd:PRK12316 2843 VTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQD 2922
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1188 LSFDRILHQIEYERMSNKNPLFQIMAILQNaGDVCQQNLRDCTLHRLPLSSGFSMFDMTWNFSVEQDAVTIELDYASELF 1267
Cdd:PRK12316 2923 LPFEQLVEALQPERSLSHSPLFQVMYNHQS-GERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLF 3001
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1268 YPASMQMLLDNYQQTLRQLLTLP-ANTAQLALNPLCEREQQWLQQLAVNADAGSRDSLLMHIGRLAHTQPDSLAVSCERQ 1346
Cdd:PRK12316 3002 DARTVERLARHWQNLLRGMVENPqRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQ 3081
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1347 QYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTD 1425
Cdd:PRK12316 3082 RLSYAELNRRANRLAHRLIERGVGPdVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ 3161
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1426 GEPE----QGWASPAV--GFDSLVSHPAAADALPipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSAR 1499
Cdd:PRK12316 3162 SHLRlplaQGVQVLDLdrGDENYAEANPAIRTMP----ENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVG 3237
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1500 DKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPL-TVL 1578
Cdd:PRK12316 3238 DRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLkRIV 3317
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1579 CGGEKMPAALLTQLrRIATRVLQVYGPTETTIWSTCADLTHEGASDC-IGTPIQATEVLVMDQAGNPLPSGAFGELWLGG 1657
Cdd:PRK12316 3318 CGGEALPADLQQQV-FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRACYILDGSLEPVPVGALGELYLGG 3396
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1658 AGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERS 1737
Cdd:PRK12316 3397 EGLARGYHNRPGLTAERFVPDPFVPGER-LYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREA 3475
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1738 LSLIVgEGQQarIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPETrySASEADY 1817
Cdd:PRK12316 3476 VVLAV-DGRQ--LVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDA--ALLQQDY 3550
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1818 TPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSLQIPQLLHAIRqQMGVSLTIREFIMHSQIRELTALALSKTAEV 1897
Cdd:PRK12316 3551 VAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRAR-QAGIRFTPKDLFQHQTIQGLARVARVGGGVA 3629
|
...
gi 1725075560 1898 ADE 1900
Cdd:PRK12316 3630 VDQ 3632
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
313-1900 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 731.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:PRK05691 1153 DGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELL 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSP----LHSGDAPC-IAPSSIDYRSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLA 467
Cdd:PRK05691 1233 LTQSHllerLPQAEGVSaIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALD 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 468 QGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPG----LRT 543
Cdd:PRK05691 1313 DSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAactsLRR 1392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 544 MIVMGDAPPA---DVVAWWAERTRLCNGYGPTEASIATSlceyrpgvPWNC---------IGKPLKNYRCHILDLHHNPL 611
Cdd:PRK05691 1393 LFSGGEALPAelrNRVLQRLPQVQLHNRYGPTETAINVT--------HWQCqaedgerspIGRPLGNVLCRVLDAELNLL 1464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 612 PVGFEGELCIAGSGLAHGYLHQEALSAEKFIIcrLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGE 691
Cdd:PRK05691 1465 PPGVAGELCIGGAGLARGYLGRPALTAERFVP--DPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEE 1542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 692 VESAVRSHPLVESACVVARSQPSG-KILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK05691 1543 IQARLLAQPGVAQAAVLVREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 771 EK--WPLDERNErltpPETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTV 848
Cdd:PRK05691 1623 PEpvWQQREHVE----PRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASEL 1698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 849 RKLAEYIENKAVAAER----AIAICDEHRA-PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEK 923
Cdd:PRK05691 1699 GAFAEQVARIQAAGERnsqgAIARVDRSQPvPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILR 1778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 924 HESLRTRFTETDGVAYQLAEPHTPIRLadHWVDGQTLSAEKWVRQLCA-------TPFDITARPPLVLRLVQYHQQHHVL 996
Cdd:PRK05691 1779 HETLRTTFPSVDGVPVQQVAEDSGLRM--DWQDFSALPADARQQRLQQladseahQPFDLERGPLLRACLVKAAEREHYF 1856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 997 IWVKHNIITDAWSEQLILNDLWQRYNE-LDDHHGLDAPQPqIQTIDI-------VNSGiasPAPADVAYWQQQLQDCRE- 1067
Cdd:PRK05691 1857 VLTLHHIVTEGWAMDIFARELGALYEAfLDDRESPLEPLP-VQYLDYsvwqrqwLESG---ERQRQLDYWKAQLGNEHPl 1932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1068 LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQ 1147
Cdd:PRK05691 1933 LELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEG 2012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1148 VSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAGDVCQQNLR 1227
Cdd:PRK05691 2013 LIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRQLA 2092
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1228 DCTLHRLPLSSGFSMFDMTWNFSVEQDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLPANtaQLALNPL--CERE 1305
Cdd:PRK05691 2093 GMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQ--RLAELPLlaAAEQ 2170
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1306 QQWLQQLAVNADAGSRDSLLMHI-GRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCH 1383
Cdd:PRK05691 2171 QQLLDSLAGEAGEARLDQTLHGLfAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPqVRVGLALERSLE 2250
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1384 VAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTD-------GEPEQGWASPAVGFD--SLVSHPAAA-DALP 1453
Cdd:PRK05691 2251 MVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDralfealGELPAGVARWCLEDDaaALAAYSDAPlPFLS 2330
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1454 IPadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLcPRE 1533
Cdd:PRK05691 2331 LP--QHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL-RAQ 2407
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1534 TAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPLTVLC--GGEKMPAALLTQLRRI--ATRVLQVYGPTETT 1609
Cdd:PRK05691 2408 GQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCitGGEALTGEHLQRIRQAfaPQLFFNAYGPTETV 2487
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1610 IW---STCADLTHEG-ASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAER 1685
Cdd:PRK05691 2488 VMplaCLAPEQLEEGaASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGG 2567
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1686 YMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYL---QLTSGEEL 1762
Cdd:PRK05691 2568 RLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLvsaVAGQDDEA 2647
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1763 N---EKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPETrySASEADYTPAANEAESAMQHIWQQVLSQT 1839
Cdd:PRK05691 2648 QaalREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDP--ELNRQAYQAPRSELEQQLAQIWREVLNVE 2725
|
1610 1620 1630 1640 1650 1660
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 1840 QISVCDSFFSLGGNSLQIPQLLHAIRQQmGVSLTIREFIMHSQIRELTALALSKTAEVADE 1900
Cdd:PRK05691 2726 RVGLGDNFFELGGDSILSIQVVSRARQL-GIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQ 2785
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
859-1901 |
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: 671.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 859 AVAAERAIAICDEHRAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVA 938
Cdd:COG1020 3 AAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 939 YQLAEPHT-----PIRLADHWVDGQTLSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLI 1013
Cdd:COG1020 83 VQVIQPVVaaplpVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1014 LNDLWQRYNELDDHHGLDAPQPQIQTIDIVNSGIA----SPAPADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIH 1088
Cdd:COG1020 163 LAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREwlqgEELARQLAYWRQQLAGLPPlLELPTDRPRPAVQSYRGARVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1089 YQLQPDVAGLLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTL 1168
Cdd:COG1020 243 FRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1169 AGLIGNMMETCIGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAgDVCQQNLRDCTLHRLPLSSGFSMFDMTWN 1248
Cdd:COG1020 323 AELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNA-PADELELPGLTLEPLELDSGTAKFDLTLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1249 FSVEQDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLPAnTAQLALNPLCEREQQWLQQLAVNADAGSRDSLLMH- 1327
Cdd:COG1020 402 VVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPD-QPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHe 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1328 -IGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHY 1405
Cdd:COG1020 481 lFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDlVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1406 PADRVSYMIENAQARLLVTDGEPEQGWAS---PAVGFDSLVSHPAAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITHG 1481
Cdd:COG1020 561 PAERLAYMLEDAGARLVLTQSALAARLPElgvPVLALDALALAAEPATNPPVPVTpDDLAYVIYTSGSTGRPKGVMVEHR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1482 NLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWS 1561
Cdd:COG1020 641 ALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1562 TIVHHLPAASQRPLTVLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTCADLT---HEGASDCIGTPIQATEVL 1636
Cdd:COG1020 721 ALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLpgARLVNLYGPTETTVDSTYYEVTppdADGGSVPIGRPIANTRVY 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1637 VMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLR-RQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIR 1715
Cdd:COG1020 801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVAdPFGFPGAR-LYRTGDLARWLPDGNLEFLGRADDQVKIR 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1716 GHRIELSEIDLSLSSLDNIERSLSLIVGEGQQA-RIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTN 1794
Cdd:COG1020 880 GFRIELGEIEAALLQHPGVREAVVVAREDAPGDkRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTG 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1795 NNKIDIRRLPAPETRYSASEADYTPAANEAESAmqhIWQQVLSQTQISVCDSFFSLGGNSLQIPQLLHAIRQQMGVSLTI 1874
Cdd:COG1020 960 NGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAA---LALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLL 1036
|
1050 1060
....*....|....*....|....*..
gi 1725075560 1875 REFIMHSQIRELTALALSKTAEVADET 1901
Cdd:COG1020 1037 LLLFLAAAAAAAAAAAAAAAAAAAAPL 1063
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
873-1884 |
7.44e-180 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 608.31 E-value: 7.44e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLA- 951
Cdd:PRK12467 49 RIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPl 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 952 DHWVDGQTLSAEKWVRQLC----ATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDH 1027
Cdd:PRK12467 129 DDLANEQGRARESQIEAYIneevARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1028 HGLDAPQPQIQTIDIvnsGI-------ASPAPADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLL 1099
Cdd:PRK12467 209 REPSLPALPIQYADY---AIwqrswleAGERERQLAYWQEQLGGEHTvLELPTDRPRPAVPSYRGARLRVDLPQALSAGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1100 ASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETC 1179
Cdd:PRK12467 286 KALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1180 IGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAG----DVCQQNLRDCTLHRLPLSSGFSMFDMTWNFSVEQDA 1255
Cdd:PRK12467 366 LGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTAtggrDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1256 VTIELDYASELFYPASMQMLLDNYQQTLRQLLTLPANT-AQLALNPLCEREQQwLQQLAVNADAGSRDSLLMHIGRLAHT 1334
Cdd:PRK12467 446 LWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRlGELPLLDAEERARE-LVRWNAPATEYAPDCVHQLIEAQARQ 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1335 QPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYM 1413
Cdd:PRK12467 525 HPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPdVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYM 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1414 IENAQARLLVTDGE-------PEQGWASPAVGFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNF 1486
Cdd:PRK12467 605 LDDSGVRLLLTQSHllaqlpvPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANY 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 TNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHH 1566
Cdd:PRK12467 685 VCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1567 LPAASQRPLT-VLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTCADLTHEGASDC---IGTPIQATEVLVMDQ 1640
Cdd:PRK12467 765 SRVALPRPQRaLVCGGEALQVDLLARVRALGpgARLINHYGPTETTVGVSTYELSDEERDFGnvpIGQPLANLGLYILDH 844
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1641 AGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrRQAFGA--ERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHR 1718
Cdd:PRK12467 845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFV-PDPFGAdgGR-LYRTGDLARYRADGVIEYLGRMDHQVKIRGFR 922
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1719 IELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYLQLTSGEELNEKA-----VRTALKARLPNIMIPSGFVVLSAFPLT 1793
Cdd:PRK12467 923 IELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQatrdeLKAQLRQVLPDYMVPAHLLLLDSLPLT 1002
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1794 NNNKIDIRRLPAPETrySASEADYTPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSLQIPQLLHAIRQQMGVSLT 1873
Cdd:PRK12467 1003 PNGKLDRKALPKPDA--SAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP 1080
|
1050
....*....|.
gi 1725075560 1874 IREFIMHSQIR 1884
Cdd:PRK12467 1081 LRTLFEHQTLA 1091
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
871-1900 |
4.11e-169 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 576.14 E-value: 4.11e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 871 EHRAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRL 950
Cdd:PRK12316 47 AERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 951 ADHWVDGQTLSAEKW-----VRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELD 1025
Cdd:PRK12316 127 EFEDCSGLPEAEQEArlrdeAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1026 DHHGLDAPQPQIQTIDIV---NSGI-ASPAPADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLA 1100
Cdd:PRK12316 207 TGAEPGLPALPIQYADYAlwqRSWLeAGEQERQLEYWRAQLGEEHPvLELPTDHPRPAVPSYRGSRYEFSIDPALAEALR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1101 SRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCI 1180
Cdd:PRK12316 287 GTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1181 GAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQN--AGDVCQQNLRDCTLHRLPLSSGFSMFDMTWNFSVEQDAVTI 1258
Cdd:PRK12316 367 GAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPlvADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1259 ELDYASELFYPASMQMLLDNYQQTLRQLLTLPaNTAQLALNPLCEREQQWLQQLAVNADAGSRDSLLMH--IGRLAHTQP 1336
Cdd:PRK12316 447 ALTYATDLFEARTVERMARHWQNLLRGMVENP-QARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHrlFEEQVERTP 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1337 DSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIE 1415
Cdd:PRK12316 526 EAPALAFGEETLDYAELNRRANRLAHALIERGVGPdVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1416 NAQARLLVTDgEPEQGWASPAVGFDSLV---------SHPAAADALPIPADDtLAYIMYTSGSTGNPKGVMITHGNLNNF 1486
Cdd:PRK12316 606 DSGVQLLLSQ-SHLGRKLPLAAGVQVLDldrpaawleGYSEENPGTELNPEN-LAYVIYTSGSTGKPKGAGNRHRALSNR 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 TNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHH 1566
Cdd:PRK12316 684 LCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1567 LPAASQRPLTVL-CGGEKMPAALLTQL--RRIATRVLQVYGPTETTIWSTCADLTHEGA-SDCIGTPIQATEVLVMDQAG 1642
Cdd:PRK12316 764 EDVASCTSLRRIvCSGEALPADAQEQVfaKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGdSVPIGRPIANLACYILDANL 843
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1643 NPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELS 1722
Cdd:PRK12316 844 EPVPVGVLGELYLAGRGLARGYHGRPGLTAERFV-PSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELG 922
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1723 EIDLSLSSLDNIeRSLSLIVGEGQQarIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRR 1802
Cdd:PRK12316 923 EIEARLLEHPWV-REAAVLAVDGKQ--LVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKA 999
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1803 LPAPETrySASEADYTPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSLQIPQLLHAIRQQmGVSLTIREFIMHSQ 1882
Cdd:PRK12316 1000 LPAPEA--SVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQT 1076
|
1050
....*....|....*...
gi 1725075560 1883 IRELTALALSKTAEVADE 1900
Cdd:PRK12316 1077 IRSLALVAKAGQATAADQ 1094
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1336-1803 |
5.95e-156 |
|
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: 487.57 E-value: 5.95e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDrVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGEPEQG--WASPAVGFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVG 1492
Cdd:cd12116 81 EDAEPALVLTDDALPDRlpAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1493 RLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWstivhHLPAASQ 1572
Cdd:cd12116 161 RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATW-----RMLLDAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1573 ----RPLTVLCGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSG 1648
Cdd:cd12116 236 wqgrAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1649 AFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd12116 316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 1729 SSLDNIERSLSLIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd12116 396 AAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
245-1109 |
1.65e-153 |
|
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: 509.40 E-value: 1.65e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 245 FNAFTDYLDALLADPADPIAA-PIVTQPHTLHRLSQFNATDDAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEID 323
Cdd:COG1020 429 AGHLVTLLEALAADPDQPLGDlPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELN 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 324 RASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSP----LH 399
Cdd:COG1020 509 ARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSAlaarLP 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 400 SGDAPCIAPSSIDYRSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLG 479
Cdd:COG1020 589 ELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLS 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 480 FDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMW---PGLRTMIVMGDAPPADVV 556
Cdd:COG1020 669 FDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPealPSLRLVLVGGEALPPELV 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 557 AWWAER---TRLCNGYGPTEASIATSLCEYRPGVPWN---CIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGY 630
Cdd:COG1020 749 RRWRARlpgARLVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGY 828
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 631 LHQEALSAEKFIICrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVAR 710
Cdd:COG1020 829 LNRPELTAERFVAD--PFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAR 906
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 711 SQPSG-KILAAFVQPASPELTIDA-LRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDERNERLTPPETE 788
Cdd:COG1020 907 EDAPGdKRLVAYVVPEAGAAAAAAlLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEE 986
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 789 TEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYIENKAVAAERAIAI 868
Cdd:COG1020 987 EEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAA 1066
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 869 CDEHRAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPI 948
Cdd:COG1020 1067 AAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAA 1146
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 949 RLADHWVDGQTLSAEKWVRQLCATPFDITARPPLVLRLVQY---HQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELD 1025
Cdd:COG1020 1147 ALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLlllLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAA 1226
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1026 DHHGLDAPQPQIQTIDIVNSGIASPAPADVAYWQQQLQDCRELDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRGKA 1105
Cdd:COG1020 1227 AAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLL 1306
|
....
gi 1725075560 1106 LGAT 1109
Cdd:COG1020 1307 LALA 1310
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1336-1803 |
3.72e-153 |
|
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: 478.95 E-value: 3.72e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDlVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGepeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL 1494
Cdd:cd05930 81 EDSGAKLVLTDP-------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1495 ALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRP 1574
Cdd:cd05930 130 PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1575 L-TVLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTCADLTHEGASD---CIGTPIQATEVLVMDQAGNPLPSG 1648
Cdd:cd05930 210 LrLVLVGGEALPPDLVRRWRELLpgARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIPNTRVYVLDENLRPVPPG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1649 AFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd05930 290 VPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGER-MYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 1729 SSLDNIERSLSLIVGEGQ-QARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05930 369 LAHPGVREAAVVAREDGDgEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
310-770 |
1.61e-150 |
|
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: 471.63 E-value: 1.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:cd05930 6 VVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQG 469
Cdd:cd05930 86 KLVLTDP-------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 470 SRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELL----PREMWPGLRTMI 545
Cdd:cd05930 135 DRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLlqelELAALPSLRLVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVAWWAE---RTRLCNGYGPTEASIATSLCEYRPG------VPwncIGKPLKNYRCHILDLHHNPLPVGFE 616
Cdd:cd05930 215 VGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYYRVPPDdeedgrVP---IGRPIPNTRVYVLDENLRPVPPGVP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 617 GELCIAGSGLAHGYLHQEALSAEKFIicRLPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAV 696
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERFV--PNPF-GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 697 RSHPLVESACVVARSQPSG-KILAAFVQPAS-PELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05930 369 LAHPGVREAAVVAREDGDGeKRLVAYVVPDEgGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
611-1888 |
2.22e-150 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 518.57 E-value: 2.22e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 611 LPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpYMAAEERLyRTGDIAkWDEQGNIIFVGRRDHQVKIRGVRIEMG 690
Cdd:PRK05691 392 LGDNRVGEIWASGPSIAHGYWRNPEASAKTFV-----EHDGRTWL-RTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQ 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 691 EVESavrshpLVESACVVARSqpsGKIlAAF-------------------VQPA-SPELTIDALRHALVTLLHPAaiPSV 750
Cdd:PRK05691 465 DIEK------TVEREVEVVRK---GRV-AAFavnhqgeegigiaaeisrsVQKIlPPQALIKSIRQAVAEACQEA--PSV 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 751 FIFLP--ALPLTINGKI----ARQQLEKWPLD-----------ERNERLTPPEtETEAILERIVANAIGCPQADVTQEFI 813
Cdd:PRK05691 533 VLLLNpgALPKTSSGKLqrsaCRLRLADGSLDsyalfpalqavEAAQTAASGD-ELQARIAAIWCEQLKVEQVAADDHFF 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 814 NLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYIENKAV---AAERAIAICDEHRA-PLSPQQNLLWYLSAL 889
Cdd:PRK05691 612 LLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAgggAAQAAIARLPRGQAlPQSLAQNRLWLLWQL 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 890 NPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTP-----IRLADHWVDGQTLSAEK 964
Cdd:PRK05691 692 DPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEfalqrIDLSDLPEAEREARAAQ 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 965 WVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDHHGLDAPQPQIQTIDIVN 1044
Cdd:PRK05691 772 IREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGA 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1045 ---SGIAS-PAPADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRGKALGATPFALLCAALS 1119
Cdd:PRK05691 852 wqrQWLAQgEAARQLAYWKAQLGDEQPvLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQ 931
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1120 LLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGAYQHQQLSFDRILHQIEY 1199
Cdd:PRK05691 932 ALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQ 1011
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1200 ERmsnKNPLFQIMAILQNAGDVCQQNLRDCTLHRLPLSSGFSMFDMtwNFSVEQDA---VTIELDYASELFYPASMQMLL 1276
Cdd:PRK05691 1012 AR---EQGLFQVMFNHQQRDLSALRRLPGLLAEELPWHSREAKFDL--QLHSEEDRngrLTLSFDYAAELFDAATIERLA 1086
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1277 DNYQQTLRQLltlpANTAQLALNP---LCEREQQWLQQLAVNADAGSRDSLLMHIGRLAHTQPDSLAVSCERQQYSYRQL 1353
Cdd:PRK05691 1087 EHFLALLEQV----CEDPQRALGDvqlLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAEL 1162
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1354 WAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTDGEPEQGW 1432
Cdd:PRK05691 1163 HAQANRLAHYLRDKGVGPdVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERL 1242
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1433 ASP----AVGFDSL--VSHPAAADALPIpADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLT 1506
Cdd:PRK05691 1243 PQAegvsAIALDSLhlDSWPSQAPGLHL-HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKA 1321
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1507 SISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPLTVL-CGGEKMP 1585
Cdd:PRK05691 1322 PISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLfSGGEALP 1401
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1586 AALLtqlRRIATRVLQV-----YGPTETTI----WSTCADlthEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLG 1656
Cdd:PRK05691 1402 AELR---NRVLQRLPQVqlhnrYGPTETAInvthWQCQAE---DGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIG 1475
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1657 GAGVSPGYWRNPTLSDKVFLRrQAFG--AERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNI 1734
Cdd:PRK05691 1476 GAGLARGYLGRPALTAERFVP-DPLGedGAR-LYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGV 1553
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1735 ERSLSLIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPETRysasE 1814
Cdd:PRK05691 1554 AQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ----Q 1629
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1815 ADYTPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSLQIPQLLHAIRQQMGVSLTIREFIMHSQIRELTA 1888
Cdd:PRK05691 1630 REHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAE 1703
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
875-1901 |
5.17e-138 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 480.61 E-value: 5.17e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGpLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRL--AD 952
Cdd:PRK12316 4104 PLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELGRPLQVVHKQVSLpfAE 4182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 953 HWVDGQT---LSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNelddhhG 1029
Cdd:PRK12316 4183 LDWRGRAdlqAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYS------G 4256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1030 LDAPQPQIQTIDIVNSGIASPAPADVAYWQQQLqdcRELDFPL----DKPRPLMPTHAGERIHYQ-LQPDVAGLLASRGK 1104
Cdd:PRK12316 4257 RPPAQPGGRYRDYIAWLQRQDAAASEAFWREQL---AALDEPTrlaqAIARADLRSANGYGEHVReLDATATARLREFAR 4333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1105 ALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAAR--DNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGA 1182
Cdd:PRK12316 4334 TQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLAL 4413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1183 YQHQQLSfdriLHQIEYERMSNKNPLFQIMAILQN--AGDVCQQN-----------LRDCTLHRLPLSSGFSmfdmtwnf 1249
Cdd:PRK12316 4414 REHEHTP----LYEIQRWAGQGGEALFDSLLVFENypVSEALQQGapgglrfgevtNHEQTNYPLTLAVGLG-------- 4481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1250 sveqDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLPANT-AQLALnpLCEREQQWLQQLAVNADAGSRDSLLMH- 1327
Cdd:PRK12316 4482 ----ETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRlGELQL--LEKAEQQRIVALWNRTDAGYPATRCVHq 4555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1328 -IGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHY 1405
Cdd:PRK12316 4556 lVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVlVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1406 PADRVSYMIENAQARLLVTDGEPEQGWASPAvGFDSLV--------SHPAAADALPIPADDtLAYIMYTSGSTGNPKGVM 1477
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQRLPIPD-GLASLAldrdedweGFPAHDPAVRLHPDN-LAYVIYTSGSTGRPKGVA 4713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1478 ITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVtLCPRETAMDPVKLYHFIERQQPSVIQATP 1557
Cdd:PRK12316 4714 VSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV-VIRDDSLWDPERLYAEIHEHRVTVLVFPP 4792
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1558 TVWSTIVHHLPAASQRP--LTVLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWST---CADLTHEGASDC-IGTP 1629
Cdd:PRK12316 4793 VYLQQLAEHAERDGEPPslRVYCFGGEAVAQASYDLAWRALkpVYLFNGYGPTETTVTVLlwkARDGDACGAAYMpIGTP 4872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1630 IQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrRQAFGAE-RYMYRTGDIVRFNRQGQLEYLGRN 1708
Cdd:PRK12316 4873 LGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFV-PDPFGAPgGRLYRTGDLARYRADGVIDYLGRV 4951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1709 DHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYL-----QLTSGEELNEK---AVRTALKARLPNIMI 1780
Cdd:PRK12316 4952 DHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVvpqdpALADADEAQAElrdELKAALRERLPEYMV 5031
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1781 PSGFVVLSAFPLTNNNKIDIRRLPAPETrySASEADYTPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSLQIPQL 1860
Cdd:PRK12316 5032 PAHLVFLARMPLTPNGKLDRKALPQPDA--SLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1725075560 1861 LHAIRQQMGVSLTIREFIMHSQIRELTAlALSKTAEVADET 1901
Cdd:PRK12316 5110 TSRIQLELGLELPLRELFQTPTLAAFVE-LAAAAGSGDDEK 5149
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
310-770 |
2.55e-132 |
|
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: 420.89 E-value: 2.55e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:cd17652 6 VVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQG 469
Cdd:cd17652 86 ALLLTTP-------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 470 SRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPGLRTMIVMGD 549
Cdd:cd17652 135 SRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDLRTLVVAGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 550 APPADVVAWWAERTRLCNGYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHG 629
Cdd:cd17652 215 ACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 630 YLHQEALSAEKFIICrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA 709
Cdd:cd17652 295 YLNRPGLTAERFVAD--PFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVV 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 710 R-SQPSGKILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17652 373 RdDRPGDKRLVAYVVPAPGAaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
875-1888 |
3.35e-129 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 453.08 E-value: 3.35e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGpLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLA--- 951
Cdd:PRK12467 2648 PLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVVYKQARLPfsr 2726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 952 -DhWVDGQTLSAE--KWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNelddhh 1028
Cdd:PRK12467 2727 lD-WRDRADLEQAldALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF------ 2799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1029 GLDAPQPQIQTIDIVNSGIASPAPADVAYWQQQLQDCREldfPLDKPRPLMPTHA----GERIHYQ-LQPDVAGLLASRG 1103
Cdd:PRK12467 2800 GQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEE---PTRLARALYPAPAeavaGHGAHYLhLDATQTRQLIEFA 2876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1104 KALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARD-NLDQT-QVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIG 1181
Cdd:PRK12467 2877 RRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPaQLRGAeQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLA 2956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1182 AYQHQ---------------QLSFDRILhqiEYERmsnknplFQIMAILQNAGDvcqQNLRDCTLHRLPLSSgfsmFDMT 1246
Cdd:PRK12467 2957 LREFEhtpladiqrwagqggEALFDSIL---VFEN-------YPISEALKQGAP---SGLRFGAVSSREQTN----YPLT 3019
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1247 WNFSVEqDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLPANT-AQLALNPLCEREQQWLQQLAVNADAGSRDSLL 1325
Cdd:PRK12467 3020 LAVGLG-DTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARlGELPTLAAHERRQVLHAWNATAAAYPSERLVH 3098
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1326 MHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVH 1404
Cdd:PRK12467 3099 QLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPdVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPE 3178
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1405 YPADRVSYMIENAQARLLVTDGEPEQGWASPAVG----FDSLVSHPAAADALPIPAD-DTLAYIMYTSGSTGNPKGVMIT 1479
Cdd:PRK12467 3179 YPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDtaltLDRLDLNGYSENNPSTRVMgENLAYVIYTSGSTGKPKGVGVR 3258
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1480 HGNLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETaMDPVKLYHFIERQQPSVIQATPTV 1559
Cdd:PRK12467 3259 HGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAY 3337
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1560 WSTIVHHLPAASQRPLT-VLCGGEKMPAALLTQLRRIATRV--LQVYGPTETTI----WSTCADLTHEGASDCIGTPIQA 1632
Cdd:PRK12467 3338 LQQFAEDAGGADCASLDiYVFGGEAVPPAAFEQVKRKLKPRglTNGYGPTEAVVtvtlWKCGGDAVCEAPYAPIGRPVAG 3417
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1633 TEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQV 1712
Cdd:PRK12467 3418 RSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQV 3497
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1713 KIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPL 1792
Cdd:PRK12467 3498 KIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPL 3577
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1793 TNNNKIDIRRLPAPETRYSASeadYTPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSLQIPQLLHAIRQQMGVSL 1872
Cdd:PRK12467 3578 GPNGKVDRKALPDPDAKGSRE---YVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKL 3654
|
1050
....*....|....*.
gi 1725075560 1873 TIREFIMHSQIRELTA 1888
Cdd:PRK12467 3655 SLRDLMSAPTIAELAG 3670
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1332-1803 |
2.12e-126 |
|
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: 406.20 E-value: 2.12e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:cd12117 7 AARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDvVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLVTDGEPEQGWASPA---VGFDSLVSHPAAADALPIPADDtLAYIMYTSGSTGNPKGVMITHGNLNNFT 1487
Cdd:cd12117 87 AFMLADAGAKVLLTDRSLAGRAGGLEvavVIDEALDAGPAGNPAVPVSPDD-LAYVMYTSGSTGRPKGVAVTHRGVVRLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1488 NDfVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHL 1567
Cdd:cd12117 166 KN-TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1568 PAASQRPLTVLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTC---ADLTHEGASDCIGTPIQATEVLVMDQAG 1642
Cdd:cd12117 245 PECFAGLRELLTGGEVVSPPHVRRVLAACpgLRLVNGYGPTENTTFTTShvvTELDEVAGSIPIGRPIANTRVYVLDEDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1643 NPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELS 1722
Cdd:cd12117 325 RPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGER-LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1723 EIDLSLSSLDNIeRSLSLIVGE--GQQARIVSYlqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDI 1800
Cdd:cd12117 404 EIEAALRAHPGV-REAVVVVREdaGGDKRLVAY--VVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
...
gi 1725075560 1801 RRL 1803
Cdd:cd12117 481 RAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
310-770 |
5.49e-125 |
|
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: 402.42 E-value: 5.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:cd17646 17 VVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSPLHSGDAPCIAPSSIDYRSLNIHAEQLPQ---SRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGL 466
Cdd:cd17646 97 AVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLvppRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 467 AQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREM----WPGLR 542
Cdd:cd17646 177 GPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPaagsCASLR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 543 TMIVMGDAPPADVVAWWAERT--RLCNGYGPTEASIATSLCEYR-----PGVPwncIGKPLKNYRCHILDLHHNPLPVGF 615
Cdd:cd17646 257 RVFCSGEALPPELAARFLALPgaELHNLYGPTEAAIDVTHWPVRgpaetPSVP---IGRPVPNTRLYVLDDALRPVPVGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 616 EGELCIAGSGLAHGYLHQEALSAEKFIICrlPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESA 695
Cdd:cd17646 334 PGELYLGGVQLARGYLGRPALTAERFVPD--PF-GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAA 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 696 VRSHPLVESACVVARSQPSG-KILAAFVQPAS--PELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17646 411 LAAHPAVTHAVVVARAAPAGaARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
318-707 |
6.10e-125 |
|
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: 399.33 E-value: 6.10e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 318 SYGEIDRASDQFACWLLEHSGA-ASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADS 396
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 397 PlHSGDAPCIAPSSIDYRSLNIHAEQ------LPQSR---DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLA 467
Cdd:TIGR01733 81 A-LASRLAGLVLPVILLDPLELAALDdapappPPDAPsgpDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 468 QGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLT-QHDIGHITITPAILELLPREMWP---GLRT 543
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIaEHPVTVLNLTPSLLALLAAALPPalaSLRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 544 MIVMGDAPPADVVAWWAER---TRLCNGYGPTEASIATSLCEY----RPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFE 616
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 617 GELCIAGSGLAHGYLHQEALSAEKFIicRLPYMA-AEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESA 695
Cdd:TIGR01733 320 GELYIGGPGVARGYLNRPELTAERFV--PDPFAGgDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 1725075560 696 VRSHPLVESACV 707
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
313-770 |
8.71e-124 |
|
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: 398.59 E-value: 8.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSPL-----HSGDAPCIAPSSIDYRSLNIHAEQLPqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLA 467
Cdd:cd12116 89 LTDDALpdrlpAGLPVLLLALAAAAAAPAAPRTPVSP---DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 468 QGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPGLR--TMI 545
Cdd:cd12116 166 PGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAglTAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVAWWAERTR-LCNGYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGS 624
Cdd:cd12116 246 CGGEALPPDLAARLLSRVGsLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 625 GLAHGYLHQEALSAEKFIicRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVES 704
Cdd:cd12116 326 GVAQGYLGRPALTAERFV--PDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQ 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 705 ACVVARSQPSGKILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd12116 404 AAVVVREDGGDRRLVAYVVLKAGAaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
313-770 |
4.17e-123 |
|
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: 396.96 E-value: 4.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSPLhSGDAPCIAPSSIDYRSLNIHAEQLPQSR---DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNhRDFIGLAQG 469
Cdd:cd12117 99 LTDRSL-AGRAGGLEVAVVIDEALDAGPAGNPAVPvspDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVTLGPD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 470 SRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPRE---MWPGLRTMIV 546
Cdd:cd12117 177 DRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEdpeCFAGLRELLT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 547 MGDA-PPADVVAWWAE--RTRLCNGYGPTEASIATSLCEYRPG------VPwncIGKPLKNYRCHILDLHHNPLPVGFEG 617
Cdd:cd12117 257 GGEVvSPPHVRRVLAAcpGLRLVNGYGPTENTTFTTSHVVTELdevagsIP---IGRPIANTRVYVLDEDGRPVPPGVPG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 618 ELCIAGSGLAHGYLHQEALSAEKFIicRLPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVR 697
Cdd:cd12117 334 ELYVGGDGLALGYLNRPALTAERFV--ADPF-GPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALR 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 698 SHPLVESACVVAR-SQPSGKILAAFVQPAsPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd12117 411 AHPGVREAVVVVReDAGGDKRLVAYVVAE-GALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1349-1737 |
3.20e-122 |
|
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: 391.63 E-value: 3.20e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHAL-----LRIDSRpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLV 1423
Cdd:TIGR01733 1 TYRELDERANRLARHLraaggVGPGDR---VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1424 TDGEPEQ---GWASPAVGFDSLVSHPAAADALPIPAD-----DTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLA 1495
Cdd:TIGR01733 78 TDSALASrlaGLVLPVILLDPLELAALDDAPAPPPPDapsgpDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1496 LSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQP-SVIQATPTVWSTIVHHLPAASQRP 1574
Cdd:TIGR01733 158 LDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPvTVLNLTPSLLALLAAALPPALASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1575 LTVLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTCADLTHEGASD----CIGTPIQATEVLVMDQAGNPLPSG 1648
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGpgARLINLYGPTETTVWSTATLVDPDDAPRespvPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1649 AFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFG-AERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLS 1727
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|
gi 1725075560 1728 LSSLDNIERS 1737
Cdd:TIGR01733 398 LLRHPGVREA 407
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
875-1898 |
6.47e-119 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 420.90 E-value: 6.47e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGpLDLGRFEQAINFIYEKHESLRTRFTETDGvayqLAEPHTPIR----- 949
Cdd:PRK12316 1558 PLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDG----LEQPLQVIHkqvel 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 950 ----LADHWVDGQTLSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNeld 1025
Cdd:PRK12316 1633 pfaeLDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYA--- 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1026 dhhGLDAPQPQIQTIDIVNSGIASPAPADVAYWQQQLQdcreldfPLDKPRPLMPTHAGER------IHYQ-LQPDVAGL 1098
Cdd:PRK12316 1710 ---GQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLA-------ALEEPTRLAQAARTEDgqvgygDHQQlLDPAQTRA 1779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1099 LASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAAR----DNLDQtQVsGFHVNTVPLRIQLSEQDTLAGLIGN 1174
Cdd:PRK12316 1780 LAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRpaelPGIEQ-QI-GLFINTLPVIAAPRPDQSVADWLQE 1857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1175 MMETCIGAYQHQQLSfdriLHQIEYERMSNKNPLFQIMAILQN--AGDVCQQ----NLRDCTLHRL-----PLSSGFSMf 1243
Cdd:PRK12316 1858 VQALNLALREHEHTP----LYDIQRWAGQGGEALFDSLLVFENypVAEALKQgapaGLVFGRVSNHeqtnyPLTLAVTL- 1932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1244 dmtwnfsveQDAVTIELDYASELFYPASMQMLLDNyqqtLRQLLTLPANTAQLALN--PLCER-EQQWLQQLAVNADAGS 1320
Cdd:PRK12316 1933 ---------GETLSLQYSYDRGHFDAAAIERLDRH----LLHLLEQMAEDAQAALGelALLDAgERQRILADWDRTPEAY 1999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1321 RDSLLMH--IGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKH 1397
Cdd:PRK12316 2000 PRGPGVHqrIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPeVRVAIAAERSFELVVALLAVLKAGGA 2079
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1398 YVPIDVHYPADRVSYMIENAQARLLVTDGE------PEQGWASpaVGFDSLVSHPAAADALPIP--ADDTLAYIMYTSGS 1469
Cdd:PRK12316 2080 YVPLDPNYPAERLAYMLEDSGAALLLTQRHllerlpLPAGVAR--LPLDRDAEWADYPDTAPAVqlAGENLAYVIYTSGS 2157
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1470 TGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPrETAMDPVKLYHFIERQQ 1549
Cdd:PRK12316 2158 TGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRD-DELWDPEQLYDEMERHG 2236
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1550 PSVIQATPTVWSTIVHHLPAASQRP--LTVLCGGEKMPAALLTQLRRI--ATRVLQVYGPTETTI----WSTCADLTHEG 1621
Cdd:PRK12316 2237 VTILDFPPVYLQQLAEHAERDGRPPavRVYCFGGEAVPAASLRLAWEAlrPVYLFNGYGPTEAVVtpllWKCRPQDPCGA 2316
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1622 ASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrRQAFGA--ERyMYRTGDIVRFNRQ 1699
Cdd:PRK12316 2317 AYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFV-PDPFSAsgER-LYRTGDLARYRAD 2394
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1700 GQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIM 1779
Cdd:PRK12316 2395 GVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYM 2474
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1780 IPSGFVVLSAFPLTNNNKIDIRRLPAPETrySASEADYTPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSLQIPQ 1859
Cdd:PRK12316 2475 VPAHWVVLERLPLNPNGKLDRKALPKPDV--SQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQ 2552
|
1050 1060 1070
....*....|....*....|....*....|....*....
gi 1725075560 1860 LLHAIRQQMGVSLTIREFIMHSQIRELTALALSKTAEVA 1898
Cdd:PRK12316 2553 VVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRA 2591
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
310-773 |
2.89e-118 |
|
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: 383.43 E-value: 2.89e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:cd05918 18 VCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSPlhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQG 469
Cdd:cd05918 98 KVVLTSSP------------------------------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 470 SRVLAIASLGFDAFGWDVYGALVSGATLyLAPSElHTDVGALHDYLTQHDIGHITITPAILELLPREMWPGLRTMIVMGD 549
Cdd:cd05918 148 SRVLQFASYTFDVSILEIFTTLAAGGCL-CIPSE-EDRLNDLAGFINRLRVTWAFLTPSVARLLDPEDVPSLRTLVLGGE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 550 APPADVVAWWAERTRLCNGYGPTEASIATSLCEYRPGVPWNCIGKPLkNYRCHILDL--HHNPLPVGFEGELCIAGSGLA 627
Cdd:cd05918 226 ALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPL-GATCWVVDPdnHDRLVPIGAVGELLIEGPILA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 628 HGYLHQEALSAEKFIiCRLPYMAAE-----ERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV 702
Cdd:cd05918 305 RGYLNDPEKTAAAFI-EDPAWLKQEgsgrgRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 703 ESACVVA----RSQPSGKILAAFVQPASPELT------------------IDALRHALVTLLHPAAIPSVFIFLPALPLT 760
Cdd:cd05918 384 AKEVVVEvvkpKDGSSSPQLVAFVVLDGSSSGsgdgdslflepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLT 463
|
490
....*....|...
gi 1725075560 761 INGKIARQQLEKW 773
Cdd:cd05918 464 ASGKIDRRALREL 476
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
310-771 |
3.67e-118 |
|
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: 383.23 E-value: 3.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:cd17651 14 LVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSPLHSGDAP-CIAPSSIDYRSLNIHAE---QLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIG 465
Cdd:cd17651 94 VLVLTHPALAGELAVeLVAVTLLDQPGAAAGADaepDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 466 LAQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPG----- 540
Cdd:cd17651 174 LGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLgvrla 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 541 -LRTMIVMGDAPP--ADVVAWWAER--TRLCNGYGPTEASIATSLCEYRPGVPW---NCIGKPLKNYRCHILDLHHNPLP 612
Cdd:cd17651 254 aLRYLLTGGEQLVltEDLREFCAGLpgLRLHNHYGPTETHVVTALSLPGDPAAWpapPPIGRPIDNTRVYVLDAALRPVP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 613 VGFEGELCIAGSGLAHGYLHQEALSAEKFIicRLPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEV 692
Cdd:cd17651 334 PGVPGELYIGGAGLARGYLNRPELTAERFV--PDPF-VPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 693 ESAVRSHPLVESACVVAR-SQPSGKILAAFVQP-ASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17651 411 EAALARHPGVREAVVLAReDRPGEKRLVAYVVGdPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
.
gi 1725075560 771 E 771
Cdd:cd17651 491 P 491
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
314-770 |
9.13e-117 |
|
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: 379.36 E-value: 9.13e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFAcWLLEHSG-AASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd17655 20 DQTLTYRELNERANQLA-RTLREKGvGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSPLHSGDAPCIAPSSIDYRSLNI-HAEQLP---QSRDaLAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQ 468
Cdd:cd17655 99 LTQSHLQPPIAFIGLIDLLDEDTIYHeESENLEpvsKSDD-LAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 469 GSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPRE---MWPGLRTMI 545
Cdd:cd17655 178 HLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAAddsEGLSLKHLI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVAWWAERTR----LCNGYGPTEASIATSLCEYRPG------VPwncIGKPLKNYRCHILDLHHNPLPVGF 615
Cdd:cd17655 258 VGGEALSTELAKKIIELFGtnptITNAYGPTETTVDASIYQYEPEtdqqvsVP---IGKPLGNTRIYILDQYGRPQPVGV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 616 EGELCIAGSGLAHGYLHQEALSAEKFIicRLPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESA 695
Cdd:cd17655 335 AGELYIGGEGVARGYLNRPELTAEKFV--DDPF-VPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEAR 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 696 VRSHPLVESACVVARSQPSG-KILAAFVQpASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17655 412 LLQHPDIKEAVVIARKDEQGqNYLCAYIV-SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
314-772 |
8.77e-115 |
|
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: 371.64 E-value: 8.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:cd17653 20 GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSplhsgdapciapssidyrslnihaeqlpqSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVL 473
Cdd:cd17653 100 TTD-----------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 474 AIASLGFDAFGWDVYGALVSGATLYLA-PSELHTDVGALHDYLtqhdighiTITPAILELLPREMWPGLRTMIVMGDAPP 552
Cdd:cd17653 151 QVLSIAFDACIGEIFSTLCNGGTLVLAdPSDPFAHVARTVDAL--------MSTPSILSTLSPQDFPNLKTIFLGGEAVP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 553 ADVVAWWAERTRLCNGYGPTEASIATSLCEYRPGVPwNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLH 632
Cdd:cd17653 223 PSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQP-VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 633 QEALSAEKFIicrLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAV-RSHPLVESACVVArs 711
Cdd:cd17653 302 NPALTASKFV---PDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIV-- 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 712 qpSGKILAAFVQPASpeLTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd17653 377 --VNGRLVAFVTPET--VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1330-1804 |
1.67e-114 |
|
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: 373.22 E-value: 1.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPAD 1408
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDlVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYMIENAQARLLVTDGE--PEQGWASPAVGFDSLVSHPAAADALPIPA--DDTLAYIMYTSGSTGNPKGVMITHGNLN 1484
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPAlaGELAVELVAVTLLDQPGAAAGADAEPDPAldADDLAYVIYTSGSTGRPKGVVMPHRSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1485 NFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIV 1564
Cdd:cd17651 163 NLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1565 HHLPAASQRPLT---VLCGGEKMPAAllTQLRRIAT-----RVLQVYGPTETTI---WSTCADLTHEGASDCIGTPIQAT 1633
Cdd:cd17651 243 EHGRPLGVRLAAlryLLTGGEQLVLT--EDLREFCAglpglRLHNHYGPTETHVvtaLSLPGDPAAWPAPPPIGRPIDNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1634 EVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVK 1713
Cdd:cd17651 321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGAR-MYRTGDLARWLPDGELEFLGRADDQVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1714 IRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQ-QARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPL 1792
Cdd:cd17651 400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPgEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
|
490
....*....|..
gi 1725075560 1793 TNNNKIDIRRLP 1804
Cdd:cd17651 480 TPNGKLDRRALP 491
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1332-1807 |
1.96e-113 |
|
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: 370.12 E-value: 1.96e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:cd17655 7 AEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTiVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLVTDGEPEQGWASP----AVGFDSLVSHPAAADALPIPADDtLAYIMYTSGSTGNPKGVMITHGNLNNF 1486
Cdd:cd17655 87 QYILEDSGADILLTQSHLQPPIAFIglidLLDEDTIYHEESENLEPVSKSDD-LAYVIYTSGSTGKPKGVMIEHRGVVNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 TNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVH- 1565
Cdd:cd17655 166 VEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAa 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1566 -HLPAASQRPLTVlcGGEKMPAAL---LTQLRRIATRVLQVYGPTETTIWST---CADLTHEGASDCIGTPIQATEVLVM 1638
Cdd:cd17655 246 dDSEGLSLKHLIV--GGEALSTELakkIIELFGTNPTITNAYGPTETTVDASiyqYEPETDQQVSVPIGKPLGNTRIYIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1639 DQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHR 1718
Cdd:cd17655 324 DQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGER-MYRTGDLARWLPDGNIEFLGRIDHQVKIRGYR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1719 IELSEIDLSLSSLDNIERSLsLIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd17655 403 IELGEIEARLLQHPDIKEAV-VIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481
|
....*....
gi 1725075560 1799 DIRRLPAPE 1807
Cdd:cd17655 482 DRKALPEPD 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
873-1896 |
2.77e-112 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 390.17 E-value: 2.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTP----- 947
Cdd:PRK10252 7 HLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTfplpe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 948 -IRLADHwvDGQTLSAEKWVRQLCATPFDIT-ARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELd 1025
Cdd:PRK10252 87 iIDLRTQ--PDPHAAAQALMQADLQQDLRVDsGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1026 dHHGLDAPQ----PQIQTIDIVNSGIASPAPA-DVAYWQQQLQDcreLDFPLD-KPRPLMPTHAGERIH-YQLQPDVAGL 1098
Cdd:PRK10252 164 -LRGEPTPAspftPFADVVEEYQRYRASEAWQrDAAFWAEQRRQ---LPPPASlSPAPLPGRSASADILrLKLEFTDGAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1099 LASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMET 1178
Cdd:PRK10252 240 RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1179 CIGAYQHQQLSFDRILHqiEYERMSNKNPLFQIMAILQnagdVCQQNLR----DCTLHRLplSSGfSMFDMTWNFSV-EQ 1253
Cdd:PRK10252 320 LKKMRRHQRYDAEQIVR--DSGRAAGDEPLFGPVLNIK----VFDYQLDfpgvQAQTHTL--ATG-PVNDLELALFPdEH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1254 DAVTIELDYASELFYPASmqmlLDNYQQTLRQLLTLPANTAQLAL---NPLCEREQQWLQQLAVNADAGSRDSLLMHIGR 1330
Cdd:PRK10252 391 GGLSIEILANPQRYDEAT----LIAHAERLKALIAQFAADPALLCgdvDILLPGEYAQLAQVNATAVEIPETTLSALVAQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1331 LAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPF-SVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADR 1409
Cdd:PRK10252 467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGdSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1410 VSYMIENAQARLLVT-DGEPEQGWASPAVGFDSLVSHPAAADA--LPIPADDTLAYIMYTSGSTGNPKGVMITHGNLnnf 1486
Cdd:PRK10252 547 LKMMLEDARPSLLITtADQLPRFADVPDLTSLCYNAPLAPQGAapLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI--- 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 tndfVGRL-------ALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQ-------PSV 1552
Cdd:PRK10252 624 ----VNRLlwmqnhyPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGvttthfvPSM 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1553 IQA---TPTVWSTivhHLPAASQRplTVLCGGEKMPAALLTQL-RRIATRVLQVYGPTET----TIWSTCAD--LTHEGA 1622
Cdd:PRK10252 700 LAAfvaSLTPEGA---RQSCASLR--QVFCSGEALPADLCREWqQLTGAPLHNLYGPTEAavdvSWYPAFGEelAAVRGS 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1623 SDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQL 1702
Cdd:PRK10252 775 SVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGER-MYRTGDVARWLDDGAV 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1703 EYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQA-------RIVSYLQLTSGEELNEKAVRTALKARL 1775
Cdd:PRK10252 854 EYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAatggdarQLVGYLVSQSGLPLDTSALQAQLRERL 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1776 PNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPETrysASEADYTPAANEAESAMQHIWQQVLSQTQISVCDSFFSLGGNSL 1855
Cdd:PRK10252 934 PPHMVPVVLLQLDQLPLSANGKLDRKALPLPEL---KAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSL 1010
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1725075560 1856 QIPQLLHAIRQQMGVSLTIREFIMHSQIRELTALALSKTAE 1896
Cdd:PRK10252 1011 LAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDE 1051
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
313-770 |
7.70e-110 |
|
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: 358.22 E-value: 7.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd17649 9 GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSPlhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd17649 89 LTHHP------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREM-------WPGLRTMI 545
Cdd:cd17649 139 LQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEAdrtgdgrPPSLRLYI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVA-WWAERTRLCNGYGPTEASIATSLCEYRPG-------VPwncIGKPLKNYRCHILDLHHNPLPVGFEG 617
Cdd:cd17649 219 FGGEALSPELLRrWLKAPVRLFNAYGPTEATVTPLVWKCEAGaaragasMP---IGRPLGGRSAYILDADLNPVPVGVTG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 618 ELCIAGSGLAHGYLHQEALSAEKFIicRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVR 697
Cdd:cd17649 296 ELYIGGEGLARGYLGRPELTAERFV--PDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 698 SHPLVESACVVARSQPSGKILAAFVQPASPE---LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17649 374 EHPGVREAAVVALDGAGGKQLVAYVVLRAAAaqpELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1336-1804 |
2.95e-108 |
|
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: 353.60 E-value: 2.95e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPeVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTdgepeqgwaspavgfdslvSHPaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL 1494
Cdd:cd17649 81 EDSGAGLLLT-------------------HHP-----------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1495 ALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQR- 1573
Cdd:cd17649 131 GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGr 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1574 --PLTVLC-GGEKMPAALLTQLRRIATRVLQVYGPTETTI----WSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLP 1646
Cdd:cd17649 211 ppSLRLYIfGGEALSPELLRRWLKAPVRLFNAYGPTEATVtplvWKCEAGAARAGASMPIGRPLGGRSAYILDADLNPVP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1647 SGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDL 1726
Cdd:cd17649 291 VGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1727 SLSSLDNIERSLSLIVGEGQQARIVSYLQLTSGEELNE--KAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLP 1804
Cdd:cd17649 371 ALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1336-1803 |
8.20e-108 |
|
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: 353.89 E-value: 8.20e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPeDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDgEPEQGWASPAVGFDSLV----SHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDF 1490
Cdd:cd17646 92 ADAGPAVVLTT-ADLAARLPAGGDVALLGdealAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1491 VGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVhHLPAA 1570
Cdd:cd17646 171 QDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFL-AEPAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1571 SQRPL--TVLCGGEKMPAALLTQLRRIATRVL-QVYGPTETTI---WSTCADlTHEGASDCIGTPIQATEVLVMDQAGNP 1644
Cdd:cd17646 250 GSCASlrRVFCSGEALPPELAARFLALPGAELhNLYGPTEAAIdvtHWPVRG-PAETPSVPIGRPVPNTRLYVLDDALRP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1645 LPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEI 1724
Cdd:cd17646 329 VPVGVPGELYLGGVQLARGYLGRPALTAERFV-PDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1725 DLSLSSLDNIERSLSLIVGEGQQA-RIVSYLQLTSGEE-LNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRR 1802
Cdd:cd17646 408 EAALAAHPAVTHAVVVARAAPAGAaRLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAA 487
|
.
gi 1725075560 1803 L 1803
Cdd:cd17646 488 L 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
189-1075 |
7.36e-107 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 382.77 E-value: 7.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 189 HTVPVADITSPAQLQHFffnETGALK-QGRYAQPRVMVDVAACGDGTQLTL-YGDDMrFNAFT---------DYLDALLA 257
Cdd:PRK12316 401 HQPLVADIEALDTVAGL---EFGQLEwKSRTTQFDLTLDTYEKGGRLHAALtYATDL-FEARTvermarhwqNLLRGMVE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 258 DPADPIAA-PIVTQPHTLHRLSQFNATDDAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEIDRASDQFACWLLEH 336
Cdd:PRK12316 477 NPQARVDElPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIER 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 337 SGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSPLHSGDAPCIAPSSIDYRS- 415
Cdd:PRK12316 557 GVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRp 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 416 ---LNIHAEQLPQSR---DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYG 489
Cdd:PRK12316 637 aawLEGYSEENPGTElnpENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFW 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 490 ALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWP----GLRTMIVMGDAPPADVV-AWWAER-- 562
Cdd:PRK12316 717 PLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVasctSLRRIVCSGEALPADAQeQVFAKLpq 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 563 TRLCNGYGPTEASIA----TSLCEYRPGVPwncIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSA 638
Cdd:PRK12316 797 AGLYNLYGPTEAAIDvthwTCVEEGGDSVP---IGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTA 873
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 639 EKFIICrlPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARsqpSGKIL 718
Cdd:PRK12316 874 ERFVPS--PF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQL 947
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 719 AAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDERNERLTPPETETEAILERIV 797
Cdd:PRK12316 948 VGYVVLESEGgDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIW 1027
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 798 ANAIGCPQADVTQEFINLGAHSLTMSKIVALvARDLCCHLSIADLFRHNTVRKLAEYIENKAVAAERAIAICDEhrAPLS 877
Cdd:PRK12316 1028 QDVLGVERVGLDDNFFELGGDSIVSIQVVSR-ARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGE--VALA 1104
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 878 PQQNllWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDG---VAYQLAEPHTPIrladhW 954
Cdd:PRK12316 1105 PVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGgwqQAYAAPQAGEVL-----W 1177
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 955 VDgQTLSAEKwVRQLC---ATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDhhGLD 1031
Cdd:PRK12316 1178 QR-QAASEEE-LLALCeeaQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDA--DLP 1253
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1725075560 1032 APQPQIQTIDIVNSGIASPAPADVAYWQQQLQDCRElDFPLDKP 1075
Cdd:PRK12316 1254 ARTSSYQAWARRLHEHAGARAEELDYWQAQLEDAPH-ELPCENP 1296
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1332-1803 |
2.82e-106 |
|
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: 347.77 E-value: 2.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:cd12115 9 AARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESrVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLVTDGepeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDF 1490
Cdd:cd12115 89 RFILEDAQARLVLTDP-------------------------------DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1491 VGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCprETAMDpvkLYHFIERQQPSVIQATPTVWSTIVHH--LP 1568
Cdd:cd12115 138 AAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA--DNVLA---LPDLPAAAEVTLINTVPSAAAELLRHdaLP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1569 AASQrplTVLCGGEKMPAALLTQLRRI--ATRVLQVYGPTETTIWSTCADLTHEGASD-CIGTPIQATEVLVMDQAGNPL 1645
Cdd:cd12115 213 ASVR---VVNLAGEPLPRDLVQRLYARlqVERVVNLYGPSEDTTYSTVAPVPPGASGEvSIGRPLANTQAYVLDRALQPV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1646 PSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRrQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEID 1725
Cdd:cd12115 290 PLGVPGELYIGGAGVARGYLGRPGLTAERFLP-DPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1726 LSLSSLDNIERslSLIVGEGQQA---RIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRR 1802
Cdd:cd12115 369 AALRSIPGVRE--AVVVAIGDAAgerRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSA 446
|
.
gi 1725075560 1803 L 1803
Cdd:cd12115 447 L 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
216-1287 |
4.19e-106 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 380.07 E-value: 4.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 216 GRYAQPRVMVDVAACGDGTQLTLYGDDMRFNAFT---------DYLDALLADPADPIAA-PIVTQPHTLHRLSQFNATDD 285
Cdd:PRK12316 2972 GAATQFDLALDTWESAEGLGASLTYATDLFDARTverlarhwqNLLRGMVENPQRSVDElAMLDAEERGQLLEAWNATAA 3051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 286 AELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSN 365
Cdd:PRK12316 3052 EYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAG 3131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 366 KTYVLLDPQAPAARNQSILDDVQPALILADSPLHSGDAP-----CIAPSSIDYRSLNIHAEQLPQSrdaLAYVCYTSGTT 440
Cdd:PRK12316 3132 GAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQgvqvlDLDRGDENYAEANPAIRTMPEN---LAYVIYTSGST 3208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 441 GKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDI 520
Cdd:PRK12316 3209 GKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGV 3288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 521 GHITITPAILELLPREMWP----GLRTMIVMGDAPPADVVAWWAERTRLCNGYGPTEASI-ATSLCEYRPGVPWNCIGKP 595
Cdd:PRK12316 3289 DVLHAYPSMLQAFLEEEDAhrctSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATItVTHWQCVEEGKDAVPIGRP 3368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 596 LKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicRLPYmAAEERLYRTGDIAKWDEQGNIIFVGR 675
Cdd:PRK12316 3369 IANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFV--PDPF-VPGERLYRTGDLARYRADGVIEYIGR 3445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 676 RDHQVKIRGVRIEMGEVESAVRSHPLVESACVVArsqPSGKILAAFVQPASPELTI-DALRHALVTLLHPAAIPSVFIFL 754
Cdd:PRK12316 3446 VDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA---VDGRQLVAYVVPEDEAGDLrEALKAHLKASLPEYMVPAHLLFL 3522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 755 PALPLTINGKIARQQLEKWPLDERNERLTPPETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALvARDLC 834
Cdd:PRK12316 3523 ERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSR-ARQAG 3601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 835 CHLSIADLFRHNTVRKLAEYIENKAVAAERAIAICDEhrAPLSPQQNLLWYLSAlnPDDCSYNLPLAIDIQGPLDLGRFE 914
Cdd:PRK12316 3602 IRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGE--TLLLPIQQQFFEEPV--PERHHWNQSLLLKPREALDAAALE 3677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 915 QAINFIYEKHESLRTRFTETDG---VAYQLAEPHTPIRLADHWVDGQTLSAekwVRQLCATPFDITARPPLVLRLVQYHQ 991
Cdd:PRK12316 3678 AALQALVEHHDALRLRFVEDAGgwtAEHLPVELGGALLWRAELDDAEELER---LGEEAQRSLDLADGPLLRALLATLAD 3754
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 992 QHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDHHGLDAPQPQIQTIDI---VNSGIASPA-PADVAYWQQQLQDCRE 1067
Cdd:PRK12316 3755 GSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWaerLQEHARGEAlKAELAYWQEQLQGVSS 3834
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1068 lDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRGKALGATPFA-LLCAALSLLLSRYTQQQDIVIGTAIAARDNL--- 1143
Cdd:PRK12316 3835 -ELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNdLLLTALARVVCRWTGEASALVQLEGHGREDLfad 3913
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1144 -DQTQVSGFHVNTVPLRiqLSEQDTLAGLIGNMMETcIGAYQHQQLSFD--RILHQIEYERMSNKNPLFQI--------- 1211
Cdd:PRK12316 3914 iDLSRTVGWFTSLFPVR--LSPVEDLGASIKAIKEQ-LRAIPNKGIGFGllRYLGDEESRRTLAGLPVPRItfnylgqfd 3990
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1212 ------MAILQNAGDVCQQNLRDCTLHRLPLSSGFSMFD----MTWNFSveqdavtieldyaSELFYPASMQMLLDNYQQ 1281
Cdd:PRK12316 3991 gsfdeeMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGgelsLDWTFS-------------REMFEEATIQRLADDYAA 4057
|
....*.
gi 1725075560 1282 TLRQLL 1287
Cdd:PRK12316 4058 ELTALV 4063
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1336-1799 |
4.29e-106 |
|
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: 347.37 E-value: 4.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDrVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGepeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLnnfTNDFVGR- 1493
Cdd:cd17643 81 ADSGPSLLLTDP-------------------------------DDLAYVIYTSGSTGRPKGVVVSHANV---LALFAATq 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1494 --LALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWStivhHLPAAS 1571
Cdd:cd17643 127 rwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFY----QLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1572 QRPLT-------VLCGGEKMPAALLTQLRR----IATRVLQVYGPTETTIWST-----CADLTHEGASDcIGTPIQATEV 1635
Cdd:cd17643 203 DRDGRdplalryVIFGGEALEAAMLRPWAGrfglDRPQLVNMYGITETTVHVTfrpldAADLPAAAASP-IGRPLPGLRV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1636 LVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIR 1715
Cdd:cd17643 282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1716 GHRIELSEIDLSLSSLDNIeRSLSLIVGEGQQ--ARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLT 1793
Cdd:cd17643 362 GFRIELGEIEAALATHPSV-RDAAVIVREDEPgdTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
....*.
gi 1725075560 1794 NNNKID 1799
Cdd:cd17643 441 VNGKLD 446
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1336-1804 |
1.01e-105 |
|
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: 345.78 E-value: 1.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERlVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGepeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL 1494
Cdd:cd17652 81 ADARPALLLTTP-------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1495 ALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTivhhLPAASQRP 1574
Cdd:cd17652 130 DVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA----LPPDDLPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1575 L-TVLCGGEKMPAALltqLRRIAT--RVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFG 1651
Cdd:cd17652 206 LrTLVVAGEACPAEL---VDRWAPgrRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1652 ELWLGGAGVSPGYWRNPTLSDKVFLrRQAFGA--ERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLS 1729
Cdd:cd17652 283 ELYIAGAGLARGYLNRPGLTAERFV-ADPFGApgSR-MYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALT 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 1730 SLDNIERSLSLIVGEGQ-QARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLP 1804
Cdd:cd17652 361 EHPGVAEAVVVVRDDRPgDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
310-770 |
6.99e-105 |
|
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: 345.03 E-value: 6.99e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFAcWLLEHSGAASS-VVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQ 388
Cdd:cd12114 6 VICGDGTLTYGELAERARRVA-GALKAAGVRPGdLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 389 PALILADSPLHSGDAPCIAPSSIDYRSLNIHAEQLPQSR--DALAYVCYTSGTTGKPKGVMIGREGLSNVAQ--NHRdfI 464
Cdd:cd12114 85 ARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVapDDLAYVIFTSGSTGTPKGVMISHRAALNTILdiNRR--F 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 465 GLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELL------PREMW 538
Cdd:cd12114 163 AVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLldvleaAQALL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 539 PGLRTMIVMGDAPPADVVAWWAERTRLCN----GyGPTEASIATSLCEYRPGVP-WNCI--GKPLKNYRCHILDLHHNPL 611
Cdd:cd12114 243 PSLRLVLLSGDWIPLDLPARLRALAPDARlislG-GATEASIWSIYHPIDEVPPdWRSIpyGRPLANQRYRVLDPRGRDC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 612 PVGFEGELCIAGSGLAHGYLHQEALSAEKFIICRLPymaaeERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGE 691
Cdd:cd12114 322 PDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDG-----ERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 692 VESAVRSHPLVESACVVARSQPSGKILAAFVQPASPELTI--DALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQ 769
Cdd:cd12114 397 IEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIapDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAA 476
|
.
gi 1725075560 770 L 770
Cdd:cd12114 477 L 477
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1336-1803 |
3.52e-103 |
|
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: 340.02 E-value: 3.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDlVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGEPEQGWASPA-VGFDSLVSHPAAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVG 1492
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFdVLILDLDALAAPAPPPPVDVApDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1493 RLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQ 1572
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1573 RPLT---VLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTCADLTH---EGASDCIGTPIQATEVLVMDQAGNP 1644
Cdd:cd12114 241 LLPSlrlVLLSGDWIPLDLPARLRALApdARLISLGGATEASIWSIYHPIDEvppDWRSIPYGRPLANQRYRVLDPRGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1645 LPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQafgAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEI 1724
Cdd:cd12114 321 CPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1725 DLSLSSLDNIERSLSLIVGEGQQARIVSYLQLTS-GEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd12114 398 EAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNdGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1332-1803 |
7.67e-103 |
|
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: 338.07 E-value: 7.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDpVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLVTDGepeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDF 1490
Cdd:cd05945 81 REILDAAKPALLIADG-------------------------------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1491 VGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVW-------STI 1563
Cdd:cd05945 130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAamcllspTFT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1564 VHHLPAASqrplTVLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTCADLTHEGASDC----IGTPIQATEVLV 1637
Cdd:cd05945 210 PESLPSLR----HFLFCGEVLPHKTARALQQRFpdARIYNTYGPTEATVAVTYIEVTPEVLDGYdrlpIGYAKPGAKLVI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1638 MDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAerymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGH 1717
Cdd:cd05945 286 LDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA----YRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1718 RIELSEIDLSLSSLDNIERSLSLIVGEGQQA-RIVSYLQLTSGEE-LNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNN 1795
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVtELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYLDELPLNAN 441
|
....*...
gi 1725075560 1796 NKIDIRRL 1803
Cdd:cd05945 442 GKIDRKAL 449
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1336-1803 |
8.15e-100 |
|
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: 329.43 E-value: 8.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSvVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDgepeqgwaspavgfdslvshpaaadalpiPADdtLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL 1494
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------------PED--LAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1495 ALSARD-KVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQR 1573
Cdd:cd17650 130 ELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1574 P--LTVLCGGEKMPAAL--LTQLRRI--ATRVLQVYGPTETTIWSTCADLTHEGASDC----IGTPIQATEVLVMDQAGN 1643
Cdd:cd17650 210 LsaMRLLIVGSDGCKAQdfKTLAARFgqGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1644 PLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRrQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSE 1723
Cdd:cd17650 290 PQPVGVAGELYIGGAGVARGYLNRPELTAERFVE-NPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1724 IDLSLSSLDNIeRSLSLIVGE--GQQARIVSYlqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIR 1801
Cdd:cd17650 369 IESQLARHPAI-DEAVVAVREdkGGEARLCAY--VVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
..
gi 1725075560 1802 RL 1803
Cdd:cd17650 446 AL 447
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
310-770 |
1.73e-99 |
|
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: 328.50 E-value: 1.73e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:cd17643 6 VVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIgreglsnvaqNHRDFIGL--A 467
Cdd:cd17643 86 SLLLTDP-------------------------------DDLAYVIYTSGSTGRPKGVVV----------SHANVLALfaA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 468 QGS--------RVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITP-AILELLPREMW 538
Cdd:cd17643 125 TQRwfgfneddVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPsAFYQLVEAADR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 539 PG-----LRTMIVMGDAPPADVVAWWAER-----TRLCNGYGPTEASIATS----LCEYRPGVPWNCIGKPLKNYRCHIL 604
Cdd:cd17643 205 DGrdplaLRYVIFGGEALEAAMLRPWAGRfgldrPQLVNMYGITETTVHVTfrplDAADLPAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 605 DLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRG 684
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFV--ANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 685 VRIEMGEVESAVRSHPLVESACVVAR-SQPSGKILAAFVQP-ASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTIN 762
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVIVReDEPGDTRLVAYVVAdDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVN 442
|
....*...
gi 1725075560 763 GKIARQQL 770
Cdd:cd17643 443 GKLDRAAL 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
248-863 |
6.67e-98 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 353.88 E-value: 6.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 248 FTDYLDALLADPADPIAA-PIVTQPHTLHRLSQFNATDDAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEIDRAS 326
Cdd:PRK12316 4507 LTNLLEAMAEDPQRRLGElQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRA 4586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 327 DQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADS------PLHS 400
Cdd:PRK12316 4587 NRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQShllqrlPIPD 4666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 401 GDAPCIAPSSIDYRSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGF 480
Cdd:PRK12316 4667 GLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSF 4746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 481 DAFGWDVYGALVSGATLYLAPSELHtDVGALHDYLTQHDIGHITITPAILELL----PREMWPG-LRTMIVMGDA-PPAD 554
Cdd:PRK12316 4747 DGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLaehaERDGEPPsLRVYCFGGEAvAQAS 4825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 555 VVAWW--AERTRLCNGYGPTEASIATSLCEYRPGVPWNC----IGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAH 628
Cdd:PRK12316 4826 YDLAWraLKPVYLFNGYGPTETTVTVLLWKARDGDACGAaympIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVAR 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 629 GYLHQEALSAEKFIICrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVV 708
Cdd:PRK12316 4906 GYLERPALTAERFVPD--PFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 709 ARSQPSGKILAAFVQPASPELT---------IDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDERN 779
Cdd:PRK12316 4984 AQEGAVGKQLVGYVVPQDPALAdadeaqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQ 5063
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 780 ERLTPPETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTvrkLAEYIENKA 859
Cdd:PRK12316 5064 QAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPT---LAAFVELAA 5140
|
....
gi 1725075560 860 VAAE 863
Cdd:PRK12316 5141 AAGS 5144
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1332-1803 |
8.45e-98 |
|
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: 324.88 E-value: 8.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:cd05918 9 ARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVfVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLvtdgepeqgwaspavgfdsLVSHPaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDF 1490
Cdd:cd05918 89 QEILQDTGAKVV-------------------LTSSP-----------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1491 VGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAhvTLC--PRETAMDpvKLYHFIERQQPSVIQATPTVwstivhhlp 1568
Cdd:cd05918 139 GRALGLTSESRVLQFASYTFDVSILEIFTTLAAGG--CLCipSEEDRLN--DLAGFINRLRVTWAFLTPSV--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1569 AASQRP-----LTVLC-GGEKMPAALLTQ-LRRIatRVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATeVLVMDQA 1641
Cdd:cd05918 206 ARLLDPedvpsLRTLVlGGEALTQSDVDTwADRV--RLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1642 GN--PLPSGAFGELWLGGAGVSPGYWRNPTLSDKVF------LRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVK 1713
Cdd:cd05918 283 NHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpawLKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1714 IRGHRIELSEID--LSLSSLDNIERSLSLIV--GEGQQARIVSYLQLTSGEELNE-----------------KAVRTALK 1772
Cdd:cd05918 363 IRGQRVELGEIEhhLRQSLPGAKEVVVEVVKpkDGSSSPQLVAFVVLDGSSSGSGdgdslflepsdefralvAELRSKLR 442
|
490 500 510
....*....|....*....|....*....|.
gi 1725075560 1773 ARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05918 443 QRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1330-1814 |
1.20e-97 |
|
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: 323.30 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPAD 1408
Cdd:COG0318 7 RAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDrVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYMIENAQARLLVTdgepeqgwaspavgfdslvshpaaadalpipaddtlAYIMYTSGSTGNPKGVMITHGNLNNFTN 1488
Cdd:COG0318 87 ELAYILEDSGARALVT------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1489 DFVGRLALSARDKVLSLTSISFDiFGL--ELFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQATPTVWSTIVHH 1566
Cdd:COG0318 131 AIAAALGLTPGDVVLVALPLFHV-FGLtvGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPTMLARLLRH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1567 lPAASQRPL----TVLCGGEKMPAALLTQLRRIA-TRVLQVYGPTETTIWSTCADLTHEGA-SDCIGTPIQATEVLVMDQ 1640
Cdd:COG0318 207 -PEFARYDLsslrLVVSGGAPLPPELLERFEERFgVRIVEGYGLTETSPVVTVNPEDPGERrPGSVGRPLPGVEVRIVDE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1641 AGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIE 1720
Cdd:COG0318 286 DGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------RDGW-LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1721 LSEIDLSLSSLDNIERslSLIVG---EGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNK 1797
Cdd:COG0318 358 PAEVEEVLAAHPGVAE--AAVVGvpdEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGK 435
|
490
....*....|....*..
gi 1725075560 1798 IDIRRLPAPETRYSASE 1814
Cdd:COG0318 436 IDRRALRERYAAGALEA 452
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1336-1804 |
1.32e-97 |
|
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: 323.62 E-value: 1.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17644 14 PDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESlVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGEpeqgwaspavgfdslvshpaaadalpipaddTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL 1494
Cdd:cd17644 94 EDAQISVLLTQPE-------------------------------NLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1495 ALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVW----STIVHHLPAA 1570
Cdd:cd17644 143 GITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWhllvLELLLSTIDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1571 SQRPLTVLCGGEKMPAALLTQLRRIAT---RVLQVYGPTETTIWSTCADLTHEGASDC----IGTPIQATEVLVMDQAGN 1643
Cdd:cd17644 223 PSSLRLVIVGGEAVQPELVRQWQKNVGnfiQLINVYGPTEATIAATVCRLTQLTERNItsvpIGRPIANTQVYILDENLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1644 PLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrRQAFGAERY--MYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIEL 1721
Cdd:cd17644 303 PVPVGVPGELHIGGVGLARGYLNRPELTAEKFI-SHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIEL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1722 SEIDLSLSSLDNIERSLsLIVGEGQ--QARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKID 1799
Cdd:cd17644 382 GEIEAVLSQHNDVKTAV-VIVREDQpgNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKID 460
|
....*
gi 1725075560 1800 IRRLP 1804
Cdd:cd17644 461 RRALP 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1336-1804 |
2.32e-97 |
|
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: 322.43 E-value: 2.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAH-----ALLRIDSRpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHyllsvAEIRPDDL---VGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLVTDgepeqgwaspavgfdslvshpaaadalpiPADdtLAYIMYTSGSTGNPKGVMITHGNLNNFTNDF 1490
Cdd:cd17648 78 QFILEDTGARVVITN-----------------------------STD--LAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1491 VGRLALSARD--KVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVwstiVHHLP 1568
Cdd:cd17648 127 SERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSV----LQQYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1569 AASQRPLT-VLCGGEKMPAALLTQLR-RIATRVLQVYGPTETTIWSTCAD-LTHEGASDCIGTPIQATEVLVMDQAGNPL 1645
Cdd:cd17648 203 LARLPHLKrVDAAGEEFTAPVFEKLRsRFAGLIINAYGPTETTVTNHKRFfPGDQRFDKSLGRPVRNTKCYVLNDAMKRV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1646 PSGAFGELWLGGAGVSPGYWRNPTLSDKVFL-------RRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHR 1718
Cdd:cd17648 283 PVGAVGELYLGGDGVARGYLNRPELTAERFLpnpfqteQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1719 IELSEIDLSLSSLDNIERSLSL------IVGEGQQARIVSYLqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPL 1792
Cdd:cd17648 363 IEPGEVEAALASYPGVRECAVVakedasQAQSRIQKYLVGYY-LPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPV 441
|
490
....*....|..
gi 1725075560 1793 TNNNKIDIRRLP 1804
Cdd:cd17648 442 TINGKLDVRALP 453
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
313-770 |
9.73e-97 |
|
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: 320.57 E-value: 9.73e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLA-QGSR 471
Cdd:cd17650 89 LTQP-------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDsFPVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 472 VLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMW------PGLRTMI 545
Cdd:cd17650 138 LLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYrngldlSAMRLLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVAWWAER----TRLCNGYGPTEASIATSLCEYRPG-------VPwncIGKPLKNYRCHILDLHHNPLPVG 614
Cdd:cd17650 218 VGSDGCKAQDFKTLAARfgqgMRIINSYGVTEATIDSTYYEEGRDplgdsanVP---IGRPLPNTAMYVLDERLQPQPVG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 615 FEGELCIAGSGLAHGYLHQEALSAEKFIicRLPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVES 694
Cdd:cd17650 295 VAGELYIGGAGVARGYLNRPELTAERFV--ENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIES 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 695 AVRSHPLVESACVVARSQPSG-KILAAFVQPASpELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17650 372 QLARHPAIDEAVVAVREDKGGeARLCAYVVAAA-TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
248-868 |
5.14e-95 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 344.45 E-value: 5.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 248 FTDYLDALLADPADPIAAPIVTQPHTLHRLSQ-FNATDDAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEIDRAS 326
Cdd:PRK12467 3051 FDRLLQAMLNNPAARLGELPTLAAHERRQVLHaWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRA 3130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 327 DQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADS------PLHS 400
Cdd:PRK12467 3131 NRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAhlleqlPAPA 3210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 401 GDAPCIapssIDYRSLNIHAEQLPQSR---DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIAS 477
Cdd:PRK12467 3211 GDTALT----LDRLDLNGYSENNPSTRvmgENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS 3286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 478 LGFDAFGWDVYGALVSGATLYLAPSElHTDVGALHDYLTQHDIGHITITPAILELL-----PREMWPgLRTMIVMGDAPP 552
Cdd:PRK12467 3287 FSFDGAQERFLWTLICGGCLVVRDND-LWDPEELWQAIHAHRISIACFPPAYLQQFaedagGADCAS-LDIYVFGGEAVP 3364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 553 ADVVAWW---AERTRLCNGYGPTEASIATSL----CEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSG 625
Cdd:PRK12467 3365 PAAFEQVkrkLKPRGLTNGYGPTEAVVTVTLwkcgGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVG 3444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 626 LAHGYLHQEALSAEKFIICrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESA 705
Cdd:PRK12467 3445 LARGYHQRPSLTAERFVAD--PFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREA 3522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 706 CVVARSQPSGKILAAFVQPASPELTI-DALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKwPLDERNERLTP 784
Cdd:PRK12467 3523 VVLARDGAGGKQLVAYVVPADPQGDWrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPD-PDAKGSREYVA 3601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 785 PETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYIENKAVAAER 864
Cdd:PRK12467 3602 PRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGDVPVNL 3681
|
....
gi 1725075560 865 AIAI 868
Cdd:PRK12467 3682 LLDL 3685
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1332-1715 |
1.89e-94 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 312.71 E-value: 1.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSC-ERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADR 1409
Cdd:pfam00501 5 AARTPDKTALEVgEGRRLTYRELDERANRLAAGLRALGVGKGDrVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1410 VSYMIENAQARLLVTDGEPEQGWASPAVGFDSLVSHPAAADALPIPAD----------------------DTLAYIMYTS 1467
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEeplpeeakpadvppppppppdpDDLAYIIYTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1468 GSTGNPKGVMITHGNLNNFTNDFVG----RLALSARDKVLSLTSISFDI-FGLELFCSLAGGAHVTLCPRETAMDPVKLY 1542
Cdd:pfam00501 165 GTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDPAALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1543 HFIERQQPSVIQATPTVWSTIVHHLPAASQRPL---TVLCGGEKMPAALLTQLRRI-ATRVLQVYGPTETTIWSTCADL- 1617
Cdd:pfam00501 245 ELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSslrLVLSGGAPLPPELARRFRELfGGALVNGYGLTETTGVVTTPLPl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1618 -THEGASDCIGTPIQATEVLVMDQA-GNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrrqafgAERyMYRTGDIVR 1695
Cdd:pfam00501 325 dEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD------EDG-WYRTGDLGR 397
|
410 420
....*....|....*....|
gi 1725075560 1696 FNRQGQLEYLGRNDHQVKIR 1715
Cdd:pfam00501 398 RDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
310-781 |
6.25e-93 |
|
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: 309.43 E-value: 6.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:COG0318 18 LVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILAdsplhsgdapciapssidyrslnihaeqlpqsrdalAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQG 469
Cdd:COG0318 98 RALVT------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 470 SRVLAIASLGFD-AFGWDVYGALVSGATLYLAPselHTDVGALHDYLTQHDIGHITITPAILELL------PREMWPGLR 542
Cdd:COG0318 142 DVVLVALPLFHVfGLTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVPTMLARLlrhpefARYDLSSLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 543 TMIVMGDAPPADVVAWWAERT--RLCNGYGPTEASIATSLC-EYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGEL 619
Cdd:COG0318 219 LVVSGGAPLPPELLERFEERFgvRIVEGYGLTETSPVVTVNpEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 620 CIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSH 699
Cdd:COG0318 299 VVRGPNVMKGYWNDPEATAEAF----------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 700 PLVESACVVARSQP-SGKILAAFVQPAS-PELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDE 777
Cdd:COG0318 369 PGVAEAAVVGVPDEkWGERVVAFVVLRPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
....
gi 1725075560 778 RNER 781
Cdd:COG0318 449 ALEA 452
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1327-1803 |
1.21e-92 |
|
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: 308.08 E-value: 1.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1327 HIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHY 1405
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDvVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1406 PADRVSYMIENAQARLLVTDgepeqgwaspavgfdslvshpaaadalpiPADDTLAYIMYTSGSTGNPKGVMITHGNLNN 1485
Cdd:cd17653 82 PSARIQAILRTSGATLLLTT-----------------------------DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1486 FTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAhvTLCPReTAMDPvkLYHFIerQQPSVIQATPTVWSTivh 1565
Cdd:cd17653 133 YVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG--TLVLA-DPSDP--FAHVA--RTVDALMSTPSILST--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1566 hLPAASQRPL-TVLCGGEKMPAALLTQ--LRRiatRVLQVYGPTETTIWSTCADLTHEGASdCIGTPIQATEVLVMDQAG 1642
Cdd:cd17653 203 -LSPQDFPNLkTIFLGGEAVPPSLLDRwsPGR---RLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTCYILDADL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1643 NPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELS 1722
Cdd:cd17653 278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSR-MYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1723 EIDLSLSSLDNIERSLSLIVGEGqqaRIVSYLqltSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRR 1802
Cdd:cd17653 357 EIEEVVLQSQPEVTQAAAIVVNG---RLVAFV---TPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKA 430
|
.
gi 1725075560 1803 L 1803
Cdd:cd17653 431 L 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
313-770 |
2.27e-92 |
|
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: 308.02 E-value: 2.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd05945 13 GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSN-VAQNHRDFIgLAQGSR 471
Cdd:cd05945 93 IADG-------------------------------DDNAYIIFTSGSTGRPKGVQISHDNLVSfTNWMLSDFP-LGPGDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 472 VLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPR------EMWPGLRTMI 545
Cdd:cd05945 141 FLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLsptftpESLPSLRHFL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVAWWAER---TRLCNGYGPTEASIATSLCEYRPGVPWNC----IGKPLKNYRCHILDLHHNPLPVGFEGE 618
Cdd:cd05945 221 FCGEVLPHKTARALQQRfpdARIYNTYGPTEATVAVTYIEVTPEVLDGYdrlpIGYAKPGAKLVILDEDGRPVPPGEKGE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 619 LCIAGSGLAHGYLHQEALSAEKFiicrlpYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRS 698
Cdd:cd05945 301 LVISGPSVSKGYLNNPEKTAAAF------FPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQ 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 699 HPLVESACVVARSQPSGKI-LAAFV--QPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05945 375 VPGVKEAVVVPKYKGEKVTeLIAFVvpKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
244-856 |
3.33e-92 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 329.31 E-value: 3.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 244 RFNAFtdyLDALLADPADPIA-APIVTqPHTLHRLSQFNATDdAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEI 322
Cdd:PRK10252 415 RLKAL---IAQFAADPALLCGdVDILL-PGEYAQLAQVNATA-VEIPETTLSALVAQQAAKTPDAPALADARYQFSYREM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 323 DRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSPLHS-- 400
Cdd:PRK10252 490 REQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPrf 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 401 GDAPCIAPSSIDYRSLNIHAEQLPQSR-DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLG 479
Cdd:PRK10252 570 ADVPDLTSLCYNAPLAPQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCS 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 480 FDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAIL-----ELLPR---EMWPGLRTMIVMGDAP 551
Cdd:PRK10252 650 FDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLaafvaSLTPEgarQSCASLRQVFCSGEAL 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 552 PADVVAWWAERT--RLCNGYGPTEASIATSlceYRPG------------VPwncIGKPLKNYRCHILDLHHNPLPVGFEG 617
Cdd:PRK10252 730 PADLCREWQQLTgaPLHNLYGPTEAAVDVS---WYPAfgeelaavrgssVP---IGYPVWNTGLRILDARMRPVPPGVAG 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 618 ELCIAGSGLAHGYLHQEALSAEKFIicRLPYMAAEeRLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVR 697
Cdd:PRK10252 804 DLYLTGIQLAQGYLGRPDLTASRFI--ADPFAPGE-RMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQ 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 698 SHPLVES----ACVVARSQPSG---KILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQ 769
Cdd:PRK10252 881 ALPDVEQavthACVINQAAATGgdaRQLVGYLVSQSGLpLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKA 960
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 770 LEKWPLDERNERLtPPETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVR 849
Cdd:PRK10252 961 LPLPELKAQVPGR-APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVA 1039
|
....*..
gi 1725075560 850 KLAEYIE 856
Cdd:PRK10252 1040 KLATLLD 1046
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
313-770 |
1.60e-91 |
|
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: 305.90 E-value: 1.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd17644 22 EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADsplhsgdapciapssidyrslnihaeqlPQSrdaLAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd17644 102 LTQ----------------------------PEN---LAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPG-------LRTMI 545
Cdd:cd17644 151 LQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLStidlpssLRLVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVAWWAE----RTRLCNGYGPTEASIATSLCEYRPGVPWNC----IGKPLKNYRCHILDLHHNPLPVGFEG 617
Cdd:cd17644 231 VGGEAVQPELVRQWQKnvgnFIQLINVYGPTEATIAATVCRLTQLTERNItsvpIGRPIANTQVYILDENLQPVPVGVPG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 618 ELCIAGSGLAHGYLHQEALSAEKFIicRLPYMAAE-ERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAV 696
Cdd:cd17644 311 ELHIGGVGLARGYLNRPELTAEKFI--SHPFNSSEsERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 697 RSHPLVESACVVARSQPSG-KILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17644 389 SQHNDVKTAVVIVREDQPGnKRLVAYIVPHYEEsPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
313-770 |
1.15e-90 |
|
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: 302.55 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd17645 20 RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKIL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd17645 100 LTNP-------------------------------DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHdigHITI----TPAILELLPREMwPGLRTMIVMG 548
Cdd:cd17645 149 LVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQE---GITIsflpTGAAEQFMQLDN-QSLRVLLTGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 549 DappadvVAWWAERT--RLCNGYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGL 626
Cdd:cd17645 225 D------KLKKIERKgyKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 627 AHGYLHQEALSAEKFIICrlPYMAAEeRLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESAC 706
Cdd:cd17645 299 ARGYLNRPELTAEKFIVH--PFVPGE-RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 707 VVARSQPSG-KILAAFVQPASpELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17645 376 VLAKEDADGrKYLVAYVTAPE-EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
310-770 |
1.34e-90 |
|
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: 302.70 E-value: 1.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLlEHSGAA-SSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQ 388
Cdd:cd12115 18 LVCGDESLTYAELNRRANRLAARL-RAAGVGpESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 389 PALILADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQ 468
Cdd:cd12115 97 ARLVLTDP-------------------------------DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 469 GSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHtdvgaLHDYLTQHDIGHI-TITPAILELLPREMWP-GLRTMIV 546
Cdd:cd12115 146 LAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLA-----LPDLPAAAEVTLInTVPSAAAELLRHDALPaSVRVVNL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 547 MGDAPPADVVAWWAER---TRLCNGYGPTEASIATSLCEYRPG-VPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIA 622
Cdd:cd12115 221 AGEPLPRDLVQRLYARlqvERVVNLYGPSEDTTYSTVAPVPPGaSGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 623 GSGLAHGYLHQEALSAEKFIICRLpymAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV 702
Cdd:cd12115 301 GAGVARGYLGRPGLTAERFLPDPF---GPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGV 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 703 ESACVVAR-SQPSGKILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd12115 378 REAVVVAIgDAAGERRLVAYIVAEPGAaGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
873-1290 |
3.38e-89 |
|
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: 297.73 E-value: 3.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLAd 952
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 953 hWVDGQTLS-------AEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELD 1025
Cdd:cd19531 80 -VVDLSGLPeaereaeAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1026 DHHGLDAPQPQIQTIDIV---NSGIASPA-PADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLA 1100
Cdd:cd19531 159 AGRPSPLPPLPIQYADYAvwqREWLQGEVlERQLAYWREQLAGAPPvLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1101 SRGKALGATPFallcaalslllsRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCI 1180
Cdd:cd19531 239 ALARREGATLFmtllaafqvllhRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1181 GAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAGDVcQQNLRDCTLHRLPLSSGFSMFDMTWNFSVEQDAVTIEL 1260
Cdd:cd19531 319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAA-ALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSL 397
|
410 420 430
....*....|....*....|....*....|
gi 1725075560 1261 DYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19531 398 EYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1336-1804 |
7.34e-88 |
|
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: 294.46 E-value: 7.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17645 12 PDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDqVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGepeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL 1494
Cdd:cd17645 92 ADSSAKILLTNP-------------------------------DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1495 ALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIErQQPSVIQATPTVWSTIVHHLPAASQRp 1574
Cdd:cd17645 141 GVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFN-QEGITISFLPTGAAEQFMQLDNQSLR- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1575 lTVLCGGEKmpaalLTQLRRIATRVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELW 1654
Cdd:cd17645 219 -VLLTGGDK-----LKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELC 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1655 LGGAGVSPGYWRNPTLSDKVFLRRQAFGAERyMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNI 1734
Cdd:cd17645 293 IAGEGLARGYLNRPELTAEKFIVHPFVPGER-MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLI 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 1735 ERSLSLIV--GEGQQArIVSYlqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLP 1804
Cdd:cd17645 372 ELAAVLAKedADGRKY-LVAY--VTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
875-1888 |
2.57e-87 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 319.42 E-value: 2.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAyQLAEPHTPIRLADHW 954
Cdd:PRK05691 3259 PLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGET-MLQVIHKPGRTPIDY 3337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 955 VDGQTLSAEKWVRQLCA-------TPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDH 1027
Cdd:PRK05691 3338 LDWRGLPEDGQEQRLQAlhkqereAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEG 3417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1028 HGLDAPQPQIQTIDIVNSGIASPAPADvAYWQQQLQDCrELDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRGKALG 1107
Cdd:PRK05691 3418 REAQLPVPPRYRDYIGWLQRQDLAQAR-QWWQDNLRGF-ERPTPIPSDRPFLREHAGDSGGMVVGDCYTRLDAADGARLR 3495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1108 A-------TPFALLCAALSLLLSRYTQQQDIVIGTAIAARD-NLDQTQVS-GFHVNTVPLRIQLSEQDT-------LAGL 1171
Cdd:PRK05691 3496 ElaqahqlTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvSMPQMQRTvGLFINSIALRVQLPAAGQrcsvrqwLQGL 3575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1172 IGNMMETcigaYQHQQLSFDRILHQIEyerMSNKNPLFQIMAILQNAgdvcqqNLRDCTLHRLPLSSGFSMFDMTW-NFS 1250
Cdd:PRK05691 3576 LDSNMEL----REYEYLPLVAIQECSE---LPKGQPLFDSLFVFENA------PVEVSVLDRAQSLNASSDSGRTHtNFP 3642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1251 VEQ-----DAVTIELDYASELFYPASMQMLLDNYQQTLRQLLT-LPANTAQLALnpLCEREQQWLQQLAVNADagsRD-S 1323
Cdd:PRK05691 3643 LTAvcypgDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQgFHGDLSELPL--LGEQERDFLLDGCNRSE---RDyP 3717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1324 LLMHIGRLAHTQ----PDSLAVSCERQQYSYRQLWAQSERVAHALL----RIDSrpfSVGVMMEKSCHVAVLLLGVLRAG 1395
Cdd:PRK05691 3718 LEQSYVRLFEAQvaahPQRIAASCLDQQWSYAELNRAANRLGHALRaagvGVDQ---PVALLAERGLDLLGMIVGSFKAG 3794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1396 KHYVPIDVHYPADRVSYMIENAQARLLV-TDGEPEQGWA----SPAVGFDSL-----VSHPAAADALP--IPADDTLAYI 1463
Cdd:PRK05691 3795 AGYLPLDPGLPAQRLQRIIELSRTPVLVcSAACREQARAlldeLGCANRPRLlvweeVQAGEVASHNPgiYSGPDNLAYV 3874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1464 MYTSGSTGNPKGVMIT-HGNLNNFTNDfVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLY 1542
Cdd:PRK05691 3875 IYTSGSTGLPKGVMVEqRGMLNNQLSK-VPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLL 3953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1543 HFIERQQPSVIQATPTvwstIVHHLPAASQRPLT----VLCGGEKMPAALLTQ--LRRIATRVLQVYGPTEttiwstCAD 1616
Cdd:PRK05691 3954 AHVQAQGITVLESVPS----LIQGMLAEDRQALDglrwMLPTGEAMPPELARQwlQRYPQIGLVNAYGPAE------CSD 4023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1617 ---------LTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRrQAFGA--ER 1685
Cdd:PRK05691 4024 dvaffrvdlASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVP-HPFGApgER 4102
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1686 yMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIeRSLSLIVGEGQQAR-IVSYLQLTSGEELNE 1764
Cdd:PRK05691 4103 -LYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEV-REAAVAVQEGVNGKhLVGYLVPHQTVLAQG 4180
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1765 ---KAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPETRYSASEaDYTPAANEAESAMQHIWQQVLSQTQI 1841
Cdd:PRK05691 4181 allERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQ-AYLAPRNELEQTLATIWADVLKVERV 4259
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 1725075560 1842 SVCDSFFSLGGNSLQIPQLLHAIRQQMGVSLTIREFIMHSQIRELTA 1888
Cdd:PRK05691 4260 GVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAE 4306
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
315-770 |
1.47e-83 |
|
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: 283.60 E-value: 1.47e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL- 393
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ----ADSPLHSGDAPCIAPSSI---DYRSLNIHAEQlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGL 466
Cdd:cd17656 92 qrhlKSKLSFNKSTILLEDPSIsqeDTSNIDYINNS-----DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 467 AQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELL--PREMWP----G 540
Cdd:cd17656 167 NFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIfsEREFINrfptC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 541 LRTMIVMGDA-----PPADVVAwwAERTRLCNGYGPTEASIATSlCEYRPGVPWNC---IGKPLKNYRCHILDLHHNPLP 612
Cdd:cd17656 247 VKHIITAGEQlvitnEFKEMLH--EHNVHLHNHYGPSETHVVTT-YTINPEAEIPElppIGKPISNTWIYILDQEQQLQP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 613 VGFEGELCIAGSGLAHGYLHQEALSAEKFIicRLPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEV 692
Cdd:cd17656 324 QGIVGELYISGASVARGYLNRQELTAEKFF--PDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 693 ESAVRSHPLVESACVVARSQPSG-KILAAFVQPASpELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17656 401 EAQLLNHPGVSEAVVLDKADDKGeKYLCAYFVMEQ-ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1336-1804 |
1.86e-82 |
|
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: 280.51 E-value: 1.86e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSiVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGE----PEQGWaSPAVGFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNN---FT 1487
Cdd:cd17656 82 LDSGVRVVLTQRHlkskLSFNK-STILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNllhFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1488 NDFVGRLAlsaRDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHL 1567
Cdd:cd17656 161 REKTNINF---SDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1568 PAASQRPLTV---LCGGEKMpaaLLTQLRRIATRVLQV-----YGPTETTIWSTCAdLTHEGASDC---IGTPIQATEVL 1636
Cdd:cd17656 238 EFINRFPTCVkhiITAGEQL---VITNEFKEMLHEHNVhlhnhYGPSETHVVTTYT-INPEAEIPElppIGKPISNTWIY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1637 VMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRrQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRG 1716
Cdd:cd17656 314 ILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFP-DPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1717 HRIELSEIDLSLSSLDNIERSLSLIVGEGQ-QARIVSYlqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNN 1795
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKgEKYLCAY--FVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPN 470
|
....*....
gi 1725075560 1796 NKIDIRRLP 1804
Cdd:cd17656 471 GKVDRKALP 479
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
311-683 |
2.85e-82 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 277.66 E-value: 2.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 311 HADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPA 390
Cdd:pfam00501 16 VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 391 LILADSPL---------HSGDAPCI-----APSSIDYRSLNIHAEQL--------PQSRDALAYVCYTSGTTGKPKGVMI 448
Cdd:pfam00501 96 VLITDDALkleellealGKLEVVKLvlvldRDPVLKEEPLPEEAKPAdvppppppPPDPDDLAYIIYTSGTTGKPKGVML 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 449 GREGLSNVAQNH----RDFIGLAQGSRVLAIASLGFDA-FGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHI 523
Cdd:pfam00501 176 THRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDPAALLELIERYKVTVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 524 TITPAILELL------PREMWPGLRTMIVMGDAPPADVVAWWAERTR--LCNGYGPTEASIATSLCEYRPG--VPWNCIG 593
Cdd:pfam00501 256 YGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELFGgaLVNGYGLTETTGVVTTPLPLDEdlRSLGSVG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 594 KPLKNYRCHILDLHH-NPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYRTGDIAKWDEQGNIIF 672
Cdd:pfam00501 336 RPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD---------EDGWYRTGDLGRRDEDGYLEI 406
|
410
....*....|.
gi 1725075560 673 VGRRDHQVKIR 683
Cdd:pfam00501 407 VGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
252-1106 |
4.08e-81 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 299.01 E-value: 4.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 252 LDALLADPADPIAA-PIVTQPHTLHRLSQFNATDDAELLAHDVIALFRHAAAAHPQQAALHADGQTYSYGEIDRASDQFA 330
Cdd:PRK05691 2148 LEALLGDPQQRLAElPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLA 2227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 331 CWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSPLHS--GDAP---- 404
Cdd:PRK05691 2228 RALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEalGELPagva 2307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 405 --CI---APSSIDYRSLNIHAEQLPQSRdalAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLG 479
Cdd:PRK05691 2308 rwCLeddAAALAAYSDAPLPFLSLPQHQ---AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSIN 2384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 480 FDAFGWDVYGALVSGATLYLApSELHTDVGALHDYLTQHDIGHITITPAILELLPR------EMWPgLRTMIVMGDAPPA 553
Cdd:PRK05691 2385 FDAASERLLVPLLCGARVVLR-AQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQwlagqgEQLP-VRMCITGGEALTG 2462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 554 DVVawwaERTR-------LCNGYGPTE------ASIA-TSLCEYRPGVPwncIGKPLKNYRCHILDLHHNPLPVGFEGEL 619
Cdd:PRK05691 2463 EHL----QRIRqafapqlFFNAYGPTEtvvmplACLApEQLEEGAASVP---IGRVVGARVAYILDADLALVPQGATGEL 2535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 620 CIAGSGLAHGYLHQEALSAEKFIICrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSH 699
Cdd:PRK05691 2536 YVGGAGLAQGYHDRPGLTAERFVAD--PFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEH 2613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 700 PLVESACVVARSQPSGKILAAFV---QPASPELTIDALRHALVTLLHPA----AIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:PRK05691 2614 PAVREAVVLALDTPSGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQlpdyMVPAHLILLDSLPLTANGKLDRRALPA 2693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 773 WPLDERNERLTPPETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALvARDLCCHLSIADLFRHNTVRKLA 852
Cdd:PRK05691 2694 PDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLA 2772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 853 eyienkAVAAERAIAICDE----HRAPLSPQQNllWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLR 928
Cdd:PRK05691 2773 ------AVATHSEAAQAEQgplqGASGLTPIQH--WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALR 2844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 929 TRFTETDGvayQLAEPHTPirladhwVDGQTLSAEKWVRQL--CATPFDITAR-------PPLVLRLVQYHQQHHVLIWV 999
Cdd:PRK05691 2845 LRFSQADG---RWQAEYRA-------VTAQELLWQVTVADFaeCAALFADAQRsldlqqgPLLRALLVDGPQGQQRLLLA 2914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1000 KHNIITDAWSEQLILNDLWQRYNELDDHHGLDAPQPQIQTIDIVnSGIASPAPAD-----VAYWQQQLQDCRElDFPLDK 1074
Cdd:PRK05691 2915 IHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWA-ARLQAYAGSEslreeLGWWQAQLGGPRA-ELPCDR 2992
|
890 900 910
....*....|....*....|....*....|..
gi 1725075560 1075 PrplmpthAGERIHYQLQPDVAGLLASRGKAL 1106
Cdd:PRK05691 2993 P-------QGGNLNRHAQTVSVRLDAERTRQL 3017
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
318-765 |
1.21e-80 |
|
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: 274.28 E-value: 1.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 318 SYGEIDRASDQFACWLLEH-SGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADS 396
Cdd:cd17648 14 TYRELNERANRLAHYLLSVaEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 397 plhsgdapciapssidyrslnihaeqlpqsRDaLAYVCYTSGTTGKPKGVMIGREGLSNV-AQNHRDFIGLAQGS-RVLA 474
Cdd:cd17648 94 ------------------------------TD-LAYAIYTSGTTGKPKGVLVEHGSVVNLrTSLSERYFGRDNGDeAVLF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 475 IASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPGLRTMIVMGDAPPAD 554
Cdd:cd17648 143 FSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARLPHLKRVDAAGEEFTAP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 555 VVAWWAER--TRLCNGYGPTEASIATSLCEYRPGVPW-NCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYL 631
Cdd:cd17648 223 VFEKLRSRfaGLIINAYGPTETTVTNHKRFFPGDQRFdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 632 HQEALSAEKFIicRLPYMAAEE-------RLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVES 704
Cdd:cd17648 303 NRPELTAERFL--PNPFQTEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRE 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 705 ACVVARSQPSG------KILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKI 765
Cdd:cd17648 381 CAVVAKEDASQaqsriqKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1323-1803 |
8.81e-75 |
|
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: 258.92 E-value: 8.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1323 SLLMHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALL-RIDSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPI 1401
Cdd:TIGR01734 1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQkRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1402 DVHYPADRVSYMIENAQARLLVTDGE-----PEQGWASPAVGFDSLVSHPAAADALPIPADDTLaYIMYTSGSTGNPKGV 1476
Cdd:TIGR01734 81 DTSIPSERIEMIIEAAGPELVIHTAElsidaVGTQIITLSALEQAETSGGPVSFDHAVKGDDNY-YIIYTSGSTGNPKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1477 MITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQAT 1556
Cdd:TIGR01734 160 QISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1557 PTvWSTIVHHLPAASQRPLT-----VLCGGE---KMPAALLTqlRRIATRVLQVYGPTETTIWSTCADLTHEGASDCIGT 1628
Cdd:TIGR01734 240 PS-FVDMCLLDPNFNQENYPhlthfLFCGEElpvKTAKALLE--RFPKATIYNTYGPTEATVAVTSVKITQEILDQYPRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1629 PI----QATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqaFGAERY-MYRTGDIVRFnRQGQLE 1703
Cdd:TIGR01734 317 PIgfakPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF-----FSHEGQpAYRTGDAGTI-TDGQLF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1704 YLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV--GEGQQARIVSYLQLTSGEELNE----KAVRTALKARLPN 1777
Cdd:TIGR01734 391 YQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKynKDHKVEYLIAAIVPETEDFEKEfqltKAIKKELKKSLPA 470
|
490 500
....*....|....*....|....*.
gi 1725075560 1778 IMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:TIGR01734 471 YMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1332-1803 |
2.29e-72 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 251.74 E-value: 2.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRI---DSRPFSV-GVMmekSCHVAVLLLGVLRAGKHYVPIDVHYPA 1407
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLklpDKSPIIVfGHM---SPEMLATFLGAVKAGHAYIPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1408 DRVSYMIENAQARLLV-TDGEPEQGWASPAVGFDSLVSHPAAADAL----PIPADDTlAYIMYTSGSTGNPKGVMITHGN 1482
Cdd:PRK04813 89 ERIEMIIEVAKPSLIIaTEELPLEILGIPVITLDELKDIFATGNPYdfdhAVKGDDN-YYIIFTSGTTGKPKGVQISHDN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1483 LNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPtvwST 1562
Cdd:PRK04813 168 LVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTP---SF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1563 I----------VHHLPAasqrpLTV--LCGGE---KMPAALLTqlRRIATRVLQVYGPTETTIWSTCADLTHEGASDC-- 1625
Cdd:PRK04813 245 AdmclldpsfnEEHLPN-----LTHflFCGEElphKTAKKLLE--RFPSATIYNTYGPTEATVAVTSIEITDEMLDQYkr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1626 --IGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAerymYRTGDIVRFNrQGQLE 1703
Cdd:PRK04813 318 lpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPA----YHTGDAGYLE-DGLLF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1704 YLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSL-IVGEGQQARIVSYLQLTSGEELNE----KAVRTALKARLPNI 1778
Cdd:PRK04813 393 YQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVpYNKDHKVQYLIAYVVPKEEDFEREfeltKAIKKELKERLMEY 472
|
490 500
....*....|....*....|....*
gi 1725075560 1779 MIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK04813 473 MIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
430-765 |
1.25e-68 |
|
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: 235.26 E-value: 1.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 430 LAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSElhtDVG 509
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 510 ALHDYLTQHDIGHITITPAILELL------PREMWPGLRTMIVMGDAPPADVVAWWAERT--RLCNGYGPTEASI-ATSL 580
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFEEAPgiKLVNGYGLTETGGtVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 581 CEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGD 660
Cdd:cd04433 159 PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD----------EDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 661 IAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPE-LTIDALRHAL 738
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEwGERVVAVVVLRPGAdLDAEELRAHV 308
|
330 340
....*....|....*....|....*..
gi 1725075560 739 VTLLHPAAIPSVFIFLPALPLTINGKI 765
Cdd:cd04433 309 RERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
314-856 |
6.68e-66 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 249.31 E-value: 6.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDdvqpaliL 393
Cdd:PRK05691 3743 DQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIE-------L 3815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSPLHSGDAPCIAPSSIDYRSLNIHA-------EQLPQSR------------DALAYVCYTSGTTGKPKGVMIGREGLS 454
Cdd:PRK05691 3816 SRTPVLVCSAACREQARALLDELGCANrprllvwEEVQAGEvashnpgiysgpDNLAYVIYTSGSTGLPKGVMVEQRGML 3895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 455 NVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELL- 533
Cdd:PRK05691 3896 NNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMl 3975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 534 --PREMWPGLRTMIVMGDAPPADVVAWWAER---TRLCNGYGPTEAS---------IATSLCEYRPgvpwncIGKPLKNY 599
Cdd:PRK05691 3976 aeDRQALDGLRWMLPTGEAMPPELARQWLQRypqIGLVNAYGPAECSddvaffrvdLASTRGSYLP------IGSPTDNN 4049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 600 RCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQ 679
Cdd:PRK05691 4050 RLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFV--PHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQ 4127
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 680 VKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSGKILAAFVQPA----SPELTIDALRHALVTLLHPAAIPSVFIFLP 755
Cdd:PRK05691 4128 VKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHqtvlAQGALLERIKQRLRAELPDYMVPLHWLWLD 4207
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 756 ALPLTINGKIARQQLEKWPLDE-RNERLTPPETETEAILERIVANAIGCPQADVTQEFINLGAHSLTMSKIVALVARDLC 834
Cdd:PRK05691 4208 RLPLNANGKLDRKALPALDIGQlQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQ 4287
|
570 580
....*....|....*....|..
gi 1725075560 835 CHLSIADLFRHNTVRKLAEYIE 856
Cdd:PRK05691 4288 RNVPLRAMFECSTVEELAEYIE 4309
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
314-770 |
3.46e-64 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 227.86 E-value: 3.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:PRK04813 25 GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLII 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 A--DSPLHSGDAPCIAPSSI--DYRSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGL-SNVAQNHRDFiGLAQ 468
Cdd:PRK04813 105 AteELPLEILGIPVITLDELkdIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLvSFTNWMLEDF-ALPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 469 GSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILE---LLP---REMWPGLR 542
Cdd:PRK04813 184 GPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSFADmclLDPsfnEEHLPNLT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 543 TMIVMGDAPPADVVAWWAER---TRLCNGYGPTEASIATS--------LCEYRPgVPwncIGKPLKNYRCHILDLHHNPL 611
Cdd:PRK04813 264 HFLFCGEELPHKTAKKLLERfpsATIYNTYGPTEATVAVTsieitdemLDQYKR-LP---IGYAKPDSPLLIIDEEGTKL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 612 PVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpYMAAEERLYRTGDIAKWDEqGNIIFVGRRDHQVKIRGVRIEMGE 691
Cdd:PRK04813 340 PDGEQGEIVISGPSVSKGYLNNPEKTAEAF------FTFDGQPAYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 692 VESAVRSHPLVESACVVArSQPSGKI--LAAFVQPA----SPELTI-DALRHALVTLLHPAAIPSVFIFLPALPLTINGK 764
Cdd:PRK04813 413 IEQNLRQSSYVESAVVVP-YNKDHKVqyLIAYVVPKeedfEREFELtKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGK 491
|
....*.
gi 1725075560 765 IARQQL 770
Cdd:PRK04813 492 IDRKAL 497
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1336-1803 |
4.46e-64 |
|
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: 226.68 E-value: 4.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd05936 13 PDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDgepeqgwaspaVGFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNL--NNFTNDFVG 1492
Cdd:cd05936 93 NDSGAKALIVA-----------VSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLvaNALQIKAWL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1493 RLALSARDKVLSLTSIsFDIFGLE--LFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQATPTVWSTIVHHlPAA 1570
Cdd:cd05936 162 EDLLEGDDVVLAALPL-FHVFGLTvaLLLPLALGATIVLIPR---FRPIGVLKEIRKHRVTIFPGVPTMYIALLNA-PEF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1571 SQRPLT----VLCGGEKMPAALLTQLRRI-ATRVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPL 1645
Cdd:cd05936 237 KKRDFSslrlCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1646 PSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRrqafGAerymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEID 1725
Cdd:cd05936 317 PPGEVGELWVRGPQVMKGYWNRPEETAEAFVD----GW----LRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1726 LSLSSLDNIErsLSLIVGEGQQAR---IVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRR 1802
Cdd:cd05936 389 EVLYEHPAVA--EAAVVGVPDPYSgeaVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRE 466
|
.
gi 1725075560 1803 L 1803
Cdd:cd05936 467 L 467
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
873-1290 |
3.76e-61 |
|
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: 216.91 E-value: 3.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQ--LAEPHTPIRL 950
Cdd:cd19540 1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQvvLPAAEARPDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 951 ADHWVDGQTLSAEkwVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILND-------------- 1016
Cdd:cd19540 81 TVVDVTEDELAAR--LAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDlatayaarragrap 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1017 -------------LWQRyNELDDHhglDAPqpqiqtidivnsgiASPAPADVAYWQQQLQDC-RELDFPLDKPRPLMPTH 1082
Cdd:cd19540 159 dwaplpvqyadyaLWQR-ELLGDE---DDP--------------DSLAARQLAYWRETLAGLpEELELPTDRPRPAVASY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1083 AGERIHYQLQPDVAGLLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDN--LDqtQVSGFHVNTVPLRI 1160
Cdd:cd19540 221 RGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDeaLD--DLVGMFVNTLVLRT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1161 QLSEQDTLAGLIGNMMETCIGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAGDVcQQNLRDCTLHRLPLSSGF 1240
Cdd:cd19540 299 DVSGDPTFAELLARVRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAA-TLELPGLTVEPVPVDTGV 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 1241 SMFDMTWNFSVEQDA------VTIELDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19540 378 AKFDLSFTLTERRDAdgapagLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1459-1799 |
2.27e-60 |
|
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: 211.37 E-value: 2.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1459 TLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFD--IFGLeLFCSLAGGAHVTLcPREtam 1536
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIggLFGL-LGALLAGGTVVLL-PKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1537 DPVKLYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPL----TVLCGGEKMPAALLTQLRRIA-TRVLQVYGPTETTIW 1611
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKA-PESAGYDLsslrALVSGGAPLPPELLERFEEAPgIKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1612 -STCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgaERYMYRT 1690
Cdd:cd04433 155 vATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1691 GDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIVG---EGQQARIVSYLQLTSGEELNEKAV 1767
Cdd:cd04433 227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE--AAVVGvpdPEWGERVVAVVVLRPGADLDAEEL 304
|
330 340 350
....*....|....*....|....*....|..
gi 1725075560 1768 RTALKARLPNIMIPSGFVVLSAFPLTNNNKID 1799
Cdd:cd04433 305 RAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
873-1290 |
3.46e-60 |
|
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: 214.05 E-value: 3.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQL----AEPHTPI 948
Cdd:cd19538 1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLileeDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 949 RLADhwVDGQTLSAEkwVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNE-LDDH 1027
Cdd:cd19538 81 EIKE--VDEEELESE--INEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRArCKGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1028 HGLDAPQPqIQTIDIV---------NSGIASPAPADVAYWQQQLQDC-RELDFPLDKPRPLMPTHAGERIHYQLQPDVAG 1097
Cdd:cd19538 157 APELAPLP-VQYADYAlwqqellgdESDPDSLIARQLAYWKKQLAGLpDEIELPTDYPRPAESSYEGGTLTFEIDSELHQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1098 LLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMME 1177
Cdd:cd19538 236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1178 TCIGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAGDVcQQNLRDCTLHRLPLSSGFSMFDMTWNF-----SVE 1252
Cdd:cd19538 316 TNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQP-SLDLPGLEAKLELRTVGSAKFDLTFELreqynDGT 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1725075560 1253 QDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19538 395 PNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
871-1309 |
1.13e-57 |
|
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: 207.57 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 871 EHRAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFT-ETDGVAYQ--LAEPHTP 947
Cdd:pfam00668 2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQviLEERPFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 948 IRLAD--HWV-DGQTLSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNEL 1024
Cdd:pfam00668 82 LEIIDisDLSeSEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1025 DDHHGLDAPQ--PQIQTIDIVNSGIASPA-PADVAYWQQQL-QDCRELDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLA 1100
Cdd:pfam00668 162 LKGEPLPLPPktPYKDYAEWLQQYLQSEDyQKDAAYWLEQLeGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1101 SRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCI 1180
Cdd:pfam00668 242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1181 GAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQN-AGDVCQQNLRDctLHRLPLSSGFSM-----FDMTWNFSVEQD 1254
Cdd:pfam00668 322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNyLGQDSQEEEFQ--LSELDLSVSSVIeeeakYDLSLTASERGG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 1255 AVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLPanTAQLA-LNPLCEREQQWL 1309
Cdd:pfam00668 400 GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHP--SQPLSeLDLLSDAEKQKL 453
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
873-1290 |
6.67e-57 |
|
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: 204.54 E-value: 6.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETD-GVAYQLAEPHTPIRLA 951
Cdd:cd19539 1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 952 -----DHWVDGQTLsAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDD 1026
Cdd:cd19539 81 vrdlsDPDSDRERR-LEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1027 HHGLDAPQPQIQTIDIV---NSGIASPAPAD-VAYWQQQLQDCRELDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASR 1102
Cdd:cd19539 160 GPAAPLPELRQQYKEYAawqREALAAPRAAElLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALREL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1103 GKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGA 1182
Cdd:cd19539 240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1183 YQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAGDvcqqNLRDCTL-----HRLPLSSGfSMFDMTWNFSVEQDAVT 1257
Cdd:cd19539 320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPA----GELELAGglsytEGSDIPDG-AKFDLNLTVTEEGTGLR 394
|
410 420 430
....*....|....*....|....*....|...
gi 1725075560 1258 IELDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19539 395 GSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1348-1803 |
1.23e-54 |
|
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: 198.46 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLR---IDSRpfSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVT 1424
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKkfqTEER--AIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1425 DGEpeqgwaspaVGFDSLVSHPAAADaLPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSaRDKVLS 1504
Cdd:cd17654 95 NKE---------LDNAPLSFTPEHRH-FNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT-SEDILF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1505 LTSI-SFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFI-ERQQPSVIQATPTVW-----STIVHHLPAASQRPLTV 1577
Cdd:cd17654 164 LTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFrrfgsQSIKSTVLSATSSLRVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1578 LCGGEKMPAALLTQLRR---IATRVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPlpsgAFGELW 1654
Cdd:cd17654 244 ALGGEPFPSLVILSSWRgkgNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSE----GTGQVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1655 LGGagvspgywrnptLSDKVFLRRQAFGAERYMYRTGDIVRFnRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLD-- 1732
Cdd:cd17654 320 LGG------------LNRVCILDDEVTVPKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLgv 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 1733 --------NIERSLSLIVGEGQQARIVSYLQLTSgeelnekavrtalkarLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd17654 387 escavtlsDQQRLIAFIVGESSSSRIHKELQLTL----------------LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
313-798 |
1.34e-51 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 192.63 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILK-----SNkTYVLLDPQAPAARnqsiLDDV 387
Cdd:COG0365 36 EERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARigavhSP-VFPGFGAEALADR----IEDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 388 QPALILADSPLHSG-----------------------------DAPCIAPSSIDYRSL------NIHAEQLPqsRDALAY 432
Cdd:COG0365 111 EAKVLITADGGLRGgkvidlkekvdealeelpslehvivvgrtGADVPMEGDLDWDELlaaasaEFEPEPTD--ADDPLF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 433 VCYTSGTTGKPKGVMIGREG-LSNVAQNHRDFIGLAQGSRVLAIASLGFdAFG-WD-VYGALVSGATLYLAP-SELHTDV 508
Cdd:COG0365 189 ILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGW-ATGhSYiVYGPLLNGATVVLYEgRPDFPDP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 509 GALHDYLTQHDIGHITITPAILELLPREM--WPG------LRTMIVMGDAPPADVVAWWAERT--RLCNGYGPTE--ASI 576
Cdd:COG0365 268 GRLWELIEKYGVTVFFTAPTAIRALMKAGdePLKkydlssLRLLGSAGEPLNPEVWEWWYEAVgvPIVDGWGQTEtgGIF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 577 ATSLC--EYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGS--GLAHGYLHQEALSAEKfiicrlpYMAAE 652
Cdd:COG0365 348 ISNLPglPVKPG----SMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRET-------YFGRF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 653 ERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV-ESAcVVARSQPS-GKILAAFV-----QPA 725
Cdd:COG0365 417 PGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVaEAA-VVGVPDEIrGQVVKAFVvlkpgVEP 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 726 SPELtIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWpldERNERLTPPET-ETEAILERIVA 798
Cdd:COG0365 496 SDEL-AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI---AEGRPLGDTSTlEDPEALDEIKE 565
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1330-1799 |
5.36e-51 |
|
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: 187.43 E-value: 5.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPAD 1408
Cdd:cd17631 3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDrVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYMIENAQARLLVTDgepeqgwaspavgfdslvshpaaadalpipaddtLAYIMYTSGSTGNPKGVMITHGNLNNFTN 1488
Cdd:cd17631 83 EVAYILADSGAKVLFDD----------------------------------LALLMYTSGTTGRPKGAMLTHRNLLWNAV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1489 DFVGRLALSARDKVLSLTSIsFDIFGLELFC--SLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQATPTVWSTIVHH 1566
Cdd:cd17631 129 NALAALDLGPDDVLLVVAPL-FHIGGLGVFTlpTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPTMIQALLQH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1567 lPAASQRPLT----VLCGGEKMPAALLTQLRRIATRVLQVYGPTETTiwSTCADLTHEGASDCI---GTPIQATEVLVMD 1639
Cdd:cd17631 205 -PRFATTDLSslraVIYGGAPMPERLLRALQARGVKFVQGYGMTETS--PGVTFLSPEDHRRKLgsaGRPVFFVEVRIVD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1640 QAGNPLPSGAFGELWLGGAGVSPGYWRNP-----TLSDKVFlrrqafgaerymyRTGDIVRFNRQGQLEYLGRNDHQVKI 1714
Cdd:cd17631 282 PDGREVPPGEVGEIVVRGPHVMAGYWNRPeataaAFRDGWF-------------HTGDLGRLDEDGYLYIVDRKKDMIIS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1715 RGHRIELSEIDLSLSSLDNIERSLSLIV-----GEGQQARIVsylqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSA 1789
Cdd:cd17631 349 GGENVYPAEVEDVLYEHPAVAEVAVIGVpdekwGEAVVAVVV----PRPGAELDEDELIAHCRERLARYKIPKSVEFVDA 424
|
490
....*....|
gi 1725075560 1790 FPLTNNNKID 1799
Cdd:cd17631 425 LPRNATGKIL 434
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1336-1805 |
6.08e-50 |
|
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: 186.53 E-value: 6.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:TIGR03098 14 PDATALVHHDRTLTYAALSERVLALASGLRGLGLARGErVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVT---------DGEPEQGWASPAVGFDSL----VSHP-----------AAADALPIP--ADDTLAYIMYTSG 1468
Cdd:TIGR03098 94 ADCNVRLLVTsserldllhPALPGCHDLRTLIIVGDPahasEGHPgeepaswpkllALGDADPPHpvIDSDMAAILYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1469 STGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDiFGL-ELFCSLAGGAHVTLCPRETAMDPVKLyhfIER 1547
Cdd:TIGR03098 174 STGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFD-YGFnQLTTAFYVGATVVLHDYLLPRDVLKA---LEK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1548 QQPSVIQATPTVWSTIVH-HLPAASQRPLTVLCG-GEKMPAALLTQLRRIA--TRVLQVYGPTEtTIWSTCADLTHEGAS 1623
Cdd:TIGR03098 250 HGITGLAAVPPLWAQLAQlDWPESAAPSLRYLTNsGGAMPRATLSRLRSFLpnARLFLMYGLTE-AFRSTYLPPEEVDRR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1624 -DCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERYMYRT----GDIVRFNR 1698
Cdd:TIGR03098 329 pDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHLPELavwsGDTVRRDE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1699 QGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGE---GQQarIVSYLQLTSGEELNEKAVRTALKARL 1775
Cdd:TIGR03098 409 EGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDptlGQA--IVLVVTPPGGEELDRAALLAECRARL 486
|
490 500 510
....*....|....*....|....*....|
gi 1725075560 1776 PNIMIPSGFVVLSAFPLTNNNKIDIRRLPA 1805
Cdd:TIGR03098 487 PNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
876-1111 |
3.02e-49 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 175.61 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 876 LSPQQNLLWYLsalNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLA---- 951
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEvvdl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 952 -DHWVDGQTLSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDHHGL 1030
Cdd:COG4908 78 sALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1031 DAPQPQIQTIDIV---NSGIASPA-PADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRGKA 1105
Cdd:COG4908 158 PLPELPIQYADYAawqRAWLQSEAlEKQLEYWRQQLAGAPPvLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*.
gi 1725075560 1106 LGATPF 1111
Cdd:COG4908 238 HGATVN 243
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
875-1286 |
2.24e-48 |
|
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: 179.53 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTP------I 948
Cdd:cd19066 3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVrfrieiI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 949 RLADHWVDGQTLSAEKWvrQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDdHH 1028
Cdd:cd19066 83 DLRNLADPEARLLELID--QIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE-RQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1029 GLDAPQPQIQTIDIV----NSGIASPAPADVAYWQQQLQDCRE-LDFPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRG 1103
Cdd:cd19066 160 KPTLPPPVGSYADYAawleKQLESEAAQADLAYWTSYLHGLPPpLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1104 KALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGAY 1183
Cdd:cd19066 240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1184 QHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAG---DVCQQNLRDCTLHRlplSSGFSMFDMTWNFSVEQDA-VTIE 1259
Cdd:cd19066 320 EHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQqqlGKTGGFIFTTPVYT---SSEGTVFDLDLEASEDPDGdLLLR 396
|
410 420
....*....|....*....|....*..
gi 1725075560 1260 LDYASELFYPASMQMLLDNYQQTLRQL 1286
Cdd:cd19066 397 LEYSRGVYDERTIDRFAERYMTALRQL 423
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
313-770 |
1.04e-46 |
|
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: 175.83 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP-AL 391
Cdd:cd05936 21 MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAkAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 392 ILADSPLHSGDAPciapssidyrslniHAEQLPQSRDA--LAYVCYTSGTTGKPKGVMIG-REGLSNVAQNHRDFIGLAQ 468
Cdd:cd05936 101 IVAVSFTDLLAAG--------------APLGERVALTPedVAVLQYTSGTTGVPKGAMLThRNLVANALQIKAWLEDLLE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 469 GS-RVLAIASLgFDAFGWDVYG--ALVSGATLYLAPSelHTDVGALHDyLTQHDIGHITITPAILELL-----PREMWP- 539
Cdd:cd05936 167 GDdVVLAALPL-FHVFGLTVALllPLALGATIVLIPR--FRPIGVLKE-IRKHRVTIFPGVPTMYIALlnapeFKKRDFs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 540 GLRTMIVMGDAPPADVVAWWAERT--RLCNGYGPTEASIATSLC----EYRPGvpwnCIGKPLKNYRCHILDLHHNPLPV 613
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTgvPIVEGYGLTETSPVVAVNpldgPRKPG----SIGIPLPGTEVKIVDDDGEELPP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 614 GFEGELCIAGSGLAHGYLHQEALSAEKFIICRLpymaaeerlyRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVE 693
Cdd:cd05936 319 GEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL----------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 694 SAVRSHPLV-ESACVVARSQPSGKILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05936 389 EVLYEHPAVaEAAVVGVPDPYSGEAVKAFVVLKEGAsLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1058-1877 |
1.15e-46 |
|
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: 184.88 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1058 WQQQLQDCRELDFPLDKPRPlmptHAGERIHYQLQPDVAGLLASRGKalGATPFALLCAALSLLLSRYTQQQDIVIGTai 1137
Cdd:TIGR03443 2 WSERLDNPTLSVLPHDYLRP----ANNRLVEATYSLQLPSAEVTAGG--GSTPFIILLAAFAALVYRLTGDEDIVLGT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1138 aaRDNLDQTQVSgfhvntvpLRIQLSEQDTLAGLIGNMMETCIGAYQHQQLSFDRILHQIEYERMSNKNP-LFQIMAilQ 1216
Cdd:TIGR03443 74 --SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAF--Q 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1217 NAGDVCQQNLrdctlhrlplsSGFSMFDMTWNFSVEQDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLPaNTAQL 1296
Cdd:TIGR03443 142 DAPDNQQTTY-----------STGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNP-DEPIG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1297 ALNPLCEREQQWLQQLAVNAD-AGSRDSLLMHIGRLAHTQPD---------SLAVSCERQQYSYRQLWAQSERVAHALLR 1366
Cdd:TIGR03443 210 KVSLITPSQKSLLPDPTKDLDwSGFRGAIHDIFADNAEKHPDrtcvvetpsFLDPSSKTRSFTYKQINEASNILAHYLLK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1367 IDSRPFSVgVMMEKSCHV--AVLLLGVLRAGKHYVPIDVHYPADR--------------------------VSYMIENAQ 1418
Cdd:TIGR03443 290 TGIKRGDV-VMIYAYRGVdlVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtldqlvRDYIDKELE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1419 ARLLV-----------TDGEPEQGWASPAVGFDSLVSHPAAADALPipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFT 1487
Cdd:TIGR03443 369 LRTEIpalalqddgslVGGSLEGGETDVLAPYQALKDTPTGVVVGP----DSNPTLSFTSGSEGIPKGVLGRHFSLAYYF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1488 NDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQpsviqatptvwSTIVHHL 1567
Cdd:TIGR03443 445 PWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYG-----------ATVTHLT 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1568 PAASQrpltVLCGGEKMPAALL---------------TQLRRIA--TRVLQVYGPTET-------TIWSTCADLTH-EGA 1622
Cdd:TIGR03443 514 PAMGQ----LLSAQATTPIPSLhhaffvgdiltkrdcLRLQTLAenVCIVNMYGTTETqravsyfEIPSRSSDSTFlKNL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1623 SDCI--GTPIQATEVLVMDQAGNPLPS--GAFGELWLGGAGVSPGYWRNPTLSDKVFL---------------------R 1677
Cdd:TIGR03443 590 KDVMpaGKGMKNVQLLVVNRNDRTQTCgvGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkennkpeR 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1678 RQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSS----LDNI---------ERSL-SLIVG 1743
Cdd:TIGR03443 670 EFWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQhplvRENVtlvrrdkdeEPTLvSYIVP 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1744 EGQQARIVSYLQLTSGEELNE-------------KAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPET-- 1808
Cdd:TIGR03443 750 QDKSDELEEFKSEVDDEESSDpvvkglikyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTaq 829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1809 --------RYSASEADYTPaaneAESAMQHIWQQVLSQ--TQISVCDSFFSLGGNSLQIPQLLHAIRQQMGVSL------ 1872
Cdd:TIGR03443 830 laavaknrSASAADEEFTE----TEREIRDLWLELLPNrpATISPDDSFFDLGGHSILATRMIFELRKKLNVELplglif 905
|
....*...
gi 1725075560 1873 ---TIREF 1877
Cdd:TIGR03443 906 kspTIKGF 913
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1335-1803 |
1.59e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 176.53 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1335 QPDSLAVSCERQQYSYRQLWAQSERVAHALLRI----DSRpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:PRK06187 19 HPDKEAVYFDGRRTTYAELDERVNRLANALRALgvkkGDR---VAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLVTDGE------------------------PEQGWASPAVGFDSLVSHPAAADALPIPADDTLAYIMYT 1466
Cdd:PRK06187 96 AYILNDAEDRVVLVDSEfvpllaailpqlptvrtvivegdgPAAPLAPEVGEYEELLAAASDTFDFPDIDENDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1467 SGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGLELF--CSLAGGAHVTlcPREtaMDPVKLYHF 1544
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLPylALMAGAKQVI--PRR--FDPENLLDL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1545 IERQQPSVIQATPTVWSTIVHHlPAASQRPLT----VLCGGEKMPAALLTQ-LRRIATRVLQVYGPTETTIWSTCADLTH 1619
Cdd:PRK06187 251 IETERVTFFFAVPTIWQMLLKA-PRAYFVDFSslrlVIYGGAALPPALLREfKEKFGIDLVQGYGMTETSPVVSVLPPED 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1620 EGASDC-----IGTPIQATEVLVMDQAGNPLP--SGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgaERYMYRTGD 1692
Cdd:PRK06187 330 QLPGQWtkrrsAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETI--------DGGWLHTGD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1693 IVRFNRQGQLEYLGRNDHQVKIRGHRI---ELSEIdlsLSSLDNI----------ERSlslivGEgqqaRIVSYLQLTSG 1759
Cdd:PRK06187 402 VGYIDEDGYLYITDRIKDVIISGGENIyprELEDA---LYGHPAVaevavigvpdEKW-----GE----RPVAVVVLKPG 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1725075560 1760 EELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK06187 470 ATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
316-770 |
1.10e-45 |
|
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: 172.27 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 316 TYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILAD 395
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 396 SplHSGDAPciapssidyRSLNIHAEQLPQSRDA-LAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQgSRVLA 474
Cdd:cd17654 96 K--ELDNAP---------LSFTPEHRHFNIRTDEcLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS-EDILF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 475 IAS-LGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYL-TQHDIGHITITPAILELLPREMWPG--------LRTM 544
Cdd:cd17654 164 LTSpLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQSIKStvlsatssLRVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 545 IVMGDAPPADVV--AWWAE--RTRLCNGYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHhnplpvGFEGELC 620
Cdd:cd17654 244 ALGGEPFPSLVIlsSWRGKgnRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQN------GSEGTGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 621 IAGSGLAHGYLHQEALSaekfiicrlpymAAEERLYRTGDIAKwDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHP 700
Cdd:cd17654 318 VFLGGLNRVCILDDEVT------------VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCL 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 701 LVESACVVARSQPsgKILAAFVQPASPELTIDALRhalVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd17654 385 GVESCAVTLSDQQ--RLIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
313-767 |
3.96e-45 |
|
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: 170.10 E-value: 3.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADsplhsgdapciapssidyrslnihaeqlpqsrdaLAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd17631 97 FDD----------------------------------LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLgFDAFGWDVYGA--LVSGATLYLAPselHTDVGALHDYLTQHDIGHITITPAILE-LLPREMW-----PGLRTM 544
Cdd:cd17631 143 LVVAPL-FHIGGLGVFTLptLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQaLLQHPRFattdlSSLRAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 545 IVMGDAPPADVVAWWAER-TRLCNGYGPTEASIATSLCE-----YRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGE 618
Cdd:cd17631 219 IYGGAPMPERLLRALQARgVKFVQGYGMTETSPGVTFLSpedhrRKLG----SAGRPVFFVEVRIVDPDGREVPPGEVGE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 619 LCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRS 698
Cdd:cd17631 295 IVVRGPHVMAGYWNRPEATAAAF----------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYE 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 699 HPLVESACVVARSQPS-GKILAAFVQPASP-ELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:cd17631 365 HPAVAEVAVIGVPDEKwGEAVVAVVVPRPGaELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1336-1803 |
2.98e-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: 169.03 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd05926 3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDrVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGE---------PEQGWASPAVGFDSLVSH--------------PAAADALPIPADDTLAYIMYTSGSTG 1471
Cdd:cd05926 83 ADLGSKLVLTPKGelgpasraaSKLGLAILELALDVGVLIrapsaeslsnlladKKNAKSEGVPLPDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1472 NPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGL--ELFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQ 1549
Cdd:cd05926 163 RPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHGLvaSLLSTLAAGGSVVLPPR---FSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1550 PSVIQATPTVWSTIV-HHLPAASQRPLT---VLCGGEKMPAALLTQL-RRIATRVLQVYGPTETTIWSTCADLTHE---- 1620
Cdd:cd05926 239 ATWYTAVPTIHQILLnRPEPNPESPPPKlrfIRSCSASLPPAVLEALeATFGAPVLEAYGMTEAAHQMTSNPLPPGprkp 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1621 GAsdcIGTPiQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTlsdkvfLRRQAFGAERYmYRTGDIVRFNRQG 1700
Cdd:cd05926 319 GS---VGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPE------ANAEAAFKDGW-FRTGDLGYLDADG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1701 QLEYLGRndhqVK---IR-GHRIELSEIDLSLSSLDNIERSLSLIVGE---GQQarIVSYLQLTSGEELNEKAVRTALKA 1773
Cdd:cd05926 388 YLFLTGR----IKeliNRgGEKISPLEVDGVLLSHPAVLEAVAFGVPDekyGEE--VAAAVVLREGASVTEEELRAFCRK 461
|
490 500 510
....*....|....*....|....*....|
gi 1725075560 1774 RLPNIMIPSGFVVLSAFPLTNNNKIDiRRL 1803
Cdd:cd05926 462 HLAAFKVPKKVYFVDELPKTATGKIQ-RRK 490
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1369-1803 |
1.19e-43 |
|
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: 166.46 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1369 SRPFSVGVMMEKSCHVAVLLLGVLRAGKH----YVPIDVHYPADRVSYMIENAQARL---------LVTDGEPEQGWASP 1435
Cdd:cd05922 16 VRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIvladagaadRLRDALPASPDPGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1436 AVGFDSLVSHPAAADALPiPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDiFGL 1515
Cdd:cd05922 96 VLDADGIRAARASAPAHE-VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYD-YGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1516 -ELFCSLAGGAHVTLCPRetAMDPVKLYHFIERQQPSVIQATPTVWS----TIVHHLPAASQRPLTVlcGGEKMPAALLT 1590
Cdd:cd05922 174 sVLNTHLLRGATLVLTND--GVLDDAFWEDLREHGATGLAGVPSTYAmltrLGFDPAKLPSLRYLTQ--AGGRLPQETIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1591 QLRRIA--TRVLQVYGPTETTIWSTC--ADLTHEgASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWR 1666
Cdd:cd05922 250 RLRELLpgAQVYVMYGQTEATRRMTYlpPERILE-KPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1667 NPTlsdkvFLRRQAFGAERymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQ 1746
Cdd:cd05922 329 DPP-----YRRKEGRGGGV--LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1747 QARIVsyLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05922 402 GEKLA--LFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
335-771 |
1.31e-43 |
|
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: 166.46 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 335 EHSGAASSVVAVSMDKSATLLIvllgilksnktYVLLDPQAPAARNQSILDDVQPALILADSPLHSGDAPCIAPSSIDYR 414
Cdd:cd05922 27 NRFTYIELSFAVAYAGGRLGLV-----------FVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDPGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 415 SLNIH--------AEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWD 486
Cdd:cd05922 96 VLDADgiraarasAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 487 VYGALVSGATLYLAPSELHTDvgALHDYLTQHDIGHITITPAILELLPREMW-----PGLRTMIVMGDAPPADVVAWWAE 561
Cdd:cd05922 176 LNTHLLRGATLVLTNDGVLDD--AFWEDLREHGATGLAGVPSTYAMLTRLGFdpaklPSLRYLTQAGGRLPQETIARLRE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 562 R---TRLCNGYGPTEASIATS-----LCEYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQ 633
Cdd:cd05922 254 LlpgAQVYVMYGQTEATRRMTylppeRILEKPG----SIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWND 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 634 EALSAEKfiicrlpyMAAEERLYrTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP 713
Cdd:cd05922 330 PPYRRKE--------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 714 SGKILAAFVQpASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLE 771
Cdd:cd05922 401 LGEKLALFVT-APDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1328-1803 |
4.18e-43 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 167.21 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1328 IGRLAHTQPDSLAVSCE-----RQQYSYRQLWAQSERVAHALLRI-----DsRpfsVGVMMEKSCHVAVLLLGVLRAGKH 1397
Cdd:COG0365 15 LDRHAEGRGDKVALIWEgedgeERTLTYAELRREVNRFANALRALgvkkgD-R---VAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1398 YVPIDVHYPADRVSYMIENAQARLLVTDGE-------------------------------------PEQGWaspaVGFD 1440
Cdd:COG0365 91 HSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidlkekvdealeelpslehvivvgrtgadvPMEGD----LDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1441 SLVSH-PAAADALPIPADDTLaYIMYTSGSTGNPKGVMITHGnlnnftnDFVGRLALSAR--------DKVLSLTSISFd 1511
Cdd:COG0365 167 ELLAAaSAEFEPEPTDADDPL-FILYTSGTTGKPKGVVHTHG-------GYLVHAATTAKyvldlkpgDVFWCTADIGW- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1512 IFGL--ELFCSLAGGAHVTLCP-RETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPA-ASQRPL----TVLCGGEK 1583
Cdd:COG0365 238 ATGHsyIVYGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEpLKKYDLsslrLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1584 MPAALLTQLRR-IATRVLQVYGPTETT-IWSTCADLT--HEGasdCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAG 1659
Cdd:COG0365 318 LNPEVWEWWYEaVGVPIVDGWGQTETGgIFISNLPGLpvKPG---SMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1660 VS--PGYWRNPTLSDKVFlrrqaFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNI-Er 1736
Cdd:COG0365 395 PGmfRGYWNDPERYRETY-----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVaE- 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 1737 slSLIVGE-----GQqaRIVSYLQLTSGEELNE---KAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIdIRRL 1803
Cdd:COG0365 469 --AAVVGVpdeirGQ--VVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPREIEFVDELPKTRSGKI-MRRL 538
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
317-772 |
7.50e-43 |
|
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: 163.28 E-value: 7.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 317 YSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYV----LLDPQAPAARnqsilddvqpali 392
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVplttLLGPKDIEYR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 ladspLHSGDAPCIAPSSIDyrslnihaeqlpqsrdaLAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd05972 68 -----LEAAGAKAIVTDAED-----------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLGFDAFGW-DVYGALVSGAT--LYLAPSelhTDVGALHDYLTQHDIGHITITPAIL-----ELLPREMWPGLRTM 544
Cdd:cd05972 126 WNIADPGWAKGAWsSFFGPWLLGATvfVYEGPR---FDAERILELLERYGVTSFCGPPTAYrmlikQDLSSYKFSHLRLV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 545 IVMGDAPPADVVAWWAERTRLC--NGYGPTE--ASIATSLC-EYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGEL 619
Cdd:cd05972 203 VSAGEPLNPEVIEWWRAATGLPirDGYGQTEtgLTVGNFPDmPVKPG----SMGRPTPGYDVAIIDDDGRELPPGEEGDI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 620 CIAGS--GLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVR 697
Cdd:cd05972 279 AIKLPppGLFLGYVGDPEKTEASI----------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 698 SHPLVESACVVARSQPS-GKILAAFV-----QPASPELTIDALRHaLVTLLHPAAIPSVFIFLPALPLTINGKIARQQLE 771
Cdd:cd05972 349 EHPAVAEAAVVGSPDPVrGEVVKAFVvltsgYEPSEELAEELQGH-VKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
.
gi 1725075560 772 K 772
Cdd:cd05972 428 D 428
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
314-770 |
3.54e-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: 161.31 E-value: 3.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADsplhsgdapciapssidyrslnihaeqlpqsrdaLAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVL 473
Cdd:cd05934 81 VD----------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 474 AIASLgF--DAFGWDVYGALVSGATLYLAP----SELHTDVgalHDYltqhdigHITIT---PAILELL----PREMWPG 540
Cdd:cd05934 127 TVLPL-FhiNAQAVSVLAALSVGATLVLLPrfsaSRFWSDV---RRY-------GATVTnylGAMLSYLlaqpPSPDDRA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 541 LRTMIVMGDAPPADVVAWWAER--TRLCNGYGPTEASIATsLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGE 618
Cdd:cd05934 196 HRLRAAYGAPNPPELHEEFEERfgVRLLEGYGMTETIVGV-IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 619 LCI---AGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESA 695
Cdd:cd05934 275 LVIrglRGWGFFKGYYNMPEATAEAM----------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERA 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 696 VRSHPLVESACVVARSQPSG--KILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05934 345 ILRHPAVREAAVVAVPDEVGedEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1327-1799 |
4.41e-41 |
|
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: 160.23 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1327 HIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHY 1405
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREErVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1406 PADRVSYMIENAQARLLVTDGEPEQ-------------------GWASPAVGFDSLVSHPAAADALPIPAD---DTLAYI 1463
Cdd:cd05959 89 TPDDYAYYLEDSRARVVVVSGELAPvlaaaltksehtlvvlivsGGAGPEAGALLLAELVAAEAEQLKPAAthaDDPAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1464 MYTSGSTGNPKGVMITHGNLNNFTNDFVGR-LALSARDKVLSLTSISFDI-FGLELFCSLAGGAHVTLCPRETAmdPVKL 1541
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYgLGNSLTFPLSVGATTVLMPERPT--PAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1542 YHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLTVL--C--GGEKMPAALLTQLR-RIATRVLQVYGPTETT-IWstCA 1615
Cdd:cd05959 247 FKRIRRYRPTVFFGVPTLYAAMLAA-PNLPSRDLSSLrlCvsAGEALPAEVGERWKaRFGLDILDGIGSTEMLhIF--LS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1616 DLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgaERYMYRTGDIVR 1695
Cdd:cd05959 324 NRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF--------QGEWTRTGDKYV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1696 FNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNI-ERSLSLIVGEGQQARIVSYLQLTSGEELNEKA---VRTAL 1771
Cdd:cd05959 396 RDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVlEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALeeeLKEFV 475
|
490 500
....*....|....*....|....*...
gi 1725075560 1772 KARLPNIMIPSGFVVLSAFPLTNNNKID 1799
Cdd:cd05959 476 KDRLAPYKYPRWIVFVDELPKTATGKIQ 503
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1340-1798 |
4.94e-41 |
|
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: 158.01 E-value: 4.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1340 AVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQ 1418
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDrVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1419 ARLLVTDgepeqgwaspavgfdslvshpaaadalpipaDDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDF-VGRLALS 1497
Cdd:cd05919 83 ARLVVTS-------------------------------ADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1498 ARDKVLSLTSISFDiFGL--ELFCSLAGGAHVTLCPreTAMDPVKLYHFIERQQPSVIQATPTVWSTIVHhLPAASQRPL 1575
Cdd:cd05919 132 PGDRVFSSAKMFFG-YGLgnSLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLD-SCAGSPDAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1576 T----VLCGGEKMPAALLTQLRR-IATRVLQVYGPTET--TIWSTCADLTHEGASdciGTPIQATEVLVMDQAGNPLPSG 1648
Cdd:cd05919 208 RslrlCVSAGEALPRGLGERWMEhFGGPILDGIGATEVghIFLSNRPGAWRLGST---GRPVPGYEIRLVDEEGHTIPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1649 AFGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAEryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd05919 285 EEGDLLVRGPSAAVGYWNNPEKS------RATFNGG--WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1729 SSLDNIERSLSLIVGEGQQA-RIVSYLQLTSGEELNEKAVR---TALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd05919 357 IQHPAVAEAAVVAVPESTGLsRLTAFVVLKSPAAPQESLARdihRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
873-1286 |
5.83e-41 |
|
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: 157.62 E-value: 5.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRF--TETDGVAYQ--LAEPhtPI 948
Cdd:cd19532 1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQgvLASS--PL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 949 RLadHWVDGQTLS-AEKWVRQLCATPFDI----TARpplvLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNe 1023
Cdd:cd19532 79 RL--EHVQISDEAeVEEEFERLKNHVYDLesgeTMR----IVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1024 lddHHGLDAPQPQ-----IQTIDIVNSGIASpapADVAYWQQQLQDCRE----LDFPLDKPRPLMPTHAGERIHYQLQPD 1094
Cdd:cd19532 152 ---GQPLLPPPLQyldfaARQRQDYESGALD---EDLAYWKSEFSTLPEplplLPFAKVKSRPPLTRYDTHTAERRLDAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1095 VAGLLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGN 1174
Cdd:cd19532 226 LAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1175 MMETCIGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAilqN--AGDVCQQNLRDCTLHRLPLSSGFSMFDMTwnFSVE 1252
Cdd:cd19532 306 TRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFI---NyrQGVAESRPFGDCELEGEEFEDARTPYDLS--LDII 380
|
410 420 430
....*....|....*....|....*....|....*..
gi 1725075560 1253 QDA---VTIELDYASELFYPASMQMLLDNYQQTLRQL 1286
Cdd:cd19532 381 DNPdgdCLLTLKVQSSLYSEEDAELLLDSYVNLLEAF 417
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
875-1280 |
2.20e-40 |
|
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: 156.27 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLADHW 954
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 955 VDGQT---LSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDDHHGLD 1031
Cdd:cd20483 83 LSEAAdpeAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1032 A-PQPQIQTIDIV---NSGIASPA-PADVAYWQQQLQDCRE----LDFPLDKPRPLMPTHAGerIHYQ-LQPDVAGLLAS 1101
Cdd:cd20483 163 TvPPPPVQYIDFTlwhNALLQSPLvQPLLDFWKEKLEGIPDasklLPFAKAERPPVKDYERS--TVEAtLDKELLARMKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1102 RGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIG 1181
Cdd:cd20483 241 ICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1182 AYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAGDVCQQNLRDCTLHRLPLSSGFSMFDMtwNFSVEQDA---VTI 1258
Cdd:cd20483 321 AYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVHGKFPEYDTGDFKFTDYDHYDIPTACDI--ALEAEEDPdggLDL 398
|
410 420
....*....|....*....|..
gi 1725075560 1259 ELDYASELFYPASMQMLLDNYQ 1280
Cdd:cd20483 399 RLEFSTTLYDSADMERFLDNFV 420
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
310-770 |
9.36e-40 |
|
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: 154.54 E-value: 9.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADgQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:cd05919 5 YAAD-RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSplhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNH-RDFIGLAQ 468
Cdd:cd05919 84 RLVVTSA-------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 469 GSRVLAIASLGFD-AFGWDVYGALVSGATLYLAPSELHTDvgALHDYLTQHDIGHITITPAI------LELLPREMWPGL 541
Cdd:cd05919 133 GDRVFSSAKMFFGyGLGNSLWFPLAVGASAVLNPGWPTAE--RVLATLARFRPTVLYGVPTFyanlldSCAGSPDALRSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 542 RTMIVMGDAPPADVVAWWAERT--RLCNGYGPTEAS---IATSLCEYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFE 616
Cdd:cd05919 211 RLCVSAGEALPRGLGERWMEHFggPILDGIGATEVGhifLSNRPGAWRLG----STGRPVPGYEIRLVDEEGHTIPPGEE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 617 GELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAV 696
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSRATF----------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 697 RSHPLVESACVVARSQPSGKI-LAAFVQPASP----ELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05919 357 IQHPAVAEAAVVAVPESTGLSrLTAFVVLKSPaapqESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
312-772 |
3.03e-39 |
|
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: 153.21 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAAS-SVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPA 390
Cdd:cd05941 7 DDGDSITYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 391 LILadsplhsgdapciapssidyrslnihaeqlpqsRDALayVCYTSGTTGKPKGVMIgreglsnvaqNHRDfigLAQGS 470
Cdd:cd05941 87 LVL---------------------------------DPAL--ILYTSGTTGRPKGVVL----------THAN---LAANV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 471 RVLAiaslgfDAFGW---DVY-----------------GALVSGATLYLAPsELHTDVGALHDYLtqhdiGHITI---TP 527
Cdd:cd05941 119 RALV------DAWRWtedDVLlhvlplhhvhglvnallCPLFAGASVEFLP-KFDPKEVAISRLM-----PSITVfmgVP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 528 AI-------LELLPREMWP-------GLRTMiVMGDAP-PADVVAWWAERT--RLCNGYGPTEASIATSlCEY----RPG 586
Cdd:cd05941 187 TIytrllqyYEAHFTDPQFaraaaaeRLRLM-VSGSAAlPVPTLEEWEAITghTLLERYGMTEIGMALS-NPLdgerRPG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 587 VpwncIGKPLKNYRCHILD-LHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWD 665
Cdd:cd05941 265 T----VGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF---------TDDGWFKTGDLGVVD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 666 EQGNIIFVGR-RDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPAS--PELTIDALRHALVTL 741
Cdd:cd05941 332 EDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGERVVAVVVLRAgaAALSLEELKEWAKQR 411
|
490 500 510
....*....|....*....|....*....|.
gi 1725075560 742 LHPAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd05941 412 LAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
317-770 |
3.81e-39 |
|
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: 152.59 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 317 YSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLdpqapaarnqsilddvqpaliladS 396
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL------------------------F 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 397 PLHSGDApciapssIDYRSLNIHAEQL-PQSRDALAYVCYTSGTTGKPKGVMIGreglsnvaqnHRDFIGLAQGsrvlai 475
Cdd:cd05971 63 ALFGPEA-------LEYRLSNSGASALvTDGSDDPALIIYTSGTTGPPKGALHA----------HRVLLGHLPG------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 476 ASLGFDAF-----------GWDVYGALVSGatlyLAPSELHT-----------DVGALHDYLTQHDIGHITITPAILELL 533
Cdd:cd05971 120 VQFPFNLFprdgdlywtpaDWAWIGGLLDV----LLPSLYFGvpvlahrmtkfDPKAALDLMSRYGVTTAFLPPTALKMM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 534 -----PREMWPGLRTMIVMGDAPPADVVAWWAERT---RLCNGYGPTEASIATSLC----EYRPGvpwnCIGKPLKNYRC 601
Cdd:cd05971 196 rqqgeQLKHAQVKLRAIATGGESLGEELLGWAREQfgvEVNEFYGQTECNLVIGNCsalfPIKPG----SMGKPIPGHRV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 602 HILDLHHNPLPVGFEGELCI--AGSGLAHGYLHQEALSAEKFIicrlpymaaeERLYRTGDIAKWDEQGNIIFVGRRDHQ 679
Cdd:cd05971 272 AIVDDNGTPLPPGEVGEIAVelPDPVAFLGYWNNPSATEKKMA----------GDWLLTGDLGRKDSDGYFWYVGRDDDV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 680 VKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFVQPASPELTIDALRHAL----VTLLHPAAIPSVFIFL 754
Cdd:cd05971 342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPiRGEIVKAFVVLNPGETPSDALAREIqelvKTRLAAHEYPREIEFV 421
|
490
....*....|....*.
gi 1725075560 755 PALPLTINGKIARQQL 770
Cdd:cd05971 422 NELPRTATGKIRRREL 437
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
312-765 |
6.53e-39 |
|
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: 153.14 E-value: 6.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPAL 391
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 392 ILAD------------------------SPLHSGDAPCIAPSSIDYRSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVM 447
Cdd:cd05911 86 IFTDpdglekvkeaakelgpkdkiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 448 IGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFD-AFG-WDVYGALVSGATLYLAPselHTDVGALHDYLTQHDIGHITI 525
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhIYGlFTTLASLLNGATVIIMP---KFDSELFLDLIEKYKITFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 526 TPAILELL------PREMWPGLRTMIVMGDAPPADVVAWWAER---TRLCNGYGPTEASIATSLCEYRPGVPwNCIGKPL 596
Cdd:cd05911 243 VPPIAAALakspllDKYDLSSLRVILSGGAPLSKELQELLAKRfpnATIKQGYGMTETGGILTVNPDGDDKP-GSVGRLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 597 KNYRCHILDLHHNP-LPVGFEGELCIAGSGLAHGYLHQEALSAEkfiicrlpyMAAEERLYRTGDIAKWDEQGNIIFVGR 675
Cdd:cd05911 322 PNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKE---------TFDEDGWLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 676 RDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFVQPA-SPELTIDALRHALVTLLHPAA--IPSVF 751
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEvSGELPRAYVVRKpGEKLTEKEVKDYVAKKVASYKqlRGGVV 472
|
490
....*....|....
gi 1725075560 752 iFLPALPLTINGKI 765
Cdd:cd05911 473 -FVDEIPKSASGKI 485
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1330-1803 |
1.14e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 153.14 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLridsrpfSVGVmmEKSCHVAVLL----------LGVLRAGKHYV 1399
Cdd:PRK07656 13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALA-------ALGI--GKGDRVAIWApnsphwviaaLGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1400 PIDVHYPADRVSYMIENAQARLLVTDG----------------------EPEQGWASPAVG--FDSLVSHPAAADALPIP 1455
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGlflgvdysattrlpalehvvicETEEDDPHTEKMktFTDFLAAGDPAERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 ADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGLE--LFCSLAGGAHVTLCPRe 1533
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPF-FHVFGYKagVNAPLMRGATILPLPV- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1534 taMDPVKLYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLTVLC----GGEKMPAALLTQLR---RIATrVLQVYGPT 1606
Cdd:PRK07656 242 --FDPDEVFRLIETERITVLPGPPTMYNSLLQH-PDRSAEDLSSLRlavtGAASMPVALLERFEselGVDI-VLTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1607 E----TTIwstC-ADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSdkvflrRQAF 1681
Cdd:PRK07656 318 EasgvTTF---NrLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEAT------AAAI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1682 GAERYMYrTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNI----------ERslsliVGEGQQARIV 1751
Cdd:PRK07656 389 DADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVaeaavigvpdER-----LGEVGKAYVV 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 1752 sylqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK07656 463 ----LKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
314-772 |
2.15e-38 |
|
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: 152.24 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:TIGR03098 23 DRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSP----LHSGDAPC-------------------IAPSSIDYRSLNIHAEQLPQSR---DALAYVCYTSGTTGKPKGVM 447
Cdd:TIGR03098 103 TSSErldlLHPALPGChdlrtliivgdpahaseghPGEEPASWPKLLALGDADPPHPvidSDMAAILYTSGSTGRPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 448 IGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATL----YLAPSELHTDVgalhdylTQHDIGHI 523
Cdd:TIGR03098 183 LSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhdYLLPRDVLKAL-------EKHGITGL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 524 TITPAILELLPREMWP-----GLRTMIVMGDAPPADVVAwwAERTRLCNG-----YGPTEASIATSL----CEYRPGvpw 589
Cdd:TIGR03098 256 AAVPPLWAQLAQLDWPesaapSLRYLTNSGGAMPRATLS--RLRSFLPNArlflmYGLTEAFRSTYLppeeVDRRPD--- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 590 nCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKF--IICRLPYMAAEERLYRTGDIAKWDEQ 667
Cdd:TIGR03098 331 -SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrpLPPFPGELHLPELAVWSGDTVRRDEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 668 GNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFVQP-----ASPELTIDALRHALVTL 741
Cdd:TIGR03098 410 GFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPtLGQAIVLVVTPpggeeLDRAALLAECRARLPNY 489
|
490 500 510
....*....|....*....|....*....|.
gi 1725075560 742 LHPAAIpsvfIFLPALPLTINGKIARQQLEK 772
Cdd:TIGR03098 490 MVPALI----HVRQALPRNANGKIDRKALAK 516
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1324-1803 |
5.87e-38 |
|
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: 150.86 E-value: 5.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1324 LLMHIGRLAhtqPDSLAVSC----ERQQYSYRQLWAQSERVAHALLRI----DSRpfsVGVMMEKSCHVAVLLLGVLRAG 1395
Cdd:cd12119 1 LLEHAARLH---GDREIVSRthegEVHRYTYAEVAERARRLANALRRLgvkpGDR---VATLAWNTHRHLELYYAVPGMG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1396 KHYVPIDVHYPADRVSYMIENAQARLLVTDGEPEQ-GWAS----PAVGFDSLVSHPAAADALPIP--------------- 1455
Cdd:cd12119 75 AVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFLPlLEAIaprlPTVEHVVVMTDDAAMPEPAGVgvlayeellaaespe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 -----ADDTLAYIM-YTSGSTGNPKGVMITH-----GNLNNFTNDFVGrlaLSARDKVLSLTSIsFDI--FGLELFCSLA 1522
Cdd:cd12119 155 ydwpdFDENTAAAIcYTSGTTGNPKGVVYSHrslvlHAMAALLTDGLG---LSESDVVLPVVPM-FHVnaWGLPYAAAMV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1523 GGAHVTLCPRetaMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPLT---VLCGGEKMPAALLTQLRRIATRV 1599
Cdd:cd12119 231 GAKLVLPGPY---LDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSlrrVVIGGSAVPRSLIEAFEERGVRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1600 LQVYGPTETTIWSTCADLTHEGASDCI----------GTPIQATEVLVMDQAGNPLPS--GAFGELWLGGAGVSPGYWRN 1667
Cdd:cd12119 308 IHAWGMTETSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1668 PtlSDKVFLRRQAFgaerymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIelseidlslSSLDnIERSLSL------- 1740
Cdd:cd12119 388 D--EESEALTEDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWI---------SSVE-LENAIMAhpavaea 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1741 -IVG---EGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd12119 450 aVIGvphPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1346-1798 |
3.55e-37 |
|
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: 147.74 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVT 1424
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDvVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1425 DGE---------------------PEQGWASPAVGFDSLVSHPAAADALPIP---ADDTLAYIMYTSGSTGNPKGVMITH 1480
Cdd:cd05911 89 DPDglekvkeaakelgpkdkiivlDDKPDGVLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1481 GNL---NNFTNDFVGrLALSARDKVLSLTSIsFDIFGL-ELFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQAT 1556
Cdd:cd05911 169 RNLianLSQVQTFLY-GNDGSNDVILGFLPL-YHIYGLfTTLASLLNGATVIIMPK---FDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1557 PTVWSTIVHH--LPAASQRPL-TVLCGGekmpAALLTQL------RRIATRVLQVYGPTETTIwSTCADLTHEGASDCIG 1627
Cdd:cd05911 244 PPIAAALAKSplLDKYDLSSLrVILSGG----APLSKELqellakRFPNATIKQGYGMTETGG-ILTVNPDGDDKPGSVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1628 TPIQATEVLVMDQAGNP-LPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgAERYMYRTGDIVRFNRQGQLEYLG 1706
Cdd:cd05911 319 RLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETF-------DEDGWLHTGDIGYFDEDGYLYIVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1707 RNDHQVKIRGHRIELSEIDLSLSSLDNI----------ERSlslivGEGQQARIVsylqLTSGEELNEKAVRTALKARLP 1776
Cdd:cd05911 392 RKKELIKYKGFQVAPAELEAVLLEHPGVadaavigipdEVS-----GELPRAYVV----RKPGEKLTEKEVKDYVAKKVA 462
|
490 500
....*....|....*....|...
gi 1725075560 1777 NI-MIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd05911 463 SYkQLRGGVVFVDEIPKSASGKI 485
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1337-1803 |
6.25e-37 |
|
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: 146.28 E-value: 6.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1337 DSLAVSCERQQYSYRQLWAQSERVAHALLRIDS--RPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKdlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDgepeqgwaspavgfdslvshpaaadalpipaddtlAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL 1494
Cdd:cd05941 81 TDSEPSLVLDP-----------------------------------ALILYTSGTTGRPKGVVLTHANLAANVRALVDAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1495 ALSARDKVLSLTSIsFDIFGL--ELFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQATPTVWSTIV----HHLP 1568
Cdd:cd05941 126 RWTEDDVLLHVLPL-HHVHGLvnALLCPLFAGASVEFLPK---FDPKEVAISRLMPSITVFMGVPTIYTRLLqyyeAHFT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1569 ------AASQRPLTVL-CGGEKMPAALLTQLRRI-ATRVLQVYGPTETTIWSTCAdLTHEGASDCIGTPIQATEV-LVMD 1639
Cdd:cd05941 202 dpqfarAAAAERLRLMvSGSAALPVPTLEEWEAItGHTLLERYGMTEIGMALSNP-LDGERRPGTVGMPLPGVQArIVDE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1640 QAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKvflrrqAFGAERYmYRTGDIVRFNRQGQLEYLGR-NDHQVKIRGHR 1718
Cdd:cd05941 281 ETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKE------EFTDDGW-FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1719 IELSEIDLSLSSLDNIerSLSLIVGE-----GQqaRIVSYLQLTSGEE-LNEKAVRTALKARLPNIMIPSGFVVLSAFPL 1792
Cdd:cd05941 354 VSALEIERVLLAHPGV--SECAVIGVpdpdwGE--RVVAVVVLRAGAAaLSLEELKEWAKQRLAPYKRPRRLILVDELPR 429
|
490
....*....|.
gi 1725075560 1793 TNNNKIDIRRL 1803
Cdd:cd05941 430 NAMGKVNKKEL 440
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
316-772 |
9.73e-37 |
|
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: 145.60 E-value: 9.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 316 TYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVlldPQAPAARNQS---ILDDVQPALI 392
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTN---PILPFFREHElafILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 ladsplhsgdapcIAPSSidYRSLNIhaEQLPqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd05903 78 -------------VVPER--FRQFDP--AAMP---DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLG-FDAFGWDVYGALVSGATLYLAPSELHTDVGALhdyLTQHDIGHITITPAILELLPR------EMWPGLRTMI 545
Cdd:cd05903 138 LVASPMAhQTGFVYGFTLPLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNaveeagEPLSRLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 546 VMGDAPPADVVAWWAER--TRLCNGYGPTEASIATSLCE-YRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIA 622
Cdd:cd05903 215 CGGATVPRSLARRAAELlgAKVCSAYGSTECPGAVTSITpAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 623 GSGLAHGYLHQEALSAEkfiicrlpymAAEERLYRTGDIAKWDEQGNIIFVGR-RDhqVKIR-GVRIEMGEVESAVRSHP 700
Cdd:cd05903 295 GPSVFLGYLDRPDLTAD----------AAPEGWFRTGDLARLDEDGYLRITGRsKD--IIIRgGENIPVLEVEDLLLGHP 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 701 LVESACVVARS-QPSGKILAAFVQPASP-ELTIDALRHALvtLLHPAA---IPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd05903 363 GVIEAAVVALPdERLGERACAVVVTKSGaLLTFDELVAYL--DRQGVAkqyWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
310-770 |
4.57e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 145.33 E-value: 4.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:PRK06187 25 VYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAED 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADS---PL-----------------HSGDAPCIAPSSIDYRS-LNIHAEQLPQ---SRDALAYVCYTSGTTGKPKG 445
Cdd:PRK06187 105 RVVLVDSefvPLlaailpqlptvrtviveGDGPAAPLAPEVGEYEElLAAASDTFDFpdiDENDAAAMLYTSGTTGHPKG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 446 VMIG-REGLSNVAQNHRdFIGLAQGSRVLAIASLgFDAFGWDV-YGALVSGATLYLAPselHTDVGALHDYLTQHDIGHI 523
Cdd:PRK06187 185 VVLShRNLFLHSLAVCA-WLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVIPR---RFDPENLLDLIETERVTFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 524 TITPAIL-----ELLPREMW-PGLRTMIVMGDAPPADVVAWWAER--TRLCNGYGPTEASIATSLCEYRPGVPWNC---- 591
Cdd:PRK06187 260 FAVPTIWqmllkAPRAYFVDfSSLRLVIYGGAALPPALLREFKEKfgIDLVQGYGMTETSPVVSVLPPEDQLPGQWtkrr 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 592 -IGKPLKNYRCHILDLHHNPLPVGFE--GELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQG 668
Cdd:PRK06187 340 sAGRPLPGVEARIVDDDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETI----------DGGWLHTGDVGYIDEDG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 669 NIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFVQPAsPELTIDA--LRHALVTLLHPA 745
Cdd:PRK06187 410 YLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEkWGERPVAVVVLK-PGATLDAkeLRAFLRGRLAKF 488
|
490 500
....*....|....*....|....*
gi 1725075560 746 AIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK06187 489 KLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1345-1804 |
4.79e-36 |
|
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: 143.20 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1345 RQQYSYRQLWAQSERVAHALL-RIDSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLV 1423
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAaLGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1424 TDgepeqgwaspavgfdslvshpaaadalpipaddtLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDkVL 1503
Cdd:cd05934 81 VD----------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDD-VY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1504 sLTSisfdifgLELF----------CSLAGGAHVTLCPRETAMdpvKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQR 1573
Cdd:cd05934 126 -LTV-------LPLFhinaqavsvlAALSVGATLVLLPRFSAS---RFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1574 --PLTVLCGGEKMPAALLTQLRRIATRVLQVYGPTETTIwSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFG 1651
Cdd:cd05934 195 ahRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIV-GVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1652 ELWL---GGAGVSPGYWRNPTLSDKVFlrrqafgaERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd05934 274 ELVIrglRGWGFFKGYYNMPEATAEAM--------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1729 SSLDNIERSL-----SLIVGEgqqaRIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05934 346 LRHPAVREAAvvavpDEVGED----EVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
.
gi 1725075560 1804 P 1804
Cdd:cd05934 422 R 422
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
315-771 |
8.76e-36 |
|
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: 144.58 E-value: 8.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPA--LI 392
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRglIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSPLHSGdapciapssidyrslnihaeqlPQSRDALAYvcyTSGTTGKPKGVMiGRE-GLSNVAQNHRDFIGLAQGSR 471
Cdd:cd17647 99 IRAAGVVVG----------------------PDSNPTLSF---TSGSEGIPKGVL-GRHfSLAYYFPWMAKRFNLSENDK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 472 VLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGALHDYLTQHDIGHITITPAILELL---PREMWPGLRTMIVMG 548
Cdd:cd17647 153 FTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLtaqATTPFPKLHHAFFVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 549 DA-PPADVVAW--WAERTRLCNGYGPTEASIATSLCEYR-----PGVPWNC-----IGKPLKNYRCHILDLHHNP--LPV 613
Cdd:cd17647 233 DIlTKRDCLRLqtLAENVRIVNMYGTTETQRAVSYFEVPsrssdPTFLKNLkdvmpAGRGMLNVQLLVVNRNDRTqiCGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 614 GFEGELCIAGSGLAHGYLHQEALSAEKFIIC-------------------RLPYMAAEERLYRTGDIAKWDEQGNIIFVG 674
Cdd:cd17647 313 GEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwRQFWLGPRDRLYRTGDLGRYLPNGDCECCG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 675 RRDHQVKIRGVRIEMGEVESAVRSHPLV-ESACVVARSQPSGKILAAFV--QPASPELT--------------------- 730
Cdd:cd17647 393 RADDQVKIRGFRIELGEIDTHISQHPLVrENITLVRRDKDEEPTLVSYIvpRFDKPDDEsfaqedvpkevstdpivkgli 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1725075560 731 -----IDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLE 771
Cdd:cd17647 473 gyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
313-770 |
2.02e-35 |
|
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: 143.28 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDD------ 386
Cdd:cd05959 26 DAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDsrarvv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 387 ---------VQPALILADSPLH----SGDAPCIAPSSIDYRSLNIHAEQLPQ---SRDALAYVCYTSGTTGKPKGVMIGR 450
Cdd:cd05959 106 vvsgelapvLAAALTKSEHTLVvlivSGGAGPEAGALLLAELVAAEAEQLKPaatHADDPAFWLYSSGSTGRPKGVVHLH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 451 EGLSNVAQNH-RDFIGLAQGSRVLAIASLGFD-AFGWDVYGALVSGATLYLAPSELHTDvgALHDYLTQHD----IGHIT 524
Cdd:cd05959 186 ADIYWTAELYaRNVLGIREDDVCFSAAKLFFAyGLGNSLTFPLSVGATTVLMPERPTPA--AVFKRIRRYRptvfFGVPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 525 ITPAIL--ELLPREMWPGLRTMIVMGDAPPADVVAWWAERTRL--CNGYGPTEA-SIatsLCEYRPG-VPWNCIGKPLKN 598
Cdd:cd05959 264 LYAAMLaaPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLdiLDGIGSTEMlHI---FLSNRPGrVRYGTTGKPVPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 599 YRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDH 678
Cdd:cd05959 341 YEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF----------QGEWTRTGDKYVRDDDGFYTYAGRADD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 679 QVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSGKI-LAAFVQPAS----PELTIDALRHALVTLLHPAAIPSVFIF 753
Cdd:cd05959 411 MLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTkPKAFVVLRPgyedSEALEEELKEFVKDRLAPYKYPRWIVF 490
|
490
....*....|....*..
gi 1725075560 754 LPALPLTINGKIARQQL 770
Cdd:cd05959 491 VDELPKTATGKIQRFKL 507
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
314-772 |
2.05e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 144.03 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 A---------------------------------DSPLHSG-DAPCIAPSS-IDY----RSLNIHAEQLPQSRDALAYVC 434
Cdd:PRK06178 136 AldqlapvveqvraetslrhvivtsladvlpaepTLPLPDSlRAPRLAAAGaIDLlpalRACTAPVPLPPPALDALAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMigreglsnvaQNHRDFIGLAQGSRVLAIA------SLGFDAFGW---DVYGALV---SGATLYL--- 499
Cdd:PRK06178 216 YTGGTTGMPKGCE----------HTQRDMVYTAAAAYAVAVVggedsvFLSFLPEFWiagENFGLLFplfSGATLVLlar 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 --------APSELHTDVGAL----------HDYLTQHDIGHITITPA---ILELLP--REMWPGLrTMIVMGDAppadvv 556
Cdd:PRK06178 286 wdavafmaAVERYRVTRTVMlvdnavelmdHPRFAEYDLSSLRQVRVvsfVKKLNPdyRQRWRAL-TGSVLAEA------ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 557 AWWAERTRLCNGYgptEASIATSLCEYRpGVPWNCiGKPLKNYRCHILDLH-HNPLPVGFEGELCIAGSGLAHGYLHQEA 635
Cdd:PRK06178 359 AWGMTETHTCDTF---TAGFQDDDFDLL-SQPVFV-GLPVPGTEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 636 LSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-S 714
Cdd:PRK06178 434 ATAEAL----------RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPdK 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 715 GKILAAFVQPAsPELTIDA--LRHALVTLLHPAAIPSVFIfLPALPLTINGKIARQQLEK 772
Cdd:PRK06178 504 GQVPVAFVQLK-PGADLTAaaLQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDLQA 561
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
873-1290 |
4.67e-35 |
|
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: 140.20 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLad 952
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 953 HWVDGQT-----LSAEKWVRQLCATPFDItARPPLV-LRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDD 1026
Cdd:cd19533 79 RHIDLSGdpdpeGAAQQWMQEDLRKPLPL-DNDPLFrHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1027 hhGLDAP-QPQIQTIDIVNSGIA---SPAPA-DVAYWQQQLQDCRELdfPLDKPRPLMPTHAGERIHYQLQPDVAGLLAS 1101
Cdd:cd19533 158 --GRPAPpAPFGSFLDLVEEEQAyrqSERFErDRAFWTEQFEDLPEP--VSLARRAPGRSLAFLRRTAELPPELTRTLLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1102 RGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIG 1181
Cdd:cd19533 234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1182 AYQHQQLSFDRILHQIEYERMSNK--NPLFQIMAILQnagdvcQQNLRDCTLHRLPLSSGfSMFDMTWNFSVEQD--AVT 1257
Cdd:cd19533 314 LLRHQRYRYEDLRRDLGLTGELHPlfGPTVNYMPFDY------GLDFGGVVGLTHNLSSG-PTNDLSIFVYDRDDesGLR 386
|
410 420 430
....*....|....*....|....*....|...
gi 1725075560 1258 IELDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19533 387 IDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
875-1290 |
1.45e-34 |
|
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: 138.88 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSP-QQNLLwYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDG---VAYQLAEPHTPIRL 950
Cdd:cd19543 3 PLSPmQEGML-FHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLgepLQVVLKDRKLPWRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 951 ADhWVDGQTLSAEKWVRQLCAT----PFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDD 1026
Cdd:cd19543 82 LD-LSHLSEAEQEAELEALAEEdrerGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1027 --HHGLDAPQPQIQTIDIVNSGIASPApadVAYWQQQLQDCRELD-FPLDKPRPLMPTHAGERIHYQLQPDVAGLLASRG 1103
Cdd:cd19543 161 gqPPSLPPVRPYRDYIAWLQRQDKEAA---EAYWREYLAGFEEPTpLPKELPADADGSYEPGEVSFELSAELTARLQELA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1104 KALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARD-NLD--QTQVsGFHVNTVPLRIQLSEQDTLAGLIGNMMETCI 1180
Cdd:cd19543 238 RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPaELPgiETMV-GLFINTLPVRVRLDPDQTVLELLKDLQAQQL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1181 GAYQHQQLSFDRILHQIEyermsNKNPLFQIMAILQNAGDvcQQNLRDCTlHRLPLS-SGFSMFDMT-WNFSV---EQDA 1255
Cdd:cd19543 317 ELREHEYVPLYEIQAWSE-----GKQALFDHLLVFENYPV--DESLEEEQ-DEDGLRiTDVSAEEQTnYPLTVvaiPGEE 388
|
410 420 430
....*....|....*....|....*....|....*
gi 1725075560 1256 VTIELDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19543 389 LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1348-1798 |
3.09e-34 |
|
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: 137.90 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTDG 1426
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDvVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1427 EPEQgwaspavgfdslvshpaaADALPIPADdtLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLT 1506
Cdd:cd05903 82 RFRQ------------------FDPAAMPDA--VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVAS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1507 SISFDI-FGLELFCSLAGGAHVTLCPRETAMDPVKLyhfIERQQPSVIQATPTVWSTIVHHLPAASQRP---LTVLCGGE 1582
Cdd:cd05903 142 PMAHQTgFVYGFTLPLLLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNAVEEAGEPLsrlRTFVCGGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1583 KMPAALLTQL-RRIATRVLQVYGPTETTIWSTCADLTHEGASDCI-GTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGV 1660
Cdd:cd05903 219 TVPRSLARRAaELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTdGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1661 SPGYWRNPTLSdkvflrrqAFGAERYMYRTGDIVRFNRQGQLEYLGRNdHQVKIRGHR----IELSEIDLSLSSLDNI-- 1734
Cdd:cd05903 299 FLGYLDRPDLT--------ADAAPEGWFRTGDLARLDEDGYLRITGRS-KDIIIRGGEnipvLEVEDLLLGHPGVIEAav 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1735 -----ERslsliVGEgqqaRIVSYLQLTSGEELNEKAVRTAL-KARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd05903 370 valpdER-----LGE----RACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
873-1290 |
4.00e-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: 137.45 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQLAEPHTPIRLAD 952
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 953 hwVDGQTLSAEK---WVRQLCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELddhhg 1029
Cdd:cd20484 81 --EDISSLKESEiiaYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQAL----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1030 LDAPQPQIQT--------IDIVNSGIASP-APADVAYWQQQLQ-DCRELDFPLDKPRPLMPTHAGERIHYQLQPDVAGLL 1099
Cdd:cd20484 154 LQGKQPTLASspasyydfVAWEQDMLAGAeGEEHRAYWKQQLSgTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1100 ASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETC 1179
Cdd:cd20484 234 KSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1180 IGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQN---AGDVcQQNLRDCTlhrlplsSGFSM-----------FDM 1245
Cdd:cd20484 314 LDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNflqSTSL-QQFLAEYQ-------DVLSIefvegihqegeYEL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1725075560 1246 TWNFSVEQDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd20484 386 VLEVYEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
316-856 |
4.58e-34 |
|
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: 144.05 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 316 TYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARnQSILDDVQ------- 388
Cdd:TIGR03443 270 SFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR-QTIYLSVAkpraliv 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 389 -------------------------PALILADS------PLHSGDAPCIAPSsidyrslnihaEQLPQSR-------DAL 430
Cdd:TIGR03443 349 iekagtldqlvrdyidkelelrteiPALALQDDgslvggSLEGGETDVLAPY-----------QALKDTPtgvvvgpDSN 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 431 AYVCYTSGTTGKPKGVMiGReglsnvaqnH-----------RDFiGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYL 499
Cdd:TIGR03443 418 PTLSFTSGSEGIPKGVL-GR---------HfslayyfpwmaKRF-GLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLV 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 APSElhtDVGA---LHDYLTQHDIGHITITPAILELL---PREMWPGLRTMIVMGDA-PPADVVAW--WAERTRLCNGYG 570
Cdd:TIGR03443 487 PTAD---DIGTpgrLAEWMAKYGATVTHLTPAMGQLLsaqATTPIPSLHHAFFVGDIlTKRDCLRLqtLAENVCIVNMYG 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 571 PTEASIATSLCEYRPG-------------VPwncIGKPLKNYRCHILDLHHNPLP--VGFEGELCIAGSGLAHGYLHQEA 635
Cdd:TIGR03443 564 TTETQRAVSYFEIPSRssdstflknlkdvMP---AGKGMKNVQLLVVNRNDRTQTcgVGEVGEIYVRAGGLAEGYLGLPE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 636 LSAEKFII-------------------CRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAV 696
Cdd:TIGR03443 641 LNAEKFVNnwfvdpshwidldkennkpEREFWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHL 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 697 RSHPLV-ESACVVARSQPSGKILAAFV--QPASPELT-------------------------IDALRHALVTLLHPAAIP 748
Cdd:TIGR03443 721 SQHPLVrENVTLVRRDKDEEPTLVSYIvpQDKSDELEefksevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIP 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 749 SVFIFLPALPLTINGKIAR--------QQLEKWPLDERNERLTPPETETEAILERIVANAIGCPQADVTQE--FINLGAH 818
Cdd:TIGR03443 801 TVIVPLKKLPLNPNGKVDKpalpfpdtAQLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDdsFFDLGGH 880
|
650 660 670
....*....|....*....|....*....|....*...
gi 1725075560 819 SLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYIE 856
Cdd:TIGR03443 881 SILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVD 918
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1336-1806 |
9.12e-34 |
|
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: 138.42 E-value: 9.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAV-------SCERQQYSYRQLWAQSERVAHALLRIDSRPFSVgVMMEKSCHV--AVLLLGVLRAGKHYVPIDVHYP 1406
Cdd:cd17647 2 PERTCVvetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDV-VMIYSYRGVdlMVAVMGVLKAGATFSVIDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1407 ADRVSYMIENAQARLLVTDGEpeqgwASPAVGFDSlvshpaaadalpIPaddTLAYimyTSGSTGNPKGVMITHGNLNNF 1486
Cdd:cd17647 81 PARQNIYLGVAKPRGLIVIRA-----AGVVVGPDS------------NP---TLSF---TSGSEGIPKGVLGRHFSLAYY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 TNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQpsviqatptvwSTIVHH 1566
Cdd:cd17647 138 FPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYG-----------ATVTHL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1567 LPAASQrpltVLCGGEKMPAA----------LLTQ--LRRIAT-----RVLQVYGPTETT-------IWSTCADLTH-EG 1621
Cdd:cd17647 207 TPAMGQ----LLTAQATTPFPklhhaffvgdILTKrdCLRLQTlaenvRIVNMYGTTETQravsyfeVPSRSSDPTFlKN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1622 ASDCI--GTPIQATEVLVMDQ--AGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFL--------------------- 1676
Cdd:cd17647 283 LKDVMpaGRGMLNVQLLVVNRndRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvepdhwnyldkdnnepw 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1677 RRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLI-VGEGQQARIVSYL- 1754
Cdd:cd17647 363 RQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVrRDKDEEPTLVSYIv 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 1755 -QLTSGEELNE-------------------------KAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAP 1806
Cdd:cd17647 443 pRFDKPDDESFaqedvpkevstdpivkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1348-1702 |
1.01e-33 |
|
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: 138.14 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLRIDSRPFSVGVMMEKSC-HVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTDG 1426
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSiEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1427 EPE---QGWASPAVGFDSLVSHPAAADAL------------PIPADDTLAyIMYTSGSTGNPKGVMITHGNLNNFTNDFV 1491
Cdd:cd05904 113 ELAeklASLALPVVLLDSAEFDSLSFSDLlfeadeaeppvvVIKQDDVAA-LLYSSGTTGRSKGVMLTHRNLIAMVAQFV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1492 -GRLALSARDKVLSLTSISFDIFGLELF--CSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQATPTVWSTIVHHlP 1568
Cdd:cd05904 192 aGEGSNSDSEDVFLCVLPMFHIYGLSSFalGLLRLGATVVVMPR---FDLEELLAAIERYKVTHLPVVPPIVLALVKS-P 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1569 AASQRPL----TVLCGGEKMPAALLTQLRRI--ATRVLQVYGPTETT--IWSTCADLTHEGASDCIGTPIQATEVLVMD- 1639
Cdd:cd05904 268 IVDKYDLsslrQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDp 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 1640 QAGNPLPSGAFGELWLGGAGVSPGYWRNP-----TLSDKVFLrrqafgaerymyRTGDIVRFNRQGQL 1702
Cdd:cd05904 348 ETGESLPPNQTGELWIRGPSIMKGYLNNPeataaTIDKEGWL------------HTGDLCYIDEDGYL 403
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
317-772 |
1.45e-33 |
|
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: 136.11 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 317 YSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLL----DPQAPAARnqsiLDDVQPALI 392
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGPKAIEHR----LRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADsplhsgdapciapssidyrslnihAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd05973 77 VTD------------------------AANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLGFdAFG--WDVYGALVSG--ATLYLAPselhTDVGALHDYLTQHDIGHITITPAILELL-----PREMWPGLRT 543
Cdd:cd05973 133 WNAADPGW-AYGlyYAITGPLALGhpTILLEGG----FSVESTWRVIERLGVTNLAGSPTAYRLLmaagaEVPARPKGRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 544 MIVMGDAPP--ADVVAWWAER--TRLCNGYGPTEAS--IATSLCEYRPgVPWNCIGKPLKNYRCHILDLHHNPLPVGFEG 617
Cdd:cd05973 208 RRVSSAGEPltPEVIRWFDAAlgVPIHDHYGQTELGmvLANHHALEHP-VHAGSAGRAMPGWRVAVLDDDGDELGPGEPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 618 ELCI--AGSGLA--HGYLHQealsaekfiicrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVE 693
Cdd:cd05973 287 RLAIdiANSPLMwfRGYQLP-------------DTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 694 SAVRSHPLVESACVVARSQP-SGKILAAFV-----QPASPELTiDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:cd05973 354 SALIEHPAVAEAAVIGVPDPeRTEVVKAFVvlrggHEGTPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
....*
gi 1725075560 768 QQLEK 772
Cdd:cd05973 433 FLLRR 437
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1330-1803 |
1.59e-33 |
|
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: 137.97 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGkhYVPIDVhYPAD 1408
Cdd:COG1021 33 RRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDrVVVQLPNVAEFVIVFFALFRAG--AIPVFA-LPAH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 R---VSYMIENAQARLLVTDGEPEQ-----------------------GWASPAVGFDSLVSHPAAADALPIPADDtLAY 1462
Cdd:COG1021 110 RraeISHFAEQSEAVAYIIPDRHRGfdyralarelqaevpslrhvlvvGDAGEFTSLDALLAAPADLSEPRPDPDD-VAF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 IMYTSGSTGNPKGVMITHgnlnnftNDF-------VGRLALSARDKVL-------SLTSISFDIFGlelfcSLAGGAHVT 1528
Cdd:COG1021 189 FQLSGGTTGLPKLIPRTH-------DDYlysvrasAEICGLDADTVYLaalpaahNFPLSSPGVLG-----VLYAGGTVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1529 LCPRETAMDPVKLyhfIERQQPSVIQATPTVWSTIVHHLPAASQRP--LTVLC-GGEKMPAALLtqlRRIAT----RVLQ 1601
Cdd:COG1021 257 LAPDPSPDTAFPL---IERERVTVTALVPPLALLWLDAAERSRYDLssLRVLQvGGAKLSPELA---RRVRPalgcTLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1602 VYG-------------PTETTIwstcadlthegasDCIGTPI-QATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRN 1667
Cdd:COG1021 331 VFGmaeglvnytrlddPEEVIL-------------TTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1668 PTLSdkvflrRQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVkIR-GHRIELSEIDLSLSSLDNIeRSLSLI----- 1741
Cdd:COG1021 398 PEHN------ARAFTPDGF-YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAV-HDAAVVampde 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1742 -VGEgqqaRIVSYLQLTsGEELNEKAVRTALKAR-LPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:COG1021 469 yLGE----RSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1344-1707 |
1.72e-33 |
|
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: 136.19 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1344 ERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIdvhYP---ADRVSYMIENAQA 1419
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDrVAILSRNRPEWTIADLAILAIGAVPVPI---YPtssAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1420 RLLVtdgepeqgwaspavgfdslVSHPaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSAR 1499
Cdd:cd05907 79 KALF-------------------VEDP-----------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1500 DKVLSL--TSISFDIFGLELFCsLAGGAHVTLCPRETAMDPVklyhfIERQQPSVIQATPTVW----STIVHHLPAASQR 1573
Cdd:cd05907 129 DRHLSFlpLAHVFERRAGLYVP-LLAGARIYFASSAETLLDD-----LSEVRPTVFLAVPRVWekvyAAIKVKAVPGLKR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1574 PL----------TVLCGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTCADLTHEGAsDCIGTPIQATEVLVMDQagn 1643
Cdd:cd05907 203 KLfdlavggrlrFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRI-GTVGKPLPGVEVRIADD--- 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1644 plpsgafGELWLGGAGVSPGYWRNPTLSDKVFLRRQAFgaerymyRTGDIVRFNRQGQLEYLGR 1707
Cdd:cd05907 279 -------GEILVRGPNVMLGYYKNPEATAEALDADGWL-------HTGDLGEIDEDGFLHITGR 328
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1332-1803 |
4.40e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 135.78 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHAL--LRIdSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADR 1409
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLhaRGI-GQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1410 VSYMIENAQARLLVTDGEPEqgwASPAVGFDSLVSHPAA--------ADALPIP-----ADDTLAYIMYTSGSTGNPKGV 1476
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFD---AIVALETPKIVIDAAAqadsrrlaQGGLEIPpqaavAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1477 MITHGNLNNFTNDFVGRLALSARDKVLSLTSI----SFDIFGLELfcsLAGGAhvTLCPrETAMDPVKLYHFIERQQPSV 1552
Cdd:PRK06145 168 MHSYGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGG--TLRI-HREFDPEAVLAAIERHRLTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1553 IQATPTVWSTIVhHLPAASQRPLT----VLCGGEKMPAALLTQLRRIAT--RVLQVYGPTETTIWSTCADLTHEgaSDCI 1626
Cdd:PRK06145 242 AWMAPVMLSRVL-TVPDRDRFDLDslawCIGGGEKTPESRIRDFTRVFTraRYIDAYGLTETCSGDTLMEAGRE--IEKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1627 GTPIQA---TEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqaFGAeryMYRTGDIVRFNRQGQLE 1703
Cdd:PRK06145 319 GSTGRAlahVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-----YGD---WFRSGDVGYLDEEGFLY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1704 YLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQA-RIVSYLQLTSGEELNEKAVRTALKARLPNIMIPS 1782
Cdd:PRK06145 391 LTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGeRITAVVVLNPGATLTLEALDRHCRQRLASFKVPR 470
|
490 500
....*....|....*....|.
gi 1725075560 1783 GFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK06145 471 QLKVRDELPRNPSGKVLKRVL 491
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1345-1802 |
6.03e-33 |
|
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: 134.48 E-value: 6.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1345 RQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLV 1423
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDrVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1424 TDGepeqgwaspavgfdslvshpaaadalpipADDtLAYIMYTSGSTGNPKGVMITH----GNL-------NNFTNDfvG 1492
Cdd:cd05971 84 TDG-----------------------------SDD-PALIIYTSGTTGPPKGALHAHrvllGHLpgvqfpfNLFPRD--G 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1493 RLALSARDKVLsltsisfdIFGL--ELFCSLAGGAHVTLCpRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAA 1570
Cdd:cd05971 132 DLYWTPADWAW--------IGGLldVLLPSLYFGVPVLAH-RMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1571 SQRPL---TVLCGGEKMPAALLTQLRR-IATRVLQVYGPTETT-IWSTCADL--THEGAsdcIGTPIQATEVLVMDQAGN 1643
Cdd:cd05971 203 KHAQVklrAIATGGESLGEELLGWAREqFGVEVNEFYGQTECNlVIGNCSALfpIKPGS---MGKPIPGHRVAIVDDNGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1644 PLPSGAFGELwlggAGVSP------GYWRNPTLSDKVFlrrqafgAERYMyRTGDIVRFNRQGQLEYLGRNDHQVKIRGH 1717
Cdd:cd05971 280 PLPPGEVGEI----AVELPdpvaflGYWNNPSATEKKM-------AGDWL-LTGDLGRKDSDGYFWYVGRDDDVITSSGY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1718 RIELSEIDLSLssLDNIERSLSLIVGEGQQAR---IVSYLQLTSGEELNE---KAVRTALKARLPNIMIPSGFVVLSAFP 1791
Cdd:cd05971 348 RIGPAEIEECL--LKHPAVLMAAVVGIPDPIRgeiVKAFVVLNPGETPSDalaREIQELVKTRLAAHEYPREIEFVNELP 425
|
490
....*....|.
gi 1725075560 1792 LTNNNKIdIRR 1802
Cdd:cd05971 426 RTATGKI-RRR 435
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1330-1707 |
1.09e-32 |
|
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: 135.44 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAV------SCERQQYSYRQLWAQSERVAHALLRIDSRPFSVGVMMEKSCHVAVLLLGVLRAGkhYVPIDV 1403
Cdd:cd05931 1 RRAAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAG--AIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1404 HYP-----ADRVSYMIENAQARLLVTDGE-----PEQGWASPAVGF------DSLVSHPAAADALPIPADDTLAYIMYTS 1467
Cdd:cd05931 79 PPPtpgrhAERLAAILADAGPRVVLTTAAalaavRAFAASRPAAGTprllvvDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1468 GSTGNPKGVMITHGNLnnFTN--DFVGRLALSARDKVLSLTSISFDiFGLE--LFCSLAGGAHVTLcpretaMDPVklyH 1543
Cdd:cd05931 159 GSTGTPKGVVVTHRNL--LANvrQIRRAYGLDPGDVVVSWLPLYHD-MGLIggLLTPLYSGGPSVL------MSPA---A 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1544 FIER-----QQPSVIQATPTV-----WSTIVHHLPAASQRPL------TVLCGGEKMPAALLTQ---------LRRIAtr 1598
Cdd:cd05931 227 FLRRplrwlRLISRYRATISAapnfaYDLCVRRVRDEDLEGLdlsswrVALNGAEPVRPATLRRfaeafapfgFRPEA-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1599 VLQVYGPTETTIWSTCADLTHEGASDCI-------------------------GTPIQATEVLVMDQAGN-PLPSGAFGE 1652
Cdd:cd05931 305 FRPSYGLAEATLFVSGGPPGTGPVVLRVdrdalagravavaaddpaarelvscGRPLPDQEVRIVDPETGrELPDGEVGE 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 1653 LWLGGAGVSPGYWRNPTLSDKVFLRRQAFGAERYMyRTGDIvRFNRQGQLEYLGR 1707
Cdd:cd05931 385 IWVRGPSVASGYWGRPEATAETFGALAATDEGGWL-RTGDL-GFLHDGELYITGR 437
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1328-1803 |
1.66e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 134.22 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1328 IGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALL-RIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHY 1405
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGErIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1406 PADRVSYMIENAQARLLVTdgEPEQGWASPAVGFDSLVSHP-----------AAADALPIPADDTLAYIMYTSGSTGNPK 1474
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFV--EKTFQNMALSMQKVSYVQRVisitslkeiedRKIDNFVEKNESASFIICYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1475 GVMITHGNL--NNFTNDFVgrLALSARDKVLSLTSIsFDIFGLELFCS---LAGGahVTLCPREtaMDPVKLYHFIERQQ 1549
Cdd:PRK06839 166 GAVLTQENMfwNALNNTFA--IDLTMHDRSIVLLPL-FHIGGIGLFAFptlFAGG--VIIVPRK--FEPTKALSMIEKHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1550 PSVIQATPTVWSTIVHhlpaASQRPLTVL-------CGGEKMPAALLTQLRRIATRVLQVYGPTETTiwSTCADLTHEGA 1622
Cdd:PRK06839 239 VTVVMGVPTIHQALIN----CSKFETTNLqsvrwfyNGGAPCPEELMREFIDRGFLFGQGFGMTETS--PTVFMLSEEDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1623 S---DCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrRQAFgaerymYRTGDIVRFNRQ 1699
Cdd:PRK06839 313 RrkvGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--QDGW------LCTGDLARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1700 GQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-----GEGQQARIVsylqLTSGEELNEKAVRTALKAR 1774
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRqhvkwGEIPIAFIV----KKSSSVLIEKDVIEHCRLF 460
|
490 500
....*....|....*....|....*....
gi 1725075560 1775 LPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK06839 461 LAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1463-1798 |
1.85e-32 |
|
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: 130.48 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 IMYTSGSTGNPKGVMITHGNLNNFTNdFVG-RLALSARDKvLSLTSISFDIFGLEL--FCSLAGGAhvTLCPRETAMDPV 1539
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGY-FIGeRLGLTEQDR-LCIPVPLFHCFGSVLgvLACLTHGA--TMVFPSPSFDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1540 KLYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLTVLC----GGEKMPAALLTQLRRI--ATRVLQVYGPTETTIWST 1613
Cdd:cd05917 83 AVLEAIEKEKCTALHGVPTMFIAELEH-PDFDKFDLSSLRtgimAGAPCPPELMKRVIEVmnMKDVTIAYGMTETSPVST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1614 CADLTHEGASDC--IGTPIQATEVLVMDQAGNPLPS-GAFGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYMyRT 1690
Cdd:cd05917 162 QTRTDDSIEKRVntVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKT------AEAIDGDGWL-HT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1691 GDIVRFNRQGQLEYLGRNDHQVkIRG-HRIELSEIDLSLSSLDNIERSLSLIV-----GEgqqaRIVSYLQLTSGEELNE 1764
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVpderyGE----EVCAWIRLKEGAELTE 309
|
330 340 350
....*....|....*....|....*....|....
gi 1725075560 1765 KAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd05917 310 EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKI 343
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1348-1791 |
3.86e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 133.08 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTDG 1426
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDrVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1427 EpEQGWASP--------------AVGFDSLVS----HPAAADALPIPADDtLAYIMYTSGSTGNPKGVMITHGNL--NNF 1486
Cdd:PRK07514 109 A-NFAWLSKiaaaagaphvetldADGTGSLLEaaaaAPDDFETVPRGADD-LAAILYTSGTTGRSKGAMLSHGNLlsNAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 T-NDFVGrlaLSARDKVLSLTSIsFDIFGleLF----CSLAGGAHVTLCPRetaMDPVKLYHFIERQqpSVIQATPTVWS 1561
Cdd:PRK07514 187 TlVDYWR---FTPDDVLIHALPI-FHTHG--LFvatnVALLAGASMIFLPK---FDPDAVLALMPRA--TVMMGVPTFYT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1562 TIVHH--LPAASQRPLTVLCGGEkmpAALLTQL-----RRIATRVLQVYGPTETTIwSTCADLTHEGASDCIGTPIQATE 1634
Cdd:PRK07514 256 RLLQEprLTREAAAHMRLFISGS---APLLAEThrefqERTGHAILERYGMTETNM-NTSNPYDGERRAGTVGFPLPGVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1635 VLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNPtlsDKVflrRQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVK 1713
Cdd:PRK07514 332 LRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMP---EKT---AEEFRADGF-FITGDLGKIDERGYVHIVGRGKDLII 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1714 IRGHRIELSEIDLSLSSLDNIERSLSLIV-----GEGQQARIVsylqLTSGEELNEKAVRTALKARLPNIMIPSGFVVLS 1788
Cdd:PRK07514 405 SGGYNVYPKEVEGEIDELPGVVESAVIGVphpdfGEGVTAVVV----PKPGAALDEAAILAALKGRLARFKQPKRVFFVD 480
|
...
gi 1725075560 1789 AFP 1791
Cdd:PRK07514 481 ELP 483
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
315-765 |
5.48e-32 |
|
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: 133.86 E-value: 5.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTY-VLLDPQAPAARNQSILDDVQPALIL 393
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHsVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSPLHSG----------DAPCIAPSSI---------------------DYRSL--NIHAEQLPQSRDAL--AYVCYTSG 438
Cdd:cd17634 163 ADGGVRAGrsvplkknvdDALNPNVTSVehvivlkrtgsdidwqegrdlWWRDLiaKASPEHQPEAMNAEdpLFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 439 TTGKPKGVMIGREG-LSNVAQNHRDFIGLAQGSRVLAIASLGFDAFG-WDVYGALVSGATLYL---APSelHTDVGALHD 513
Cdd:cd17634 243 TTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHsYLLYGPLACGATTLLyegVPN--WPTPARMWQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 514 YLTQHDIGHITITP-AILELLP-------REMWPGLRTMIVMGDAPPADVVAWW-----AERTRLCNGYGPTEASIAtsL 580
Cdd:cd17634 321 VVDKHGVNILYTAPtAIRALMAagddaieGTDRSSLRILGSVGEPINPEAYEWYwkkigKEKCPVVDTWWQTETGGF--M 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 581 CEYRPG---VPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGS--GLAHGYLHQEalsaEKFIICrlpYMAAEERL 655
Cdd:cd17634 399 ITPLPGaieLKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQT---YFSTFKGM 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 656 YRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFV-----QPASPEL 729
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAiKGQAPYAYVvlnhgVEPSPEL 551
|
490 500 510
....*....|....*....|....*....|....*.
gi 1725075560 730 TiDALRHALVTLLHPAAIPSVFIFLPALPLTINGKI 765
Cdd:cd17634 552 Y-AELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
874-1290 |
8.00e-32 |
|
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: 130.65 E-value: 8.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 874 APLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETD-GVAYQLAEPHT--PIRL 950
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAqvPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 951 ADHW-VDGQTLSAEKWVRQLCATPFDITARPPLVLRLVQYHQQHH-VLIWVKHNIITDAWSEQLILNDLWQRYNELDDHH 1028
Cdd:cd19536 82 LDLTpLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1029 GLDAPQPQIQTIDIVNSGIASPAPADVAYWQQQLQDCReldfpLDKPRPLMPTH---AGERIHYQLQPDVAGLLASRGKA 1105
Cdd:cd19536 162 PLSLPPAQPYRDFVAHERASIQQAASERYWREYLAGAT-----LATLPALSEAVgggPEQDSELLVSVPLPVRSRSLAKR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1106 LGATPFALLCAALSLLLSRYTQQQDIVIGTAIAAR--DNLDQTQVSGFHVNTVPLRIQLSEQDTLaGLIGNMMETCIGAY 1183
Cdd:cd19536 237 SGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTLSEETVE-DLLKRAQEQELESL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1184 QHQQLSFDRIlhqieyERMSNKNPLFQIMAILQNaGDVCQQNLRDCTLHRLPLSSGFSMFDMTW--NFSV--EQDAVTIE 1259
Cdd:cd19536 316 SHEQVPLADI------QRCSEGEPLFDSIVNFRH-FDLDFGLPEWGSDEGMRRGLLFSEFKSNYdvNLSVlpKQDRLELK 388
|
410 420 430
....*....|....*....|....*....|.
gi 1725075560 1260 LDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19536 389 LAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1332-1803 |
9.28e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 131.62 E-value: 9.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSE----RVAHALLRIDSRpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPA 1407
Cdd:PRK03640 12 AFLTPDRTAIEFEEKKVTFMELHEAVVsvagKLAALGVKKGDR---VALLMKNGMEMILVIHALQQLGAVAVLLNTRLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1408 DRVSYMIENAQARLLVTDGEPEQGWASPA-VGFDSLVSHPAAADAL--PIPADDTlAYIMYTSGSTGNPKGVMITHGN-- 1482
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDFEAKLIPGIsVKFAELMNGPKEEAEIqeEFDLDEV-ATIMYTSGTTGKPKGVIQTYGNhw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1483 -------LNnftndfvgrLALSARDKVLSLTSIsFDIFGLE-LFCSLAGGAHVTLcprETAMDPVKLYHFIERQQPSVIQ 1554
Cdd:PRK03640 168 wsavgsaLN---------LGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVL---VEKFDAEKINKLLQTGGVTIIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1555 ATPTVWSTIVHHLPAASQRP--LTVLCGGEKMPAALLTQLRRIATRVLQVYGPTETTiwSTCADLTHEGASDCIGT---P 1629
Cdd:PRK03640 235 VVSTMLQRLLERLGEGTYPSsfRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETA--SQIVTLSPEDALTKLGSagkP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1630 IQATEVLVMDQaGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgaERYMYRTGDIVRFNRQGQLEYLGRND 1709
Cdd:PRK03640 313 LFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF--------QDGWFKTGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1710 HQVKIRGHRIELSEIDLSLSSLDNIERslSLIVGE-----GQqariVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGF 1784
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAE--AGVVGVpddkwGQ----VPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRF 457
|
490
....*....|....*....
gi 1725075560 1785 VVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK03640 458 YFVEELPRNASGKLLRHEL 476
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1328-1668 |
1.12e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.98 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1328 IGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYP 1406
Cdd:PRK08316 17 LRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDrVAALGHNSDAYALLWLACARAGAVHVPVNFMLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1407 ADRVSYMIENAQARLLVTD---------------------------GEPEQGWASpavgFDSLVSHPAAADALPIPADDT 1459
Cdd:PRK08316 97 GEELAYILDHSGARAFLVDpalaptaeaalallpvdtlilslvlggREAPGGWLD----FADWAEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1460 LAYIMYTSGSTGNPKGVMITHGNL-NNFTNDFVGrLALSARDKVL-SLT---SISFDIFgleLFCSLAGGAHVTLCPret 1534
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRALiAEYVSCIVA-GDMSADDIPLhALPlyhCAQLDVF---LGPYLYVGATNVILD--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1535 AMDPVKLYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLTVLC----GGEKMPAALLTQLRRI--ATRVLQVYGPTET 1608
Cdd:PRK08316 246 APDPELILRTIEAERITSFFAPPTVWISLLRH-PDFDTRDLSSLRkgyyGASIMPVEVLKELRERlpGLRFYNCYGQTEI 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1609 TIWSTCA---DltHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELwlggAGVSP----GYWRNP 1668
Cdd:PRK08316 325 APLATVLgpeE--HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI----VHRSPqlmlGYWDDP 385
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1336-1803 |
2.34e-31 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 131.33 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAV------SCERQQYSYRQLWAQSERVAHALLRIDSRPFSVgVMME--KSCHVAVLLLGVLRAGKHYVPIDVHYPA 1407
Cdd:PRK13295 38 PDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDV-VSCQlpNWWEFTVLYLACSRIGAVLNPLMPIFRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1408 DRVSYMIENAQARLL-----------------------------VTDGEPeqgwaspAVGFDSLVSHPA---AADALPI- 1454
Cdd:PRK13295 117 RELSFMLKHAESKVLvvpktfrgfdhaamarrlrpelpalrhvvVVGGDG-------ADSFEALLITPAweqEPDAPAIl 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1455 ----PADDTLAYIMYTSGSTGNPKGVMITHGNLnnFTN--DFVGRLALSARDKVLSLTSIS----FdIFGLELFCSLagG 1524
Cdd:PRK13295 190 arlrPGPDDVTQLIYTSGTTGEPKGVMHTANTL--MANivPYAERLGLGADDVILMASPMAhqtgF-MYGLMMPVML--G 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1525 AHVTLcprETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPL----TVLCGGEKMPAALLTQLRRI-ATRV 1599
Cdd:PRK13295 265 ATAVL---QDIWDPARAAELIRTEGVTFTMASTPFLTDLTRA-VKESGRPVsslrTFLCAGAPIPGALVERARAAlGAKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1600 LQVYGPTETTIWS-TCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSdkvflrr 1678
Cdd:PRK13295 341 VSAWGMTENGAVTlTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN------- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1679 qAFGAERYmYRTGDIVRFNRQGQLEYLGRNdHQVKIRG-HRIELSEIDLSLssLDNIERSLSLIVG---EGQQARIVSYL 1754
Cdd:PRK13295 414 -GTDADGW-FDTGDLARIDADGYIRISGRS-KDVIIRGgENIPVVEIEALL--YRHPAIAQVAIVAypdERLGERACAFV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1755 QLTSGEELNEKAVRTALKA-RLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK13295 489 VPRPGQSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
312-770 |
1.20e-30 |
|
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: 128.58 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPAL 391
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 392 ILADSplhSGDAPCI-APSSIDYRSLNIH-----------AEQLPQS--------------RDALAYVCYTSGTTGKPKG 445
Cdd:cd05926 90 VLTPK---GELGPASrAASKLGLAILELAldvgvlirapsAESLSNLladkknaksegvplPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 446 VMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLgfdafgWDVYG-------ALVSGATLYLAP----SELHTDVgalhdy 514
Cdd:cd05926 167 VPLTHRNLAASATNITNTYKLTPDDRTLVVMPL------FHVHGlvasllsTLAAGGSVVLPPrfsaSTFWPDV------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 515 lTQHDIGHITITPAILELL-------PREMWPGLRtMIVMGDAPPADVVAWWAERT---RLCNGYGPTEASIATSLCEYR 584
Cdd:cd05926 235 -RDYNATWYTAVPTIHQILlnrpepnPESPPPKLR-FIRSCSASLPPAVLEALEATfgaPVLEAYGMTEAAHQMTSNPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 585 PGVP-WNCIGKPlKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYRTGDIAK 663
Cdd:cd05926 313 PGPRkPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF---------KDGWFRTGDLGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 664 WDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQP-ASPELTIDALRHALVTL 741
Cdd:cd05926 383 LDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEEVAAAVVLrEGASVTEEELRAFCRKH 462
|
490 500
....*....|....*....|....*....
gi 1725075560 742 LHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05926 463 LAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
315-784 |
1.35e-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: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILA 394
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 395 DSPlhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLA 474
Cdd:cd05907 84 EDP------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 475 IASLG--FDAFGWdVYGALVSGATLYLAPSelhtdVGALHDYLTQhdighitITPAILELLPReMW------------PG 540
Cdd:cd05907 134 FLPLAhvFERRAG-LYVPLLAGARIYFASS-----AETLLDDLSE-------VRPTVFLAVPR-VWekvyaaikvkavPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 541 LR------------TMIVMGDAP-PADVVAWWaertR-----LCNGYGPTEASIATSLceYRPGVPW-NCIGKPLKNYRC 601
Cdd:cd05907 200 LKrklfdlavggrlRFAASGGAPlPAELLHFF----RalgipVYEGYGLTETSAVVTL--NPPGDNRiGTVGKPLPGVEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 602 HILDlhhnplpvgfEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYRTGDIAKWDEQGNIIFVGR-RDHQV 680
Cdd:cd05907 274 RIAD----------DGEILVRGPNVMLGYYKNPEATAEALD---------ADGWLHTGDLGEIDEDGFLHITGRkKDLII 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 681 KIRGVRIEMGEVESAVRSHPLVESACVVARSQPSgkiLAAFVQPASPELTIDALRH--ALVTLLHPAAIPSVFIFLPALP 758
Cdd:cd05907 335 TSGGKNISPEPIENALKASPLISQAVVIGDGRPF---LVALIVPDPEALEAWAEEHgiAYTDVAELAANPAVRAEIEAAV 411
|
490 500 510
....*....|....*....|....*....|..
gi 1725075560 759 LTINGKIAR-QQLEKW-----PLDERNERLTP 784
Cdd:cd05907 412 EAANARLSRyEQIKKFlllpePFTIENGELTP 443
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1348-1728 |
2.11e-30 |
|
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: 126.30 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALlridsrpfsVGVMMEKSCHVAVLL----------LGVLRAGKHYVPIDVHYPADRVSYMIENA 1417
Cdd:cd05972 1 WSFRELKRESAKAANVL---------AKLGLRKGDRVAVLLprvpelwaviLAVIKLGAVYVPLTTLLGPKDIEYRLEAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1418 QARLLVTDgepeqgwaspavgfdslvshpaaadalpipADDTlAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALS 1497
Cdd:cd05972 72 GAKAIVTD------------------------------AEDP-ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1498 ARDKVLSLTS------ISFDIFGlelfcSLAGGAHVTLCpRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAAS 1571
Cdd:cd05972 121 PDDIHWNIADpgwakgAWSSFFG-----PWLLGATVFVY-EGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1572 QRPL--TVLCGGEKM-PAALLTQLRRIATRVLQVYGPTETTIwsTCADL----THEGAsdcIGTPIQATEVLVMDQAGNP 1644
Cdd:cd05972 195 KFSHlrLVVSAGEPLnPEVIEWWRAATGLPIRDGYGQTETGL--TVGNFpdmpVKPGS---MGRPTPGYDVAIIDDDGRE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1645 LPSGAFGELW--LGGAGVSPGYWRNPtlsdkvfLRRQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELS 1722
Cdd:cd05972 270 LPPGEEGDIAikLPPPGLFLGYVGDP-------EKTEASIRGDY-YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPF 341
|
....*.
gi 1725075560 1723 EIDLSL 1728
Cdd:cd05972 342 EVESAL 347
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
338-773 |
2.96e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 127.03 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 338 GAASSV---------VAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSPLHSGDAPCIaP 408
Cdd:PRK07787 33 GAATAVaervagarrVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPAGLPHV-P 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 409 SSIDYRSLNIHAEQLPqsrDALAYVCYTSGTTGKPKGVMIGREGLSNvaqnhrDFIGLAqgsrvlaiaslgfDAFGWDVY 488
Cdd:PRK07787 112 VRLHARSWHRYPEPDP---DAPALIVYTSGTTGPPKGVVLSRRAIAA------DLDALA-------------EAWQWTAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 489 GALVSGATLYlapsELHTDV----GALHDYLTQHDIGHITITPAILELLPR-EMWPGLRTM------------------- 544
Cdd:PRK07787 170 DVLVHGLPLF----HVHGLVlgvlGPLRIGNRFVHTGRPTPEAYAQALSEGgTLYFGVPTVwsriaadpeaaralrgarl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 545 IVMGDAP-PADVVAWWAERT--RLCNGYGPTEASIATSL---CEYRPGvpWncIGKPLKNYRCHILDLHHNPLPVGFE-- 616
Cdd:PRK07787 246 LVSGSAAlPVPVFDRLAALTghRPVERYGMTETLITLSTradGERRPG--W--VGLPLAGVETRLVDEDGGPVPHDGEtv 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 617 GELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQ-VKIRGVRIEMGEVESA 695
Cdd:PRK07787 322 GELQVRGPTLFDGYLNRPDATAAAF---------TADGWFRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIETA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 696 VRSHPLVESACVVARSQPS-GKILAAFVQPASPeLTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKW 773
Cdd:PRK07787 393 LLGHPGVREAAVVGVPDDDlGQRIVAYVVGADD-VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
312-778 |
2.89e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.15 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPAL 391
Cdd:PRK09088 18 ALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 392 ILADSPLHSGDApciAPSSIDYRSLNIHAEQL----PQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLA 467
Cdd:PRK09088 98 LLGDDAVAAGRT---DVEDLAAFIASADALEPadtpSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 468 QGSRVLAIASLgFDAFGW--DVYGALVSGATLYLAPSelhTDVGALHDYLTQHDIG--HITITPAILELLPREmwPG--- 540
Cdd:PRK09088 175 AHSSFLCDAPM-FHIIGLitSVRPVLAVGGSILVSNG---FEPKRTLGRLGDPALGitHYFCVPQMAQAFRAQ--PGfda 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 541 --LR--TMIVMGDAPPA--DVVAWWAERTRLCNGYGPTEAsiATSLceyrpGVPWNC---------IGKPLKNYRCHILD 605
Cdd:PRK09088 249 aaLRhlTALFTGGAPHAaeDILGWLDDGIPMVDGFGMSEA--GTVF-----GMSVDCdvirakagaAGIPTPTVQTRVVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 606 LHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGV 685
Cdd:PRK09088 322 DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF---------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 686 RIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPAsPELTIDA--LRHALVTLLHPAAIPSVFIFLPALPLTIN 762
Cdd:PRK09088 393 NVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPA-DGAPLDLerIRSHLSTRLAKYKVPKHLRLVDALPRTAS 471
|
490
....*....|....*.
gi 1725075560 763 GKIARQQLEKWPLDER 778
Cdd:PRK09088 472 GKLQKARLRDALAAGR 487
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
317-775 |
5.14e-29 |
|
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: 122.61 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 317 YSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVlldpqapaarnqsilddvqpalilads 396
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 397 PLHSGdapcIAPSSIDYRSLN------IHAEQLPQSRDA--LAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQ 468
Cdd:cd05969 54 PLFSA----FGPEAIRDRLENseakvlITTEELYERTDPedPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 469 GSRVLAIASLGF---DAFGwdVYGALVSGATLYLAPSELhtDVGALHDYLTQHDIGHITITPAILELLPRE--------M 537
Cdd:cd05969 130 DDIYWCTADPGWvtgTVYG--IWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEgdelarkyD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 538 WPGLRTMIVMGDAPPADVVAWWAE--RTRLCNGYGPTEAS---IATSLC-EYRPGvpwnCIGKPLKNYRCHILDLHHNPL 611
Cdd:cd05969 206 LSSLRFIHSVGEPLNPEAIRWGMEvfGVPIHDTWWQTETGsimIANYPCmPIKPG----SMGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 612 PVGFEGELCIAGS--GLAHGYLHQEALSAEKFIicrlpymaaeERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEM 689
Cdd:cd05969 282 PPGTKGILALKPGwpSMFRGIWNDEERYKNSFI----------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 690 GEVESAVRSHPLVESACVVARSQP-SGKILAAFVQPASPELTIDALRHALVTL----LHPAAIPSVFIFLPALPLTINGK 764
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPlRGEIIKAFISLKEGFEPSDELKEEIINFvrqkLGAHVAPREIEFVDNLPKTRSGK 431
|
490
....*....|.
gi 1725075560 765 IARQQLEKWPL 775
Cdd:cd05969 432 IMRRVLKAKEL 442
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
419-767 |
1.75e-28 |
|
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: 122.60 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 419 HAEQLPQSRDaLAYVCYTSGTTGKPKGVM------IGREGLSNVAQNHRDfiglaqGSRVLAIASLGFDAFGW-DVYGAL 491
Cdd:cd05970 177 TANSYPCGED-ILLVYFSSGTTGMPKMVEhdftypLGHIVTAKYWQNVRE------GGLHLTVADTGWGKAVWgKIYGQW 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 492 VSGATLYLAPSELHtDVGALHDYLTQHDIGHITITPAILELLPREM-----WPGLRTMIVMGDAPPADVVAWWAERT--R 564
Cdd:cd05970 250 IAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLIREDlsrydLSSLRYCTTAGEALNPEVFNTFKEKTgiK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 565 LCNGYGPTEA--SIATSLC-EYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGS-----GLAHGYLHQEAL 636
Cdd:cd05970 329 LMEGFGQTETtlTIATFPWmEPKPG----SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 637 SAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SG 715
Cdd:cd05970 405 TAEVW----------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPiRG 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 716 KILAAFV-----QPASPELTIDALRHAL-VTLLHPAaiPSVFIFLPALPLTINGKIAR 767
Cdd:cd05970 475 QVVKATIvlakgYEPSEELKKELQDHVKkVTAPYKY--PRIVEFVDELPKTISGKIRR 530
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1346-1772 |
1.92e-28 |
|
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: 121.31 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVT 1424
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEkVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1425 DGEPeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLS 1504
Cdd:cd17640 84 ENDS-----------------------------DDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1505 LTSIsFDIF--GLELFCSLAGGAHVTLCPRETAMDpvklyhfIERQQPSVIQATPTVWSTI-------VHHLPAASQRPL 1575
Cdd:cd17640 135 ILPI-WHSYerSAEYFIFACGCSQAYTSIRTLKDD-------LKRVKPHYIVSVPRLWESLysgiqkqVSKSSPIKQFLF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1576 ----------TVLCGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTCADLTHEGASDCiGTPIQATEVLVMDQAGN-P 1644
Cdd:cd17640 207 lfflsggifkFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSV-GRPLPGTEIKIVDPEGNvV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1645 LPSGAFGELWLGGAGVSPGYWRNPTLSDKVfLRRQAFgaerymYRTGDIVRFNRQGQLEYLGR-NDHQVKIRGHRIELSE 1723
Cdd:cd17640 286 LPPGEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGW------FNTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQP 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 1724 IDLSLSSLDNIERslSLIVGEGQQ---ARIVSYLqltsgEELNEKAVRTALK 1772
Cdd:cd17640 359 IEEALMRSPFIEQ--IMVVGQDQKrlgALIVPNF-----EELEKWAKESGVK 403
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1327-1801 |
4.61e-28 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 121.54 E-value: 4.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1327 HIGRLAHTQPDSLAVSCER----------QQYSYRQLWAQSERVAHALLRIDSRPfsvG----VMMEKSCHVAVLLLGVL 1392
Cdd:PRK09274 11 HLPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGR---GmravLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1393 RAGkhYVPIDVHYPADRVSYM-------------IENAQ-ARLLVTDGEP--------EQGWASPAVGFDSLVSHPAAAD 1450
Cdd:PRK09274 88 KAG--AVPVLVDPGMGIKNLKqclaeaqpdafigIPKAHlARRLFGWGKPsvrrlvtvGGRLLWGGTTLATLLRDGAAAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1451 -ALPIPADDTLAYIMYTSGSTGNPKGVMITHGNlnnftndFVGRL-ALSA--------RDkvlsltSISFDIFGLelFCS 1520
Cdd:PRK09274 166 fPMADLAPDDMAAILFTSGSTGTPKGVVYTHGM-------FEAQIeALREdygiepgeID------LPTFPLFAL--FGP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1521 LAGGAhvTLCP-----RETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLpAASQRPL----TVLCGGEKMPAALLTQ 1591
Cdd:PRK09274 231 ALGMT--SVIPdmdptRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYG-EANGIKLpslrRVISAGAPVPIAVIER 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1592 LRRI---ATRVLQVYGPTE---------TTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNP---------LPSGAF 1650
Cdd:PRK09274 308 FRAMlppDAEILTPYGATEalpissiesREILFATRAATDNGAGICVGRPVDGVEVRIIAISDAPipewddalrLATGEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1651 GELWLGGAGVSPGYWRNP--TLSDKVFLRRQAFgaeryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHR---IELSEId 1725
Cdd:PRK09274 388 GEIVVAGPMVTRSYYNRPeaTRLAKIPDGQGDV-----WHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTlytIPCERI- 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 1726 lsLSSLDNIERSLSLIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARL---PNIMIPSGFVVLSAFPltnnnkIDIR 1801
Cdd:PRK09274 462 --FNTHPGVKRSALVGVGVPGAQRPVLCVELEPGVACSKSALYQELRALAaahPHTAGIERFLIHPSFP------VDIR 532
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
316-770 |
6.86e-28 |
|
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: 118.60 E-value: 6.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 316 TYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALilad 395
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 396 splhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAI 475
Cdd:cd05912 77 --------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 476 ASLgFDAFGWDV-YGALVSGATLYLAPselHTDVGALHDYLTQHDIGHITITPA----ILELLPREMWPGLRTMIVMGDA 550
Cdd:cd05912 125 LPL-FHISGLSIlMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTmlqrLLEILGEGYPNNLRCILLGGGP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 551 PPADVVAWWAER-TRLCNGYGPTEAS--IATSLCEY---RPGvpwnCIGKPLKNYRchiLDLHHNPLPVGFEGELCIAGS 624
Cdd:cd05912 201 APKPLLEQCKEKgIPVYQSYGMTETCsqIVTLSPEDalnKIG----SAGKPLFPVE---LKIEDDGQPPYEVGEILLKGP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 625 GLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVES 704
Cdd:cd05912 274 NVTKGYLNRPDATEESF----------ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKE 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 705 ACVVARSQPS-GKILAAFVQpASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05912 344 AGVVGIPDDKwGQVPVAFVV-SERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1330-1803 |
7.55e-28 |
|
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: 119.92 E-value: 7.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCERQQY--SYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYP 1406
Cdd:cd05923 9 RAASRAPDACAIADPARGLrlTYSELRARIEAVAARLHARGLRPGQrVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1407 ADRVSYMIENAQARLLV--TDGEPEQGWA---------SPAVGFDSLVSH-PAAADALPIPADDtlAYIMYTSGSTGNPK 1474
Cdd:cd05923 89 AAELAELIERGEMTAAViaVDAQVMDAIFqsgvrvlalSDLVGLGEPESAgPLIEDPPREPEQP--AFVFYTSGTTGLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1475 GVMITHGNLNN---FTNDFVGrLALSARDKVLSLTSISFDI--FGLeLFCSLAGGAhvTLCPREtAMDPVKLYHFIERQQ 1549
Cdd:cd05923 167 GAVIPQRAAESrvlFMSTQAG-LRHGRHNVVLGLMPLYHVIgfFAV-LVAALALDG--TYVVVE-EFDPADALKLIEQER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1550 PSVIQATPTVWSTIVHHLPAASQR---PLTVLCGGEKMPAALLTQLRR-IATRVLQVYGPTEtTIWSTCADLTHEGASdc 1625
Cdd:cd05923 242 VTSLFATPTHLDALAAAAEFAGLKlssLRHVTFAGATMPDAVLERVNQhLPGEKVNIYGTTE-AMNSLYMRDARTGTE-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1626 iGTPIQATEVLVMDQAGNP---LPSGAFGELWLGGAGVSP--GYWRNP--TLSDKVFlrrqafgaerYMYRTGDIVRFNR 1698
Cdd:cd05923 319 -MRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAftGYLNQPeaTAKKLQD----------GWYRTGDVGYVDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1699 QGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-----GEGQQARIVSYLQLTSGEELNEkavrTALKA 1773
Cdd:cd05923 388 SGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVaderwGQSVTACVVPREGTLSADELDQ----FCRAS 463
|
490 500 510
....*....|....*....|....*....|
gi 1725075560 1774 RLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05923 464 ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1342-1737 |
2.65e-27 |
|
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: 118.92 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1342 SCERQqySYRQLWAQSERVAHALLRIDSRPF-SVGVMMEKSCHVAVLLLGVLRAGkhYVPIDVHYPADrvsYMIENA--- 1417
Cdd:cd05906 36 SEEFQ--SYQDLLEDARRLAAGLRQLGLRPGdSVILQFDDNEDFIPAFWACVLAG--FVPAPLTVPPT---YDEPNArlr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1418 ----------QARLLVTDG--------EPEQGWASPAVGFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMIT 1479
Cdd:cd05906 109 klrhiwqllgSPVVLTDAElvaefaglETLSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1480 HGNL----------NNFTNDFVGrLALSARDKVLSLTSISfdifgleLFCSLAGGAHVTLCPRETAMDPVKLYHFIERQQ 1549
Cdd:cd05906 189 HRNIlarsagkiqhNGLTPQDVF-LNWVPLDHVGGLVELH-------LRAVYLGCQQVHVPTEEILADPLRWLDLIDRYR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1550 PSVIQATPTVWSTIVHHLPAASQRPLTVLC------GGE----KMPAALLTQLRRI---ATRVLQVYGPTET---TIWS- 1612
Cdd:cd05906 261 VTITWAPNFAFALLNDLLEEIEDGTWDLSSlrylvnAGEavvaKTIRRLLRLLEPYglpPDAIRPAFGMTETcsgVIYSr 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1613 TCADLTHEGASD--CIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrrqafgaERYMYRT 1690
Cdd:cd05906 341 SFPTYDHSQALEfvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFT-------EDGWFRT 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1725075560 1691 GDIVrFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERS 1737
Cdd:cd05906 414 GDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPS 459
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1336-1798 |
4.53e-27 |
|
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: 118.83 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCE------RQQYSYRQLWAQSERVAHALLRID-SRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPAD 1408
Cdd:cd17634 67 GDRTAIIYEgddtsqSRTISYRELHREVCRFAGTLLDLGvKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYMIENAQARLLVT-DGEPEQGWASP---------------------------AVGFDS---------LVSHPAAADA 1451
Cdd:cd17634 147 AVAGRIIDSSSRLLITaDGGVRAGRSVPlkknvddalnpnvtsvehvivlkrtgsDIDWQEgrdlwwrdlIAKASPEHQP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1452 LPIPADDTLaYIMYTSGSTGNPKGVMITHGN-LNNFTNDFVGRLALSARDKVLSLTSISFDIFGLEL-FCSLAGGAHVTL 1529
Cdd:cd17634 227 EAMNAEDPL-FILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLlYGPLACGATTLL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1530 CP-RETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQR----PLTVLCG-GEKM-PAALLTQLRRIATR---V 1599
Cdd:cd17634 306 YEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGtdrsSLRILGSvGEPInPEAYEWYWKKIGKEkcpV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1600 LQVYGPTETTiWSTCADL--THEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGA--GVSPGYWRNPTLSDKVF 1675
Cdd:cd17634 386 VDTWWQTETG-GFMITPLpgAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTY 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1676 LRRqaFGAeryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIVG-----EGQqaRI 1750
Cdd:cd17634 465 FST--FKG---MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE--AAVVGiphaiKGQ--AP 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 1751 VSYLQLTSGEE-----LNEkaVRTALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd17634 536 YAYVVLNHGVEpspelYAE--LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1332-1803 |
7.48e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 116.83 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVS--CERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPAD 1408
Cdd:PRK09088 5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGErLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYMIENAQARLLVTDGEPEQGWASPA--VGFDSLVSHPAAADALPIPADdTLAYIMYTSGSTGNPKGVMITHGNLNNF 1486
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVAAGRTDVEdlAAFIASADALEPADTPSIPPE-RVSLILFTSGTSGQPKGVMLSERNLQQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 TNDFvGRLALSARDKVLSLTSISFDIFGL--ELFCSLAGGAHVTLCPretAMDPVK------------LYHFIERQQPSV 1552
Cdd:PRK09088 164 AHNF-GVLGRVDAHSSFLCDAPMFHIIGLitSVRPVLAVGGSILVSN---GFEPKRtlgrlgdpalgiTHYFCVPQMAQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1553 IQATPTvwstivhhLPAASQRPLTVL-CGGEKMPAALLTQLRRIATRVLQVYGPTET-TIWSTCADLTH-EGASDCIGTP 1629
Cdd:PRK09088 240 FRAQPG--------FDAAALRHLTALfTGGAPHAAEDILGWLDDGIPMVDGFGMSEAgTVFGMSVDCDViRAKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1630 IQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgAERYMYRTGDIVRFNRQGQLEYLGRND 1709
Cdd:PRK09088 312 TPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-------TGDGWFRTGDIARRDADGFFWVVDRKK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1710 HQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARiVSYLQLTSGEE--LNEKAVRTALKARLPNIMIPSGFVVL 1787
Cdd:PRK09088 385 DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE-VGYLAIVPADGapLDLERIRSHLSTRLAKYKVPKHLRLV 463
|
490
....*....|....*.
gi 1725075560 1788 SAFPLTNNNKIDIRRL 1803
Cdd:PRK09088 464 DALPRTASGKLQKARL 479
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
427-772 |
1.23e-26 |
|
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: 116.58 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 427 RDAlAYVCYTSGTTGKPKGVMIGREglSNV----AQNHRDFIGLAQGSRVLAIASLgFDAFGWDV-YGALVSGATLYLaP 501
Cdd:cd12119 163 NTA-AAICYTSGTTGNPKGVVYSHR--SLVlhamAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL-P 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 SElHTDVGALHDYLTQHDIGHITITPAILELL-------PREMwPGLRTMIVMGDAPPADVVAWWAER-TRLCNGYGPTE 573
Cdd:cd12119 238 GP-YLDPASLAELIEREGVTFAAGVPTVWQGLldhleanGRDL-SSLRRVVIGGSAVPRSLIEAFEERgVRVIHAWGMTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 574 ASIATSLCEYRPGVP----------WNCIGKPLKNYRCHILDLHHNPLPV-GFE-GELCIAGSGLAHGYLHQEALSAEKF 641
Cdd:cd12119 316 TSPLGTVARPPSEHSnlsedeqlalRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALT 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 642 iicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVArsQPSGKI---- 717
Cdd:cd12119 396 ----------EDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIG--VPHPKWgerp 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 718 LAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd12119 464 LAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
429-773 |
1.36e-26 |
|
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: 112.81 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 429 ALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGL-AQGSRVLA-----IASLGFdafgwdVYGALVSGATLYLAPS 502
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFgGGDSWLLSlplyhVGGLAI------LVRSLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 503 ELhtdvgALHDYLTQHDIGHITITPAIL-----ELLPREMWPGLRTMIVMGDA-PPADVVAWWAERTRLCNGYGPTEASI 576
Cdd:cd17630 75 NQ-----ALAEDLAPPGVTHVSLVPTQLqrlldSGQGPAALKSLRAVLLGGAPiPPELLERAADRGIPLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 577 ATSLCEYrPGVPWNCIGKPLKNYRCHILDlhhnplpvgfEGELCIAGSGLAHGYLHQealsaekfiicRLPYMAAEERLY 656
Cdd:cd17630 150 QVATKRP-DGFGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRG-----------QLVPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 657 RTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVArsQPS---GKILAAFVQPASPeLTIDA 733
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVG--VPDeelGQRPVAVIVGRGP-ADPAE 284
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1725075560 734 LRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKW 773
Cdd:cd17630 285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
312-726 |
1.43e-26 |
|
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: 116.18 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPAL 391
Cdd:cd05904 28 ATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 392 ILADSP----LHSGDAPCIAPSSIDYRSLNI-------HAEQLPQSR---DALAYVCYTSGTTGKPKGVMIGREGL-SNV 456
Cdd:cd05904 108 AFTTAElaekLASLALPVVLLDSAEFDSLSFsdllfeaDEAEPPVVVikqDDVAALLYSSGTTGRSKGVMLTHRNLiAMV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 457 AQNHRDF-IGLAQGSRVLAIASL----GFDAFgwdVYGALVSGATLYLAPS-ELHTDVGALHDYltqhDIGHITITPAIL 530
Cdd:cd05904 188 AQFVAGEgSNSDSEDVFLCVLPMfhiyGLSSF---ALGLLRLGATVVVMPRfDLEELLAAIERY----KVTHLPVVPPIV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 531 ------ELLPREMWPGLRtMIVMGDAP-PADVVAWWAER---TRLCNGYGPTEASIATSLC------EYRPGvpwnCIGK 594
Cdd:cd05904 261 lalvksPIVDKYDLSSLR-QIMSGAAPlGKELIEAFRAKfpnVDLGQGYGMTESTGVVAMCfapekdRAKYG----SVGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 595 PLKNYRCHILDLHHN-PLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYRTGDIAKWDEQGNIIFV 673
Cdd:cd05904 336 LVPNVEAKIVDPETGeSLPPNQTGELWIRGPSIMKGYLNNPEATAATID---------KEGWLHTGDLCYIDEDGYLFIV 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 674 GRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFV--QPAS 726
Cdd:cd05904 407 DRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEeAGEVPMAFVvrKPGS 462
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1323-1803 |
1.43e-26 |
|
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: 115.89 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1323 SLLMHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPF-SVGVMMEKSCHVAVLLLGVLRAGKHYVpi 1401
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGdRVVVQLPNVAEFVVLFFALLRLGAVPV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1402 dVHYPADR---VSYMIENAQARLLVTDGEpEQGWASPAVGFDSLVSHPaaadalpipaddTLAYIMYTSGSTGNPKGVMI 1478
Cdd:cd05920 94 -LALPSHRrseLSAFCAHAEAVAYIVPDR-HAGFDHRALARELAESIP------------EVALFLLSGGTTGTPKLIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1479 THgnlnnftNDF---VGRLA----LSARDKVLSLTSISFDiFGLE---LFCSLAGGAHVTLCPREtamDPVKLYHFIERQ 1548
Cdd:cd05920 160 TH-------NDYaynVRASAevcgLDQDTVYLAVLPAAHN-FPLAcpgVLGTLLAGGRVVLAPDP---SPDAAFPLIERE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1549 QpsvIQATPTVWSTIVHHLPAASQRP-----LTVL-CGGEKMPAALLTQLRR-IATRVLQVYGPTETTIWSTCADLTHEG 1621
Cdd:cd05920 229 G---VTVTALVPALVSLWLDAAASRRadlssLRLLqVGGARLSPALARRVPPvLGCTLQQVFGMAEGLLNYTRLDDPDEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1622 ASDCIGTPIQA-TEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYmYRTGDIVRFNRQG 1700
Cdd:cd05920 306 IIHTQGRPMSPdDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHN------ARAFTPDGF-YRTGDLVRRTPDG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1701 QLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-----GEgqqaRIVSYLQLTsGEELNEKAVRTALKAR- 1774
Cdd:cd05920 379 YLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMpdellGE----RSCAFVVLR-DPPPSAAQLRRFLRERg 453
|
490 500
....*....|....*....|....*....
gi 1725075560 1775 LPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05920 454 LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1346-1803 |
1.54e-26 |
|
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: 115.25 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDvhypadrvsymienaqarllvt 1424
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRgMRAVLMVPPGPDFFALTFALFKAGAVPVLID---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1425 dgepeqgwasPAVGFDSLVS--HPAAADA-LPIPADDTLAYIMYTSGSTGNPKGVMITHGNlnnftndFVGRLALSARDk 1501
Cdd:cd05910 59 ----------PGMGRKNLKQclQEAEPDAfIGIPKADEPAAILFTSGSTGTPKGVVYRHGT-------FAAQIDALRQL- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1502 vLSLTSISFDIFGLELFCSLAGGAHVT--------LCPRETamDPVKLYHFIERQQPSVIQATPTVWSTIVHHLpAASQR 1573
Cdd:cd05910 121 -YGIRPGEVDLATFPLFALFGPALGLTsvipdmdpTRPARA--DPQKLVGAIRQYGVSIVFGSPALLERVARYC-AQHGI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1574 PLT----VLCGGEKMPAALLTQLRRI---ATRVLQVYGPTET---------TIWSTCADLTHEGASDCIGTPIQATEVLV 1637
Cdd:cd05910 197 TLPslrrVLSAGAPVPIALAARLRKMlsdEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTCVGRPIPGVRVRI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1638 MDQAGNP---------LPSGAFGELWLGGAGVSPGYWRNPtlsDKVFLRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRN 1708
Cdd:cd05910 277 IEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRP---VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1709 DHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARL---PNIMIPSGFV 1785
Cdd:cd05910 354 AHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAkdyPHTQRIGRFL 433
|
490 500
....*....|....*....|
gi 1725075560 1786 VLSAFP--LTNNNKIDIRRL 1803
Cdd:cd05910 434 IHPSFPvdIRHNAKIFREKL 453
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
873-1290 |
1.87e-26 |
|
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: 114.88 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 873 RAPLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGVAYQ------------ 940
Cdd:cd19546 4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQrildadaarpel 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 941 ----LAEPHTPIRLADHwvdgqtlsaekwvrqlCATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILND 1016
Cdd:cd19546 84 pvvpATEEELPALLADR----------------AAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1017 LWQRYNELDDHHGLD-APQPqIQTIDIV---------NSGIASPAPADVAYWQQQLQDC-RELDFPLDKPRPLMPTHAGE 1085
Cdd:cd19546 148 LAAAYGARREGRAPErAPLP-LQFADYAlwerellagEDDRDSLIGDQIAYWRDALAGApDELELPTDRPRPVLPSRRAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1086 RIHYQLQPDVAGLLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNL-DQTQVSGFHVNTVPLRIQLSE 1164
Cdd:cd19546 227 AVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1165 QDTLAGLIGNMMETCIGAYQHQQLSFDRILHQIEYERMSNKNPLFQIMAILQNAG----DVCQqnLRDCTLHRLPLSSGF 1240
Cdd:cd19546 307 DPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDndpwDAPE--LPGLRTSPVPLGTEA 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 1241 SMFDMTWNFSVEQ------DAVTIELDYASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19546 385 MELDLSLALTERRnddgdpDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
426-769 |
2.44e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 116.25 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 426 SRDALAYVCYTSGTTGKPKGVMIGREGL-SNVAQNHRDFIGLAQG-SRVLAIASLgFDAFGWDVYGALVS--GATLYLAP 501
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLfANAAQGKAWVPGLGDGpERVLAALPM-FHAYGLTLCLTLAVsiGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 SelhTDVGALHDYLTQHDIghiTITPAILELLPREM---------WPGLRTMIVMGDAPPADVVAWWAERT--RLCNGYG 570
Cdd:PRK05605 296 A---PDIDLILDAMKKHPP---TWLPGVPPLYEKIAeaaeergvdLSGVRNAFSGAMALPVSTVELWEKLTggLLVEGYG 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 571 PTEAS-IAtsLC-----EYRPGVpwncIGKPLKNYRCHILDlHHNP---LPVGFEGELCIAGSGLAHGYLHQEALSAEKF 641
Cdd:PRK05605 370 LTETSpII--VGnpmsdDRRPGY----VGVPFPDTEVRIVD-PEDPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSF 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 642 iicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRrdhqvkIRGVRIEMG------EVESAVRSHPLVESACVVARSQPSG 715
Cdd:PRK05605 443 ----------LDGWFRTGDVVVMEEDGFIRIVDR------IKELIITGGfnvypaEVEEVLREHPGVEDAAVVGLPREDG 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 716 --KILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQ 769
Cdd:PRK05605 507 seEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1346-1707 |
3.29e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 116.35 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLRIDSRPF-SVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVT 1424
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLLALGVKPGdRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1425 DG-----------------------EPEQGWASP-AVGFDSL------VSHPAAADALPIPAD-DTLAYIMYTSGSTGNP 1473
Cdd:COG1022 119 EDqeqldkllevrdelpslrhivvlDPRGLRDDPrLLSLDELlalgreVADPAELEARRAAVKpDDLATIIYTSGTTGRP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1474 KGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFdIFG--LELFCsLAGGAHVTLCPR-ETAMDPVKLYhfierqQP 1550
Cdd:COG1022 199 KGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAH-VFErtVSYYA-LAAGATVAFAESpDTLAEDLREV------KP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1551 SVIQATPTVWSTI----------------------------VHHLPAASQRPLTVL------------------------ 1578
Cdd:COG1022 271 TFMLAVPRVWEKVyagiqakaeeagglkrklfrwalavgrrYARARLAGKSPSLLLrlkhaladklvfsklrealggrlr 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1579 ---CGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTCadlTHEGAS--DCIGTPIQATEVLVMDQagnplpsgafGEL 1653
Cdd:COG1022 351 favSGGAALGPELARFFRALGIPVLEGYGLTETSPVITV---NRPGDNriGTVGPPLPGVEVKIAED----------GEI 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1654 WLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYmYRTGDIVRFNRQGQLEYLGR 1707
Cdd:COG1022 418 LVRGPNVMKGYYKNPEAT------AEAFDADGW-LHTGDIGELDEDGFLRITGR 464
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1327-1806 |
2.19e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 113.33 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1327 HIGRLAHTQPDSLAVSCERQQ--YSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDV 1403
Cdd:PRK12583 23 AFDATVARFPDREALVVRHQAlrYTWRQLADAVDRLARGLLALGVQPGDrVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1404 HYPADRVSYMIENAQARLLVT------------------------DGE------PEQGW-----ASPAVGFDSLVSHPAA 1448
Cdd:PRK12583 103 AYRASELEYALGQSGVRWVICadafktsdyhamlqellpglaegqPGAlacerlPELRGvvslaPAPPPGFLAWHELQAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1449 ADALP----------IPADDTLAyIMYTSGSTGNPKGVMITHGN-LNNftNDFVG-RLALSARDKvLSLTSISFDIFGL- 1515
Cdd:PRK12583 183 GETVSrealaerqasLDRDDPIN-IQYTSGTTGFPKGATLSHHNiLNN--GYFVAeSLGLTEHDR-LCVPVPLYHCFGMv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1516 --ELFCsLAGGAHVTLcPREtAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLTVL----CGGEKMPAALL 1589
Cdd:PRK12583 259 laNLGC-MTVGACLVY-PNE-AFDPLATLQAVEEERCTALYGVPTMFIAELDH-PQRGNFDLSSLrtgiMAGAPCPIEVM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1590 tqlRRI-----ATRVLQVYGPTETT--IWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSP 1662
Cdd:PRK12583 335 ---RRVmdemhMAEVQIAYGMTETSpvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1663 GYWRNPTLSdkvflrRQAFGAERYMYrTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEI-DLSLSSLDNIERSLSLI 1741
Cdd:PRK12583 412 GYWNNPEAT------AESIDEDGWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIeEFLFTHPAVADVQVFGV 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 1742 VGEGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNK--------IDIRRLPAP 1806
Cdd:PRK12583 485 PDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKvqkfrmreISIEELALP 557
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
318-770 |
2.34e-25 |
|
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: 111.42 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 318 SYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPqapaarnqsILDDVQPALILADSp 397
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP---------MLKERELEYILNDS- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 398 lhsgdapciapssiDYRSLNIHAEQlpqsrDALAYVCYTSGTTGKPKGVMIG-REGLSNVAQNHRDFiGLAQGSRVLAIA 476
Cdd:cd05935 73 --------------GAKVAVVGSEL-----DDLALIPYTSGTTGLPKGCMHThFSAAANALQSAVWT-GLTPSDVILACL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 477 SLGFDA-FGWDVYGALVSGATLYLAPselHTDVGALHDYLTQHDIGHIT-ITPAILELL--PR---EMWPGLRTMIVMGD 549
Cdd:cd05935 133 PLFHVTgFVGSLNTAVYVGGTYVLMA---RWDRETALELIEKYKVTFWTnIPTMLVDLLatPEfktRDLSSLKVLTGGGA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 550 APPADVVAWWAERT--RLCNGYGPTEASIATSLCEyrPGVP-WNCIGKPLKNYRCHILDLHHN-PLPVGFEGELCIAGSG 625
Cdd:cd05935 210 PMPPAVAEKLLKLTglRFVEGYGLTETMSQTHTNP--PLRPkLQCLGIP*FGVDARVIDIETGrELPPNEVGEIVVRGPQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 626 LAHGYLHQEALSAEKFIicrlpYMAAEeRLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESA 705
Cdd:cd05935 288 IFKGYWNRPEETEESFI-----EIKGR-RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 706 CVVARSQP-SGKILAAFV--QP-----ASPELTIDALRhalvTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05935 362 CVISVPDErVGEEVKAFIvlRPeyrgkVTEEDIIEWAR----EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1458-1798 |
2.43e-25 |
|
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: 109.66 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1458 DTLAyIMYTSGSTGNPKGVMITHGNLnnFT---NDFVGRLALSARDKVLSLTSISFdIFGL--ELFCSLAGGAHVTLCPR 1532
Cdd:cd17635 2 DPLA-VIFTSGTTGEPKAVLLANKTF--FAvpdILQKEGLNWVVGDVTYLPLPATH-IGGLwwILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1533 ETAMdpvKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPLTVLC---GGE-----KMPAALLTQLrriaTRVLQVYG 1604
Cdd:cd17635 78 TTYK---SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLigyGGSraiaaDVRFIEATGL----TNTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1605 PTETTIwSTCADlTHEGASD--CIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrrqafg 1682
Cdd:cd17635 151 LSETGT-ALCLP-TDDDSIEinAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1683 aERYMYrTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSyLQLTSGEEL 1762
Cdd:cd17635 223 -DGWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVG-LAVVASAEL 299
|
330 340 350
....*....|....*....|....*....|....*....
gi 1725075560 1763 NEKAVRT---ALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd17635 300 DENAIRAlkhTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1348-1803 |
3.42e-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: 110.51 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLlvtdg 1426
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDrVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1427 epeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLT 1506
Cdd:cd05912 77 -------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCAL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1507 SIsFDIFGLE-LFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPL-TVLCGGEKM 1584
Cdd:cd05912 126 PL-FHISGLSiLMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLrCILLGGGPA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1585 PAALLTQLRRIATRVLQVYGPTETTiwSTCADLTHEGASDCIGT---PIQATEVLVMDQAGNPlpsGAFGELWLGGAGVS 1661
Cdd:cd05912 202 PKPLLEQCKEKGIPVYQSYGMTETC--SQIVTLSPEDALNKIGSagkPLFPVELKIEDDGQPP---YEVGEILLKGPNVT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1662 PGYWRNPTLSDKVFlrrqafgaERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLI 1741
Cdd:cd05912 277 KGYLNRPDATEESF--------ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKE--AGV 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1742 VGE-----GQqariVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05912 347 VGIpddkwGQ----VPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1322-1875 |
6.96e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.11 E-value: 6.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1322 DSLLMHIGRLAHTQPDSLAVSC------ERQQYSYRQLWAQSERVAHALLRiDSRPFSVGVMMEKSC--HVAVLLlGVLR 1393
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQA-RASFGDRAVLLFPSGpdYVAAFF-GCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1394 AGKHYVPIdvhYPAD--------RVSYMIENAQARLLVTD----------GEPEQGWASPAVGFDSLVSHPAAADALPIP 1455
Cdd:PRK05691 87 AGVIAVPA---YPPEsarrhhqeRLLSIIADAEPRLLLTVadlrdsllqmEELAAANAPELLCVDTLDPALAEAWQEPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 ADDTLAYIMYTSGSTGNPKGVMITHGNLnnFTNDFVGR----LALSARDKVLSLTSISFDIfGL--ELFCSLAGGAHVTL 1529
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNL--VANEQLIRhgfgIDLNPDDVIVSWLPLYHDM-GLigGLLQPIFSGVPCVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1530 cpretaMDPVklyHFIERqqpsviqatPTVWstivhhLPAASQRPLTV---------LCGGEKMPAAL------------ 1588
Cdd:PRK05691 241 ------MSPA---YFLER---------PLRW------LEAISEYGGTIsggpdfayrLCSERVSESALerldlsrwrvay 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1589 -------LTQLRRIATRV----------LQVYGPTETTIWST------------------CADLTHEGASD---CIGTPI 1630
Cdd:PRK05691 297 sgsepirQDSLERFAEKFaacgfdpdsfFASYGLAEATLFVSggrrgqgipaleldaealARNRAEPGTGSvlmSCGRSQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1631 QATEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRqafgAERYMYRTGDIvRFNRQGQLEYLGRND 1709
Cdd:PRK05691 377 PGHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGRTWLRTGDL-GFLRDGELFVTGRLK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1710 HQVKIRGHrielseidlSLSSLDnIERSLSLIVGEGQQARIVSYLQLTSGEELNEKAV---RTALKARLPNIMI------ 1780
Cdd:PRK05691 452 DMLIVRGH---------NLYPQD-IEKTVEREVEVVRKGRVAAFAVNHQGEEGIGIAAeisRSVQKILPPQALIksirqa 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1781 --------PSGFVVLS--AFPLTNNNKID---------------IRRLPAPETrysaSEADYTPAA-NEAESAMQHIWQQ 1834
Cdd:PRK05691 522 vaeacqeaPSVVLLLNpgALPKTSSGKLQrsacrlrladgsldsYALFPALQA----VEAAQTAASgDELQARIAAIWCE 597
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1725075560 1835 VLSQTQISVCDSFFSLGGNSLQIPQLLHAIRQQMGVSLTIR 1875
Cdd:PRK05691 598 QLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLR 638
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
313-770 |
7.52e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 111.15 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:PRK07656 27 GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LA-------DSPLH-------------SGDAPCIAPSSIDYRSLNIHAEQLPQSR----DALAYVCYTSGTTGKPKGVMI 448
Cdd:PRK07656 107 FVlglflgvDYSATtrlpalehvviceTEEDDPHTEKMKTFTDFLAAGDPAERAPevdpDDVADILFTSGTTGRPKGAML 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 449 G-REGLSNvAQNHRDFIGLAQGSRVLAIASLgFDAFGWDV--YGALVSGATLYLA----PSELHTDVGA----------- 510
Cdd:PRK07656 187 ThRQLLSN-AADWAEYLGLTEGDRYLAANPF-FHVFGYKAgvNAPLMRGATILPLpvfdPDEVFRLIETeritvlpgppt 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 511 LHDYLTQH------DIGHI--------TITPAILELLPREmwpgLRTMIVMgdappadvvawwaertrlcNGYGPTEASI 576
Cdd:PRK07656 265 MYNSLLQHpdrsaeDLSSLrlavtgaaSMPVALLERFESE----LGVDIVL-------------------TGYGLSEASG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 577 ATSLCeyRPG-----VPwNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKfiicrlpyMAA 651
Cdd:PRK07656 322 VTTFN--RLDddrktVA-GTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA--------IDA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 652 EERLYrTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPA-SPEL 729
Cdd:PRK07656 391 DGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERlGEVGKAYVVLKpGAEL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1725075560 730 TIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK07656 470 TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1332-1803 |
8.06e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 111.67 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRV 1410
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDrVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1411 SYMIENAQARLLVT---------DGEPEQGW-------------ASPAVGFDSLVSHPAAADA----------------- 1451
Cdd:PRK06178 123 SYELNDAGAEVLLAldqlapvveQVRAETSLrhvivtsladvlpAEPTLPLPDSLRAPRLAAAgaidllpalractapvp 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1452 LPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKV-LSLTSIsFDI----FGL--ELFCslagG 1524
Cdd:PRK06178 203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVfLSFLPE-FWIagenFGLlfPLFS----G 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1525 AHVTLCPR---ETAMDPVKLYhfierqqpSVIQATPTVWST--IVHHlPAASQRPLTVL----CGG--EKMPAALLTQLR 1593
Cdd:PRK06178 278 ATLVLLARwdaVAFMAAVERY--------RVTRTVMLVDNAveLMDH-PRFAEYDLSSLrqvrVVSfvKKLNPDYRQRWR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1594 RIATRVLQ--VYGPTETtiwSTCADLThEGASD----------CIGTPIQATEVLVMD-QAGNPLPSGAFGELWLGGAGV 1660
Cdd:PRK06178 349 ALTGSVLAeaAWGMTET---HTCDTFT-AGFQDddfdllsqpvFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1661 SPGYWRNPTLSDKVFlrRQAFgaerymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSL 1740
Cdd:PRK06178 425 LKGYWNKPEATAEAL--RDGW------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG--SA 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 1741 IVG-----EGQQAriVSYLQLTSGEELNEKAVRTALKARLPNIMIPSgFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK06178 495 VVGrpdpdKGQVP--VAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1458-1803 |
1.26e-24 |
|
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: 110.11 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1458 DTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGLE--LFCSLAGGAHVTLCPreTA 1535
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPF-FHSFGLTgcLWLPLLSGIKVVFHP--NP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1536 MDPVKLYHFIERQQPSVIQATPTVWSTIV---HHLPAASQRplTVLCGGEKMPAALLTQ-LRRIATRVLQVYGPTETtiw 1611
Cdd:cd05909 224 LDYKKIPELIYDKKATILLGTPTFLRGYAraaHPEDFSSLR--LVVAGAEKLKDTLRQEfQEKFGIRILEGYGTTEC--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1612 STCADLT------HEGasdCIGTPIQATEVLVMDQAGN-PLPSGAFGELWLGGAGVSPGYWRNPTLsdkvflrrQAFGAE 1684
Cdd:cd05909 299 SPVISVNtpqspnKEG---TVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPEL--------TSFAFG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1685 RYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIER--SLSLIVGEGQQARIVSylqLTSGEEL 1762
Cdd:cd05909 368 DGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNevAVVSVPDGRKGEKIVL---LTTTTDT 444
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1725075560 1763 NEKAVRTALK-ARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd05909 445 DPSSLNDILKnAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1336-1803 |
1.26e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 110.61 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCER-QQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYM 1413
Cdd:PRK06087 37 PDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDrVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1414 IENAQARLLV-------TDGEP-------EQGWASPAVGFDSL---VSHPAAADAL--------PIPAD-DTLAYIMYTS 1467
Cdd:PRK06087 117 LNKCQAKMFFaptlfkqTRPVDlilplqnQLPQLQQIVGVDKLapaTSSLSLSQIIadyeplttAITTHgDELAAVLFTS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1468 GSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVL---SLTSISFDIFGLELfCSLAGGAHVTLcpreTAMDPVKLYHF 1544
Cdd:PRK06087 197 GTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMmpaPLGHATGFLHGVTA-PFLIGARSVLL----DIFTPDACLAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1545 IERQQPS-VIQATPTVWStIVHHLPAASQRPLTV---LCGGEKMPAALLTQLRRIATRVLQVYGPTETT--IWSTCAD-L 1617
Cdd:PRK06087 272 LEQQRCTcMLGATPFIYD-LLNLLEKQPADLSALrffLCGGTTIPKKVARECQQRGIKLLSVYGSTESSphAVVNLDDpL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1618 THEGASDciGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKvflrrqAFGAERYMYrTGDIVRFN 1697
Cdd:PRK06087 351 SRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR------ALDEEGWYY-SGDLCRMD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1698 RQGQLEYLGRNDhQVKIR-GHRIELSEIDLSLSSLDNI----------ERslsliVGEgqqaRIVSYLQLTSGEELNEKA 1766
Cdd:PRK06087 422 EAGYIKITGRKK-DIIVRgGENISSREVEDILLQHPKIhdacvvampdER-----LGE----RSCAYVVLKAPHHSLTLE 491
|
490 500 510
....*....|....*....|....*....|....*....
gi 1725075560 1767 VRTAL--KARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK06087 492 EVVAFfsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
315-773 |
1.28e-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: 109.47 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFAcWLLEHSGAASSVVAVSMDKSATLLIVL-LGILKSNKTYVLLDPQAPAARNQSILDDVQP-ALI 392
Cdd:cd05910 1 SRLSFRELDERSDRIA-QGLTAYGIRRGMRAVLMVPPGPDFFALtFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPdAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 ---LADSPlhsgdapciapssidyrslnihaeqlpqsrdalAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQG 469
Cdd:cd05910 80 gipKADEP---------------------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 470 SRVLAiaslGFDAFGwdVYGALVSGATL-----YLAPSElhTDVGALHDYLTQHDIGHITITPAILELLPR------EMW 538
Cdd:cd05910 127 EVDLA----TFPLFA--LFGPALGLTSVipdmdPTRPAR--ADPQKLVGAIRQYGVSIVFGSPALLERVARycaqhgITL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 539 PGLRTMIVMGDAPPADVVAWW----AERTRLCNGYGPTEA----SIA-----TSLCEYRPGVPWNCIGKPLKNYRCHILD 605
Cdd:cd05910 199 PSLRRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEAlpvsSIGsrellATTTAATSGGAGTCVGRPIPGVRVRIIE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 606 LHHNP---------LPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpYMAAEERLYRTGDIAKWDEQGNIIFVGRR 676
Cdd:cd05910 279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKI-----DDNSEGFWHRMGDLGYLDDEGRLWFCGRK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 677 DHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSGKILAAFVQP-ASPELTIDALRHALVTLL--HP-AAIPSVFI 752
Cdd:cd05910 354 AHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPlPGTITPRARLEQELRALAkdYPhTQRIGRFL 433
|
490 500
....*....|....*....|...
gi 1725075560 753 FLPALPLTI--NGKIARQQLEKW 773
Cdd:cd05910 434 IHPSFPVDIrhNAKIFREKLAVW 456
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
424-765 |
1.36e-24 |
|
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: 110.11 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 424 PQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLgFDAFGWDVYG--ALVSGATLYLAP 501
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPF-FHSFGLTGCLwlPLLSGIKVVFHP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 SELHTD-VGAL-HDYLTQHDIGHITITPAILELLPREMWPGLRTMIVMGDAPPADVVAWWAER--TRLCNGYGPTEAS-- 575
Cdd:cd05909 222 NPLDYKkIPELiYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSpv 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 IATSLCEY--RPGvpwnCIGKPLKNYRCHILDLH-HNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaE 652
Cdd:cd05909 302 ISVNTPQSpnKEG----TVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF----------G 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 653 ERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVArSQPSGK-----ILAAFVQPASP 727
Cdd:cd05909 368 DGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVV-SVPDGRkgekiVLLTTTTDTDP 446
|
330 340 350
....*....|....*....|....*....|....*...
gi 1725075560 728 ELTIDALRHALVTLLHpaaIPSVFIFLPALPLTINGKI 765
Cdd:cd05909 447 SSLNDILKNAGISNLA---KPSYIHQVEEIPLLGTGKP 481
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
313-770 |
1.45e-24 |
|
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: 109.72 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLldpQAPAARNQSILDDVQpali 392
Cdd:cd05920 37 GDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL---ALPSHRRSELSAFCA---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 ladsplHSGDAPCIAP---SSIDYRSLnihAEQLPQSRDALAYVCYTSGTTGKPKgvMIGReglsnvaqNHRDFI----- 464
Cdd:cd05920 110 ------HAEAVAYIVPdrhAGFDHRAL---ARELAESIPEVALFLLSGGTTGTPK--LIPR--------THNDYAynvra 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 465 -----GLAQGSRVLAIASLG--FDAFGWDVYGALVSGATLYLAPSELHTDVGALHDyltQHDIGHITITPAILEL-LPRE 536
Cdd:cd05920 171 saevcGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLIE---REGVTVTALVPALVSLwLDAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 537 MWPG-----LRTMIVmGDAPPADVVAWWAERT---RLCNGYGPTEASiatsLCEYRPGVPWNCI----GKPLKNY-RCHI 603
Cdd:cd05920 248 ASRRadlssLRLLQV-GGARLSPALARRVPPVlgcTLQQVFGMAEGL----LNYTRLDDPDEVIihtqGRPMSPDdEIRV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 604 LDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIR 683
Cdd:cd05920 323 VDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF---------TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 684 GVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPELTIDALRHALVTL-LHPAAIPSVFIFLPALPLTI 761
Cdd:cd05920 394 GEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERSCAFVVLRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTA 473
|
....*....
gi 1725075560 762 NGKIARQQL 770
Cdd:cd05920 474 VGKIDKKAL 482
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1318-1817 |
1.63e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 110.22 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1318 AGSRDSLLMHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGK 1396
Cdd:PRK06164 6 APRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDrVAVWLPNCIEWVVLFLACARLGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1397 HYVPIDVHYPADRVSYMIENAQARLLV----------------------------------TDGEPEQGWASPAVGFDSL 1442
Cdd:PRK06164 86 TVIAVNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaavppdalpplraiavvddaADATPAPAPGARVQLFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1443 VSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFtNDFVGR-LALSARDKVLSLTSISfDIFGLE-LFCS 1520
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRH-ARAIARaYGYDPGAVLLAALPFC-GVFGFStLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1521 LAGGAHVTLCPretAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPLTVLCGGekmpAALLTQLRRIATRVL 1600
Cdd:PRK06164 244 LAGGAPLVCEP---VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGF----ASFAPALGELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1601 Q-------VYGPTETTIWSTCADLT------HEGAsdciGTPIQA-TEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYW 1665
Cdd:PRK06164 317 ArgvpltgLYGSSEVQALVALQPATdpvsvrIEGG----GRPASPeARVRARDpQDGALLPDGESGEIEIRAPSLMRGYL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1666 RNPTLSdkvflrRQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEG 1745
Cdd:PRK06164 393 DNPDAT------ARALTDDGY-FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 1746 QQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLT---NNNKIDIRRLPAPETRYSASEADY 1817
Cdd:PRK06164 466 GKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRLREMAQARLAAERAA 540
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1337-1700 |
3.60e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 109.28 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1337 DSLAVSCER-----------QQYSYRQLWAQSERVA---HALLRIdSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPID 1402
Cdd:PRK08314 14 HNLEVSARRypdktaivfygRAISYRELLEEAERLAgylQQECGV-RKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1403 VHYPADRVSYMIENAQARLLVT--------------------------DGEPEQGWASPAVGFDslVSHPAAA------- 1449
Cdd:PRK08314 93 PMNREEELAHYVTDSGARVAIVgselapkvapavgnlrlrhvivaqysDYLPAEPEIAVPAWLR--AEPPLQAlapggvv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1450 ---DAL-----PIPAD---DTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGLE-- 1516
Cdd:PRK08314 171 awkEALaaglaPPPHTagpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTGMVhs 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1517 LFCSLAGGAHVTLCP---RETAMDpvklyhFIERQQPSVIQATPTVwstIVHHL--PAASQRPLTVLC----GGEKMPAA 1587
Cdd:PRK08314 250 MNAPIYAGATVVLMPrwdREAAAR------LIERYRVTHWTNIPTM---VVDFLasPGLAERDLSSLRyiggGGAAMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1588 LLTQLR-RIATRVLQVYGPTETtiwstcADLTHEGASD-----CIGTPIQATEVLVMD-QAGNPLPSGAFGELWLGGAGV 1660
Cdd:PRK08314 321 VAERLKeLTGLDYVEGYGLTET------MAQTHSNPPDrpklqCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1725075560 1661 SPGYWRNPTLSDKVFLRrqaFGAERYmYRTGDIVRFNRQG 1700
Cdd:PRK08314 395 FKGYWNRPEATAEAFIE---IDGKRF-FRTGDLGRMDEEG 430
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
310-770 |
4.20e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 109.08 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:PRK06155 40 LVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSP----LHSGDAPCIA---------------PSSIDYRSLNIHAEQLP----QSRDALAyVCYTSGTTGKPKGV 446
Cdd:PRK06155 120 RLLVVEAAllaaLEAADPGDLPlpavwlldapasvsvPAGWSTAPLPPLDAPAPaaavQPGDTAA-ILYTSGTTGPSKGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 447 MIGREGLSNVAQNHRDFIGLAQGSRVLAIASL----GFDAFgwdvYGALVSGATLYLAP----SELHTDV---GALHDYL 515
Cdd:PRK06155 199 CCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLfhtnALNAF----FQALLAGATYVLEPrfsaSGFWPAVrrhGATVTYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 516 tqhdIGhiTITPAILELLPREMWPGLRTMIVMGDAPPADVVAWWAERT--RLCNGYGPTEAS--IATSLCEYRPGVpwnc 591
Cdd:PRK06155 275 ----LG--AMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFgvDLLDGYGSTETNfvIAVTHGSQRPGS---- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 592 IGKPLKNYRCHILDLHHNPLPVGFEGELCIAGS---GLAHGYLHQealsAEKFIicrlpymAAEERL-YRTGDIAKWDEQ 667
Cdd:PRK06155 345 MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGM----PEKTV-------EAWRNLwFHTGDRVVRDAD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 668 GNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA-RSQPSG-KILAAFV----QPASPEltiDALRHALVTL 741
Cdd:PRK06155 414 GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPvPSELGEdEVMAAVVlrdgTALEPV---ALVRHCEPRL 490
|
490 500
....*....|....*....|....*....
gi 1725075560 742 LHpAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK06155 491 AY-FAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
433-777 |
4.88e-24 |
|
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: 109.50 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 433 VCYTSGTTGKPKGVMIGREGLS-NVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYL---APSelHTDV 508
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVHAGFPlKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPD--HPKA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 509 GALHDYLTQHDIGHITITPAILE-LLPREMWP----GLRTMIVMGD-APPADVVAW-WAERTRL------CNGYGPTEAS 575
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRaLKPRGDAPvnahDLSSLRVLGStGEPWNPEPWnWLFETVGkgrnpiINYSGGTEIS 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 iATSLCEY--RPGVPWNCIGkPLKNYRCHILDLHHNPLPvGFEGELCIAGS--GLAHGYLHQEALSAEKfiicrlpYMAA 651
Cdd:cd05968 399 -GGILGNVliKPIKPSSFNG-PVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWRDEDRYLET-------YWSR 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 652 EERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV-ESACVVARSQPSGKILAAFV--QPA--- 725
Cdd:cd05968 469 FDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVlESAAIGVPHPVKGEAIVCFVvlKPGvtp 548
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 726 SPELTiDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDE 777
Cdd:cd05968 549 TEALA-EELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK 599
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1293-1700 |
6.24e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 108.33 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1293 TAQLALNPLCEREQQWLQQLAvnadagsrdsllmhigRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRidsRPF 1372
Cdd:PRK07786 4 LTLAQEQPYLARRQNWVNQLA----------------RHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSR---RGV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1373 SVG----VMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTD----------------------- 1425
Cdd:PRK07786 65 GFGdrvlILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEaalapvatavrdivpllstvvva 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1426 -GEPEQGwaspAVGFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLS 1504
Cdd:PRK07786 145 gGSSDDS----VLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1505 LTSISFDIFGL-ELFCSLAGGAHVTLCPReTAMDPVKLYHFIERQQPSVIQATPTVWSTIvhhLPAASQRP----LTVLC 1579
Cdd:PRK07786 221 VGVPLFHIAGIgSMLPGLLLGAPTVIYPL-GAFDPGQLLDVLEAEKVTGIFLVPAQWQAV---CAEQQARPrdlaLRVLS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1580 GGEKmPAAlLTQLRRIA-----TRVLQVYGPTETTIwSTCADLTHEGASD--CIGTPIQATEVLVMDQAGNPLPSGAFGE 1652
Cdd:PRK07786 297 WGAA-PAS-DTLLRQMAatfpeAQILAAFGQTEMSP-VTCMLLGEDAIRKlgSVGKVIPTVAARVVDENMNDVPVGEVGE 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1725075560 1653 LWLGGAGVSPGYWRNPTLSDKVFlrrqAFGaeryMYRTGDIVRFNRQG 1700
Cdd:PRK07786 374 IVYRAPTLMSGYWNNPEATAEAF----AGG----WFHSGDLVRQDEEG 413
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
435-772 |
9.54e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 106.50 E-value: 9.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMigreglsnvaQNHRDF----------IGLAQGSRVLAIASLGFDAFGWDVYGA-LVSGATLYLApSE 503
Cdd:cd05974 92 FTSGTTSKPKLVE----------HTHRSYpvghlstmywIGLKPGDVHWNISSPGWAKHAWSCFFApWNAGATVFLF-NY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 504 LHTDVGALHDYLTQHDIGHITITPAILELLPREMWPGLRTMI--VMGDAPPAD------VVAWWAERTRlcNGYGPTEAs 575
Cdd:cd05974 161 ARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLreVVGAGEPLNpevieqVRRAWGLTIR--DGYGQTET- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 iaTSLCEYRPGVPW--NCIGKPLKNYRCHILDLHHNPLPvgfEGELCIAGS-----GLAHGYLHQEALSAEkfiicrlpy 648
Cdd:cd05974 238 --TALVGNSPGQPVkaGSMGRPLPGYRVALLDPDGAPAT---EGEVALDLGdtrpvGLMKGYAGDPDKTAH--------- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 649 mAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-------SGKILAAF 721
Cdd:cd05974 304 -AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPvrlsvpkAFIVLRAG 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 722 VQPaSPELTIDALRHALVTLlhpAAIPSV-FIFLPALPLTINGKIARQQLEK 772
Cdd:cd05974 383 YEP-SPETALEIFRFSRERL---APYKRIrRLEFAELPKTISGKIRRVELRR 430
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
315-764 |
1.07e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 107.66 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKS-------NKTYV------LL---DPQAP-- 376
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAravpvnvNYRYVedelryLLddsDAVALvy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 377 ----AARNQSILDD---VQPALILADsplhsGDAPCIAPSSIDYRSL--NIHAEQL--PQSRDALaYVCYTSGTTGKPKG 445
Cdd:PRK07798 107 erefAPRVAEVLPRlpkLRTLVVVED-----GSGNDLLPGAVDYEDAlaAGSPERDfgERSPDDL-YLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 446 VMIGREGLSNVAQNHRDFIG---------LAQ------GSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSElHTDVGA 510
Cdd:PRK07798 181 VMWRQEDIFRVLLGGRDFATgepiedeeeLAKraaagpGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLLPDV-RFDADE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 511 LHDYLTQHDIGHITIT------PAILELLPREMW--PGLRTMIVMGdappadvvAWWAERTR-----------LCNGYGP 571
Cdd:PRK07798 260 VWRTIEREKVNVITIVgdamarPLLDALEARGPYdlSSLFAIASGG--------ALFSPSVKeallellpnvvLTDSIGS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 572 TEA----SIATSLCEYRPGVPWNCIGKplknyRCHILDLHHNPLPVGFEGELCIAGSG-LAHGYLHQEALSAEKFIIcrl 646
Cdd:PRK07798 332 SETgfggSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEKTAETFPT--- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 647 pymAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARsqPS---GKILAAFVQ 723
Cdd:PRK07798 404 ---IDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGV--PDerwGQEVVAVVQ 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1725075560 724 PAS-PELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGK 764
Cdd:PRK07798 479 LREgARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
875-1290 |
1.18e-23 |
|
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: 105.85 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDdcSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTET--DGVAYQ--LAEPHTPIRl 950
Cdd:cd19542 3 PCTPMQEGMLLSQLRSPG--LYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESsaEGTFLQvvLKSLDPPIE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 951 adhWVDGQTLSAEKWVRQLCATPFDITaRPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELddhhgL 1030
Cdd:cd19542 80 ---EVETDEDSLDALTRDLLDDPTLFG-QPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQ-----L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1031 DAPQPQIQtiDIVNSGIASPAPADVAYWQQQLQDCRELDFP-LDKPRPLMPTHAGERIHYQLqpdvaglLASRGKALGAT 1109
Cdd:cd19542 151 LPPAPPFS--DYISYLQSQSQEESLQYWRKYLQGASPCAFPsLSPKRPAERSLSSTRRSLAK-------LEAFCASLGVT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1110 PFALLCAALSLLLSRYTQQQDIVIGTAIAARDNLDQT--QVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGAYQHQQ 1187
Cdd:cd19542 222 LASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGidDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1188 LSFDRILHQIeyeRMSNKNPLFQIMAILQNAGDVCQQNLRDCTLHRLPLSSGFSMFDMTWNFSVEQDAVTIELDYASELF 1267
Cdd:cd19542 302 LSLREIQRAL---GLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVL 378
|
410 420
....*....|....*....|...
gi 1725075560 1268 YPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19542 379 SEEQAEELLEQFDDILEALLANP 401
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
432-796 |
1.26e-23 |
|
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: 108.17 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 432 YVCYTSGTTGKPKGVMIGREGLSnVAQNH--RDFIGLAQGSRVLAIASLgfdafGWDV------YGALVSGAT--LYLAP 501
Cdd:cd05967 234 YILYTSGTTGKPKGVVRDNGGHA-VALNWsmRNIYGIKPGDVWWAASDV-----GWVVghsyivYGPLLHGATtvLYEGK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 SELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPG----------LRTMIVMGDapPADV-VAWWAERTR---LCN 567
Cdd:cd05967 308 PVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGkyikkydlssLRTLFLAGE--RLDPpTLEWAENTLgvpVID 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 568 GYGPTE---ASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSgLAHGYLHQEALSAEKFiic 644
Cdd:cd05967 386 HWWQTEtgwPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWKNDERF--- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 645 RLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA-RSQPSGKILAAFVQ 723
Cdd:cd05967 462 KKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGvRDELKGQVPLGLVV 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 724 P-ASPELTIDALRHALVTLLH----PAAIPSVFIFLPALPLTINGKIARQQLEKWpldERNERLTPPET-ETEAILERI 796
Cdd:cd05967 542 LkEGVKITAEELEKELVALVReqigPVAAFRLVIFVKRLPKTRSGKILRRTLRKI---ADGEDYTIPSTiEDPSVLDEI 617
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1433-1802 |
1.28e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 107.78 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1433 ASPAVGFDSLVSHPAAAD----ALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLnnFTNDFVGRL---ALSARDKVLSL 1505
Cdd:PRK05605 190 APGTVPWETLVDAAIGGDgsdvSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNL--FANAAQGKAwvpGLGDGPERVLA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1506 TSISFDIFGLELFCSLAG--GAHVTLCPRETA---MDPVKlyhfieRQQPSVIQATPTVWSTIVHhlpAASQR--PLT-- 1576
Cdd:PRK05605 268 ALPMFHAYGLTLCLTLAVsiGGELVLLPAPDIdliLDAMK------KHPPTWLPGVPPLYEKIAE---AAEERgvDLSgv 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1577 --VLCGGEKMPAALLTQLRRiATRVLQV--YGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAgNP---LPSGA 1649
Cdd:PRK05605 339 rnAFSGAMALPVSTVELWEK-LTGGLLVegYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPE-DPdetMPDGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1650 FGELWLGGAGVSPGYWRNPTLSDKVFLRRqafgaeryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLS 1729
Cdd:PRK05605 417 EGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 1730 SLDNIERslSLIVG---EGQQARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIdIRR 1802
Cdd:PRK05605 489 EHPGVED--AAVVGlprEDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV-RRR 561
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
874-1290 |
2.37e-23 |
|
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: 104.69 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 874 APLSPQQNLLWYLSALNPDdcSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDGV-AYQLAEPHTPIrlad 952
Cdd:cd19545 2 YPCTPLQEGLMALTARQPG--AYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGgLLQVVVKESPI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 953 HWVDGQTLSAekWVRQLCATPFDITArpPLV-LRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYnelddHHGLD 1031
Cdd:cd19545 76 SWTESTSLDE--YLEEDRAAPMGLGG--PLVrLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY-----QGEPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1032 APQPQ-------IQTIDIVNSgiaspapadVAYWQQQLQDCRELDFPLDKPRPLMPTHAGERIHYqlqpdvagLLASRGK 1104
Cdd:cd19545 147 PQPPPfsrfvkyLRQLDDEAA---------AEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHS--------ISLPSSA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1105 ALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAARDNL--DQTQVSGFHVNTVPLRIQLSEQDTLAGLIGNMMETCIGA 1182
Cdd:cd19545 210 SSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPvpGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1183 YQHQQLSFDRILHQIEYERmsnKNPLFQIMAILQNAGDVCQQNLRDCTLHRLPL-SSGFSMFDMTWNFSVEQDAVTIELD 1261
Cdd:cd19545 290 IPFEHTGLQNIRRLGPDAR---AACNFQTLLVVQPALPSSTSESLELGIEEESEdLEDFSSYGLTLECQLSGSGLRVRAR 366
|
410 420
....*....|....*....|....*....
gi 1725075560 1262 YASELFYPASMQMLLDNYQQTLRQLLTLP 1290
Cdd:cd19545 367 YDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
310-770 |
2.42e-23 |
|
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: 105.25 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAA-SSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQ 388
Cdd:cd05958 4 LRSPEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 389 PALILADSPLHSGDAPCIapssidyrslnihaeqlpqsrdalayVCYTSGTTGKPKGVMIGREGLSNVAQNH-RDFIGLA 467
Cdd:cd05958 84 ITVALCAHALTASDDICI--------------------------LAFTSGTTGAPKATMHFHRDPLASADRYaVNVLRLR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 468 QGSRVLAIASLGFD-AFGWDVYGALVSGATLYLAPSELHTDV-GALHDYLTQHDIGHITITPAILELLPR--EMWPGLRT 543
Cdd:cd05958 138 EDDRFVGSPPLAFTfGLGGVLLFPFGVGASGVLLEEATPDLLlSAIARYKPTVLFTAPTAYRAMLAHPDAagPDLSSLRK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 544 MIVMGDAPPADVVAWWAERT--RLCNGYGPTEA---SIATSLCEYRPGVpwncIGKPLKNYRCHILDLHHNPLPVGFEGE 618
Cdd:cd05958 218 CVSAGEALPAALHRAWKEATgiPIIDGIGSTEMfhiFISARPGDARPGA----TGKPVPGYEAKVVDDEGNPVPDGTIGR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 619 LCIAGSGlahGYLHQEALSAEKFIicrlpymaAEERLYrTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRS 698
Cdd:cd05958 294 LAVRGPT---GCRYLADKRQRTYV--------QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQ 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 699 HPLVESACVVARSQPS-GKILAAFVQPASPELTIDALRHALV----TLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05958 362 HPAVAECAVVGHPDESrGVVVKAFVVLRPGVIPGPVLARELQdhakAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
424-770 |
3.56e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 105.71 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 424 PQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASL----GFDAFgwdVYGALVSGATLyL 499
Cdd:PRK06839 145 EKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLfhigGIGLF---AFPTLFAGGVI-I 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 APSELHTD--VGALHDYLTQHDIGHITITPAILELLPREMwPGLRT--MIVMGDAP-PADVVAWWAERT-RLCNGYGPTE 573
Cdd:PRK06839 221 VPRKFEPTkaLSMIEKHKVTVVMGVPTIHQALINCSKFET-TNLQSvrWFYNGGAPcPEELMREFIDRGfLFGQGFGMTE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 574 AS-----IATSLCEYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEkfiicrlpy 648
Cdd:PRK06839 300 TSptvfmLSEEDARRKVG----SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 649 mAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASP 727
Cdd:PRK06839 367 -TIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKKSS 445
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1725075560 728 ELTIDA-LRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK06839 446 SVLIEKdVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
435-770 |
8.98e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 101.97 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMigregLS--NVAQNHRdFIGLAQGSR---VLAIASLGFDAFGWdVYGALVS---GATL------YLA 500
Cdd:cd05917 9 FTSGTTGSPKGAT-----LThhNIVNNGY-FIGERLGLTeqdRLCIPVPLFHCFGS-VLGVLAClthGATMvfpspsFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 501 PSELHTDV----GALHdyltqhdiGHITITPAILELLPREMWP--GLRTMIVMGDAPPADVVAWWAER---TRLCNGYGP 571
Cdd:cd05917 82 LAVLEAIEkekcTALH--------GVPTMFIAELEHPDFDKFDlsSLRTGIMAGAPCPPELMKRVIEVmnmKDVTIAYGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 572 TEAS--IATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLP-VGFEGELCIAGSGLAHGYLHQEALSAEkfiicrlpy 648
Cdd:cd05917 154 TETSpvSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAE--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 649 MAAEERLYRTGDIAKWDEQGNIIFVGR-RDhqVKIRGVR-IEMGEVESAVRSHPLVESACVVA-RSQPSGKILAAFVQPA 725
Cdd:cd05917 225 AIDGDGWLHTGDLAVMDEDGYCRIVGRiKD--MIIRGGEnIYPREIEEFLHTHPKVSDVQVVGvPDERYGEEVCAWIRLK 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1725075560 726 -SPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05917 303 eGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
344-773 |
9.12e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 104.27 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 344 VAVSMDKSATLLIVLLGILKSNKTYVLLDPQ-APAARNQSiLDDVQPALILADSPLHSGDAPCIapsSIDYRSLNIHAEQ 422
Cdd:PRK03640 55 VALLMKNGMEMILVIHALQQLGAVAVLLNTRlSREELLWQ-LDDAEVKCLITDDDFEAKLIPGI---SVKFAELMNGPKE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 423 LPQ-----SRDALAYVCYTSGTTGKPKGVM--IGREGLSNV--AQNhrdfIGLAQGSRVLAIASL----GFDAfgwdVYG 489
Cdd:PRK03640 131 EAEiqeefDLDEVATIMYTSGTTGKPKGVIqtYGNHWWSAVgsALN----LGLTEDDCWLAAVPIfhisGLSI----LMR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 490 ALVSGATLYLAPselHTDVGALHDYLTQHDIGHITITPA----ILELLPREMWPG-LRTMIVMGDAPPADVVAWWAER-T 563
Cdd:PRK03640 203 SVIYGMRVVLVE---KFDAEKINKLLQTGGVTIISVVSTmlqrLLERLGEGTYPSsFRCMLLGGGPAPKPLLEQCKEKgI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 564 RLCNGYGPTE-AS-IATSLCEY---RPGvpwnCIGKPLKNYRCHILDlHHNPLPVGFEGELCIAGSGLAHGYLHQEALSA 638
Cdd:PRK03640 280 PVYQSYGMTEtASqIVTLSPEDaltKLG----SAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 639 EKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKI 717
Cdd:PRK03640 355 ETF----------QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwGQV 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 718 LAAFVQpASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKW 773
Cdd:PRK03640 425 PVAFVV-KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
314-791 |
1.12e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.83 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:PRK06087 47 GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSPLHSGDA-----PCI---------------APSSI---------DYRSLNihaEQLPQSRDALAYVCYTSGTTGKPK 444
Cdd:PRK06087 127 APTLFKQTRPvdlilPLQnqlpqlqqivgvdklAPATSslslsqiiaDYEPLT---TAITTHGDELAAVLFTSGTEGLPK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 445 GVMIGReglSNVAQNHRDFIGlaqgsrVLAIASLgfdafgwDVYgalvsgatlyLAPSELHTDVGALHDYLTQHDIGHIT 524
Cdd:PRK06087 204 GVMLTH---NNILASERAYCA------RLNLTWQ-------DVF----------MMPAPLGHATGFLHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 525 I-----TP-AILELLPRE--MW----------------------PGLRTMIVMGDAPPADVVAWWAER-TRLCNGYGPTE 573
Cdd:PRK06087 258 VlldifTPdACLALLEQQrcTCmlgatpfiydllnllekqpadlSALRFFLCGGTTIPKKVARECQQRgIKLLSVYGSTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 574 aSIATSLCEYRPGVPWN--CIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaA 651
Cdd:PRK06087 338 -SSPHAVVNLDDPLSRFmhTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARAL---------D 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 652 EERLYRTGDIAKWDEQGNIIFVGRRDhQVKIR-GVRIEMGEVESAVRSHPLVESACVVArsQPS---GKILAAFVQPASP 727
Cdd:PRK06087 408 EEGWYYSGDLCRMDEAGYIKITGRKK-DIIVRgGENISSREVEDILLQHPKIHDACVVA--MPDerlGERSCAYVVLKAP 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 728 ELTI---DALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKwpldERNERLTPPETETEA 791
Cdd:PRK06087 485 HHSLtleEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK----DIMRRLTQDVCEEIE 547
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
344-770 |
1.28e-22 |
|
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: 103.74 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 344 VAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAA-----------RNQSILDDVQP--------ALILADSPLHSGDAP 404
Cdd:cd05923 56 VAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAelaeliergemTAAVIAVDAQVmdaifqsgVRVLALSDLVGLGEP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 405 CIAPSSIDYRslnihaeqlPQSRDALAYVCYTSGTTGKPKGVMIGREG-------LSNVAQN----HRDFIGL-----AQ 468
Cdd:cd05923 136 ESAGPLIEDP---------PREPEQPAFVFYTSGTTGLPKGAVIPQRAaesrvlfMSTQAGLrhgrHNVVLGLmplyhVI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 469 GSRVLAIASLGFDAFgWDVYGALVSGATLYLAPSElhtDVGALHDYLTQHD--IGHITITPAILEllpremwpGLRTMIV 546
Cdd:cd05923 207 GFFAVLVAALALDGT-YVVVEEFDPADALKLIEQE---RVTSLFATPTHLDalAAAAEFAGLKLS--------SLRHVTF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 547 MGDAPPADVVawwaERTRLC------NGYGPTEASIATSLCEYRPGVpwncIGKPLKNYRCHILDLHHNP---LPVGFEG 617
Cdd:cd05923 275 AGATMPDAVL----ERVNQHlpgekvNIYGTTEAMNSLYMRDARTGT----EMRPGFFSEVRIVRIGGSPdeaLANGEEG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 618 ELCIAGSGLA--HGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESA 695
Cdd:cd05923 347 ELIVAAAADAafTGYLNQPEATAKKL----------QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERV 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 696 VRSHPLVESACVVA-RSQPSGKILAAFVQPASPELTIDAL-RHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05923 417 LSRHPGVTEVVVIGvADERWGQSVTACVVPREGTLSADELdQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1349-1728 |
1.42e-22 |
|
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: 102.94 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTDGE 1427
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDrVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1428 PeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLnnftndfVGRLALSARDKVLSLTS 1507
Cdd:cd05935 83 L-----------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-------AANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1508 IS------FDIFGLE--LFCSLAGGAHVTLCP---RETAMDpvklyhFIERQQPSVIQATPTVWSTIVHHlPAASQRPLT 1576
Cdd:cd05935 127 VIlaclplFHVTGFVgsLNTAVYVGGTYVLMArwdRETALE------LIEKYKVTFWTNIPTMLVDLLAT-PEFKTRDLS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1577 VL----CGGEKMPAALLTQLR-RIATRVLQVYGPTEtTIWSTCADLTHEGASDCIGTPIQATEVLVMD-QAGNPLPSGAF 1650
Cdd:cd05935 200 SLkvltGGGAPMPPAVAEKLLkLTGLRFVEGYGLTE-TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEV 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 1651 GELWLGGAGVSPGYWRNPTLSDKVFLRrqaFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRF-FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1348-1807 |
1.46e-22 |
|
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: 102.97 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTdg 1426
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDrVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1427 epeqgwaspavgfdslvsHPAAADALPIpadDTLAYIMYTSGSTGNPKGVMITHGNLnnFTNDFVGR--LALSARDKVLS 1504
Cdd:cd05969 79 ------------------TEELYERTDP---EDPTLLHYTSGTTGTPKGVLHVHDAM--IFYYFTGKyvLDLHPDDIYWC 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1505 ------LTSISFDIFGlelfcSLAGGahVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHH-LPAASQRPLT- 1576
Cdd:cd05969 136 tadpgwVTGTVYGIWA-----PWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgDELARKYDLSs 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1577 ---VLCGGEKM-PAALLTQLRRIATRVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGE 1652
Cdd:cd05969 209 lrfIHSVGEPLnPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1653 LWL--GGAGVSPGYWRNPTLSDKVFLRRqafgaeryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLss 1730
Cdd:cd05969 289 LALkpGWPSMFRGIWNDEERYKNSFIDG--------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESAL-- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1731 LDNIERSLSLIVGE-----GQqaRIVSYLQLTSGEELNEK---AVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRR 1802
Cdd:cd05969 359 MEHPAVAEAGVIGKpdplrGE--IIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436
|
....*
gi 1725075560 1803 LPAPE 1807
Cdd:cd05969 437 LKAKE 441
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1346-1803 |
1.56e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 103.99 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLridsrpfSVGVmmEKSCHVAVLL----------LGVLRAGKHYVPIDVHYPADRVSYMIE 1415
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFY-------SLGI--RKGDKVALHLdncpefifcwFGLAKIGAIMVPINARLLREESAWILQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1416 NAQARLLVTDGE-----------------------PEQGWASPAVGFDSLVSHPAAA--DALPIPADDTlAYIMYTSGST 1470
Cdd:PRK08008 107 NSQASLLVTSAQfypmyrqiqqedatplrhicltrVALPADDGVSSFTQLKAQQPATlcYAPPLSTDDT-AEILFTSGTT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1471 GNPKGVMITHGNLNnftndFVG-----RLALSARDKVLSLTSiSFDIfglELFCSLA-----GGAHVTLCPRETAMdpvK 1540
Cdd:PRK08008 186 SRPKGVVITHYNLR-----FAGyysawQCALRDDDVYLTVMP-AFHI---DCQCTAAmaafsAGATFVLLEKYSAR---A 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1541 LYHFIERQQPSVIQATPTVWSTIVHHLPAASQR-----------PLTVlcgGEKmpaalLTQLRRIATRVLQVYGPTETT 1609
Cdd:PRK08008 254 FWGQVCKYRATITECIPMMIRTLMVQPPSANDRqhclrevmfylNLSD---QEK-----DAFEERFGVRLLTSYGMTETI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1610 IWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAgvsPG------YWRNPTLSDKVflrrqaFGA 1683
Cdd:PRK08008 326 VGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGV---PGktifkeYYLDPKATAKV------LEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1684 ERYMYrTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIVGEGQQAR---IVSYLQLTSGE 1760
Cdd:PRK08008 397 DGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQD--IVVVGIKDSIRdeaIKAFVVLNEGE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1725075560 1761 ELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK08008 474 TLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
315-776 |
2.50e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 103.82 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKsNKTYV---------------LLDPQA---- 375
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALK-NGAIVgplfeafmeeavrdrLEDSEAkvli 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 376 --PAARNQSILDDVqPAL---ILADSPlhsGDAPciaPSSIDYRSLNIHA----EQLPQSRDALAYVCYTSGTTGKPKGV 446
Cdd:PRK04319 151 ttPALLERKPADDL-PSLkhvLLVGED---VEEG---PGTLDFNALMEQAsdefDIEWTDREDGAILHYTSGSTGKPKGV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 447 ------MIGREGLSNVAQN-HRDFI-------GLAQGSRVLAIASL--G---------FDAFGWdvYGALVS-GATL-YL 499
Cdd:PRK04319 224 lhvhnaMLQHYQTGKYVLDlHEDDVywctadpGWVTGTSYGIFAPWlnGatnvidggrFSPERW--YRILEDyKVTVwYT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 APSELHTDVGALHDYLTQHDIGHititpailellpremwpgLRTMIVMGDAPPADVVaWWAERT---RLCNGYGPTEAS- 575
Cdd:PRK04319 302 APTAIRMLMGAGDDLVKKYDLSS------------------LRHILSVGEPLNPEVV-RWGMKVfglPIHDNWWMTETGg 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 --IATSLC-EYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAgSG---LAHGYLHQEALSAEKFIicrlpym 649
Cdd:PRK04319 363 imIANYPAmDIKPG----SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFA------- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 650 aaeERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFV------ 722
Cdd:PRK04319 431 ---GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPvRGEIIKAFValrpgy 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 723 QPaSPELTIDALRHALvTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLD 776
Cdd:PRK04319 508 EP-SEELKEEIRGFVK-KGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
314-770 |
5.95e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 102.59 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSG-AASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDP--QAPAARNQsILDDVQPA 390
Cdd:PRK12492 47 GVTLSYAELERHSAAFAAYLQQHTDlVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPlyTAREMRHQ-FKDSGARA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 391 LI------------LADSPLHS------GDAPCIA---------------------PSSIDYRSL-----NIHAEQLPQS 426
Cdd:PRK12492 126 LVylnmfgklvqevLPDTGIEYlieakmGDLLPAAkgwlvntvvdkvkkmvpayhlPQAVPFKQAlrqgrGLSLKPVPVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 427 RDALAYVCYTSGTTGKPKGVMIGREGL-SNVAQNHRDFIGLA--------QGSRVLaIASLGFD---AFGWDVYGALVSG 494
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNLvANMLQVRACLSQLGpdgqplmkEGQEVM-IAPLPLYhiyAFTANCMCMMVSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 495 A--TLYLAPSELHTDVGALHDYLTQHDIGHITITPAILEllpremWPGLRTMIVM--------GDAPPADVVAWWAERT- 563
Cdd:PRK12492 285 NhnVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMD------HPGFKDLDFSalkltnsgGTALVKATAERWEQLTg 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 564 -RLCNGYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFi 642
Cdd:PRK12492 359 cTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 643 icrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVES-ACVVARSQPSGKILAAF 721
Cdd:PRK12492 438 --------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANcAAIGVPDERSGEAVKLF 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1725075560 722 VQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK12492 510 VVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1455-1713 |
6.13e-22 |
|
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: 101.91 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1455 PADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL--ALSARDKVLS---LTSIsfdifgLEL---FCSLAGGAH 1526
Cdd:cd17639 85 GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeLLGPDDRYLAylpLAHI------FELaaeNVCLYRGGT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1527 V------TLCP---RETAMDPVKLyhfierqQPSVIQATPTVWSTI-----------------------------VHHLP 1568
Cdd:cd17639 159 IgygsprTLTDkskRGCKGDLTEF-------KPTLMVGVPAIWDTIrkgvlaklnpmgglkrtlfwtayqsklkaLKEGP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1569 AASQ---------RPLT------VLCGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTCADLtHEGASDCIGTPIQAT 1633
Cdd:cd17639 232 GTPLldelvfkkvRAALggrlryMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDP-GDLETGRVGPPLPCC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1634 EVLVMD--QAG----NPLPSgafGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYmYRTGDIVRFNRQGQLEYLGR 1707
Cdd:cd17639 311 EIKLVDweEGGystdKPPPR---GEILIRGPNVFKGYYKNPEKT------KEAFDGDGW-FHTGDIGEFHPDGTLKIIDR 380
|
....*.
gi 1725075560 1708 NDHQVK 1713
Cdd:cd17639 381 KKDLVK 386
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
311-774 |
1.04e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.88 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 311 HADGQTYSYGEIDRASDQFACWLL-EHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDP-QAPAARNQSILDDVQ 388
Cdd:PRK08751 45 HSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPlYTPRELKHQLIDSGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 389 PAL------------ILADSPLHS------GDAPCIAPSSI-------------DYRSLNI--HAEQLPQSR-------- 427
Cdd:PRK08751 125 SVLvvidnfgttvqqVIADTPVKQvittglGDMLGFPKAALvnfvvkyvkklvpEYRINGAirFREALALGRkhsmptlq 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 ---DALAYVCYTSGTTGKPKGVMIG-REGLSNVAQNHRDFIG---LAQGSRVLAIASLGFDAFGWDVYGAL---VSGAT- 496
Cdd:PRK08751 205 iepDDIAFLQYTGGTTGVAKGAMLThRNLVANMQQAHQWLAGtgkLEEGCEVVITALPLYHIFALTANGLVfmkIGGCNh 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 497 LYLAPSELHTDVGALHDYLTQHDIGHITI------TPAILELlpreMWPGLRTMIVMGDAPPADVVAWWAERT--RLCNG 568
Cdd:PRK08751 285 LISNPRDMPGFVKELKKTRFTAFTGVNTLfngllnTPGFDQI----DFSSLKMTLGGGMAVQRSVAERWKQVTglTLVEA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 569 YGPTEASIAT-----SLCEYRpgvpwNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEkfii 643
Cdd:PRK08751 361 YGLTETSPAAcinplTLKEYN-----GSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAK---- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 644 crlpYMAAEERLyRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHP-LVESACVVARSQPSGKILAAFV 722
Cdd:PRK08751 432 ----VMDADGWL-HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPgVLEVAAVGVPDEKSGEIVKVVI 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 723 QPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWP 774
Cdd:PRK08751 507 VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1346-1775 |
5.48e-21 |
|
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: 99.08 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLRIDSRPFSVGVMMEKSC-HVAVLLLGVLRAGKHYVPIdvhYP---ADRVSYMIENAQARL 1421
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCaEWFITDLAIWMAGHISVPL---YPtlnPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1422 LVT----------DGEPEQGWASPAV---------GFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGN 1482
Cdd:cd05932 82 LFVgklddwkamaPGVPEGLISISLPppsaancqyQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1483 LNNFTNDFVGRLALSARDKVLS---LTSISFDIFgLELfCSLAGGAHVTLcpretamdPVKLYHFIE---RQQPSVIQAT 1556
Cdd:cd05932 162 FAWAAQAGIEHIGTEENDRMLSylpLAHVTERVF-VEG-GSLYGGVLVAF--------AESLDTFVEdvqRARPTLFFSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1557 PTVWST----IVHHLPAAS-QRPLTV-----------------------LCGGEKMPAALLTQLRRIATRVLQVYGPTET 1608
Cdd:cd05932 232 PRLWTKfqqgVQDKIPQQKlNLLLKIpvvnslvkrkvlkglgldqcrlaGCGSAPVPPALLEWYRSLGLNILEAYGMTEN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1609 TIWSTcadLTHEGASD--CIGTPIQATEVLVMDQagnplpsgafGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERY 1686
Cdd:cd05932 312 FAYSH---LNYPGRDKigTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEAT------AEAFTADGF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1687 MyRTGDIVRFNRQGQLEYLGRNDHQVKI-RGHRIELSEIDLSLSSLDNIErsLSLIVGEGQQARIvSYLQLtsGEELNEK 1765
Cdd:cd05932 373 L-RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVE--MVCVIGSGLPAPL-ALVVL--SEEARLR 446
|
490
....*....|...
gi 1725075560 1766 AV---RTALKARL 1775
Cdd:cd05932 447 ADafaRAELEASL 459
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
370-770 |
6.25e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 98.90 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 370 LLDPQAPAARNQSILDDVqPAL--ILADSPlhSGDAPCIAPSSIDYRSLNIHAEQLPqsrDALAYVCYTSGTTGKPKGVM 447
Cdd:PRK06188 114 IVDPAPFVERALALLARV-PSLkhVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALP---PDIAGLAYTGGTTGKPKGVM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 448 IGREGLSNVAQnhrdfIGLA-----QGSRVLAIASLGfDAFGWDVYGALVSGATLYLAPSelhTDVGALHDYLTQHDIGH 522
Cdd:PRK06188 188 GTHRSIATMAQ-----IQLAewewpADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLAK---FDPAEVLRAIEEQRITA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 523 ITITPAILELLPREmwPGLRT-------MIVMGDAPPADVvawwaertRLCNG-----------YGPTEASIATSL---- 580
Cdd:PRK06188 259 TFLVPTMIYALLDH--PDLRTrdlssleTVYYGASPMSPV--------RLAEAierfgpifaqyYGQTEAPMVITYlrkr 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 581 --CEYRPGVPWNCiGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicRLPYMaaeerlyRT 658
Cdd:PRK06188 329 dhDPDDPKRLTSC-GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF---RDGWL-------HT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 659 GDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFV-----QPASPELTID 732
Cdd:PRK06188 398 GDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEAVTAVVvlrpgAAVDAAELQA 477
|
410 420 430
....*....|....*....|....*....|....*...
gi 1725075560 733 ALRHAlvtlLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK06188 478 HVKER----KGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1331-1798 |
9.19e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 98.57 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1331 LAH--TQ-----PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFSVGVMMEKSC-HVAVLLLGVLRAGKHYVPID 1402
Cdd:PRK07470 9 LAHflRQaarrfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCnQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1403 VHYPADRVSYMIENAQARLL------------VTDGEPEQGW------ASPAVGFDSLVSHPAAADALPIPAD-DTLAYI 1463
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMichadfpehaaaVRAASPDLTHvvaiggARAGLDYEALVARHLGARVANAAVDhDDPCWF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1464 MYTSGSTGNPKGVMITHGNLNNFTNDFVGRL--ALSARDKVLSLTSISFDIfGLELFCSLAGGAHVTLCPRETaMDPVKL 1541
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHGQMAFVITNHLADLmpGTTEQDASLVVAPLSHGA-GIHQLCQVARGAATVLLPSER-FDPAEV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1542 YHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLT----VLCGGEKMPAAllTQ---LRRIATRVLQVYGPTETT----I 1610
Cdd:PRK07470 247 WALVERHRVTNLFTVPTILKMLVEH-PAVDRYDHSslryVIYAGAPMYRA--DQkraLAKLGKVLVQYFGLGEVTgnitV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1611 WSTCADLTHEGASDCIGT---PIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrRQAFgaerym 1687
Cdd:PRK07470 324 LPPALHDAEDGPDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF--RDGW------ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1688 YRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-----GEGQQARIVsylqLTSGEEL 1762
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVpdpvwGEVGVAVCV----ARDGAPV 471
|
490 500 510
....*....|....*....|....*....|....*.
gi 1725075560 1763 NEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:PRK07470 472 DEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
314-771 |
1.08e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 98.49 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGA-ASSVVAVSMDKSATLLIVLLGILKSNKT--------------YVLLDPQAPAA 378
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQECGVrKGDRVLLYMQNSPQFVIAYYAILRANAVvvpvnpmnreeelaHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 379 -RNQSILDDVQPA--------LILAD----SPLHSGDAP----CIAPSSIDYRSLNIH------AEQLPQ-----SRDAL 430
Cdd:PRK08314 113 iVGSELAPKVAPAvgnlrlrhVIVAQysdyLPAEPEIAVpawlRAEPPLQALAPGGVVawkealAAGLAPpphtaGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 431 AYVCYTSGTTGKPKGVM-IGREGLSNVAQNHrDFIGLAQGSRVLAIASLgFDAFGWdVYG---ALVSGATLYLAPselHT 506
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMhTHRTVMANAVGSV-LWSNSTPESVVLAVLPL-FHVTGM-VHSmnaPIYAGATVVLMP---RW 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 507 DVGALHDYLTQHDIGHITITPAIL-ELLpreMWPGLR-------TMIVMGDAP-PADVVAWWAERTRL--CNGYGPTEaS 575
Cdd:PRK08314 267 DREAAARLIERYRVTHWTNIPTMVvDFL---ASPGLAerdlsslRYIGGGGAAmPEAVAERLKELTGLdyVEGYGLTE-T 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 IATSLCE--YRPGVpwNCIGKPLKNYRCHILDLHH-NPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaE 652
Cdd:PRK08314 343 MAQTHSNppDRPKL--QCLGIPTFGVDARVIDPETlEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI---------E 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 653 ---ERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA-RSQPSGKILAAFVQP---- 724
Cdd:PRK08314 412 idgKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAtPDPRRGETVKAVVVLrpea 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 725 ---ASPELTIDALRHalvtllHPAA--IPSVFIFLPALPLTINGKIARQQLE 771
Cdd:PRK08314 492 rgkTTEEEIIAWARE------HMAAykYPRIVEFVDSLPKSGSGKILWRQLQ 537
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
426-772 |
1.11e-20 |
|
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: 98.31 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 426 SRDALAyVCYTSGTTGKPKgvMI----GREGLSNVAqNHRDFIGLAQGSRVLAIASLGF-DAFGWDVYGALVSGATLYLa 500
Cdd:cd05928 173 SQEPMA-IYFTSGTTGSPK--MAehshSSLGLGLKV-NGRYWLDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGACVFV- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 501 pselHT----DVGALHDYLTQHDIGHITITPAILELL-----PREMWPGLRTMIVMGDAPPADVVAWWAERT--RLCNGY 569
Cdd:cd05928 248 ----HHlprfDPLVILKTLSSYPITTFCGAPTVYRMLvqqdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTglDIYEGY 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 570 GPTEASIatsLC------EYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGS-----GLAHGYLHqealSA 638
Cdd:cd05928 324 GQTETGL---ICanfkgmKIKPG----SMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVD----NP 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 639 EKfiicrlpyMAAEER--LYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV-ESACVVARSQPSG 715
Cdd:cd05928 393 EK--------TAATIRgdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVvESAVVSSPDPIRG 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 716 KILAAFVQPAS------PELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd05928 465 EVVKAFVVLAPqflshdPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1460-1801 |
1.27e-20 |
|
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: 95.09 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1460 LAYIMYTSGSTGNPKGVMITHGNLnnfTNDFVG---RLALSARDKVLsLTSISFDIFGLE-LFCSLAGGAHVTLCPRETA 1535
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANL---LASAAGlhsRLGFGGGDSWL-LSLPLYHVGGLAiLVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1536 mdpvkLYHFIERQQPSVIQATPT-VWSTIVHHLPAASQRPL-TVLCGGEKMPAALLTQLRRIATRVLQVYGPTET--TIW 1611
Cdd:cd17630 78 -----LAEDLAPPGVTHVSLVPTqLQRLLDSGQGPAALKSLrAVLLGGAPIPPELLERAADRGIPLYTTYGMTETasQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1612 STCADLTHEGASdciGTPIQATEVLVMDQagnplpsgafGELWLGGAGVSPGYWRNPTLSDkvflrrqafGAERYMYRTG 1691
Cdd:cd17630 153 TKRPDGFGRGGV---GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPE---------FNEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1692 DIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIVGE-----GQqaRIVSYlqLTSGEELNEKA 1766
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD--AFVVGVpdeelGQ--RPVAV--IVGRGPADPAE 284
|
330 340 350
....*....|....*....|....*....|....*
gi 1725075560 1767 VRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIR 1801
Cdd:cd17630 285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
429-767 |
1.57e-20 |
|
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: 94.78 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 429 ALAYVCYTSGTTGKPKGVmigreglsnvAQNHRDFIG-------LAQGSRVLAIAslgfdafgwdVYGALVSGATLYLAP 501
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAY----------YRSERSWIEsfvcnedLFNISGEDAIL----------APGPLSHSLFLYGAI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 SELHTDvGALH-----------DYLTQHDIGHITITPAILELLPREMWPGLRTMIVM--GDAPPAD---VVAWWAERTRL 565
Cdd:cd17633 61 SALYLG-GTFIgqrkfnpkswiRKINQYNATVIYLVPTMLQALARTLEPESKIKSIFssGQKLFEStkkKLKNIFPKANL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 566 CNGYGPTEASIATSLCeYRPGVPWNCIGKPLKNYRCHILDLHHNPLpvgfeGELCIAGSGLAHGYLHQEALSAEKFiicr 645
Cdd:cd17633 140 IEFYGTSELSFITYNF-NQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVRGGFSNPDGW---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 646 lpymaaeerlYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQp 724
Cdd:cd17633 210 ----------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARfGEIAVALYS- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1725075560 725 aSPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:cd17633 279 -GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1456-1803 |
1.80e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 99.23 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 ADDTLAyIMYTSGSTGNPKGVMITHGNLnnFTN----DFVgrLALSARDKVLSLTSIsFDIFGL--ELFCSLAGGAHVTL 1529
Cdd:PRK08633 781 PDDTAT-IIFSSGSEGEPKGVMLSHHNI--LSNieqiSDV--FNLRNDDVILSSLPF-FHSFGLtvTLWLPLLEGIKVVY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1530 CPRETamDPVKLYHFIERQQPSVIQATPTVWSTI-----VHHLPAASQRplTVLCGGEKMPAALLTQLR-RIATRVLQVY 1603
Cdd:PRK08633 855 HPDPT--DALGIAKLVAKHRATILLGTPTFLRLYlrnkkLHPLMFASLR--LVVAGAEKLKPEVADAFEeKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1604 GPTETT--------------IWSTCAdlTHEGAsdcIGTPIQATEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNP 1668
Cdd:PRK08633 931 GATETSpvasvnlpdvlaadFKRQTG--SKEGS---VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDP 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1669 TLSDKVFlrrQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNiERSLSLIV------ 1742
Cdd:PRK08633 1006 EKTAEVI---KDIDGIGW-YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALG-GEEVVFAVtavpde 1080
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 1743 --GEgqqaRIVsyLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK08633 1081 kkGE----KLV--VLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1347-1803 |
2.36e-20 |
|
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: 96.39 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1347 QYSYRQLWAQSERVAHAL-----LRIDSRpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARL 1421
Cdd:cd05958 10 EWTYRDLLALANRIANVLvgelgIVPGNR---VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1422 LVTDGEpeqgwaspavgfdslVSHpaaadalpipADDTlAYIMYTSGSTGNPKGVMITHGNLNNfTNDFVGRLALSAR-- 1499
Cdd:cd05958 87 ALCAHA---------------LTA----------SDDI-CILAFTSGTTGAPKATMHFHRDPLA-SADRYAVNVLRLRed 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1500 DKVLSLTSISFDI-FGLELFCSLAGGAHVTLCPRETamdPVKLYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLT-- 1576
Cdd:cd05958 140 DRFVGSPPLAFTFgLGGVLLFPFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAMLAH-PDAAGPDLSsl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1577 VLC--GGEKMPAALLTQLRR-IATRVLQVYGPTET--TIWSTCADLTHEGASdciGTPIQATEVLVMDQAGNPLPSGAFG 1651
Cdd:cd05958 216 RKCvsAGEALPAALHRAWKEaTGIPIIDGIGSTEMfhIFISARPGDARPGAT---GKPVPGYEAKVVDDEGNPVPDGTIG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1652 ELWLGGagvSPGYWRnptLSDKvflRRQAFGAERYMYrTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSL 1731
Cdd:cd05958 293 RLAVRG---PTGCRY---LADK---RQRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQH 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1732 DNIERslSLIVGEGQQARIV---SYLQLTSG--------EELNEKAVRTALKARLPNIMipsgfVVLSAFPLTNNNKIDI 1800
Cdd:cd05958 363 PAVAE--CAVVGHPDESRGVvvkAFVVLRPGvipgpvlaRELQDHAKAHIAPYKYPRAI-----EFVTELPRTATGKLQR 435
|
...
gi 1725075560 1801 RRL 1803
Cdd:cd05958 436 FAL 438
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
435-770 |
2.89e-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: 96.29 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMIGREGLSNVAQNHRDF---IGLAQGSRVLAIASLGFDA-FGWdVYGALVSGATLYLAPselHTDVGA 510
Cdd:cd05929 132 YSGGTTGRPKGIKRGLPGGPPDNDTLMAAalgFGPGADSVYLSPAPLYHAApFRW-SMTALFMGGTLVLME---KFDPEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 511 LHDYLTQHDIGHITITPAI---LELLPREM-----WPGLRTMIVMGDAPPADV----VAWWAERtrLCNGYGPTEAsIAT 578
Cdd:cd05929 208 FLRLIERYRVTFAQFVPTMfvrLLKLPEAVrnaydLSSLKRVIHAAAPCPPWVkeqwIDWGGPI--IWEYYGGTEG-QGL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 579 SLCEyrpGVPW----NCIGKPLKNyRCHILDLHHNPLPVGFEGELCIAGSG--LAHGYLHQEALsaekfiicrlpymAAE 652
Cdd:cd05929 285 TIIN---GEEWlthpGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPgfEYTNDPEKTAA-------------ARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 653 ERLYRT-GDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPELT 730
Cdd:cd05929 348 EGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEElGQRVHAVVQPAPGADA 427
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1725075560 731 IDALRHALVTL----LHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:cd05929 428 GTALAEELIAFlrdrLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1325-1798 |
3.93e-20 |
|
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: 96.21 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1325 LMHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDV 1403
Cdd:cd12118 7 LSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDtVAVLAPNTPAMYELHFGVPMAGAVLNALNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1404 HYPADRVSYMIENAQARLLVTDGEPEqgwaspavgFDSLVSHpAAADALPIPADD-----TLAYimyTSGSTGNPKGVMI 1478
Cdd:cd12118 87 RLDAEEIAFILRHSEAKVLFVDREFE---------YEDLLAE-GDPDFEWIPPADewdpiALNY---TSGTTGRPKGVVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1479 TH--GNLNNFTNDFVGRLALSARdkvlSLTSIsfDIFGLELFC-----SLAGGAHVTLcpREtaMDPVKLYHFIERQQPS 1551
Cdd:cd12118 154 HHrgAYLNALANILEWEMKQHPV----YLWTL--PMFHCNGWCfpwtvAAVGGTNVCL--RK--VDAKAIYDLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1552 VIQATPTVWSTIVHHlPAASQRPLT----VLCGGEKMPAALLTQLRRIATRVLQVYGPTETT------IWSTCADLTHEG 1621
Cdd:cd12118 224 HFCGAPTVLNMLANA-PPSDARPLPhrvhVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpatvcAWKPEWDELPTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1622 ------ASDCIGTPIQaTEVLVMD-QAGNPLPSGA--FGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgaERYMYRTGD 1692
Cdd:cd12118 303 erarlkARQGVRYVGL-EEVDVLDpETMKPVPRDGktIGEIVFRGNIVMKGYLKNPEATAEAF--------RGGWFHSGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1693 IVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDlslSSLDNIERSLSLIV--------GEGQQARIVsylqLTSGEELNE 1764
Cdd:cd12118 374 LAVIHPDGYIEIKDRSKDIIISGGENISSVEVE---GVLYKHPAVLEAAVvarpdekwGEVPCAFVE----LKEGAKVTE 446
|
490 500 510
....*....|....*....|....*....|....
gi 1725075560 1765 KAVRTALKARLPNIMIPSGfVVLSAFPLTNNNKI 1798
Cdd:cd12118 447 EEIIAFCREHLAGFMVPKT-VVFGELPKTSTGKI 479
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
426-772 |
4.63e-20 |
|
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: 96.86 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 426 SRDALaYVCYTSGTTGKPKGVMIGREG-LSNVAQNHRDFIGLAQGSRVLAIASLGfdafgW------DVYGALVSGAT-- 496
Cdd:cd05966 230 SEDPL-FILYTSGSTGKPKGVVHTTGGyLLYAATTFKYVFDYHPDDIYWCTADIG-----WitghsyIVYGPLANGATtv 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 497 -------------------------LYLAPselhTDVGALH----DYLTQHDIGHITITPAILELLPREMWPGLRTMIVM 547
Cdd:cd05966 304 mfegtptypdpgrywdivekhkvtiFYTAP----TAIRALMkfgdEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 548 GDAPPADvvAWWAERTrlcNGYGPTEASIATSLceyRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGS--G 625
Cdd:cd05966 380 ERCPIVD--TWWQTET---GGIMITPLPGATPL---KPG----SATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 626 LAHGYLHQEalsaEKFIICrlpYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESA 705
Cdd:cd05966 448 MARTIYGDH----ERYEDT---YFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEA 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 706 CVVARSQP-SGKILAAFV-----QPASPELtIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd05966 521 AVVGRPHDiKGEAIYAFVtlkdgEEPSDEL-RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1348-1798 |
5.07e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 95.28 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTDg 1426
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDvVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1427 epeqgwaspavgfdslvshpaaADALPIPADDTLAyIMYTSGSTGNPKGVMITHGNLNNFTNDFvgRLALSARDKvlslt 1506
Cdd:cd05973 80 ----------------------AANRHKLDSDPFV-MMFTSGTTGLPKGVPVPLRALAAFGAYL--RDAVDLRPE----- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1507 sisfDIF----------GL--ELFCSLAGGAHVTLcpRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRP 1574
Cdd:cd05973 130 ----DSFwnaadpgwayGLyyAITGPLALGHPTIL--LEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1575 LTVL----CGGEKMPAALLTQLR-RIATRVLQVYGPTETTI-----WSTcADLTHEGASdciGTPIQATEVLVMDQAGNP 1644
Cdd:cd05973 204 KGRLrrvsSAGEPLTPEVIRWFDaALGVPIHDHYGQTELGMvlanhHAL-EHPVHAGSA---GRAMPGWRVAVLDDDGDE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1645 LPSGAFGELWLGGAGvSP-----GYWRNPTLSdkvflrrqafgAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRI 1719
Cdd:cd05973 280 LGPGEPGRLAIDIAN-SPlmwfrGYQLPDTPA-----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1720 ELSEIDLSLSSLDNIERSLSLIVGEGQQARIV-SYLQLTSGEELN---EKAVRTALKARLPNIMIPSGFVVLSAFPLTNN 1795
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVkAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
...
gi 1725075560 1796 NKI 1798
Cdd:cd05973 428 GKI 430
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
426-770 |
6.08e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 96.28 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 426 SRDALAYVCYTSGTTGKPKGVMIG-REGLSNVAQNHRDFIGLAQGSRVLAIASLG-FDAFGWDVYGALV--SGAT--LYL 499
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLThRNMLANLEQAKAAYGPLLHPGKELVVTALPlYHIFALTVNCLLFieLGGQnlLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 APSELHTDVGALHDYLTQHDIGHITITPAIL--ELLPREMWPGLRTMIVMGDAPPADVVAWWAERT--RLCNGYGPTEAS 575
Cdd:PRK08974 284 NPRDIPGFVKELKKYPFTAITGVNTLFNALLnnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTgqYLLEGYGLTECS 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 IATSLCeyrpgvPWNC------IGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEkfiICRLPYM 649
Cdd:PRK08974 364 PLVSVN------PYDLdyysgsIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE---VIKDGWL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 650 AaeerlyrTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV-ESACVVARSQPSGKILAAFVQPASPE 728
Cdd:PRK08974 435 A-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVlEVAAVGVPSEVSGEAVKIFVVKKDPS 507
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1725075560 729 LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK08974 508 LTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1316-1824 |
7.23e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 96.18 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1316 ADAGSRDSLLMHIGRLAHTQPDSLAVSC--------ERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAV 1386
Cdd:PRK07529 19 AARDLPASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDvVAFLLPNLPETHF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1387 LLLGVLRAGKhYVPIDVHYPADRVSYMIENAQARLLVT---------------------------------DGEPEQGWA 1433
Cdd:PRK07529 99 ALWGGEAAGI-ANPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvaevlaalpelrtvvevdlarYLPGPKRLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1434 SPAV---------GFDSLV---SHPAAADALPIPADDTLAYImYTSGSTGNPKGVMITHGNLnnFTNDFVGRLALSAR-D 1500
Cdd:PRK07529 178 VPLIrrkaharilDFDAELarqPGDRLFSGRPIGPDDVAAYF-HTGGTTGMPKLAQHTHGNE--VANAWLGALLLGLGpG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1501 KVLsltsisfdIFGLELF----------CSLAGGAHVTLCPRETAMDPVKLYHF---IERQQPSVIQATPTVWStivhhl 1567
Cdd:PRK07529 255 DTV--------FCGLPLFhvnallvtglAPLARGAHVVLATPQGYRGPGVIANFwkiVERYRINFLSGVPTVYA------ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1568 pAASQRPL---------TVLCGGEKMPAALLTQLRRiAT--RVLQVYGPTETTIWSTCADLTHEGASDCIGTPI--QATE 1634
Cdd:PRK07529 321 -ALLQVPVdghdisslrYALCGAAPLPVEVFRRFEA-ATgvRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLpyQRVR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1635 VLVMDQAGN---PLPSGAFGELWLGGAGVSPGYwrnpTLSDKvflRRQAFGAERYMyRTGDIVRFNRQGQLEYLGRndhq 1711
Cdd:PRK07529 399 VVILDDAGRylrDCAVDEVGVLCIAGPNVFSGY----LEAAH---NKGLWLEDGWL-NTGDLGRIDADGYFWLTGR---- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1712 VK---IR-GHRIELSEIDLSLSSLDNIerSLSLIVGE-----GQQAriVSYLQLTSGEELNEKAVRTALKARLPN-IMIP 1781
Cdd:PRK07529 467 AKdliIRgGHNIDPAAIEEALLRHPAV--ALAAAVGRpdahaGELP--VAYVQLKPGASATEAELLAFARDHIAErAAVP 542
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1725075560 1782 SGFVVLSAFPLTNNNKIDirrlpAPETRYSASEADYTPAANEA 1824
Cdd:PRK07529 543 KHVRILDALPKTAVGKIF-----KPALRRDAIRRVLRAALRDA 580
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1325-1675 |
7.57e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 95.78 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1325 LMHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRID-SRPFSVGVMMEKS-----CHVAVLLLG-VLRAgkh 1397
Cdd:PRK08162 21 LSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGiGRGDTVAVLLPNIpamveAHFGVPMAGaVLNT--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1398 yvpIDVHYPADRVSYMIENAQARLLVTDGE------------------------PEQGWASP--AVGFDSLVSHPAAADA 1451
Cdd:PRK08162 98 ---LNTRLDAASIAFMLRHGEAKVLIVDTEfaevarealallpgpkplvidvddPEYPGGRFigALDYEAFLASGDPDFA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1452 LPIPAD--DTLAyIMYTSGSTGNPKGVMITHgnlnnftndfvgRLA-LSARDKVLS--LTSISFDIFGLELF-C------ 1519
Cdd:PRK08162 175 WTLPADewDAIA-LNYTSGTTGNPKGVVYHH------------RGAyLNALSNILAwgMPKHPVYLWTLPMFhCngwcfp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1520 -SLAGGAHVTLCPREtaMDPVKLYHFIERQQPSVIQATPTVWSTIVhHLPAASQRPLT----VLCGGEKMPAALLTQLRR 1594
Cdd:PRK08162 242 wTVAARAGTNVCLRK--VDPKLIFDLIREHGVTHYCGAPIVLSALI-NAPAEWRAGIDhpvhAMVAGAAPPAAVIAKMEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1595 IATRVLQVYGPTETTIWST-CA------DLTHEGASDC-----IGTPIQAtEVLVMD-QAGNPLPSGA--FGELWLGGAG 1659
Cdd:PRK08162 319 IGFDLTHVYGLTETYGPATvCAwqpewdALPLDERAQLkarqgVRYPLQE-GVTVLDpDTMQPVPADGetIGEIMFRGNI 397
|
410
....*....|....*.
gi 1725075560 1660 VSPGYWRNPTLSDKVF 1675
Cdd:PRK08162 398 VMKGYLKNPKATEEAF 413
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1348-1772 |
8.00e-20 |
|
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: 94.82 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVaHALLRIDSRPFS--VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTD 1425
Cdd:cd05914 8 LTYKDLADNIAKF-ALLLKINGVGTGdrVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1426 GEpeqgwaspavgfdslvshpaaadalpipadDTLAYIMYTSGSTGNPKGVMITHGNLnnFTN-DFVGR-LALSARDKVL 1503
Cdd:cd05914 87 DE------------------------------DDVALINYTSGTTGNSKGVMLTYRNI--VSNvDGVKEvVLLGKGDKIL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1504 SLTSISfDIFGL--ELFCSLAGGAHVtlcpretamdpvklyHFIERQQPSVI------QATPTVWST---IVHHLPAASQ 1572
Cdd:cd05914 135 SILPLH-HIYPLtfTLLLPLLNGAHV---------------VFLDKIPSAKIialafaQVTPTLGVPvplVIEKIFKMDI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1573 RPLTVL------------------------------------CGGEKMPAALLTQLRRIATRVLQVYGPTET------TI 1610
Cdd:cd05914 199 IPKLTLkkfkfklakkinnrkirklafkkvheafggnikefvIGGAKINPDVEEFLRTIGFPYTIGYGMTETapiisySP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1611 WSTCadlthegASDCIGTPIQATEVLVMDqagnPLPSGAFGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYmYRT 1690
Cdd:cd05914 279 PNRI-------RLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEAT------AEAFDKDGW-FHT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1691 GDIVRFNRQGQLEYLGRNDHQ-VKIRGHRIELSEIDLSLSSLDNIERSLsLIVGEGQ-QARIVSYLQLTSGEELNEKAVR 1768
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESL-VVVQEKKlVALAYIDPDFLDVKALKQRNII 419
|
....
gi 1725075560 1769 TALK 1772
Cdd:cd05914 420 DAIK 423
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1330-1798 |
1.31e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 94.83 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPAD 1408
Cdd:PRK06155 29 RQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDrVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYMIENAQARLLVTDGE--------PEQGWASPAV---GFDSLVSHPAAADALPIPA------------DDTLAyIMY 1465
Cdd:PRK06155 109 QLEHILRNSGARLLVVEAAllaaleaaDPGDLPLPAVwllDAPASVSVPAGWSTAPLPPldapapaaavqpGDTAA-ILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1466 TSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDkVLSLTSISFDIFGLELFCS-LAGGAHVTLCPRETAmdpvklyhf 1544
Cdd:PRK06155 188 TSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-VLYTTLPLFHTNALNAFFQaLLAGATYVLEPRFSA--------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1545 iERQQPSVI--QATPT-VWSTIVHHL----PAASQRPLTVLCG-GEKMPAALLTQLR-RIATRVLQVYGPTETTiwSTCA 1615
Cdd:PRK06155 258 -SGFWPAVRrhGATVTyLLGAMVSILlsqpARESDRAHRVRVAlGPGVPAALHAAFReRFGVDLLDGYGSTETN--FVIA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1616 DLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGA---GVSPGYWRNPTlsdkvflrrQAFGAERYM-YRTG 1691
Cdd:PRK06155 335 VTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPE---------KTVEAWRNLwFHTG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1692 DIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-GEGQQARIVSYLQLTSGEELNEKAVRTA 1770
Cdd:PRK06155 406 DRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVpSELGEDEVMAAVVLRDGTALEPVALVRH 485
|
490 500
....*....|....*....|....*...
gi 1725075560 1771 LKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:PRK06155 486 CEPRLAYFAVPRYVEFVAALPKTENGKV 513
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
314-782 |
1.63e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 94.83 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSG-AASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDD--VQPA 390
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLQQHTDlKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDsgAKAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 391 LILAD----------------------SPLHSGDAPCIAPSSIDYRSLNIHAEQLPQS---RDAL--------------- 430
Cdd:PRK05677 127 VCLANmahlaekvlpktgvkhvivtevADMLPPLKRLLINAVVKHVKKMVPAYHLPQAvkfNDALakgagqpvteanpqa 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 431 ---AYVCYTSGTTGKPKGVMIGREGL-SNVAQNhRDFIG--LAQGSRVLaIASLGFD---AFGWDVYGALVSGA--TLYL 499
Cdd:PRK05677 207 ddvAVLQYTGGTTGVAKGAMLTHRNLvANMLQC-RALMGsnLNEGCEIL-IAPLPLYhiyAFTFHCMAMMLIGNhnILIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 APSELHTDVGALHDYLTQHDIGHITITPAIL--ELLPREMWPGLRTMIVMGDAPPADVVAWWAERT--RLCNGYGPTEAS 575
Cdd:PRK05677 285 NPRDLPAMVKELGKWKFSGFVGLNTLFVALCnnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTgcAICEGYGMTETS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 IATSLCEYRpGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEkfiicrlpyMAAEERL 655
Cdd:PRK05677 365 PVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE---------ILDSDGW 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 656 YRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHP-LVESACVVARSQPSGKILAAF-VQPASPELTIDA 733
Cdd:PRK05677 435 LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPgVLQCAAIGVPDEKSGEAIKVFvVVKPGETLTKEQ 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1725075560 734 LRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEkwplDERNERL 782
Cdd:PRK05677 515 VMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR----DEELKKA 559
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
426-724 |
2.70e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 94.40 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 426 SRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASL--GFD-AFGwdvYGALVSGATLYLAPS 502
Cdd:COG1022 181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLahVFErTVS---YYALAAGATVAFAES 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 503 -----------------------E-LHTDV-----------GALHD----------------------YLTQHDIGHITI 525
Cdd:COG1022 258 pdtlaedlrevkptfmlavprvwEkVYAGIqakaeeagglkRKLFRwalavgrryararlagkspsllLRLKHALADKLV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 526 TPAILELLpremwpG--LRTMIVmGDAP-PADVVAW-WAERTRLCNGYGPTEASIATSLC---EYRPGvpwnCIGKPLKN 598
Cdd:COG1022 338 FSKLREAL------GgrLRFAVS-GGAAlGPELARFfRALGIPVLEGYGLTETSPVITVNrpgDNRIG----TVGPPLPG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 599 YRCHILDlhhnplpvgfEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDH 678
Cdd:COG1022 407 VEVKIAE----------DGEILVRGPNVMKGYYKNPEATAEAF---------DADGWLHTGDIGELDEDGFLRITGRKKD 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1725075560 679 QVKIR-GVRIEMGEVESAVRSHPLVESACVVARSQPSgkiLAAFVQP 724
Cdd:COG1022 468 LIVTSgGKNVAPQPIENALKASPLIEQAVVVGDGRPF---LAALIVP 511
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
312-773 |
2.82e-19 |
|
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: 93.67 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSN------------------------KT 367
Cdd:COG1021 46 DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGaipvfalpahrraeishfaeqseaVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 368 YV------LLDPQAPAARNQSILDDVQPALILADS-PLHSGDAPCIAPSSIDYRSLNIhaeqlpqsrDALAYVCYTSGTT 440
Cdd:COG1021 126 YIipdrhrGFDYRALARELQAEVPSLRHVLVVGDAgEFTSLDALLAAPADLSEPRPDP---------DDVAFFQLSGGTT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 441 GKPKgvMIGREglsnvaqnHRDFI----------GLAQGSRVLAI---------ASLGFdafgwdvYGALVSGATLYLAP 501
Cdd:COG1021 197 GLPK--LIPRT--------HDDYLysvrasaeicGLDADTVYLAAlpaahnfplSSPGV-------LGVLYAGGTVVLAP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 SelhTDVGALHDYLTQHDIGHITITPAI----LELLPREMW--PGLRTMIVmGDAPPADVVAwwaERTR------LCNGY 569
Cdd:COG1021 260 D---PSPDTAFPLIERERVTVTALVPPLallwLDAAERSRYdlSSLRVLQV-GGAKLSPELA---RRVRpalgctLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 570 GpteasIATSLCEY-RPGVPW----NCIGKPLKNY---RchILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKF 641
Cdd:COG1021 333 G-----MAEGLVNYtRLDDPEevilTTQGRPISPDdevR--IVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 642 IicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVkIR-GVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILA 719
Cdd:COG1021 406 T---------PDGFYRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYlGERSC 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 720 AFVQPASPELTIDALRHALVTlLHPAA--IPSVFIFLPALPLTINGKIARQQLEKW 773
Cdd:COG1021 476 AFVVPRGEPLTLAELRRFLRE-RGLAAfkLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
314-770 |
2.97e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 93.41 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSPLhsgDAPCIAPSSI---------DYRSLNIH----AEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNH 460
Cdd:PRK06145 105 VDEEF---DAIVALETPKividaaaqaDSRRLAQGgleiPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 461 RDFIGLAQGSRVLAIASL----GFDAFGWDVygaLVSGATLYLapsELHTDVGALHDYLTQHDIGHITITP----AILEL 532
Cdd:PRK06145 182 VIALGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGGTLRI---HREFDPEAVLAAIERHRLTCAWMAPvmlsRVLTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 533 LPREMW--PGLRTMIVMGDAPPADVVAWWAE---RTRLCNGYGPTEASIATSLCEY-RPGVPWNCIGKPLKNYRCHILDL 606
Cdd:PRK06145 256 PDRDRFdlDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTETCSGDTLMEAgREIEKIGSTGRALAHVEIRIADG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 607 HHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaeERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVR 686
Cdd:PRK06145 336 AGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY----------GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 687 IEMGEVESAVRSHPLVESACVVARSQP--SGKILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGK 764
Cdd:PRK06145 406 IASSEVERVIYELPEVAEAAVIGVHDDrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGK 485
|
....*.
gi 1725075560 765 IARQQL 770
Cdd:PRK06145 486 VLKRVL 491
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
316-770 |
3.96e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 93.45 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 316 TYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLD-----PQ--APAARNQ------- 381
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNtgfsgPQlaEVAAREGvkalvyd 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 382 ----SILDDVQPALILADS-PLHSGDAPCIAPSSIDYRSLNIH--AEQLPQSRDALAYVCYTSGTTGKPKGVMIGR-EGL 453
Cdd:PRK07788 154 deftDLLSALPPDLGRLRAwGGNPDDDEPSGSTDETLDDLIAGssTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEpSPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 454 SNVAQnHRDFIGLAQGSRVLAIASLgFDAFGWDVYG-ALVSGATLYLA----PSElhtdvgALHDyLTQHDIGHITITPA 528
Cdd:PRK07788 234 APLAG-LLSRVPFRAGETTLLPAPM-FHATGWAHLTlAMALGSTVVLRrrfdPEA------TLED-IAKHKATALVVVPV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 529 ----ILELLPrEMWPG-----LRTMIVMGDAPPADVVAWWAER--TRLCNGYGPTEASIAT--SLCEYR--PGvpwnCIG 593
Cdd:PRK07788 305 mlsrILDLGP-EVLAKydtssLKIIFVSGSALSPELATRALEAfgPVLYNLYGSTEVAFATiaTPEDLAeaPG----TVG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 594 KPLKNYRCHILDLHHNPLPVGFEGELcIAGSGLA-HGYLHqealSAEKFIIcrlpymaaeERLYRTGDIAKWDEQGNIIF 672
Cdd:PRK07788 380 RPPKGVTVKILDENGNEVPRGVVGRI-FVGNGFPfEGYTD----GRDKQII---------DGLLSSGDVGYFDEDGLLFV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 673 VGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSV 750
Cdd:PRK07788 446 DGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEfGQRLRAFVVKAPGAaLDEDAIKDYVRDNLARYKVPRD 525
|
490 500
....*....|....*....|
gi 1725075560 751 FIFLPALPLTINGKIARQQL 770
Cdd:PRK07788 526 VVFLDELPRNPTGKVLKREL 545
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1331-1827 |
4.04e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 93.55 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1331 LAHTQPDSLAVSCERQQYSYRQLWAQSERVAHAL--LRIDSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDvhyPAD 1408
Cdd:PRK13388 10 RDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALiaLADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLN---TTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYM---IENAQARLLVTDGEPE---QGWASPAVGFdSLVSHPAAADALPIPAD---------DTLAYIMYTSGSTGNP 1473
Cdd:PRK13388 87 RGAALaadIRRADCQLLVTDAEHRpllDGLDLPGVRV-LDVDTPAYAELVAAAGAltphrevdaMDPFMLIFTSGTTGAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1474 KGVMITHGNLNNFTNDFVGRLALSARDkvlsltsisFDIFGLELFCS----------LAGGAHVTLCPRETA---MDPVK 1540
Cdd:PRK13388 166 KAVRCSHGRLAFAGRALTERFGLTRDD---------VCYVSMPLFHSnavmagwapaVASGAAVALPAKFSAsgfLDDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1541 LYH---FIERQQP-SVIQATPtvwstivhHLPAASQRPLTVLCGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTCAD 1616
Cdd:PRK13388 237 RYGatyFNYVGKPlAYILATP--------ERPDDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1617 LTHEGAsdcIGTPIQATEVL-----------VMDQAGNPL-PSGAFGELW-LGGAGVSPGYWRNPtlsdkvflrrqAFGA 1683
Cdd:PRK13388 309 GTPPGS---IGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELVnTAGAGFFEGYYNNP-----------EATA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1684 ERY---MYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGE---GQQarIVSYLQLT 1757
Cdd:PRK13388 375 ERMrhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDervGDQ--VMAALVLR 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1758 SGEELNEKAVRTALKAR--LPNIMIPsGFVVLSA-FPLTNNNKIDIRRL-------PAPETRYS-ASEADYTPAANEAES 1826
Cdd:PRK13388 453 DGATFDPDAFAAFLAAQpdLGTKAWP-RYVRIAAdLPSTATNKVLKRELiaqgwatGDPVTLWVrRGGPAYRLMSEPAKA 531
|
.
gi 1725075560 1827 A 1827
Cdd:PRK13388 532 A 532
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
310-781 |
4.42e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 92.92 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAaSSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:PRK07638 20 IKENDRVLTYKDWFESVCKVANWLNEKESK-NKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILAD----SPLHSGDAPCIapsSIDYRSLNIHAE-----QLPQSRDALAYVCYTSGTTGKPKG-VMIGREGLSNVAQN 459
Cdd:PRK07638 99 DMIVTEryklNDLPDEEGRVI---EIDEWKRMIEKYlptyaPIENVQNAPFYMGFTSGSTGKPKAfLRAQQSWLHSFDCN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 460 HRDFiGLAQGSRVLAIASLGFDAFgwdVYGA---LVSGATLYLAPSelHTDVGALhDYLTQHDIGHITITPAILELLPRE 536
Cdd:PRK07638 176 VHDF-HMKREDSVLIAGTLVHSLF---LYGAistLYVGQTVHLMRK--FIPNQVL-DKLETENISVMYTVPTMLESLYKE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 537 mwPGLR----TMIVMGDAPPADVVAWWAER---TRLCNGYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHN 609
Cdd:PRK07638 249 --NRVIenkmKIISSGAKWEAEAKEKIKNIfpyAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 610 PLPVGFEGELCIAGSGLAHGYLHQEALSAEkfiicrlpymAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEM 689
Cdd:PRK07638 327 EVQKGEIGTVYVKSPQFFMGYIIGGVLARE----------LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 690 GEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASpelTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQ 768
Cdd:PRK07638 397 EEIESVLHEHPAVDEIVVIGVPDSYwGEKPVAIIKGSA---TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARM 473
|
490
....*....|...
gi 1725075560 769 QLEKWpLDERNER 781
Cdd:PRK07638 474 EAKSW-IENQEKI 485
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
428-765 |
4.60e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 93.19 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIGREGL-SNVAqNHRDFIGLAQGSRVLaIAS-----LGFdafgwdVYGALVS---GATLY 498
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLmANIV-PYAERLGLGADDVIL-MASpmahqTGF------MYGLMMPvmlGATAV 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 499 LAPSelhTDVGALHDYLTQHDIGH-ITITPAILEL-----LPREMWPGLRTMIVMGDAPPADVV--AWWAERTRLCNGYG 570
Cdd:PRK13295 269 LQDI---WDPARAAELIRTEGVTFtMASTPFLTDLtravkESGRPVSSLRTFLCAGAPIPGALVerARAALGAKIVSAWG 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 571 PTEASIATSLCEYRP-GVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAekfiicrlpyM 649
Cdd:PRK13295 346 MTENGAVTLTKLDDPdERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG----------T 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 650 AAEErLYRTGDIAKWDEQGNIIFVGR-RDhqVKIRGVR-IEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQP-A 725
Cdd:PRK13295 416 DADG-WFDTGDLARIDADGYIRISGRsKD--VIIRGGEnIPVVEIEALLYRHPAIAQVAIVAYPDERlGERACAFVVPrP 492
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1725075560 726 SPELTIDA----LRHALVTLLHpaaIPSVFIFLPALPLTINGKI 765
Cdd:PRK13295 493 GQSLDFEEmvefLKAQKVAKQY---IPERLVVRDALPRTPSGKI 533
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
313-768 |
6.23e-19 |
|
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: 92.69 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAV---SMDksatLLIVLLGILKSNKTYV-LLDPQAP--AARNQSILDD 386
Cdd:cd05931 21 REETLTYAELDRRARAIAARLQAVGKPGDRVLLLappGLD----FVAAFLGCLYAGAIAVpLPPPTPGrhAERLAAILAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 387 VQPALILADSPLHSGDAPCIAPSSIDYRSLNIHAEQLP-----------QSRDALAYVCYTSGTTGKPKGVMIGREGL-S 454
Cdd:cd05931 97 AGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPdtsaadwpppsPDPDDIAYLQYTSGSTGTPKGVVVTHRNLlA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 455 NVAQNHRDFiGLAQGSRVLaiaslgfdafGW-----D---VYG---ALVSGATLYL-APS----------ELHTDVGALH 512
Cdd:cd05931 177 NVRQIRRAY-GLDPGDVVV----------SWlplyhDmglIGGlltPLYSGGPSVLmSPAaflrrplrwlRLISRYRATI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 513 --------DY---------LTQHDIGHIT--------ITPAILELLPREMWP-GLR-------------TMIVMGDAPPA 553
Cdd:cd05931 246 saapnfayDLcvrrvrdedLEGLDLSSWRvalngaepVRPATLRRFAEAFAPfGFRpeafrpsyglaeaTLFVSGGPPGT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 554 DVVAWWAERTRLcngygptEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHN-PLPVGFEGELCIAGSGLAHGYLH 632
Cdd:cd05931 326 GPVVLRVDRDAL-------AGRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 633 QEALSAEKFiicrLPYMAAEERLY-RTGDIA-KWDeqGNIIFVGRRDHQVKIRGVRIEMGEVESAVR-SHPLVESACVVA 709
Cdd:cd05931 399 RPEATAETF----GALAATDEGGWlRTGDLGfLHD--GELYITGRLKDLIIVRGRNHYPQDIEATAEeAHPALRPGCVAA 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 710 RSQPSGKILAAFV--------QPASPELTIDALRHALVTL--LHPAAIpsVFIFLPALPLTINGKIARQ 768
Cdd:cd05931 473 FSVPDDGEERLVVvaevergaDPADLAAIAAAIRAAVAREhgVAPADV--VLVRPGSIPRTSSGKIQRR 539
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1451-1803 |
7.71e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.63 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1451 ALPIPADDtLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSAR---DKVLSLTSIS-FDIFGLE----LFCSLA 1522
Cdd:PRK08751 202 TLQIEPDD-IAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleeGCEVVITALPlYHIFALTanglVFMKIG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1523 GGAHVTLCPRetamDPVKLYHFIERQQPSVIQATPTVWSTIVHhLPAASQRPLT----VLCGGEKMPAALLTQLRRIATR 1598
Cdd:PRK08751 281 GCNHLISNPR----DMPGFVKELKKTRFTAFTGVNTLFNGLLN-TPGFDQIDFSslkmTLGGGMAVQRSVAERWKQVTGL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1599 VL-QVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVflr 1677
Cdd:PRK08751 356 TLvEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV--- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1678 rqaFGAERYMyRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYLQLT 1757
Cdd:PRK08751 433 ---MDADGWL-HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVK 508
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1725075560 1758 SGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK08751 509 KDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1349-1806 |
8.15e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 92.36 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRIDSRPFSVGVMMEKSCH------VAVLLLGVLRAGKHyvPI---DVHypadrvSYMIENAQA 1419
Cdd:PRK06188 39 TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPevlmaiGAAQLAGLRRTALH--PLgslDDH------AYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1420 RLLVTDGEP--EQGWA--------------SPAVGFDSLVSHPAAADALPIPADDT---LAYIMYTSGSTGNPKGVMITH 1480
Cdd:PRK06188 111 STLIVDPAPfvERALAllarvpslkhvltlGPVPDGVDLLAAAAKFGPAPLVAAALppdIAGLAYTGGTTGKPKGVMGTH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1481 GNLNNFTNDFVGRLALSARDKVLSLTSISfDIFGLELFCSLAGGAHVTLCPretAMDPVKLYHFIERQQpsvIQAT---P 1557
Cdd:PRK06188 191 RSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLA---KFDPAEVLRAIEEQR---ITATflvP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1558 TVWSTIVHHlPAASQRPL----TVLCGGEKM-PAALLTQLRRIATRVLQVYGPTET--TIwSTCADLTHEGASD-----C 1625
Cdd:PRK06188 264 TMIYALLDH-PDLRTRDLssleTVYYGASPMsPVRLAEAIERFGPIFAQYYGQTEApmVI-TYLRKRDHDPDDPkrltsC 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1626 iGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgAERYMyRTGDIVRFNRQGQLEYL 1705
Cdd:PRK06188 342 -GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGWL-HTGDVAREDEDGFYYIV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1706 GRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-----GEGQQARIVsylqLTSGEELNEKAVRTALKARLPNIMI 1780
Cdd:PRK06188 413 DRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVpdekwGEAVTAVVV----LRPGAAVDAAELQAHVKERKGSVHA 488
|
490 500
....*....|....*....|....*.
gi 1725075560 1781 PSGFVVLSAFPLTNNNKIDIRRLPAP 1806
Cdd:PRK06188 489 PKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1463-1798 |
1.35e-18 |
|
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: 89.10 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 IMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGLELFC--SLAGGAhvTLCPrETAMDPVK 1540
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF-FHTFGYKAGIvaCLLTGA--TVVP-VAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1541 LYHFIERQQPSVIQATPTVWSTIVHHlPAASQRPLTVL----CGGEKMPAALLTQLRR---IATrVLQVYGPTETTIWST 1613
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDH-PGRKKFDLSSLraavTGAATVPVELVRRMRSelgFET-VLTAYGLTEAGVATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1614 C--ADLTHEGASDCiGTPIQATEVLVMDQagnplpsgafGELWLGGAGVSPGYWRNPTLSDKvflrrqAFGAERYMYrTG 1691
Cdd:cd17638 159 CrpGDDAETVATTC-GRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAE------AIDADGWLH-TG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1692 DIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGE---GQQARivSYLQLTSGEELNEKAVR 1768
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDermGEVGK--AFVVARPGVTLTEEDVI 298
|
330 340 350
....*....|....*....|....*....|
gi 1725075560 1769 TALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd17638 299 AWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
313-769 |
1.65e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 91.09 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:PRK07514 25 DGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSPLHSGDAPCIAPSSIDY----------------RSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNV 456
Cdd:PRK07514 105 VCDPANFAWLSKIAAAAGAPHvetldadgtgslleaaAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 457 AQNHRDFIGLAQGSrVLAIASLGFDAFGWDV--YGALVSGATLYLAPSelhTDVgalhdyltqhdighititPAILELLP 534
Cdd:PRK07514 185 ALTLVDYWRFTPDD-VLIHALPIFHTHGLFVatNVALLAGASMIFLPK---FDP------------------DAVLALMP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 535 RE---MW-----------PGL-----RTM--IVMGDAP-PADVVAWWAERT--RLCNGYGPTEASIATS---LCEYRPGV 587
Cdd:PRK07514 243 RAtvmMGvptfytrllqePRLtreaaAHMrlFISGSAPlLAETHREFQERTghAILERYGMTETNMNTSnpyDGERRAGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 588 pwncIGKPLKNYRCHILDLHHN-PLPVGFEGELCIAGSGLAHGYLhqealsaekfiicRLPYMAAEE----RLYRTGDIA 662
Cdd:PRK07514 323 ----VGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYW-------------RMPEKTAEEfradGFFITGDLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 663 KWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHP-LVESAcVVARSQPS-GKILAAFVQP-ASPELTIDALRHALV 739
Cdd:PRK07514 386 KIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPgVVESA-VIGVPHPDfGEGVTAVVVPkPGAALDEAAILAALK 464
|
490 500 510
....*....|....*....|....*....|....
gi 1725075560 740 TLLHPAAIPSVFIFLPALPLTINGK----IARQQ 769
Cdd:PRK07514 465 GRLARFKQPKRVFFVDELPRNTMGKvqknLLREQ 498
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
419-770 |
1.88e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 91.36 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 419 HAEQLPQSRDALAYVC-YTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLaQGSRVLAIASLGFDAFGWdvygalvsgATL 497
Cdd:PRK13382 186 HAGQRPEPTGRKGRVIlLTSGTTGTPKGARRSGPGGIGTLKAILDRTPW-RAEEPTVIVAPMFHAWGF---------SQL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 498 YLAPSELHT-------DVGALHDYLTQHDIGHITITPA----ILELLP----REMWPGLRTMIVMGDAPPADVVAWWAER 562
Cdd:PRK13382 256 VLAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVmfdrIMDLPAevrnRYSGRSLRFAAASGSRMRPDVVIAFMDQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 563 --TRLCNGYGPTEAS-IATSLCEYRPGVPwNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYlhqEALSAE 639
Cdd:PRK13382 336 fgDVIYNNYNATEAGmIATATPADLRAAP-DTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTK 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 640 KFIIcrlPYMAaeerlyrTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKIL 718
Cdd:PRK13382 412 DFHD---GFMA-------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQyGQRL 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 719 AAFVQPAS-PELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK13382 482 AAFVVLKPgASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
426-764 |
2.85e-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: 88.98 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 426 SRDALaYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDF----------IGLAQ----GSRVLAIASLGFDAFGWDVYGAL 491
Cdd:cd05924 2 SADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFgtgeftpsedAHKAAaaaaGTVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 492 VSGATLYLAPSELHTDvgALHDYLTQHDIGHITIT------PAILELL---PREMwPGLRTMIVMGdappadvvAWWAE- 561
Cdd:cd05924 81 LGGQTVVLPDDRFDPE--EVWRTIEKHKVTSMTIVgdamarPLIDALRdagPYDL-SSLFAISSGG--------ALLSPe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 562 -RTRLC---------NGYGPTEASiATSLCEYRPGVPWNCIGKPLkNYRCHILDLHHNPLPVGFEGELCIAGSGL-AHGY 630
Cdd:cd05924 150 vKQGLLelvpnitlvDAFGSSETG-FTGSGHSAGSGPETGPFTRA-NPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 631 LHQEALSAEKFIIcrlpymAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVAR 710
Cdd:cd05924 228 YGDEAKTAETFPE------VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGR 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 711 SQPS-GKILAAFVQPASP-ELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGK 764
Cdd:cd05924 302 PDERwGQEVVAVVQLREGaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
428-772 |
3.29e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 90.61 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGwdvYGALVSGATLYlAPSELHT- 506
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAG---IGSMLPGLLLG-APTVIYPl 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 507 ---DVGALHDYLTQHDIGHITITPAILELL-------PREMwpGLRtMIVMGDAPPADVV----AWWAERTRLCNGYGPT 572
Cdd:PRK07786 250 gafDPGQLLDVLEAEKVTGIFLVPAQWQAVcaeqqarPRDL--ALR-VLSWGAAPASDTLlrqmAATFPEAQILAAFGQT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 573 EASIATSLCEYRPGV-PWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaa 651
Cdd:PRK07786 327 EMSPVTCMLLGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 652 EERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASP--E 728
Cdd:PRK07786 397 AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRNDdaA 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1725075560 729 LTIDALRHALVTLL----HPAAIpsvfIFLPALPLTINGKIARQQLEK 772
Cdd:PRK07786 477 LTLEDLAEFLTDRLarykHPKAL----EIVDALPRNPAGKVLKTELRE 520
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1332-1805 |
3.35e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 90.37 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKS------------CHVAVLLLG-------- 1390
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDgVAVLARNHrgfvlalyaagkVGARIILLNtgfsgpql 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1391 ---VLRAGKHYVPIDVHYpADRVSYMI-ENAQARLLVTDGEPEQGWASPAVGFDSLVshpAAADALPIPADDTLA-YIMY 1465
Cdd:PRK07788 139 aevAAREGVKALVYDDEF-TDLLSALPpDLGRLRAWGGNPDDDEPSGSTDETLDDLI---AGSSTAPLPKPPKPGgIVIL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1466 TSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLsLTSISFDIFGLELF-CSLAGGAHVTLCPRetaMDPVKLYHF 1544
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTL-LPAPMFHATGWAHLtLAMALGSTVVLRRR---FDPEATLED 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1545 IERQQPSVIQATPTVWSTIVHHLPAASQRPLT-----VLCGGEKMPAALLTQ-LRRIATRVLQVYGPTE---TTIwSTCA 1615
Cdd:PRK07788 291 IAKHKATALVVVPVMLSRILDLGPEVLAKYDTsslkiIFVSGSALSPELATRaLEAFGPVLYNLYGSTEvafATI-ATPE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1616 DLTHegASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYW--RNPTLSDKvflrrqafgaeryMYRTGDI 1693
Cdd:PRK07788 370 DLAE--APGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTdgRDKQIIDG-------------LLSSGDV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1694 VRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIeRSLSLIVGEGQQ--ARIVSYLQLTSGEELNEKAVRTAL 1771
Cdd:PRK07788 435 GYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDV-VEAAVIGVDDEEfgQRLRAFVVKAPGAALDEDAIKDYV 513
|
490 500 510
....*....|....*....|....*....|....
gi 1725075560 1772 KARLPNIMIPSGFVVLSAFPLTNNNKIDIRRLPA 1805
Cdd:PRK07788 514 RDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1337-1823 |
3.55e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 90.51 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1337 DSLAVSCERQQYSYRQLWAQSERVAHALL-RID-SRPFSVGVMMEKSCHVAVLLLGVLRAGkhYVPIDVHyPADRVSYM- 1413
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRaRLDpTRPPHVGVLLDNTPEFSLLLGAAALSG--IVPVGLN-PTRRGAALa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1414 --IENAQARLLVTDGEPEQGWASPAVG----------FDSLVSHPAAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITH 1480
Cdd:PRK07867 95 rdIAHADCQLVLTESAHAELLDGLDPGvrvinvdspaWADELAAHRDAEPPFRVADpDDLFMLIFTSGTSGDPKAVRCTH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1481 GNLNNFTNDFVGRLALSaRDKVLSLTsisfdifgLELFCS----------LAGGAHVTLCPRETA---MDPVKLY---HF 1544
Cdd:PRK07867 175 RKVASAGVMLAQRFGLG-PDDVCYVS--------MPLFHSnavmagwavaLAAGASIALRRKFSAsgfLPDVRRYgatYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1545 IERQQP-SVIQATPtvwstivhHLPAASQRPLTVLCGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTCADLTHEGAs 1623
Cdd:PRK07867 246 NYVGKPlSYVLATP--------ERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGVAITRTPDTPPGA- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1624 dcIGTPIQATEVL-----------VMDQAGNPLPSGAFGELW-LGGAGVSPGYWRNPtlsdkvflrrqAFGAERY---MY 1688
Cdd:PRK07867 317 --LGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDP-----------EADAERMrggVY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1689 RTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSL-----IVGEgqqaRIVSYLQLTSGEELN 1763
Cdd:PRK07867 384 WSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYavpdpVVGD----QVMAALVLAPGAKFD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1764 EKAVRTALKAR--LPNIMIPSGFVVLSAFPLTNNNKIDIRRLPAPETRYS--------ASEADYTPAANE 1823
Cdd:PRK07867 460 PDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCAdpvwwirrLTPSDYAALADE 529
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
424-773 |
3.76e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 90.78 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 424 PQSRDALAYVCyTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLgFDAFGWDVYG--ALVSGATLYLAP 501
Cdd:PRK07529 210 IGPDDVAAYFH-TGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL-FHVNALLVTGlaPLARGAHVVLAT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 SELHTDVGALHDY---LTQHDIGHITITPAILELL---PREMW--PGLRTMIVmGDAP-PADVVAWWAERT--RLCNGYG 570
Cdd:PRK07529 288 PQGYRGPGVIANFwkiVERYRINFLSGVPTVYAALlqvPVDGHdiSSLRYALC-GAAPlPVEVFRRFEAATgvRIVEGYG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 571 PTEASIATSLC----EYRPGvpwnCIGKPLKNYRCHILDLHHN-----PLPVGFEGELCIAGSGLAHGYLHQEAlsaEKF 641
Cdd:PRK07529 367 LTEATCVSSVNppdgERRIG----SVGLRLPYQRVRVVILDDAgrylrDCAVDEVGVLCIAGPNVFSGYLEAAH---NKG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 642 IIcrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVkIRGVR-IEMGEVESAVRSHPLVESACVVARSQP-SGKILA 719
Cdd:PRK07529 440 LW-------LEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRGGHnIDPAAIEEALLRHPAVALAAAVGRPDAhAGELPV 511
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 720 AFVQPAsPELTIDA---LRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKW 773
Cdd:PRK07529 512 AYVQLK-PGASATEaelLAFARDHIAERAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1349-1754 |
4.50e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 89.66 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRIDSrpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVtDGEP 1428
Cdd:PRK07787 27 SRSDLAGAATAVAERVAGARR----VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL-GPAP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1429 EQGWASPAVGFDSlvsHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMIThgnlnnftndfvgRLALSAR--------- 1499
Cdd:PRK07787 102 DDPAGLPHVPVRL---HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLS-------------RRAIAADldalaeawq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1500 ---DKVLsltsisfdIFGLELFcslaggaHV------TLCP-------RETAMDPVKLYHFIERQQPSVIQATPTVWSTI 1563
Cdd:PRK07787 166 wtaDDVL--------VHGLPLF-------HVhglvlgVLGPlrignrfVHTGRPTPEAYAQALSEGGTLYFGVPTVWSRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1564 VHHLPAA----SQRPLtvLCGGEKMPAALLTQLRRIA-TRVLQVYGPTETTI-WSTCADltHEGASDCIGTPIQATEVLV 1637
Cdd:PRK07787 231 AADPEAAralrGARLL--VSGSAALPVPVFDRLAALTgHRPVERYGMTETLItLSTRAD--GERRPGWVGLPLAGVETRL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1638 MDQAGNPLPSG--AFGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQ-VKI 1714
Cdd:PRK07787 307 VDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDAT------AAAFTADGW-FRTGDVAVVDPDGMHRIVGRESTDlIKS 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1725075560 1715 RGHRIELSEIDLSLssLDNIERSLSLIVGE-----GQqaRIVSYL 1754
Cdd:PRK07787 380 GGYRIGAGEIETAL--LGHPGVREAAVVGVpdddlGQ--RIVAYV 420
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1405-1814 |
4.65e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 90.09 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1405 YPADRVSYMIENAQARLLVTDGEPE--QGWASPAVGFDSlvshpaAADALPIPADDtLAYIMYTSGSTGNPKGVMITHGN 1482
Cdd:PRK06710 158 FPKNLLYPFVQKKQSNLVVKVSESEtiHLWNSVEKEVNT------GVEVPCDPEND-LALLQYTGGTTGFPKGVMLTHKN 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1483 LnnFTNDFVGRLAL----SARDKVLSLTSIsFDIFGLE--LFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQAT 1556
Cdd:PRK06710 231 L--VSNTLMGVQWLynckEGEEVVLGVLPF-FHVYGMTavMNLSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1557 PTVW-----STIVHHLPAASQRplTVLCGGEKMPAALLTQLRRI-ATRVLQVYGPTETTIWSTCADLTHEGASDCIGTPI 1630
Cdd:PRK06710 305 PTIYiallnSPLLKEYDISSIR--ACISGSAPLPVEVQEKFETVtGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPW 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1631 QATEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqafgaERYMYRTGDIVRFNRQGQLEYLGRND 1709
Cdd:PRK06710 383 PDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL--------QDGWLHTGDVGYMDEDGFFYVKDRKK 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1710 HQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIV-SYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLS 1788
Cdd:PRK06710 455 DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVkAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRD 534
|
410 420
....*....|....*....|....*.
gi 1725075560 1789 AFPLTNNNKIDIRRLPAPETRYSASE 1814
Cdd:PRK06710 535 ELPKTTVGKILRRVLIEEEKRKNEDE 560
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1336-1693 |
6.58e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 89.69 E-value: 6.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAhALLRidSRPFS----VGVMMEKSCHVAVLLLGVLRAGkhYVPIDVH--YPADR 1409
Cdd:PRK07059 37 ADRPAFICMGKAITYGELDELSRALA-AWLQ--SRGLAkgarVAIMMPNVLQYPVAIAAVLRAG--YVVVNVNplYTPRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1410 VSYMIENAQARLLVT----DGEPEQGWASPAV------------GFD------------------SLVSHPAAADAL--- 1452
Cdd:PRK07059 112 LEHQLKDSGAEAIVVlenfATTVQQVLAKTAVkhvvvasmgdllGFKghivnfvvrrvkkmvpawSLPGHVRFNDALaeg 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1453 -------PIPADDTLAYIMYTSGSTGNPKGVMITHGNL--NNFTNDFVGRLALSARDKVLSLTSIS----FDIFGLELfC 1519
Cdd:PRK07059 192 arqtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIvaNVLQMEAWLQPAFEKKPRPDQLNFVCalplYHIFALTV-C 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1520 SLAG---GAHVTLCPretamDPVKLYHFI---ERQQPSVIQATPTVWSTIVHHlPAASQ---RPLTVLCGGekmpaALLT 1590
Cdd:PRK07059 271 GLLGmrtGGRNILIP-----NPRDIPGFIkelKKYQVHIFPAVNTLYNALLNN-PDFDKldfSKLIVANGG-----GMAV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1591 QlRRIATRVLQV--------YGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSP 1662
Cdd:PRK07059 340 Q-RPVAERWLEMtgcpitegYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMA 418
|
410 420 430
....*....|....*....|....*....|.
gi 1725075560 1663 GYWRNPTLSDKVFLrrqafgAERYmYRTGDI 1693
Cdd:PRK07059 419 GYWNRPDETAKVMT------ADGF-FRTGDV 442
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1336-1806 |
1.12e-17 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 88.66 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSR-PFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:PRK13382 57 PDRPGLIDELGTLTWRELDERSDALAAALQALPIGePRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGE------------PE----QGWASPAVGFDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMI 1478
Cdd:PRK13382 137 TREGVDTVIYDEEfsatvdraladcPQatriVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1479 THGNLNNFTNDFVGRLALSARDKVLsLTSISFDIFG---LELFCSLAggahvtlCPRET--AMDPVKLYHFIERQQPSVI 1553
Cdd:PRK13382 217 SGPGGIGTLKAILDRTPWRAEEPTV-IVAPMFHAWGfsqLVLAASLA-------CTIVTrrRFDPEATLDLIDRHRATGL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1554 QATPTVWSTIVHhLPA-----ASQRPLTVLCG-GEKMPAALLTQ-LRRIATRVLQVYGPTETTIWSTC--ADLthEGASD 1624
Cdd:PRK13382 289 AVVPVMFDRIMD-LPAevrnrYSGRSLRFAAAsGSRMRPDVVIAfMDQFGDVIYNNYNATEAGMIATAtpADL--RAAPD 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1625 CIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYwrnPTLSDKVFLrrqafgaERYMyRTGDIVRFNRQGQLEY 1704
Cdd:PRK13382 366 TAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFH-------DGFM-ASGDVGYLDENGRLFV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1705 LGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGE---GQqaRIVSYLQLTSGEELNEKAVRTALKARLPNIMIP 1781
Cdd:PRK13382 435 VGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDeqyGQ--RLAAFVVLKPGASATPETLKQHVRDNLANYKVP 512
|
490 500
....*....|....*....|....*
gi 1725075560 1782 SGFVVLSAFPLTNNNKIDIRRLPAP 1806
Cdd:PRK13382 513 RDIVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
428-772 |
1.67e-17 |
|
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: 86.38 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKgvmIGREGLSNVAQNHR--DFIGLAQGSRVLAIASLGFDAFGWDVYG--ALVSGATLYLAPSE 503
Cdd:cd05944 2 DDVAAYFHTGGTTGTPK---LAQHTHSNEVYNAWmlALNSLFDPDDVLLCGLPLFHVNGSVVTLltPLASGAHVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 504 LHTDVGALHDY---LTQHDIGHITITPAILELLPREmwPG------LRTMIVMGDAPPADVVAWWAERTRL--CNGYGPT 572
Cdd:cd05944 79 GYRNPGLFDNFwklVERYRITSLSTVPTVYAALLQV--PVnadissLRFAMSGAAPLPVELRARFEDATGLpvVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 573 EASIATSLC----EYRPGvpwnCIGKPLKNYRCHILDLH---HNPLPVGFE--GELCIAGSGLAHGYLHQEaLSAEKFIi 643
Cdd:cd05944 157 EATCLVAVNppdgPKRPG----SVGLRLPYARVRIKVLDgvgRLLRDCAPDevGEICVAGPGVFGGYLYTE-GNKNAFV- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 644 crlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVkIRGVR-IEMGEVESAVRSHPLVESACVVARSQP-SGKILAAF 721
Cdd:cd05944 231 --------ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHnIDPALIEEALLRHPAVAFAGAVGQPDAhAGELPVAY 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 722 VQ--PASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd05944 302 VQlkPGAVVEEEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1458-1799 |
2.26e-17 |
|
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: 86.00 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1458 DTLAYIMYTSGSTGNPKGVMITHGNLnNFTNDFVGRLALSARDKVLSLTSISFDIFGL--ELFCSLAGGAHVTLCPRETA 1535
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNE-VYNAWMLALNSLFDPDDVLLCGLPLFHVNGSvvTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1536 MDPV---KLYHFIERQQPSVIQATPTVWStivhhlpAASQRPLT--------VLCGGEKMPAALLTQLR-RIATRVLQVY 1603
Cdd:cd05944 81 RNPGlfdNFWKLVERYRITSLSTVPTVYA-------ALLQVPVNadisslrfAMSGAAPLPVELRARFEdATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1604 GPTETTIWSTCADLTHEGASDCIGTPI--QATEVLVMDQAGN---PLPSGAFGELWLGGAGVSPGYwrnptLSDKvfLRR 1678
Cdd:cd05944 154 GLTEATCLVAVNPPDGPKRPGSVGLRLpyARVRIKVLDGVGRllrDCAPDEVGEICVAGPGVFGGY-----LYTE--GNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1679 QAFGAERYMyRTGDIVRFNRQGQLEYLGRNDHQVkIR-GHRIELSEIDLSLSSldNIERSLSLIVGE-----GQQAriVS 1752
Cdd:cd05944 227 NAFVADGWL-NTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLR--HPAVAFAGAVGQpdahaGELP--VA 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1725075560 1753 YLQLTSGEELNEKAVRTALKARLPN-IMIPSGFVVLSAFPLTNNNKID 1799
Cdd:cd05944 301 YVQLKPGAVVEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVF 348
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1332-1801 |
2.28e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 87.63 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDS--LAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPAD 1408
Cdd:PRK05852 26 ATRLPEApaLVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDrVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RVSYMIENAQARLLVTDGEPEQGWASPA---------VGFDSLVS--------------HPAAADALPIPADDtlAYIMY 1465
Cdd:PRK05852 106 EQRVRSQAAGARVVLIDADGPHDRAEPTtrwwpltvnVGGDSGPSggtlsvhldaatepTPATSTPEGLRPDD--AMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1466 TSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGL--ELFCSLAGGAHVTLCPREtamdpvklyH 1543
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPL-YHGHGLiaALLATLASGGAVLLPARG---------R 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1544 FIERQQPSVIQATPTVWSTIV---HHL--------PAASQRP---LTVLCGGEKMPAALLTQLRRIATRVLQVYGPTETT 1609
Cdd:PRK05852 254 FSAHTFWDDIKAVGATWYTAVptiHQIlleraatePSGRKPAalrFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1610 IWSTCadlTHEGASDCIGTPIQAT---------EVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRRqa 1680
Cdd:PRK05852 334 HQVTT---TQIEGIGQTENPVVSTglvgrstgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG-- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1681 fgaeryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-----GEGQQARIVSYLQ 1755
Cdd:PRK05852 409 ------WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVpdqlyGEAVAAVIVPRES 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1725075560 1756 LT-SGEELNEKAvrtalKARLPNIMIPSGFVVLSAFPLTNNNKIDIR 1801
Cdd:PRK05852 483 APpTAEELVQFC-----RERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
315-773 |
2.28e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 88.03 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFAcWLLEHSGAASSVVAVSMDKSATLLIVLL-GILKSNKTYVLLDPQAPAARNQSILDDVQP-ALI 392
Cdd:PRK09274 40 DELSFAELDARSDAIA-HGLNAAGIGRGMRAVLMVTPSLEFFALTfALFKAGAVPVLVDPGMGIKNLKQCLAEAQPdAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 ------LADSPLHSGDA---------PCIAPSSIDYRSLNIHAE----QLPQS-RDALAYVCYTSGTTGKPKGVMigREG 452
Cdd:PRK09274 119 gipkahLARRLFGWGKPsvrrlvtvgGRLLWGGTTLATLLRDGAaapfPMADLaPDDMAAILFTSGSTGTPKGVV--YTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 453 LSNVAQNH--RDFIGLAQGSRVLAiaslGFDAFGwdVYGALVSGATL--YLAPSELHT-DVGALHDYLTQHDIGHITITP 527
Cdd:PRK09274 197 GMFEAQIEalREDYGIEPGEIDLP----TFPLFA--LFGPALGMTSVipDMDPTRPATvDPAKLFAAIERYGVTNLFGSP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 528 AILELLPRE------MWPGLRTMIVMGdAP-PADVVA----WWAERTRLCNGYGPTEA----SIATS--LCEYR------ 584
Cdd:PRK09274 271 ALLERLGRYgeangiKLPSLRRVISAG-APvPIAVIErfraMLPPDAEILTPYGATEAlpisSIESReiLFATRaatdng 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 585 PGVpwnCIGKPLKNYRCHILDLHHNP---------LPVGFEGELCIAGSGLAHGYLHQEALSAEKFIICRLPYMaaeerL 655
Cdd:PRK09274 350 AGI---CVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDV-----W 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 656 YRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLvesacvVARS-----QPSGKILAAFVQPASPELT 730
Cdd:PRK09274 422 HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPG------VKRSalvgvGVPGAQRPVLCVELEPGVA 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 731 IDA------LRHALVTLLHPAAIpSVFIFLPALPLTI--NGKIARQQLEKW 773
Cdd:PRK09274 496 CSKsalyqeLRALAAAHPHTAGI-ERFLIHPSFPVDIrhNAKIFREKLAVW 545
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
538-767 |
2.85e-17 |
|
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: 85.40 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 538 WPGLRtmIVMG-DAPpaDVVAWWAERTRLC--NGYGPTEASIATSLCEY--RPGvpwnCIGKPLKNYRCHILDLHHNPLP 612
Cdd:cd17637 113 LSSLR--HVLGlDAP--ETIQRFEETTGATfwSLYGQTETSGLVTLSPYreRPG----SAGRPGPLVRVRIVDDNDRPVP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 613 VGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQ--VKIRGVRIEMG 690
Cdd:cd17637 185 AGETGEIVVRGPLVFQGYWNLPELTAYTF----------RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPA 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 691 EVESAVRSHPLVESACV--VARSQPSGKILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:cd17637 255 EVEKVILEHPAIAEVCVigVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1326-1799 |
2.88e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 87.14 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1326 MHIG----RLAHTQPDSLAVSCERQQYSYRQlWAQS-ERVAHALLRIDSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVP 1400
Cdd:PRK07638 1 MGITkeykKHASLQPNKIAIKENDRVLTYKD-WFESvCKVANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1401 IDVHYPADRVSYMIENAQARLLVTD---GEPEQGWASPAVGFDS---LVSHPAAADALPIPADDTLAYIMYTSGSTGNPK 1474
Cdd:PRK07638 80 LDIKWKQDELKERLAISNADMIVTErykLNDLPDEEGRVIEIDEwkrMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1475 GVMITHGN-LNNFT---NDFvgrlALSARDKVL---SLTSISFdIFGleLFCSLAGGAHVTLCPRETamdPVKLYHFIER 1547
Cdd:PRK07638 160 AFLRAQQSwLHSFDcnvHDF----HMKREDSVLiagTLVHSLF-LYG--AISTLYVGQTVHLMRKFI---PNQVLDKLET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1548 QQPSVIQATPTVWSTIVhHLPAASQRPLTVLCGGEKMPAallTQLRRIATRVLQV-----YGPTETTIWSTCADLTHEGA 1622
Cdd:PRK07638 230 ENISVMYTVPTMLESLY-KENRVIENKMKIISSGAKWEA---EAKEKIKNIFPYAklyefYGASELSFVTALVDEESERR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1623 SDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYwrnptLSDKVFLRRqaFGAERYMyRTGDIVRFNRQGQL 1702
Cdd:PRK07638 306 PNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARE--LNADGWM-TVRDVGYEDEEGFI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1703 EYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIVGE-----GQQAriVSYLQltsGEElNEKAVRTALKARLPN 1777
Cdd:PRK07638 378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDE--IVVIGVpdsywGEKP--VAIIK---GSA-TKQQLKSFCLQRLSS 449
|
490 500
....*....|....*....|..
gi 1725075560 1778 IMIPSGFVVLSAFPLTNNNKID 1799
Cdd:PRK07638 450 FKIPKEWHFVDEIPYTNSGKIA 471
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1453-1767 |
3.02e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 87.59 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1453 PIPADDTLAyIMYTSGSTGNPKGVMITHGNLNNFTNDFV----GRLALSARDKVLSLTSISFDIFGLELFCS--LAGGAH 1526
Cdd:PLN02574 194 VIKQDDVAA-IMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPGSDNVYLAALPMFHIYGLSLFVVglLSLGST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1527 VTLCPRETAMDPVKLyhfIERQQPSVIQATPTVWSTIVHHLPAASQRPLTVL----CGGEKMPAALLTQLRRIATRV--L 1600
Cdd:PLN02574 273 IVVMRRFDASDMVKV---IDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLkqvsCGAAPLSGKFIQDFVQTLPHVdfI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1601 QVYGPTETTIWSTCADLTHEGAS-DCIGTPIQATEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrr 1678
Cdd:PLN02574 350 QGYGMTESTAVGTRGFNTEKLSKySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTID-- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1679 qafgaERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARI-VSYLQLT 1757
Cdd:PLN02574 428 -----KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIpVAFVVRR 502
|
330
....*....|
gi 1725075560 1758 SGEELNEKAV 1767
Cdd:PLN02574 503 QGSTLSQEAV 512
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
313-773 |
4.43e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.11 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLG----------------------ILKSNKTYVL 370
Cdd:PRK06164 32 EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAcarlgatviavntryrshevahILGRGRARWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 371 LdpQAPAARN---QSILDDVQPALILA---------DSPLHSGDAPCIAPSSIDYRSLNIH-AEQLPQSRDALAYVCYT- 436
Cdd:PRK06164 112 V--VWPGFKGidfAAILAAVPPDALPPlraiavvddAADATPAPAPGARVQLFALPDPAPPaAAGERAADPDAGALLFTt 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 437 SGTTGKPKGVMIGREGLsnVAQNHRD--FIGLAQGSRVLAIASLGfDAFGWD-VYGALVSGATLYLAPS-ELHTDVGALH 512
Cdd:PRK06164 190 SGTTSGPKLVLHRQATL--LRHARAIarAYGYDPGAVLLAALPFC-GVFGFStLLGALAGGAPLVCEPVfDAARTARALR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 513 DYLTQHDIGHITITPAILELLP-REMWPGLRTMIVMGDAPPADVVAWWAeRTR---LCNGYGPTEAsIATSLCEYRP--- 585
Cdd:PRK06164 267 RHRVTHTFGNDEMLRRILDTAGeRADFPSARLFGFASFAPALGELAALA-RARgvpLTGLYGSSEV-QALVALQPATdpv 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 586 GVPWNCIGKPLK-NYRCHILD-LHHNPLPVGFEGELCIAGSGLAHGYLH-----QEALSAEKFiicrlpymaaeerlYRT 658
Cdd:PRK06164 345 SVRIEGGGRPASpEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDnpdatARALTDDGY--------------FRT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 659 GDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSGKILAAFVQP-----ASPELTIDA 733
Cdd:PRK06164 411 GDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPtdgasPDEAGLMAA 490
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1725075560 734 LRHALVtllhPAAIPSVFIFLPALPLTING---KIARQQLEKW 773
Cdd:PRK06164 491 CREALA----GFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1463-1707 |
5.09e-17 |
|
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: 84.63 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 IMYTSGSTGNPKGVMITHGNL--NNFtnDFVGRLALSARDKVLSLTSIsFDIFGLEL-FCSL-AGGAHVTLcpreTAMDP 1538
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLiaANL--QLIHAMGLTEADVYLNMLPL-FHIAGLNLaLATFhAGGANVVM----EKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1539 VKLYHFIERQQPSVIQATPTVWSTIvhhLPAASQRPLTV----LCGGEKMPAALLTQLRRIATRVLQVYGPTETTIWSTC 1614
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNL---LDAAEKSGVDLsslrHVLGLDAPETIQRFEETTGATFWSLYGQTETSGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1615 ADLTHegASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrRQAFgaerymYRTGDIV 1694
Cdd:cd17637 155 SPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--RNGW------HHTGDLG 224
|
250
....*....|...
gi 1725075560 1695 RFNRQGQLEYLGR 1707
Cdd:cd17637 225 RFDEDGYLWYAGR 237
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1322-1803 |
5.40e-17 |
|
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: 87.16 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1322 DSLLMHIGRLAHTQPdslAVSCERQQ-----YSYRQLWAQSERVAHALLRID-SRPFSVGVMMEKSCHVAVLLLGVLRAG 1395
Cdd:cd05968 64 EQLLDKWLADTRTRP---ALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGvGKGDRVGIYLPMIPEIVPAFLAVARIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1396 KHYVPIDVHYPADRVSYMIENAQARLLVT-DGEPEQGW-------ASPAVGFDSLVSH-----PAAADALPIPADDtLAY 1462
Cdd:cd05968 141 GIVVPIFSGFGKEAAATRLQDAEAKALITaDGFTRRGRevnlkeeADKACAQCPTVEKvvvvrHLGNDFTPAKGRD-LSY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 ---------------------IMYTSGSTGNPKGVMITHGNLN-NFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCS 1520
Cdd:cd05968 220 deeketagdgaertesedplmIIYTSGTTGKPKGTVHVHAGFPlKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1521 LAGGAHVTLcpRETAMD---PVKLYHFIERQQPSVIQATPTVWSTIVHH----LPAASQRPLTVLCG-GEKM---PAALL 1589
Cdd:cd05968 300 LILGATMVL--YDGAPDhpkADRLWRMVEDHEITHLGLSPTLIRALKPRgdapVNAHDLSSLRVLGStGEPWnpePWNWL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1590 TQLRRIATRVLQVY-GPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPsGAFGELWLGGA--GVSPGYWR 1666
Cdd:cd05968 378 FETVGKGRNPIINYsGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWR 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1667 NptlsDKVFLrrqafgaERYMYRT------GDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSL 1740
Cdd:cd05968 457 D----EDRYL-------ETYWSRFdnvwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 1741 IV-----GEGQQARIVSYLQLTSGEELnEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIdIRRL 1803
Cdd:cd05968 526 GVphpvkGEAIVCFVVLKPGVTPTEAL-AEELMERVADELGKPLSPERILFVKDLPKTRNAKV-MRRV 591
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1457-1799 |
5.47e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 86.73 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1457 DDTLAYIMYTSGSTGNPKGVMITHGN--LNNFTNDFVGRLALSARDKVLSLTSIsF--DIFGLELFCSLAGGAHVTLCPR 1532
Cdd:PRK06018 176 ENTAAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPL-FhaNSWGIAFSAPSMGTKLVMPGAK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1533 etaMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAAS-QRPL--TVLCGGEKMPAALLTQLRRIATRVLQVYGPTETT 1609
Cdd:PRK06018 255 ---LDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGlKLPHlkMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMS 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1610 IWSTCA-------DLTHEGASDCI---GTPIQATEVLVMDQAGNPLPSG--AFGELWLGGAGVSPGYWRnptlSDKVFLR 1677
Cdd:PRK06018 332 PLGTLAalkppfsKLPGDARLDVLqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYR----VDGEILD 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1678 RQAFgaerymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIelSEIDLSLSSLDNIERSLSLIVGEGQ---QARIVSYL 1754
Cdd:PRK06018 408 DDGF------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWI--SSIDLENLAVGHPKVAEAAVIGVYHpkwDERPLLIV 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1725075560 1755 QLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKID 1799
Cdd:PRK06018 480 QLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKIL 524
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
314-767 |
6.05e-17 |
|
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: 85.96 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSPlhsgdapciapssidyrslnihaeqlpqsrDALAYVCYTSGTTGKPKGVMI-GREGLSNVAQNHRDFIgLAQGSRV 472
Cdd:cd05914 85 VSDE------------------------------DDVALINYTSGTTGNSKGVMLtYRNIVSNVDGVKEVVL-LGKGDKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLGfDAFG--WDVYGALVSGATLYL---APSelhtdvgALHDYLTQHDIGHITITP--------AILELLPR---- 535
Cdd:cd05914 134 LSILPLH-HIYPltFTLLLPLLNGAHVVFldkIPS-------AKIIALAFAQVTPTLGVPvplviekiFKMDIIPKltlk 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 536 ------------------------EMWPG-LRTMIVMGDAPPADVVAWWAE-RTRLCNGYGPTEASIATSlceyrpGVPW 589
Cdd:cd05914 206 kfkfklakkinnrkirklafkkvhEAFGGnIKEFVIGGAKINPDVEEFLRTiGFPYTIGYGMTETAPIIS------YSPP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 590 NCI-----GKPLKNYRCHILDlhhnPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYRTGDIAKW 664
Cdd:cd05914 280 NRIrlgsaGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFD---------KDGWFHTGDLGKI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 665 DEQGNIIFVGRRDHQ-VKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSgkILAAFVQPA---SPELTIDALRHAL-- 738
Cdd:cd05914 347 DAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL--VALAYIDPDfldVKALKQRNIIDAIkw 424
|
490 500 510
....*....|....*....|....*....|....*.
gi 1725075560 739 -------VTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:cd05914 425 evrdkvnQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1323-1726 |
6.08e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 86.30 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1323 SLLMHIGRLA-HTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIdsrpfsvGVmmEKSCHVAVL----------LLGV 1391
Cdd:PRK07008 14 SLIAHAARHAgDTEIVSRRVEGDIHRYTYRDCERRAKQLAQALAAL-------GV--EPGDRVGTLawngyrhleaYYGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1392 LRAGK--HYVPIDVHypADRVSYMIENAQARLLVTDG---------EPE----QGW------------ASPAVGFDSLVS 1444
Cdd:PRK07008 85 SGSGAvcHTINPRLF--PEQIAYIVNHAEDRYVLFDLtflplvdalAPQcpnvKGWvamtdaahlpagSTPLLCYETLVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1445 HPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGN--LNNFTNDFVGRLALSARDKVLSLTSIsFDI--FGLELFCS 1520
Cdd:PRK07008 163 AQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPM-FHVnaWGLPYSAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1521 LAGGAHVTLCPretAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQR--PL--TVLcGGEKMPAALLTQLRR-I 1595
Cdd:PRK07008 242 LTGAKLVLPGP---DLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRfsTLrrTVI-GGSACPPAMIRTFEDeY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1596 ATRVLQVYGPTETTIWSTCADLT--HEGASDCI--------GTPIQATEVLVMDQAGNPLP--SGAFGELWLGGAGVSPG 1663
Cdd:PRK07008 318 GVEVIHAWGMTEMSPLGTLCKLKwkHSQLPLDEqrkllekqGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVRGPWVIDR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 1664 YWRNptlsDKVFLRRQAFgaerymyRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIelSEIDL 1726
Cdd:PRK07008 398 YFRG----DASPLVDGWF-------PTGDVATIDADGFMQITDRSKDVIKSGGEWI--SSIDI 447
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1458-1754 |
1.34e-16 |
|
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: 85.23 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1458 DTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDIfGL---ELFCSLAGGAHVTLCPRET 1534
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDM-GLiafHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1535 AMDPVKLYHFIERQQPSVI------------QATPTV---WSTIVHHLPAASQRPLTV-LCgGEKMPAALLTQLRRIAtr 1598
Cdd:cd05908 185 IRRPILWLKKASEHKATIVsspnfgykyflkTLKPEKandWDLSSIRMILNGAEPIDYeLC-HEFLDHMSKYGLKRNA-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1599 VLQVYGPTETTIWSTCAD---------LTHEGA-------------SDC-----IGTPIQATEVLVMDQAGNPLPSGAFG 1651
Cdd:cd05908 262 ILPVYGLAEASVGASLPKaqspfktitLGRRHVthgepepevdkkdSECltfveVGKPIDETDIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1652 ELWLGGAGVSPGYWRNPTLSDKVFlrrqafgAERYMYRTGDIvRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSL 1731
Cdd:cd05908 342 HIQIRGKNVTPGYYNNPEATAKVF-------TDDGWLKTGDL-GFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEEL 413
|
330 340
....*....|....*....|....*..
gi 1725075560 1732 DNIERSLSLIVG----EGQQARIVSYL 1754
Cdd:cd05908 414 EGVELGRVVACGvnnsNTRNEEIFCFI 440
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1458-1707 |
1.60e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.11 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1458 DTLAYIMYTSGSTGNPKGVMITHGNLnnFTNDFVGRLALS---ARDKVLSLTSIS-FDIFGLE----LFCSLAGGAHVTL 1529
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNM--LANLEQAKAAYGpllHPGKELVVTALPlYHIFALTvnclLFIELGGQNLLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1530 CPR--ETAMDPVKLYHFierqqpSVIQATPTVWSTIV-----HHLPAASQRpLTVlCGGEKMPAALLTQLRRIA-TRVLQ 1601
Cdd:PRK08974 284 NPRdiPGFVKELKKYPF------TAITGVNTLFNALLnneefQELDFSSLK-LSV-GGGMAVQQAVAERWVKLTgQYLLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1602 VYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFlrrqaf 1681
Cdd:PRK08974 356 GYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI------ 429
|
250 260
....*....|....*....|....*.
gi 1725075560 1682 gAERYMyRTGDIVRFNRQGQLEYLGR 1707
Cdd:PRK08974 430 -KDGWL-ATGDIAVMDEEGFLRIVDR 453
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
318-770 |
2.07e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 85.47 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 318 SYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSP 397
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 398 LHSGDAPCIAPSSIDYRSLNIHAEQL---PQSRDALAYVCYTSGTTGKPKGVmIGREG--LSNVAQNHRDFIGLAQGSRV 472
Cdd:PRK06060 112 LRDRFQPSRVAEAAELMSEAARVAPGgyePMGGDALAYATYTSGTTGPPKAA-IHRHAdpLTFVDAMCRKALRLTPEDTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 LAIASLGFD-AFGWDVYGALVSGATLYLAPSELHTDVGALhdyLTQHdighitITPAILELLPR-----------EMWPG 540
Cdd:PRK06060 191 LCSARMYFAyGLGNSVWFPLATGGSAVINSAPVTPEAAAI---LSAR------FGPSVLYGVPNffarvidscspDSFRS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 541 LRTMIVMGDA-PPAdvvawWAER-------TRLCNGYGPTEAS---IATSLCEYRPGVpwncIGKPLKNYRCHILDLHHN 609
Cdd:PRK06060 262 LRCVVSAGEAlELG-----LAERlmeffggIPILDGIGSTEVGqtfVSNRVDEWRLGT----LGRVLPPYEIRVVAPDGT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 610 PLPVGFEGELCIAGSGLAHGYLHQEAlsaekfiicrlPYMAAEERLyRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEM 689
Cdd:PRK06060 333 TAGPGVEGDLWVRGPAIAKGYWNRPD-----------SPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 690 GEVESAVRSHPLVESACVVARSQPSG-KILAAFVQPASPELtID--ALRHA---LVTLLHPAAIPSVFIFLPALPLTING 763
Cdd:PRK06060 401 REVERLIIEDEAVAEAAVVAVRESTGaSTLQAFLVATSGAT-IDgsVMRDLhrgLLNRLSAFKVPHRFAVVDRLPRTPNG 479
|
....*..
gi 1725075560 764 KIARQQL 770
Cdd:PRK06060 480 KLVRGAL 486
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1333-1803 |
2.09e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 84.66 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1333 HTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRidsRPFSVG----VMMEKSCHVAVLLLGVLRAGkhYVPIDVHYPAD 1408
Cdd:PRK10946 34 HAASDAIAVICGERQFSYRELNQASDNLACSLRR---QGIKPGdtalVQLGNVAEFYITFFALLKLG--VAPVNALFSHQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1409 RV---SYmIENAQARLLVTDGEPEQ----------------------GWASPAVGFDSLVSHPAAA-DALPIPADDtLAY 1462
Cdd:PRK10946 109 RSelnAY-ASQIEPALLIADRQHALfsdddflntlvaehsslrvvllLNDDGEHSLDDAINHPAEDfTATPSPADE-VAF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 IMYTSGSTGNPKGVMITHgnlnnftNDFVgrlaLSARDkvlsltsiSFDIFGLE----LFCSL----------------- 1521
Cdd:PRK10946 187 FQLSGGSTGTPKLIPRTH-------NDYY----YSVRR--------SVEICGFTpqtrYLCALpaahnypmsspgalgvf 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1522 -AGGAhVTLCPretamDPVKLYHF--IERQQPSVIQATPTVWSTIVHHLPAASQR----PLTVL-CGGEKMPAALLtqlR 1593
Cdd:PRK10946 248 lAGGT-VVLAP-----DPSATLCFplIEKHQVNVTALVPPAVSLWLQAIAEGGSRaqlaSLKLLqVGGARLSETLA---R 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1594 RIAT----RVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQ-ATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNP 1668
Cdd:PRK10946 319 RIPAelgcQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1669 TLSdkvflrRQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEID-LSLSSLDNIERSLSLIV----G 1743
Cdd:PRK10946 399 QHN------ASAFDANGF-YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIEnLLLRHPAVIHAALVSMEdelmG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 1744 EGQQARIVSylqltsGEELNEKAVRTALKAR-LPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK10946 472 EKSCAFLVV------KEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1408-1798 |
2.34e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 85.08 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1408 DRVSYMIENAQARLLVTDGEPEQGWA-SPAVGFDSLVSHPAAADalpiPAD------DTLAYIMYTSGSTGNPKGVMITH 1480
Cdd:PRK06060 92 DDHALAARNTEPALVVTSDALRDRFQpSRVAEAAELMSEAARVA----PGGyepmggDALAYATYTSGTTGPPKAAIHRH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1481 GNLNNFTNDFVGR-LALSARDKVLSLTSISFdIFGL--ELFCSLAGGAHVTLCPRETAMDPVKLYHfiERQQPSVIQATP 1557
Cdd:PRK06060 168 ADPLTFVDAMCRKaLRLTPEDTGLCSARMYF-AYGLgnSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1558 TVWSTIVHHLPAASQRPL-TVLCGGEKMPAALLTQLRRI--ATRVLQVYGPTET--TIWSTCADLTHEGAsdcIGTPIQA 1632
Cdd:PRK06060 245 NFFARVIDSCSPDSFRSLrCVVSAGEALELGLAERLMEFfgGIPILDGIGSTEVgqTFVSNRVDEWRLGT---LGRVLPP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1633 TEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWR--NPTLSDKVFLrrqafgaerymyRTGDIVRFNRQGQLEYLGRNDH 1710
Cdd:PRK06060 322 YEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNrpDSPVANEGWL------------DTRDRVCIDSDGWVTYRCRADD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1711 QVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIV-SYLQLTSGEELNEKAVRTA---LKARLPNIMIPSGFVV 1786
Cdd:PRK06060 390 TEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLqAFLVATSGATIDGSVMRDLhrgLLNRLSAFKVPHRFAV 469
|
410
....*....|..
gi 1725075560 1787 LSAFPLTNNNKI 1798
Cdd:PRK06060 470 VDRLPRTPNGKL 481
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
433-767 |
3.16e-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: 82.16 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 433 VCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLgFDAFGWD--VYGALVSGATLYlaPSELHtDVGA 510
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF-FHTFGYKagIVACLLTGATVV--PVAVF-DVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 511 LHDYLTQHDI----GHITITPAILE--LLPREMWPGLRTMIVMGDAPPADVVawwaERTR-------LCNGYGPTEASIA 577
Cdd:cd17638 81 ILEAIERERItvlpGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELV----RRMRselgfetVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 578 TsLCeyRPGVPW----NCIGKPLKNYRCHILDlhhnplpvgfEGELCIAGSGLAHGYLHQEALSAEKfiicrlpyMAAEE 653
Cdd:cd17638 157 T-MC--RPGDDAetvaTTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEA--------IDADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 654 RLYrTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA-RSQPSGKILAAFVQPASPE-LTI 731
Cdd:cd17638 216 WLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGvPDERMGEVGKAFVVARPGVtLTE 294
|
330 340 350
....*....|....*....|....*....|....*.
gi 1725075560 732 DALRHALVTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:cd17638 295 EDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1330-1696 |
3.59e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 84.16 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAH---TQPDSLAVsCER------QQYSYRQLWAQSERVAHALLRID---SRPfsVGVMMEKSCHVAVLLLGVLRAGKH 1397
Cdd:PRK08180 44 RLVHwaqEAPDRVFL-AERgadggwRRLTYAEALERVRAIAQALLDRGlsaERP--LMILSGNSIEHALLALAAMYAGVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1398 YVPIDVHY---PAD--RVSYMIENAQ-ARLLVTDGEPEQG-------------------WASPAVGFDSLV---SHPAAA 1449
Cdd:PRK08180 121 YAPVSPAYslvSQDfgKLRHVLELLTpGLVFADDGAAFARalaavvpadvevvavrgavPGRAATPFAALLatpPTAAVD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1450 DALPIPADDTLAYIMYTSGSTGNPKGVMITHGNlnnftndfvgrlaLSARDKVLSLTSISFDIFGLELFCSL-----AGG 1524
Cdd:PRK08180 201 AAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRM-------------LCANQQMLAQTFPFLAEEPPVLVDWLpwnhtFGG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1525 AH-VTLCpretamdpvkLYH----FIERQQPSV------------IQAT-----PTVWSTIVHHLPAASQ------RPLT 1576
Cdd:PRK08180 268 NHnLGIV----------LYNggtlYIDDGKPTPggfdetlrnlreISPTvyfnvPKGWEMLVPALERDAAlrrrffSRLK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1577 VLC-GGEKMPAALLTQLRRIATRVL--QV-----YGPTETtiwSTCADLTHEGASD--CIGTPIQATEV-LVmdqagnpl 1645
Cdd:PRK08180 338 LLFyAGAALSQDVWDRLDRVAEATCgeRIrmmtgLGMTET---APSATFTTGPLSRagNIGLPAPGCEVkLV-------- 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 1646 PSGAFGELWLGGAGVSPGYWRNPTLSDKvflrrqAFGAERYmYRTGDIVRF 1696
Cdd:PRK08180 407 PVGGKLEVRVKGPNVTPGYWRAPELTAE------AFDEEGY-YRSGDAVRF 450
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
361-770 |
5.71e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 83.21 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 361 ILKSNKTYV------LLDPQAPA-ARNQSILDDVQPALILADSPLhsGDAPCIAP-SSIDYRS-LNIHAEQLPQSRDALA 431
Cdd:PRK12406 78 ILEDSGARVliahadLLHGLASAlPAGVTVLSVPTPPEIAAAYRI--SPALLTPPaGAIDWEGwLAQQEPYDGPPVPQPQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 432 YVCYTSGTTGKPKGVMigR-----EGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFgwDVYG--ALVSGATLYLAPsel 504
Cdd:PRK12406 156 SMIYTSGTTGHPKGVR--RaaptpEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAP--NAYGlrAGRLGGVLVLQP--- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 505 HTDVGALHDYLTQHDIGHITITPAI---LELLPREMWPG-----LRtMIVMGDAP-PADV----VAWWAerTRLCNGYGP 571
Cdd:PRK12406 229 RFDPEELLQLIERHRITHMHMVPTMfirLLKLPEEVRAKydvssLR-HVIHAAAPcPADVkramIEWWG--PVIYEYYGS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 572 TEASIATsLCEY-----RPGVpwncIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLA----HGylHQEALsaekfi 642
Cdd:PRK12406 306 TESGAVT-FATSedalsHPGT----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPdftyHN--KPEKR------ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 643 icrlpymAAEER--LYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILA 719
Cdd:PRK12406 373 -------AEIDRggFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEfGEALM 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 720 AFVQPaSPELTIDA--LRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK12406 446 AVVEP-QPGATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
435-765 |
6.01e-16 |
|
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: 83.12 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMIGREG-----LSNVAQNhrdfiGLAQGSRVLAIASLgFDAFGWD-VYGALVSGATLYLAPselHTDV 508
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGaylnaLANILEW-----EMKQHPVYLWTLPM-FHCNGWCfPWTVAAVGGTNVCLR---KVDA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 509 GALHDYLTQHDIGHITITPAILELL----PREMWPGLRTMIVM--GDAPPADVVAWWAERT-RLCNGYGPTEASIATSLC 581
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLanapPSDARPLPHRVHVMtaGAPPPAAVLAKMEELGfDVTHVYGLTETYGPATVC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 582 EYRPgvPWNciGKPLK-NYRCH--------------ILDLH-HNPLPVGFE--GELCIAGSGLAHGYLHQEALSAEKFii 643
Cdd:cd12118 291 AWKP--EWD--ELPTEeRARLKarqgvryvgleevdVLDPEtMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 644 crlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFV 722
Cdd:cd12118 365 --------RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwGEVPCAFV 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1725075560 723 -----QPASPELTIDALRHALVTLLhpaaIPSVFIFLPaLPLTINGKI 765
Cdd:cd12118 437 elkegAKVTEEEIIAFCREHLAGFM----VPKTVVFGE-LPKTSTGKI 479
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
312-772 |
6.28e-16 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 83.49 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDP---------QAPAARNQS 382
Cdd:PLN02330 51 VTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPtaleseikkQAEAAGAKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 383 ILDDVQ----------PALILADSPLHSG-------DAPCIAPSSIDYrslnihaEQLPQSRdaLAYVCYTSGTTGKPKG 445
Cdd:PLN02330 131 IVTNDTnygkvkglglPVIVLGEEKIEGAvnwkellEAADRAGDTSDN-------EEILQTD--LCALPFSSGTTGISKG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 446 VMIgreglsnvaqNHRDFIG------LAQGSRVLA-IASLGFDAFgWDVYGAL-VSGATL-------YLAPSELHTDVGA 510
Cdd:PLN02330 202 VML----------THRNLVAnlcsslFSVGPEMIGqVVTLGLIPF-FHIYGITgICCATLrnkgkvvVMSRFELRTFLNA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 511 LhdylTQHDIGHITITPAILELLPREM------WPGLRTMIVMGDAPP--ADVVAWWAER---TRLCNGYGPTEASIATs 579
Cdd:PLN02330 271 L----ITQEVSFAPIVPPIILNLVKNPiveefdLSKLKLQAIMTAAAPlaPELLTAFEAKfpgVQVQEAYGLTEHSCIT- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 580 LCEYRP----GVP-WNCIGKPLKNYRCHILDLHHN-PLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEE 653
Cdd:PLN02330 346 LTHGDPekghGIAkKNSVGFILPNLEVKFIDPDTGrSLPKNTPGELCVRSQCVMQGYYNNKEETDRTI---------DED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 654 RLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA-RSQPSGKILAAFV--QPASPELT 730
Cdd:PLN02330 417 GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPlPDEEAGEIPAACVviNPKAKESE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1725075560 731 IDALRHALVTLLHPAAIPSVFiFLPALPLTINGKIARQQLEK 772
Cdd:PLN02330 497 EDILNFVAANVAHYKKVRVVQ-FVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1336-1805 |
6.61e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 83.12 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRP-FSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMI 1414
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPgRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1415 ENAQARLLVTDGEPEQGWAspAVGFDSLVSHPAAADALPIPADDTLA----YIMYTSGSTGNPKGV----MITHGNLNNF 1486
Cdd:PRK13383 129 RAHHISTVVADNEFAERIA--GADDAVAVIDPATAGAEESGGRPAVAapgrIVLLTSGTTGKPKGVprapQLRSAVGVWV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 TNDFVGRLALSARdkvLSLTSISFDIFGL-ELFCSLAGGAHVtLCPR----ETAMDPVKLYhfierqQPSVIQATPTVWS 1561
Cdd:PRK13383 207 TILDRTRLRTGSR---ISVAMPMFHGLGLgMLMLTIALGGTV-LTHRhfdaEAALAQASLH------RADAFTAVPVVLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1562 TIVHHLPAASQR-PL----TVLCGGEKMPAALLTQLRRIATRVL-QVYGPTETTI--WSTCADLthEGASDCIGTPIQAT 1633
Cdd:PRK13383 277 RILELPPRVRARnPLpqlrVVMSSGDRLDPTLGQRFMDTYGDILyNGYGSTEVGIgaLATPADL--RDAPETVGKPVAGC 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1634 EVLVMDQAGNPLPSGAFGELWLGGAGVSPGYwrnptlSDKvflrrqafGAERY---MYRTGDIVRFNRQGQLEYLGRNDH 1710
Cdd:PRK13383 355 PVRILDRNNRPVGPRVTGRIFVGGELAGTRY------TDG--------GGKAVvdgMTSTGDMGYLDNAGRLFIVGREDD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1711 QVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQ-QARIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSA 1789
Cdd:PRK13383 421 MIISGGENVYPRAVENALAAHPAVADNAVIGVPDERfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSS 500
|
490
....*....|....*.
gi 1725075560 1790 FPLTNNNKIDIRRLPA 1805
Cdd:PRK13383 501 IPRNPTGKVLRKELPG 516
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
427-767 |
8.74e-16 |
|
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: 80.77 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 427 RDALAyVCYTSGTTGKPKGVMIGREGLSNVAQN-HRDFIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSelH 505
Cdd:cd17635 1 EDPLA-VIFTSGTTGEPKAVLLANKTFFAVPDIlQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--N 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 506 TDVGALHDYLTQHDIGHITITPAILELLPREM------WPGLRTMIVMGDAPPAD--VVAWWAERTRLCNGYGPTEASIA 577
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELksanatVPSLRLIGYGGSRAIAAdvRFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 578 TSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYr 657
Cdd:cd17635 158 LCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI---------DGWVN- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 658 TGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV-ESACVVARSQPSGKILAAFVqPASPEL---TIDA 733
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVqECACYEISDEEFGELVGLAV-VASAELdenAIRA 306
|
330 340 350
....*....|....*....|....*....|....
gi 1725075560 734 LRHALVTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:cd17635 307 LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1336-1801 |
9.36e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 82.63 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1336 PDSLAVSCERQQYSYRQLWAQSERVAHAL----LRIDSRpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVS 1411
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLiaqgLGPGDH---VGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1412 YMIENAQAR------------------------LLVTDGEPEQGWASPAVGFDSLVSHpAAADALPIP--ADDTlaYIMY 1465
Cdd:PRK07798 94 YLLDDSDAValvyerefaprvaevlprlpklrtLVVVEDGSGNDLLPGAVDYEDALAA-GSPERDFGErsPDDL--YLLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1466 TSGSTGNPKGVMITHGNLnnFTNDFVGRLALSA---RDKVlSLTSISFDIFGLELFCS----------------LAGGAH 1526
Cdd:PRK07798 171 TGGTTGMPKGVMWRQEDI--FRVLLGGRDFATGepiEDEE-ELAKRAAAGPGMRRFPApplmhgagqwaafaalFSGQTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1527 VTLcpRETAMDPVKLYHFIERQQPSVIQ------ATPtvwstIVHHLPAASQRPLTVL----CGG----EKMPAALLTQL 1592
Cdd:PRK07798 248 VLL--PDVRFDADEVWRTIEREKVNVITivgdamARP-----LLDALEARGPYDLSSLfaiaSGGalfsPSVKEALLELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1593 RRIAtrVLQVYGPTETTIWSTcaDLTHEGASDCIGTPIQATE-VLVMDQAGNPLPSGAFGELWLGGAGVSP-GYWRNPTL 1670
Cdd:PRK07798 321 PNVV--LTDSIGSSETGFGGS--GTVAKGAVHTGGPRFTIGPrTVVLDEDGNPVEPGSGEIGWIARRGHIPlGYYKDPEK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1671 SDKVFLRrqaFGAERYMYrTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIVGE-----G 1745
Cdd:PRK07798 397 TAETFPT---IDGVRYAI-PGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD--ALVVGVpderwG 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 1746 QqaRIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIR 1801
Cdd:PRK07798 471 Q--EVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
432-782 |
1.10e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 82.87 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 432 YVCYTSGTTGKPKGVMIGREG-LSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLYLAPSELHTDVGA 510
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGPhLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKNKHI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 511 LHDY---LTQHDIGHITITPAILELLPReMWPG------------LRTMIVMGDAPPADVVAWWAERTRLC--NGYGPTE 573
Cdd:PTZ00237 338 EDDLwntIEKHKVTHTLTLPKTIRYLIK-TDPEatiirskydlsnLKEIWCGGEVIEESIPEYIENKLKIKssRGYGQTE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 574 ASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIA---GSGLAHGYLHQEalsaEKF--IICRLP- 647
Cdd:PTZ00237 417 IGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKND----EKFkqLFSKFPg 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 648 YmaaeerlYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA------RSQPSGkILAAF 721
Cdd:PTZ00237 493 Y-------YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGiydpdcYNVPIG-LLVLK 564
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 722 VQPASPELTIDALRHALVTLL----HPAAIPSVFIFLPALPLTINGKIARQQLEKWpLDERNERL 782
Cdd:PTZ00237 565 QDQSNQSIDLNKLKNEINNIItqdiESLAVLRKIIIVNQLPKTKTGKIPRQIISKF-LNDSNYQL 628
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
315-724 |
2.92e-15 |
|
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: 80.87 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILA 394
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 395 DSplhsgdapciapssidyrslnihaeqlpqSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLA 474
Cdd:cd17640 84 EN-----------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 475 IASLgfdafgWDVYGALVSGATLYLAPSELHTDVGALHDYLTQhdighitITPAILELLPReMWPGLRTMIVM------- 547
Cdd:cd17640 135 ILPI------WHSYERSAEYFIFACGCSQAYTSIRTLKDDLKR-------VKPHYIVSVPR-LWESLYSGIQKqvskssp 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 548 ---------------------GDAPPADVVAWW-AERTRLCNGYGPTEASIATSlCEYRPGVPWNCIGKPLKNYRCHILD 605
Cdd:cd17640 201 ikqflflfflsggifkfgisgGGALPPHVDTFFeAIGIEVLNGYGLTETSPVVS-ARRLKCNVRGSVGRPLPGTEIKIVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 606 LHHN-PLPVGFEGELCIAGSGLAHGYLHQ-----EALSAEKFiicrlpymaaeerlYRTGDIAKWDEQGNIIFVGR-RDH 678
Cdd:cd17640 280 PEGNvVLPPGEKGIVWVRGPQVMKGYYKNpeatsKVLDSDGW--------------FNTGDLGWLTCGGELVLTGRaKDT 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1725075560 679 QVKIRGVRIEMGEVESAVRSHPLVESACVVARSQpsgKILAAFVQP 724
Cdd:cd17640 346 IVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQ---KRLGALIVP 388
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
313-770 |
3.29e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 80.81 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALI 392
Cdd:PRK13383 57 DDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 LADSPL-----HSGDA-PCIAPSSIDYRSLNIHAEQLPQSRdalaYVCYTSGTTGKPKGVMIG---REGLSnVAQNHRDF 463
Cdd:PRK13383 137 VADNEFaeriaGADDAvAVIDPATAGAEESGGRPAVAAPGR----IVLLTSGTTGKPKGVPRApqlRSAVG-VWVTILDR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 464 IGLAQGSRVlAIASLGFDAFGwdvYGALVsgATLYLAPSEL---HTDVGALHDYLTQHDIGHITITPA----ILELLP-- 534
Cdd:PRK13383 212 TRLRTGSRI-SVAMPMFHGLG---LGMLM--LTIALGGTVLthrHFDAEAALAQASLHRADAFTAVPVvlarILELPPrv 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 535 --REMWPGLRTMIVMGDAPPADVVAWWAER--TRLCNGYGPTEASIAT--SLCEYRPgvpW-NCIGKPLKNYRCHILDLH 607
Cdd:PRK13383 286 raRNPLPQLRVVMSSGDRLDPTLGQRFMDTygDILYNGYGSTEVGIGAlaTPADLRD---ApETVGKPVAGCPVRILDRN 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 608 HNPLPVGFEGELCIAGSGLAHGYlhqeALSAEKFIIcrlpymaaeERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRI 687
Cdd:PRK13383 363 NRPVGPRVTGRIFVGGELAGTRY----TDGGGKAVV---------DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 688 EMGEVESAVRSHPLV-ESACVVARSQPSGKILAAFV--QPASpELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGK 764
Cdd:PRK13383 430 YPRAVENALAAHPAVaDNAVIGVPDERFGHRLAAFVvlHPGS-GVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGK 508
|
....*.
gi 1725075560 765 IARQQL 770
Cdd:PRK13383 509 VLRKEL 514
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
576-863 |
4.41e-15 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 77.87 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 IATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIICRLPYMAAEERL 655
Cdd:COG3433 2 AIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 656 YRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSGKILAAFVQP-ASPELTIDAL 734
Cdd:COG3433 82 ADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVaALDGLAAAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 735 RHALVTLLHPAAIPSVFIFLPALPLTINGKIARQ----QLEKWPLDERNERLTPPETETEAILERIVANAIGCPQADVTQ 810
Cdd:COG3433 162 LAALDKVPPDVVAASAVVALDALLLLALKVVARAapalAAAEALLAAASPAPALETALTEEELRADVAELLGVDPEEIDP 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 811 E--FINLGAHSLTMSKIVALvARDLCCHLSIADLFRHNTVRKLAEYIENKAVAAE 863
Cdd:COG3433 242 DdnLFDLGLDSIRLMQLVER-WRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
381-773 |
4.89e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.04 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 381 QSILDDVQPALILADSPLHSGDAPCIAPSSIdyrslnihAEQLPQSRDALAyvcyTSGTTGKPKGVMIGREGLSNVAQNH 460
Cdd:PRK07445 85 QQVLNLVQPDQIWGLDQLKLSHPPPLPSQGI--------LPNLETGWIMIP----TGGSSGQIRFAIHTWETLTASVQGF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 461 RDFIglaQGSRVLAIASL------GFDAFgwdvYGALVSGATLYLAPselhtdvgaLHDyLTQHDIGHITITPAILELLP 534
Cdd:PRK07445 153 QRYF---QLQQVNSFCVLplyhvsGLMQF----MRSFLTGGKLVILP---------YKR-LKSGQELPPNPSDFFLSLVP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 535 REM---------WPGLRTMIVMGDAPPadvvawWAE--------RTRLCNGYGPTEAsiATSLCEYRPGVPW---NCIGK 594
Cdd:PRK07445 216 TQLqrllqlrpqWLAQFRTILLGGAPA------WPSlleqarqlQLRLAPTYGMTET--ASQIATLKPDDFLagnNSSGQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 595 PLKNYRchiLDLHHNPLpvgfeGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaeerlyrTGDIAKWDEQGNIIFVG 674
Cdd:PRK07445 288 VLPHAQ---ITIPANQT-----GNITIQAQSLALGYYPQILDSQGIFE---------------TDDLGYLDAQGYLHILG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 675 RRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIF 753
Cdd:PRK07445 345 RNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIP 424
|
410 420
....*....|....*....|
gi 1725075560 754 LPALPLTINGKIARQQLEKW 773
Cdd:PRK07445 425 VPQLPRNPQGKINRQQLQQI 444
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1349-1567 |
5.29e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 79.95 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHAL----LRIDSRpfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVT 1424
Cdd:PRK08276 13 TYGELEARSNRLAHGLralgLREGDV---VAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1425 DG---EPEQGWAS--------------PAVGFDSLVSHPAAADALPIPaDDTLAYIM-YTSGSTGNPKGVmithgnlnnf 1486
Cdd:PRK08276 90 SAalaDTAAELAAelpagvplllvvagPVPGFRSYEEALAAQPDTPIA-DETAGADMlYSSGTTGRPKGI---------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 tndfvgRLALSARD----KVLSLTSISFDIFGlelfcslaGGAHVTLCPRetamdPvkLYHfierqqpsviqATPTVWST 1562
Cdd:PRK08276 159 ------KRPLPGLDpdeaPGMMLALLGFGMYG--------GPDSVYLSPA-----P--LYH-----------TAPLRFGM 206
|
....*
gi 1725075560 1563 IVHHL 1567
Cdd:PRK08276 207 SALAL 211
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
428-772 |
6.43e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 80.23 E-value: 6.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIgreglsnvaqNHRDFIglAQGSRVLAIASLGFDafgwDVY---------GALVSGATLY 498
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTI----------SHSALI--VQSLAKIAIVGYGED----DVYlhtaplchiGGLSSALAML 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 499 LapselhtdVGALH------------DYLTQHDIGHITITPAILELLPR-----EMW---PGLRTMIVMGDAPPADVVAW 558
Cdd:PLN02860 236 M--------VGACHvllpkfdakaalQAIKQHNVTSMITVPAMMADLISltrksMTWkvfPSVRKILNGGGSLSSRLLPD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 559 WAE---RTRLCNGYGPTEAsiATSLCEYRPGVPWNCIGKPLKNYRCHILDLHhNPLPVGF-------------------- 615
Cdd:PLN02860 308 AKKlfpNAKLFSAYGMTEA--CSSLTFMTLHDPTLESPKQTLQTVNQTKSSS-VHQPQGVcvgkpaphvelkigldessr 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 616 EGELCIAGSGLAHGYLHQEALSAEKfiicrlpymAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESA 695
Cdd:PLN02860 385 VGRILTRGPHVMLGYWGQNSETASV---------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAV 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 696 VRSHPLVESACVV----ARsqpSGKILAAFV---------------QPASPELTIDALRHALVTL-LHPAAIPSVFI-FL 754
Cdd:PLN02860 456 LSQHPGVASVVVVgvpdSR---LTEMVVACVrlrdgwiwsdnekenAKKNLTLSSETLRHHCREKnLSRFKIPKLFVqWR 532
|
410
....*....|....*...
gi 1725075560 755 PALPLTINGKIARQQLEK 772
Cdd:PLN02860 533 KPFPLTTTGKIRRDEVRR 550
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1317-1798 |
7.62e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 79.85 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1317 DAGSRDSLLMH--IGRL----AHTQPDSLA-VSCERQ-QYSYRQLWAQSERVAHALLRIdsrpfsvGVmmEKSCHVAV-- 1386
Cdd:PRK08315 5 VRGPTDVPLLEqtIGQLldrtAARYPDREAlVYRDQGlRWTYREFNEEVDALAKGLLAL-------GI--EKGDRVGIwa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1387 --------LLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVT-DG-------------EPEQGWASPA-------- 1436
Cdd:PRK08315 76 pnvpewvlTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAaDGfkdsdyvamlyelAPELATCEPGqlqsarlp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1437 -------VG---------FDSLVSHPAAADalpipaDDTLAYIM------------YTSGSTGNPKGVMITHGN-LNN-F 1486
Cdd:PRK08315 156 elrrvifLGdekhpgmlnFDELLALGRAVD------DAELAARQatldpddpiniqYTSGTTGFPKGATLTHRNiLNNgY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 tndFVGR-LALSARDKV-----LsltsisFDIFGL---ELFCSLAGGAHVTlcPREtAMDPVKLYHFIERQQPSVIQATP 1557
Cdd:PRK08315 230 ---FIGEaMKLTEEDRLcipvpL------YHCFGMvlgNLACVTHGATMVY--PGE-GFDPLATLAAVEEERCTALYGVP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1558 TVWSTIVHHlPAASQRPLTVL---------CGGEKMpaalltqlRRI-----ATRVLQVYGPTETT--IWSTCADLTHEG 1621
Cdd:PRK08315 298 TMFIAELDH-PDFARFDLSSLrtgimagspCPIEVM--------KRVidkmhMSEVTIAYGMTETSpvSTQTRTDDPLEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1622 ASDCIGTPIQATEVLVMDQA-GNPLPSGAFGELWLGGAGVSPGYWRNPtlsDKVflrRQAFGAERYMyRTGDIVRFNRQG 1700
Cdd:PRK08315 369 RVTTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDP---EKT---AEAIDADGWM-HTGDLAVMDEEG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1701 QLEYLGRNDHQVkIR-GHRIELSEIDLSLSSLDNI----------ERslsliVGEGQQARIVsylqLTSGEELNEKAVRT 1769
Cdd:PRK08315 442 YVNIVGRIKDMI-IRgGENIYPREIEEFLYTHPKIqdvqvvgvpdEK-----YGEEVCAWII----LRPGATLTEEDVRD 511
|
570 580
....*....|....*....|....*....
gi 1725075560 1770 ALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:PRK08315 512 FCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1323-1798 |
8.66e-15 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 79.67 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1323 SLLMHIGRLAHTQPDSLAVS-CE-RQQYSYRQLWAQSERVAHAL-LRIDSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYV 1399
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRrCDgTSALRYRELVAEVGGLAADLrAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1400 PIDVHYPADRVSYMIENAQ-ARLLVTDG-------EPEQGWASPAVGFDSLVSHPAAADALPIP---------ADDTLAY 1462
Cdd:PRK05857 95 MADGNLPIAAIERFCQITDpAAALVAPGskmassaVPEALHSIPVIAVDIAAVTRESEHSLDAAslagnadqgSEDPLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 ImYTSGSTGNPKGVMIThgNLNNFT-NDFVGRLALSARDKVLSLTSIS----FDIFGLE--LFCSLAGGAHVTlcpreTA 1535
Cdd:PRK05857 175 I-FTSGTTGEPKAVLLA--NRTFFAvPDILQKEGLNWVTWVVGETTYSplpaTHIGGLWwiLTCLMHGGLCVT-----GG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1536 MDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQR--PLTVLC-GGEKMPAALLTQLRRIATRVLQVYGPTETTIWS 1612
Cdd:PRK05857 247 ENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGyGGSRAIAADVRFIEATGVRTAQVYGLSETGCTA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1613 TCADLTHEGASD----CIGTPIQATEVLVMDQAG------NPLPSGAFGELWLGGAGVSPGYWRNPTlsdkvflRRQAFG 1682
Cdd:PRK05857 327 LCLPTDDGSIVKieagAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPE-------RTAEVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1683 AERYMyRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSyLQLTSGEEL 1762
Cdd:PRK05857 400 IDGWV-NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVG-LAVVASAEL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1725075560 1763 NEKAVRtALKARLP--------NIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:PRK05857 478 DESAAR-ALKHTIAarfrresePMARPSTIVIVTDIPRTQSGKV 520
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
414-770 |
9.03e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 79.69 E-value: 9.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 414 RSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGL-SNVAQNHRDFIGLAQGSRVLaiasLGFDAFgWDVYG--- 489
Cdd:PRK06710 192 KEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEEVV----LGVLPF-FHVYGmta 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 490 ----ALVSGATLYLAPSelhTDVGALHDYLTQHDI----GHITITPAILE--LLPREMWPGLRTMIvMGDAP-PADVVAW 558
Cdd:PRK06710 267 vmnlSIMQGYKMVLIPK---FDMKMVFEAIKKHKVtlfpGAPTIYIALLNspLLKEYDISSIRACI-SGSAPlPVEVQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 559 WAERT--RLCNGYGPTEASIATS---LCEYR-PGvpwnCIGKPLKNYRCHILDLHHNP-LPVGFEGELCIAGSGLAHGYL 631
Cdd:PRK06710 343 FETVTggKLVEGYGLTESSPVTHsnfLWEKRvPG----SIGVPWPDTEAMIMSLETGEaLPPGEIGEIVVKGPQIMKGYW 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 632 HQEALSAEkfiicrlpymAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARS 711
Cdd:PRK06710 419 NKPEETAA----------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVP 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 712 QP-SGKILAAF-VQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK06710 489 DPyRGETVKAFvVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1326-1476 |
9.95e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 79.35 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1326 MHIGRLAHTQPDSLAV--SCERQQYSYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPID 1402
Cdd:PRK13391 1 MYPGIHAQTTPDKPAVimASTGEVVTYRELDERSNRLAHLFRSLGLKRGDhVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1403 VHYPADRVSYMIENAQARLLVT-----DGEPEQGWASPAV-------------GFDSLVSHPAAADALPIPADDTLAYIM 1464
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITsaaklDVARALLKQCPGVrhrlvldgdgeleGFVGYAEAVAGLPATPIADESLGTDML 160
|
170
....*....|..
gi 1725075560 1465 YTSGSTGNPKGV 1476
Cdd:PRK13391 161 YSSGTTGRPKGI 172
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1326-1798 |
1.10e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1326 MHIGRLAHTQPDSLAVSCER--QQYSYRQLWAQSERVAHALLRIDSRPFSVGVMM-EKSCHVAVLLLGVLRAGKHYVPID 1402
Cdd:PRK13390 1 MYPGTHAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLsDNSPEALVVLWAALRSGLYITAIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1403 VHYPADRVSYMIENAQARLLVT----DGEPEQGWASPAV---------GFDSLVSHPAAADAlPIPADDTLAYIMYTSGS 1469
Cdd:PRK13390 81 HHLTAPEADYIVGDSGARVLVAsaalDGLAAKVGADLPLrlsfggeidGFGSFEAALAGAGP-RLTEQPCGAVMLYSSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1470 TGNPKGVMithgnlnnftNDFVGRLALSARDKVLSLTSISFDIFGLELF--------------CSL--AGGAHVTLCPRE 1533
Cdd:PRK13390 160 TGFPKGIQ----------PDLPGRDVDAPGDPIVAIARAFYDISESDIYyssapiyhaaplrwCSMvhALGGTVVLAKRF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1534 TAMDPVKlyhFIERQQPSVIQATPTVWSTIV---------HHLP-------AASQRPLTVlcggekmPAALLTQLRRIat 1597
Cdd:PRK13390 230 DAQATLG---HVERYRITVTQMVPTMFVRLLkldadvrtrYDVSslravihAAAPCPVDV-------KHAMIDWLGPI-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1598 rVLQVYGPTET---TIWSTCADLTHEGAsdcIGTPIQATeVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKV 1674
Cdd:PRK13390 298 -VYEYYSSTEAhgmTFIDSPDWLAHPGS---VGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1675 flrrqAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGE---GQQARIV 1751
Cdd:PRK13390 373 -----QHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpemGEQVKAV 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1752 syLQLTSGEELNEKAVRTAL---KARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:PRK13390 448 --IQLVEGIRGSDELARELIdytRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
313-771 |
1.12e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 79.34 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYG----EIDRASDQFacwlLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQ 388
Cdd:PRK08008 34 VVRRYSYLelneEINRTANLF----YSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 389 PALILADSP--------LHSGDAP----CIA-------PSSIDY-RSLNIHAEQL----PQSRDALAYVCYTSGTTGKPK 444
Cdd:PRK08008 110 ASLLVTSAQfypmyrqiQQEDATPlrhiCLTrvalpadDGVSSFtQLKAQQPATLcyapPLSTDDTAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 445 GVMIGREGLSnvaqnhrdFIG--------LAQGSRVLAIaslgFDAFGWD-----VYGALVSGATLYLapselhtdvgaL 511
Cdd:PRK08008 190 GVVITHYNLR--------FAGyysawqcaLRDDDVYLTV----MPAFHIDcqctaAMAAFSAGATFVL-----------L 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 512 HDYLTQHDIGHI-----TIT---PAILELL------PREMWPGLRTMIV---MGDAPPADvvawWAER--TRLCNGYGPT 572
Cdd:PRK08008 247 EKYSARAFWGQVckyraTITeciPMMIRTLmvqppsANDRQHCLREVMFylnLSDQEKDA----FEERfgVRLLTSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 573 EASIAtsLCEYRPGVP--WNCIGKPLKNYRCHILDLHHNPLPVGFEGELCI---AGSGLAHGYLHQEALSAEKFiicrlp 647
Cdd:PRK08008 323 ETIVG--IIGDRPGDKrrWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVL------ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 648 ymAAEERLYrTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFVQPAS 726
Cdd:PRK08008 395 --EADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSiRDEAIKAFVVLNE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1725075560 727 PE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLE 771
Cdd:PRK08008 472 GEtLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
428-770 |
1.23e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 79.21 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIGREGLsnVAQNHRDFIGLAQGSRVLAIASL------GFDAF-GWDVYgalvSGATLYLA 500
Cdd:PRK08316 171 DDLAQILYTSGTESLPKGAMLTHRAL--IAEYVSCIVAGDMSADDIPLHALplyhcaQLDVFlGPYLY----VGATNVIL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 501 PSE-----LHT----DVGAL------------HDYLTQHDIGHIT-------ITP-AILELLpREMWPGLRtmivmgdap 551
Cdd:PRK08316 245 DAPdpeliLRTieaeRITSFfapptvwisllrHPDFDTRDLSSLRkgyygasIMPvEVLKEL-RERLPGLR--------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 552 padvvawwaertrLCNGYGPTE-ASIATSL----CEYRPGvpwnCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGL 626
Cdd:PRK08316 315 -------------FYNCYGQTEiAPLATVLgpeeHLRRPG----SAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 627 AHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESAC 706
Cdd:PRK08316 378 MLGYWDDPEKTAEAF----------RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVA 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 707 VVARSQPS-GKILAAFVQP-ASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK08316 448 VIGLPDPKwIEAVTAVVVPkAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1349-1696 |
1.41e-14 |
|
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: 79.01 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRID-SRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPA-----DRVSYMIENAQARLL 1422
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGlSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFELLKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1423 -VTDGEP-------------------EQGWASPAVGFDSLVSHPAAADALPIPAD---DTLAYIMYTSGSTGNPKGVMIT 1479
Cdd:cd05921 107 fAQDAAPfaralaaifplgtplvvsrNAVAGRGAISFAELAATPPTAAVDAAFAAvgpDTVAKFLFTSGSTGLPKAVINT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1480 HGNLnnfTNDFVGRLALSAR----DKVL------SLTSISFDIFGLELFcslAGGahvTLcpretamdpvklyhFIERQQ 1549
Cdd:cd05921 187 QRML---CANQAMLEQTYPFfgeePPVLvdwlpwNHTFGGNHNFNLVLY---NGG---TL--------------YIDDGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1550 PS----------VIQATPTVWSTIV--HHLPAASQRPLTVLC------------GGEKMPAALLTQLRRIAT-------R 1598
Cdd:cd05921 244 PMpggfeetlrnLREISPTVYFNVPagWEMLVAALEKDEALRrrffkrlklmfyAGAGLSQDVWDRLQALAVatvgeriP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1599 VLQVYGPTETTIWSTcadLTHEGA--SDCIGTPIQATEV-LVmdqagnplPSGAFGELWLGGAGVSPGYWRNPTLSdkvf 1675
Cdd:cd05921 324 MMAGLGATETAPTAT---FTHWPTerSGLIGLPAPGTELkLV--------PSGGKYEVRVKGPNVTPGYWRQPELT---- 388
|
410 420
....*....|....*....|.
gi 1725075560 1676 lrRQAFGAERYmYRTGDIVRF 1696
Cdd:cd05921 389 --AQAFDEEGF-YCLGDAAKL 406
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
384-765 |
2.02e-14 |
|
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: 78.85 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 384 LDDVQPALILADSPL-HSGDAPCIAPSSI------DYRSLNIHAEQLPqsRDALAYVCYTSGTTGKPKGVMIGREG-LSN 455
Cdd:cd05943 200 LPSLLAVVVVPYTVAaGQPDLSKIAKALTledflaTGAAGELEFEPLP--FDHPLYILYSSGTTGLPKCIVHGAGGtLLQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 456 VAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVyGALVSGATLYLAP-SELHTDVGALHDYLTQHDIGHITITPA-ILELL 533
Cdd:cd05943 278 HLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV-SGLAVGATIVLYDgSPFYPDTNALWDLADEEGITVFGTSAKyLDALE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 534 PREMWPG-------LRTMIVMGDAPPADVVAW----WAERTRLCNGYGpteasiATSLCEyrpgvpwncigkplknyrCH 602
Cdd:cd05943 357 KAGLKPAethdlssLRTILSTGSPLKPESFDYvydhIKPDVLLASISG------GTDIIS------------------CF 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 603 ILdlhHNP-LPVgFEGELCIAGSGLA------HGylhqEALSAEK-FIICRLP--------------------YMAAEER 654
Cdd:cd05943 413 VG---GNPlLPV-YRGEIQCRGLGMAveafdeEG----KPVWGEKgELVCTKPfpsmpvgfwndpdgsryraaYFAKYPG 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 655 LYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPSGK---ILaaFV-----QPAS 726
Cdd:cd05943 485 VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDervIL--FVklregVELD 562
|
410 420 430
....*....|....*....|....*....|....*....
gi 1725075560 727 PELTiDALRHALVTLLHPAAIPSVFIFLPALPLTINGKI 765
Cdd:cd05943 563 DELR-KRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
312-770 |
3.85e-14 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 77.71 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDP---------QAPAARNQS 382
Cdd:PLN02246 46 ATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPfytpaeiakQAKASGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 383 IL------DDVQPALILADSPLHSGDAP---C------IAPSSIDYRSLNIHAEqlpqsrDALAyVCYTSGTTGKPKGVM 447
Cdd:PLN02246 126 IItqscyvDKLKGLAEDDGVTVVTIDDPpegClhfselTQADENELPEVEISPD------DVVA-LPYSSGTTGLPKGVM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 448 IGREGL-SNVAQ-------NhrdfIGLAQGSRVLAIASLgFDAFGWD--VYGALVSGATLYLAPSelhTDVGALHDYLTQ 517
Cdd:PLN02246 199 LTHKGLvTSVAQqvdgenpN----LYFHSDDVILCVLPM-FHIYSLNsvLLCGLRVGAAILIMPK---FEIGALLELIQR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 518 HDIGHITITPAI-LELLPREM-----WPGLRtMIVMGDAPPA----DVVawwaeRTRLCN-----GYGPTEASIATSLC- 581
Cdd:PLN02246 271 HKVTIAPFVPPIvLAIAKSPVvekydLSSIR-MVLSGAAPLGkeleDAF-----RAKLPNavlgqGYGMTEAGPVLAMCl 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 582 ----EYRPGVPWNCiGKPLKNYRCHILDlhhnP-----LPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAE 652
Cdd:PLN02246 345 afakEPFPVKSGSC-GTVVRNAELKIVD----PetgasLPRNQPGEICIRGPQIMKGYLNDPEATANTI---------DK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 653 ERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFV-QPASPELT 730
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEvAGEVPVAFVvRSNGSEIT 490
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1725075560 731 IDALRHALVT-LLHPAAIPSVFiFLPALPLTINGKIARQQL 770
Cdd:PLN02246 491 EDEIKQFVAKqVVFYKRIHKVF-FVDSIPKAPSGKILRKDL 530
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1328-1728 |
4.43e-14 |
|
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: 77.54 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1328 IGRLAHTQPDSLA-VSC----ERQQYSYRQLWAQSERVAHALLRID-SRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPI 1401
Cdd:cd05970 23 VDAMAKEYPDKLAlVWCddagEERIFTFAELADYSDKTANFFKAMGiGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1402 DVHYPADRVSYMIENAQARLLVTDGE---PEQ-GWASPAVGFDS-LVS------------HPAAADALPI---------P 1455
Cdd:cd05970 103 THQLTAKDIVYRIESADIKMIVAIAEdniPEEiEKAAPECPSKPkLVWvgdpvpegwidfRKLIKNASPDferptansyP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 ADDTLAYIMYTSGSTGNPKgvMITHGNLNNFTNDFVGRLALSARDKVLSLTsISFDIFGLELFCSLAG----GAHVTLCP 1531
Cdd:cd05970 183 CGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREGGLHLT-VADTGWGKAVWGKIYGqwiaGAAVFVYD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1532 RETaMDPVKLYHFIERQQPSVIQATPTVWSTIVH----HLPAASQRPLTVlcGGEKM-PAALLTQLRRIATRVLQVYGPT 1606
Cdd:cd05970 260 YDK-FDPKALLEKLSKYGVTTFCAPPTIYRFLIRedlsRYDLSSLRYCTT--AGEALnPEVFNTFKEKTGIKLMEGFGQT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1607 ETTIwsTCADLT-HEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGA-----GVSPGYWRNPTLSDKVFlrrqa 1680
Cdd:cd05970 337 ETTL--TIATFPwMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW----- 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1725075560 1681 fgaERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd05970 410 ---HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL 454
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
316-763 |
7.19e-14 |
|
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: 76.73 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 316 TYSYGEI-DRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPAlILA 394
Cdd:cd17632 67 TITYAELwERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPR-LLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 395 DSPLHSGDAPCI-----APSSI---DYR-SLNIHAEQL-----------------------------------PQSRDAL 430
Cdd:cd17632 146 VSAEHLDLAVEAvleggTPPRLvvfDHRpEVDAHRAALesarerlaavgipvttltliavrgrdlppaplfrpEPDDDPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 431 AYVCYTSGTTGKPKGVMIGREglsNVAQNHRDFIGLaQGSRVLAIASLGF------DAFGWdVYGALVSGATLYLAP--- 501
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTER---LVATFWLKVSSI-QDIRPPASITLNFmpmshiAGRIS-LYGTLARGGTAYFAAasd 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 -SELHTDVGALH-----------DYLTQH---DIGHITITPAILELLPREMWPGLR--------TMIVMGDAPPADVVAW 558
Cdd:cd17632 301 mSTLFDDLALVRptelflvprvcDMLFQRyqaELDRRSVAGADAETLAERVKAELRervlggrlLAAVCGSAPLSAEMKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 559 WAERT---RLCNGYGPTEASIATSLCEY-RPgvpwncigkPLKNYRchILD-------LHHNPLPvgfEGELCIAGSGLA 627
Cdd:cd17632 381 FMESLldlDLHDGYGSTEAGAVILDGVIvRP---------PVLDYK--LVDvpelgyfRTDRPHP---RGELLVKTDTLF 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 628 HGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKI-RGVRIEMGEVESAVRSHPLVESAC 706
Cdd:cd17632 447 PGYYKRPEVTAEVF---------DEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIF 517
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 707 VVARSQPSgKILAAFV--QPASPELTIDALRHALVTLLHPAA---------IPSVFIFLPAlPLTI-NG 763
Cdd:cd17632 518 VYGNSERA-YLLAVVVptQDALAGEDTARLRAALAESLQRIAreaglqsyeIPRDFLIETE-PFTIaNG 584
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1436-1802 |
7.84e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 76.73 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1436 AVGFDSLVSHPAAADALPI-PADDTLAYIMYTSGSTGNPKGVMITHGNLnnFTNDFVGRLALSARDKVLSLTSIS----F 1510
Cdd:PRK05677 184 AVKFNDALAKGAGQPVTEAnPQADDVAVLQYTGGTTGVAKGAMLTHRNL--VANMLQCRALMGSNLNEGCEILIAplplY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1511 DIFGLELFC--SLAGGAHVTLCPretamDPVKLYHFIE---RQQPSVIQATPTVWSTIVHHLPAA----SQRPLTvLCGG 1581
Cdd:PRK05677 262 HIYAFTFHCmaMMLIGNHNILIS-----NPRDLPAMVKelgKWKFSGFVGLNTLFVALCNNEAFRkldfSALKLT-LSGG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1582 EKMPAALLTQLRRI-ATRVLQVYGPTETTIWSTCADLTHEGASdCIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGV 1660
Cdd:PRK05677 336 MALQLATAERWKEVtGCAICEGYGMTETSPVVSVNPSQAIQVG-TIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1661 SPGYWRNPTLSDKVflrrqaFGAERYMyRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSL 1740
Cdd:PRK05677 415 MKGYWQRPEATDEI------LDSDGWL-KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAI 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1741 IV-----GEGQQARIVSylqlTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIdIRR 1802
Cdd:PRK05677 488 GVpdeksGEAIKVFVVV----KPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKI-LRR 549
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
875-1172 |
8.68e-14 |
|
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: 75.81 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSPQQNLLWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDgvayqLAEPHTPIR--LAD 952
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRD-----RAEPLQYVRddLAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 953 HWV------DGQTLSAEKWVRQLC---ATPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNE 1023
Cdd:cd19547 78 PWAlldwsgEDPDRRAELLERLLAddrAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1024 LddHHGldaPQPQIQTI----DIVNSGIASPAPADVA--YWQQQLQDCRELDF---PLDKPRPLmpthagERIHYQLQPD 1094
Cdd:cd19547 158 L--AHG---REPQLSPCrpyrDYVRWIRARTAQSEESerFWREYLRDLTPSPFstaPADREGEF------DTVVHEFPEQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1095 VAGLLASRGKALGATPFALLCAALSLLLSRYTQQQDIVIGTAIAAR-DNLDQTQ-VSGFHVNTVPLRIQLSEQDTLAGLI 1172
Cdd:cd19547 227 LTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRpPELEGSEhMVGIFINTIPLRIRLDPDQTVTGLL 306
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1462-1799 |
9.61e-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: 74.36 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1462 YIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAHVTLcprETAMDPVKL 1541
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1542 YHFIERQQPSVIQATPT----VWSTIVHHLPAASqrpltVLCGGEKMPAALLTQLRRIA--TRVLQVYGPTETTIWSTCA 1615
Cdd:cd17633 81 IRKINQYNATVIYLVPTmlqaLARTLEPESKIKS-----IFSSGQKLFESTKKKLKNIFpkANLIEFYGTSELSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1616 DLTHEGASDcIGTPIQATEVLVMDQAGnplpsGAFGELWLGGAGVSPGYwrnptlsdkvfLRRQAFGAERYMyRTGDIVR 1695
Cdd:cd17633 156 NQESRPPNS-VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGY-----------VRGGFSNPDGWM-SVGDIGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1696 FNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLslIVGEGQQARIVSYLQLTSGEELNEKAVRTALKARL 1775
Cdd:cd17633 218 VDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAI--VVGIPDARFGEIAVALYSGDKLTYKQLKRFLKQKL 295
|
330 340
....*....|....*....|....
gi 1725075560 1776 PNIMIPSGFVVLSAFPLTNNNKID 1799
Cdd:cd17633 296 SRYEIPKKIIFVDSLPYTSSGKIA 319
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
421-742 |
1.05e-13 |
|
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: 75.97 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 421 EQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFDAFGWDVY-GALVSGATLYL 499
Cdd:cd05932 130 ERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVAF 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 APSeLHTDVGAL----------------------HDYLTQHDIGHITITPAILELLPREMWPGLR----TMIVMGDAP-P 552
Cdd:cd05932 210 AES-LDTFVEDVqrarptlffsvprlwtkfqqgvQDKIPQQKLNLLLKIPVVNSLVKRKVLKGLGldqcRLAGCGSAPvP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 553 ADVVAWWAE-RTRLCNGYGPTEASIATSLCeyRPG---VPWncIGKPLKNYRCHILDlhhnplpvgfEGELCIAGSGLAH 628
Cdd:cd05932 289 PALLEWYRSlGLNILEAYGMTENFAYSHLN--YPGrdkIGT--VGNAGPGVEVRISE----------DGEILVRSPALMM 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 629 GYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKI-RGVRIEMGEVESAVRSHPLVESACV 707
Cdd:cd05932 355 GYYKDPEATAEAF---------TADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCV 425
|
330 340 350
....*....|....*....|....*....|....*...
gi 1725075560 708 VARSQPSG---KILAAFVQPASPELTIDALRHALVTLL 742
Cdd:cd05932 426 IGSGLPAPlalVVLSEEARLRADAFARAELEASLRAHL 463
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
424-782 |
1.09e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 76.03 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 424 PQSRDALAYVCYTSGTTGKPKGVMIgreglsnvaqNHRDFIGL-------------AQGSRVLAIASLG-FDAFGWDVY- 488
Cdd:PLN02574 194 VIKQDDVAAIMYSSGTTGASKGVVL----------THRNLIAMvelfvrfeasqyeYPGSDNVYLAALPmFHIYGLSLFv 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 489 -GALVSGATLYLAPSelhTDVGALHDYLTQHDIGHITITPAILELLPREMWP------GLRTMIVMGDAPPA-----DVV 556
Cdd:PLN02574 264 vGLLSLGSTIVVMRR---FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGvcgevlKSLKQVSCGAAPLSgkfiqDFV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 557 AWWAErTRLCNGYGPTE-ASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLHHNP-LPVGFEGELCIAGSGLAHGYLHQE 634
Cdd:PLN02574 341 QTLPH-VDFIQGYGMTEsTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNP 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 635 ALSAEKFIicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA-RSQP 713
Cdd:PLN02574 420 KATQSTID---------KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAvPDKE 490
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 714 SGKILAAFV--QPASpELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEKWPLDERNERL 782
Cdd:PLN02574 491 CGEIPVAFVvrRQGS-TLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSSRL 560
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
310-773 |
1.09e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 75.87 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSV-VAVSMDKSATLLIVLLGILKSNKTYVLLDP--QAPAARNQSILDD 386
Cdd:PRK07867 22 LYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPtrRGAALARDIAHAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 387 VQpaLILADS---PLHSGDAPCIAPSSIDYRS----LNIHAEQLPQSRDA----LAYVCYTSGTTGKPK----------- 444
Cdd:PRK07867 102 CQ--LVLTESahaELLDGLDPGVRVINVDSPAwadeLAAHRDAEPPFRVAdpddLFMLIFTSGTSGDPKavrcthrkvas 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 445 -GVMI-GREGLSnvaqnhRDFIG-----LAQGSRVLAiaslgfdafGWDVygALVSGATLYLAP----SELHTDV---GA 510
Cdd:PRK07867 180 aGVMLaQRFGLG------PDDVCyvsmpLFHSNAVMA---------GWAV--ALAAGASIALRRkfsaSGFLPDVrryGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 511 LHDYLTQHDIGHITITPAilelLPREMWPGLRtmIVMG-DAPPADVvAWWAER--TRLCNGYGPTEASIATSlceYRPGV 587
Cdd:PRK07867 243 TYANYVGKPLSYVLATPE----RPDDADNPLR--IVYGnEGAPGDI-ARFARRfgCVVVDGFGSTEGGVAIT---RTPDT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 588 PWNCIGKPLKNYRchILDLHH-NPLPVG-FE-----------GELC-IAGSGLAHGYLHQEAlsaekfiicrlpymAAEE 653
Cdd:PRK07867 313 PPGALGPLPPGVA--IVDPDTgTECPPAeDAdgrllnadeaiGELVnTAGPGGFEGYYNDPE--------------ADAE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 654 RL----YRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SG-KILAAFVQPASP 727
Cdd:PRK07867 377 RMrggvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPvVGdQVMAALVLAPGA 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1725075560 728 ELTIDALRHALV--TLLHPAAIPSVFIFLPALPLTINGKIARQQL--EKW 773
Cdd:PRK07867 457 KFDPDAFAEFLAaqPDLGPKQWPSYVRVCAELPRTATFKVLKRQLsaEGV 506
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
313-770 |
1.11e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 76.10 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDD------ 386
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDsgakvl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 387 -VQPAL------ILADSPLHSGDAPCIAPSSIDYRS----LNIHAEQLPQSRDALAYVCYTSGTTGKPKGVmigREGLSN 455
Cdd:PRK08276 88 iVSAALadtaaeLAAELPAGVPLLLVVAGPVPGFRSyeeaLAAQPDTPIADETAGADMLYSSGTTGRPKGI---KRPLPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 456 VAQnhrdfigLAQGSRVLAIASLGFDAFGWDVYgalVSGATLY-LAPSEL--------HTDV--------GALhDYLTQH 518
Cdd:PRK08276 165 LDP-------DEAPGMMLALLGFGMYGGPDSVY---LSPAPLYhTAPLRFgmsalalgGTVVvmekfdaeEAL-ALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 519 DIGHITITPAI---LELLPREMWPG-----LRTMIVMGdAP-PADV----VAWWaertrlcnG------YGPTEA---SI 576
Cdd:PRK08276 234 RVTHSQLVPTMfvrMLKLPEEVRARydvssLRVAIHAA-APcPVEVkramIDWW--------GpiiheyYASSEGggvTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 577 ATS---LCeyRPGvpwnCIGKPLKNyRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEE 653
Cdd:PRK08276 305 ITSedwLA--HPG----SVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN---------PH 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 654 RLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPELTID 732
Cdd:PRK08276 369 GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEmGERVKAVVQPADGADAGD 448
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1725075560 733 ALRHALVTLLHP--AAI--PSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK08276 449 ALAAELIAWLRGrlAHYkcPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1451-1799 |
1.29e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.54 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1451 ALPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSIsFDIFGlelfcsLAGGAHVTLc 1530
Cdd:PRK06814 786 YFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPV-FHSFG------LTGGLVLPL- 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1531 preTAMDPVKLY----HFieRQQPSVIQATPtvwSTIV--------------HHLPAASQRplTVLCGGEKMPAALL-TQ 1591
Cdd:PRK06814 858 ---LSGVKVFLYpsplHY--RIIPELIYDTN---ATILfgtdtflngyaryaHPYDFRSLR--YVFAGAEKVKEETRqTW 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1592 LRRIATRVLQVYGPTETtiwstcadlthegasdcigTPIQATEVLVMDQAGN-------------PLP---SGafGELWL 1655
Cdd:PRK06814 928 MEKFGIRILEGYGVTET-------------------APVIALNTPMHNKAGTvgrllpgieyrlePVPgidEG--GRLFV 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1656 GGAGVSPGYWR--NPTLsdkvfLRRQAFGaeryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDn 1733
Cdd:PRK06814 987 RGPNVMLGYLRaeNPGV-----LEPPADG----WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELW- 1056
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1734 iERSLSLIV-------GEgqqaRIVsylQLTSGEELNEKAVRTALKAR-LPNIMIPSGFVVLSAFPLTNNNKID 1799
Cdd:PRK06814 1057 -PDALHAAVsipdarkGE----RII---LLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1389-1675 |
1.95e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 75.36 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1389 LGVLRAGKHYVPIDVHYPA---DRVSYMIENAQARLLVTD----------GEPEQGWASPAV-GFDSL-VSHPAAADALP 1453
Cdd:PRK05850 77 LGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTsavvddvteyVAPQPGQSAPPViEVDLLdLDSPRGSDARP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1454 IPADDTlAYIMYTSGSTGNPKGVMITHGNLN-NFTNDFVGRLAlsARDKVLSL--TSISFDIF----GLEL--FCSLAGG 1524
Cdd:PRK05850 157 RDLPST-AYLQYTSGSTRTPAGVMVSHRNVIaNFEQLMSDYFG--DTGGVPPPdtTVVSWLPFyhdmGLVLgvCAPILGG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1525 AHVTLcpretaMDPVKlyhFIERqqpsviqatPTVWStivhHLPAASQRP-----------------------------L 1575
Cdd:PRK05850 234 CPAVL------TSPVA---FLQR---------PARWM----QLLASNPHAfsaapnfafelavrktsdddmagldlggvL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1576 TVLCGGEKMPAAlltQLRRIATR----------VLQVYGPTETTI------WSTCADLTH----------------EGAS 1623
Cdd:PRK05850 292 GIISGSERVHPA---TLKRFADRfapfnlretaIRPSYGLAEATVyvatrePGQPPESVRfdyeklsaghakrcetGGGT 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 1624 DCI--GTPiQATEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVF 1675
Cdd:PRK05850 369 PLVsyGSP-RSPTVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTF 422
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
435-770 |
2.26e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 75.27 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLgFDAFGWDVYGAL--VSGATLYLApselHTDVGALH 512
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPM-FHCNGWCFTWTLaaLCGTNICLR----QVTAKAIY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 513 DYLTQHDIGHITITPAILELL---PRE--MWPGLRTMIVM--GDAPPADVVAWWAERT-RLCNGYGPTEASIATSLCEYR 584
Cdd:PLN02479 277 SAIANYGVTHFCAAPVVLNTIvnaPKSetILPLPRVVHVMtaGAAPPPSVLFAMSEKGfRVTHTYGLSETYGPSTVCAWK 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 585 PgvPWNCIgKPLKNYRCH--------------ILDLHHN-PLPVGFE--GELCIAGSGLAHGYLHQEALSAEKFiicrlp 647
Cdd:PLN02479 357 P--EWDSL-PPEEQARLNarqgvryiglegldVVDTKTMkPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF------ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 648 ymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPAS 726
Cdd:PLN02479 428 ----ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERwGESPCAFVTLKP 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 727 -------PELTIDALRHALVTLlhPAA-IPSVFIFLPaLPLTINGKIARQQL 770
Cdd:PLN02479 504 gvdksdeAALAEDIMKFCRERL--PAYwVPKSVVFGP-LPKTATGKIQKHVL 552
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
426-772 |
2.82e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.69 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 426 SRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNH-RDFI-GLAQGSRVLAIASLGFDAfGWDVYGALVSGATLYLAPSE 503
Cdd:PRK07470 161 DHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHlADLMpGTTEQDASLVVAPLSHGA-GIHQLCQVARGAATVLLPSE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 504 lHTDVGALHDYLTQHDIGHITITPAILELL------PREMWPGLRTMIVMGdAPpadvvAWWAERTR--------LCNGY 569
Cdd:PRK07470 240 -RFDPAEVWALVERHRVTNLFTVPTILKMLvehpavDRYDHSSLRYVIYAG-AP-----MYRADQKRalaklgkvLVQYF 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 570 GPTEASIA-TSL------CEYRPGVPWNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFi 642
Cdd:PRK07470 313 GLGEVTGNiTVLppalhdAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 643 icrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKI-LAA 720
Cdd:PRK07470 392 ---------RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwGEVgVAV 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 721 FVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIA----RQQLEK 772
Cdd:PRK07470 463 CVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITkkmvREELEE 518
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
428-765 |
3.35e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 75.35 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMI-GREGLSNVAQnHRDFIGLAQGSRVLAIASLgFDAFGWDV--YGALVSGatlylAPSEL 504
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLsHHNILSNIEQ-ISDVFNLRNDDVILSSLPF-FHSFGLTVtlWLPLLEG-----IKVVY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 505 HTD------VGALhdyLTQHdigHITI---TPAILELLPR------EMWPGLRTMIVMGDAPPADVVAWWAER--TRLCN 567
Cdd:PRK08633 855 HPDptdalgIAKL---VAKH---RATIllgTPTFLRLYLRnkklhpLMFASLRLVVAGAEKLKPEVADAFEEKfgIRILE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 568 GYGPTEAS--IATSLCEYRPGVPW-------NCIGKPLKNYRCHILDLHH-NPLPVGFEGELCIAGSGLAHGYLHQEALS 637
Cdd:PRK08633 929 GYGATETSpvASVNLPDVLAADFKrqtgskeGSVGMPLPGVAVRIVDPETfEELPPGEDGLILIGGPQVMKGYLGDPEKT 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 638 AEkfIICRLPYMaaeeRLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS--- 714
Cdd:PRK08633 1009 AE--VIKDIDGI----GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVPDekk 1082
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 715 GKILAAFVQPasPELTIDALRHALVTL-LHPAAIPSVFIFLPALPLTINGKI 765
Cdd:PRK08633 1083 GEKLVVLHTC--GAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
435-772 |
4.45e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 74.41 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMIGREG-LSNVAQNHRDFIGLAQGsrvlaiaslgfDAF------GW------DVYGALVSGAT----- 496
Cdd:PRK00174 252 YTSGSTGKPKGVLHTTGGyLVYAAMTMKYVFDYKDG-----------DVYwctadvGWvtghsyIVYGPLANGATtlmfe 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 497 ----------------------LYLAPselhTDVGALH----DYLTQHDIghititpAILELL--------PrEMWPGLR 542
Cdd:PRK00174 321 gvpnypdpgrfwevidkhkvtiFYTAP----TAIRALMkegdEHPKKYDL-------SSLRLLgsvgepinP-EAWEWYY 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 543 TMIVMGDAPPADvvAWWAertrlcngygpTE-ASI-------ATSLceyRPGvpwnCIGKPLKNYRCHILDLHHNPLPVG 614
Cdd:PRK00174 389 KVVGGERCPIVD--TWWQ-----------TEtGGImitplpgATPL---KPG----SATRPLPGIQPAVVDEEGNPLEGG 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 615 FEGELCIAGS--GLAHGYL--HqealsaEKFIicrLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMG 690
Cdd:PRK00174 449 EGGNLVIKDPwpGMMRTIYgdH------ERFV---KTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 691 EVESAVRSHPLVESACVVARSQP-SGKILAAFV-----QPASPELtIDALRHALVTLLHPAAIPSVFIFLPALPLTINGK 764
Cdd:PRK00174 520 EIESALVAHPKVAEAAVVGRPDDiKGQGIYAFVtlkggEEPSDEL-RKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGK 598
|
....*...
gi 1725075560 765 IARQQLEK 772
Cdd:PRK00174 599 IMRRILRK 606
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
691-764 |
5.18e-13 |
|
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: 66.03 E-value: 5.18e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 691 EVESAVRSHPLVESACVVARSQP-SGKILAAFVQP-ASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGK 764
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDElKGEAPVAFVVLkPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
428-722 |
5.59e-13 |
|
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: 73.72 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASL--GFDAFG-WDVYGALVSGATLYLAPS-E 503
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVipFHHGFGmFTTLGYLICGFRVVLMYKfE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 504 LHTDVGALHDYLTQHDIghitITPAILELLPREMWPGLRTM-----IVMGDAPPA-DVVAWWAERTRLC---NGYGPTEA 574
Cdd:cd17642 264 EELFLRSLQDYKVQSAL----LVPTLFAFFAKSTLVDKYDLsnlheIASGGAPLSkEVGEAVAKRFKLPgirQGYGLTET 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 575 SIA---TSLCEYRPGvpwnCIGKPLKNYRCHILDLHHNP-LPVGFEGELCIAGSGLAHGYLHQEalSAEKFIIcrlpyma 650
Cdd:cd17642 340 TSAiliTPEGDDKPG----AVGKVVPFFYAKVVDLDTGKtLGPNERGELCVKGPMIMKGYVNNP--EATKALI------- 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 651 AEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFV 722
Cdd:cd17642 407 DKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEdAGELPAAVV 479
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1344-1719 |
6.13e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 73.78 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1344 ERQQYSYRQLWAQSERVAHALLRID----SRPFsvgVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQA 1419
Cdd:PRK04319 70 RKEKYTYKELKELSNKFANVLKELGvekgDRVF---IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1420 RLLVT------------------------DGEPEQGwaspAVGFDSLVShpAAADALPIPADDT--LAYIMYTSGSTGNP 1473
Cdd:PRK04319 147 KVLITtpallerkpaddlpslkhvllvgeDVEEGPG----TLDFNALME--QASDEFDIEWTDRedGAILHYTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1474 KGVMITHGNLnnFTNDFVGRLALSARDK-----------VlslTSISFDIFGlelfcSLAGGahVTLCPRETAMDPVKLY 1542
Cdd:PRK04319 221 KGVLHVHNAM--LQHYQTGKYVLDLHEDdvywctadpgwV---TGTSYGIFA-----PWLNG--ATNVIDGGRFSPERWY 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1543 HFIERQQpsViqatpTVWSTIvhhlPAAsqrpLTVLCGGEKMPAAL--LTQLRRIATrV------------LQVYG-PTE 1607
Cdd:PRK04319 289 RILEDYK--V-----TVWYTA----PTA----IRMLMGAGDDLVKKydLSSLRHILS-VgeplnpevvrwgMKVFGlPIH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1608 TTIWST-----------CADLtHEGAsdcIGTPIQATEVLVMDQAGNPLPSGAFGELWL--GGAGVSPGYWRNPtlsdkv 1674
Cdd:PRK04319 353 DNWWMTetggimianypAMDI-KPGS---MGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNP------ 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 1675 flrrqafgaERY-------MYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRI 1719
Cdd:PRK04319 423 ---------EKYesyfagdWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERV 465
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1347-1483 |
6.25e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 73.89 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1347 QYSYRQLWAQSERVAHALLRIDSRPF-SVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYP-ADRVSY------MIENAQ 1418
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGdRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfGGRESYiaqlrgMLASAQ 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1419 ARLLVTDGEPEqGWASPAVG---------FDSLVSHPAAADALPIPADDTLAYIMYTSGSTGNPKGVMITHGNL 1483
Cdd:PRK09192 129 PAAIITPDELL-PWVNEATHgnpllhvlsHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1349-1696 |
7.70e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.54 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRI---DSRPfsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPA-----DRVSYMIENAQAR 1420
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLgldPGRP--VMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1421 L-LVTDGEPEQ-------------------GWASPAVGFDSLVSHP------AAADALpipADDTLAYIMYTSGSTGNPK 1474
Cdd:PRK12582 160 VvFAQSGAPFAralaaldlldvtvvhvtgpGEGIASIAFADLAATPptaavaAAIAAI---TPDTVAKYLFTSGSTGMPK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1475 GVMITHGNLnnfTNDFVGRLALSARDKVLSLtSISFD------------IFGLELFcslAGGahvTLcpretAMDPVK-L 1541
Cdd:PRK12582 237 AVINTQRMM---CANIAMQEQLRPREPDPPP-PVSLDwmpwnhtmggnaNFNGLLW---GGG---TL-----YIDDGKpL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1542 YHFIERQQPSVIQATPTVWSTIvhhlPAAsqrpLTVLC----------------------GGEKMPAALLTQLRRIATR- 1598
Cdd:PRK12582 302 PGMFEETIRNLREISPTVYGNV----PAG----YAMLAeamekddalrrsffknlrlmayGGATLSDDLYERMQALAVRt 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1599 ------VLQVYGPTET--TIWSTCADLTHEGAsdcIGTPIQATEVLVmdqagnpLPSGAFGELWLGGAGVSPGYWRNPTL 1670
Cdd:PRK12582 374 tghripFYTGYGATETapTTTGTHWDTERVGL---IGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPEL 443
|
410 420
....*....|....*....|....*.
gi 1725075560 1671 SdkvflrRQAFGAERYmYRTGDIVRF 1696
Cdd:PRK12582 444 T------AAAFDEEGF-YRLGDAARF 462
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
428-772 |
9.32e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 72.00 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGlAQGSRVLA-----IASL---------GFDAFGWDV-----Y 488
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLAlpahhIAGLqvlvrsviaGSEPVELDVsagfdP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 489 GALVsGATLYLAPSELHTDVGAlhdylTQHD--IGHITITPAILELlpremwpglrTMIVMGDAP-PADVVAWWAE-RTR 564
Cdd:PRK07824 114 TALP-RAVAELGGGRRYTSLVP-----MQLAkaLDDPAATAALAEL----------DAVLVGGGPaPAPVLDAAAAaGIN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 565 LCNGYGPTEASIAtslCEYRpgvpwnciGKPLKNYRCHILDlhhnplpvgfeGELCIAGSGLAHGYLHQEAlsaekfiic 644
Cdd:PRK07824 178 VVRTYGMSETSGG---CVYD--------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 645 rlPYMAAEERLYRTGDIAKWDEqGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP--SGKILAAFV 722
Cdd:PRK07824 227 --PDPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDrlGQRVVAAVV 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1725075560 723 QPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:PRK07824 304 GDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
318-675 |
9.95e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.16 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 318 SYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNktyVLLDPQAPA--------ARNQSILDDVQP 389
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG---VPAAPVSPAyslmshdhAKLKHLFDLVKP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADS----------------PLHSGDAPCIAPSSIDYRSLNIHA--EQLPQSRDAL-----AYVCYTSGTTGKPKGV 446
Cdd:PRK12582 159 RVVFAQSgapfaralaaldlldvTVVHVTGPGEGIASIAFADLAATPptAAVAAAIAAItpdtvAKYLFTSGSTGMPKAV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 447 MigreglsnvaQNHRDFIGLAQGSRVL------AIASLGFDAFGWD--------VYGALVSGATLYL-----APSELHTD 507
Cdd:PRK12582 239 I----------NTQRMMCANIAMQEQLrprepdPPPPVSLDWMPWNhtmggnanFNGLLWGGGTLYIddgkpLPGMFEET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 508 VGALHD----YLTQHDIGHITITPAIL--ELLPREMWPGLRTMIVMGDAPPADV--------VAWWAERTRLCNGYGPTE 573
Cdd:PRK12582 309 IRNLREisptVYGNVPAGYAMLAEAMEkdDALRRSFFKNLRLMAYGGATLSDDLyermqalaVRTTGHRIPFYTGYGATE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 574 ASiATSLCEY----RPGVpwncIGKPLKNYRchiLDLhhnpLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpym 649
Cdd:PRK12582 389 TA-PTTTGTHwdteRVGL----IGLPLPGVE---LKL----APVGDKYEVRVKGPNVTPGYHKDPELTAAAF-------- 448
|
410 420 430
....*....|....*....|....*....|.
gi 1725075560 650 aAEERLYRTGDIAKW-----DEQGnIIFVGR 675
Cdd:PRK12582 449 -DEEGFYRLGDAARFvdpddPEKG-LIFDGR 477
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1407-1710 |
2.32e-12 |
|
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: 71.86 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1407 ADRVSYMIENAQARLLVTDGepeqGWasPAVGFDSLVSHPAAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITHGNLNN 1485
Cdd:cd05927 68 PEAIEYILNHAEISIVFCDA----GV--KVYSLEEFEKLGKKNKVPPPPPKpEDLATICYTSGTTGNPKGVMLTHGNIVS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1486 FT---NDFVGRLALSARDKV----LSLTSIsFDIFGLELFCSLagGAHV---------------TLCPRETAMDPvKLYH 1543
Cdd:cd05927 142 NVagvFKILEILNKINPTDVyisyLPLAHI-FERVVEALFLYH--GAKIgfysgdirlllddikALKPTVFPGVP-RVLN 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1544 FIERQQPSVIQATPTVWSTIVH--------HLPAASQRPLT--------------------VLCGGEKMPAALLTQLRRI 1595
Cdd:cd05927 218 RIYDKIFNKVQAKGPLKRKLFNfalnyklaELRSGVVRASPfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1596 -ATRVLQVYGPTETTIWSTcadLTHEGASD--CIGTPIQATEV-LV----M--DQAGNPLPsgafGELWLGGAGVSPGYW 1665
Cdd:cd05927 298 lGCPVLEGYGQTECTAGAT---LTLPGDTSvgHVGGPLPCAEVkLVdvpeMnyDAKDPNPR----GEVCIRGPNVFSGYY 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1725075560 1666 RNPTLSDKVFlrrqafgAERYMYRTGDIVRFNRQGQLEYLGRNDH 1710
Cdd:cd05927 371 KDPEKTAEAL-------DEDGWLHTGDIGEWLPNGTLKIIDRKKN 408
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
332-770 |
2.71e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 71.73 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 332 WLLEHSGAaSSVVAVSMDKSATLLIVLLGI---LKSNKTYVLLDPQAPAARNQSILDDVQPALILADSPLHSgdapciAP 408
Cdd:PRK12583 111 YALGQSGV-RWVICADAFKTSDYHAMLQELlpgLAEGQPGALACERLPELRGVVSLAPAPPPGFLAWHELQA------RG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 409 SSIDYRSLNIHAEQLpqSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLgFDAFG--WD 486
Cdd:PRK12583 184 ETVSREALAERQASL--DRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL-YHCFGmvLA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 487 VYGALVSGATLyLAPSElHTD------------VGALHdyltqhdiGHITITPAILELLPREMW--PGLRTMIVMGDAPP 552
Cdd:PRK12583 261 NLGCMTVGACL-VYPNE-AFDplatlqaveeerCTALY--------GVPTMFIAELDHPQRGNFdlSSLRTGIMAGAPCP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 553 ADVVAWWAERTRLCN---GYGPTEASIATSLCEYRPGVPW--NCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLA 627
Cdd:PRK12583 331 IEVMRRVMDEMHMAEvqiAYGMTETSPVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVM 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 628 HGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACV 707
Cdd:PRK12583 411 KGYWNNPEATAESI---------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQV 481
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 708 VA-RSQPSGKILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK12583 482 FGvPDEKYGEEIVAWVRLHPGHaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
408-770 |
3.51e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.20 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 408 PSSIDyRSLNIHAEQLPQSRDalayvcYTSGTTGKPKGVMIGREG--LSNVAQnhrdFIGLAQGSRVLAIASLG-FDAFG 484
Cdd:PLN03102 173 PSLVA-RMFRIQDEHDPISLN------YTSGTTADPKGVVISHRGayLSTLSA----IIGWEMGTCPVYLWTLPmFHCNG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 485 WD-VYGALVSGATlylAPSELHTDVGALHDYLTQHDIGHITITPAILELLPRemwpGLRT---------MIVMGDAPPAD 554
Cdd:PLN03102 242 WTfTWGTAARGGT---SVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK----GNSLdlsprsgpvHVLTGGSPPPA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 555 VVAWWAERT--RLCNGYGPTEASIATSLCEYRPgvPWNCIG----------KPLKNYRCHILDLHHN------PLPVGFE 616
Cdd:PLN03102 315 ALVKKVQRLgfQVMHAYGLTEATGPVLFCEWQD--EWNRLPenqqmelkarQGVSILGLADVDVKNKetqesvPRDGKTM 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 617 GELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAV 696
Cdd:PLN03102 393 GEIVIKGSSIMKGYLKNPKATSEAF----------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 697 RSHPLVESACVVARSQPS-GKILAAFVQPASPELTIDALRHALVT------------LLHpAAIPSVFIFLPALPLTING 763
Cdd:PLN03102 463 YKYPKVLETAVVAMPHPTwGETPCAFVVLEKGETTKEDRVDKLVTrerdlieycrenLPH-FMCPRKVVFLQELPKNGNG 541
|
....*..
gi 1725075560 764 KIARQQL 770
Cdd:PLN03102 542 KILKPKL 548
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
424-770 |
3.96e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 71.20 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 424 PQSRDALAYVCYTSGTTGKPKG-VMIGREGLSNVAQNHR----DFIGLAQGSRVLAIASLG-FDAFGWDVYG--ALVSGA 495
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGaTLLHRNIVANVLQMEAwlqpAFEKKPRPDQLNFVCALPlYHIFALTVCGllGMRTGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 496 TLYLAPSELhtDVGALHDYLTQHDIghiTITPAILELLPREM---------WPGLRTMIVMGDAPPADVVAWWAERTR-- 564
Cdd:PRK07059 280 RNILIPNPR--DIPGFIKELKKYQV---HIFPAVNTLYNALLnnpdfdkldFSKLIVANGGGMAVQRPVAERWLEMTGcp 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 565 LCNGYGPTEAS-IAT----SLCEYRpgvpwNCIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQ-----E 634
Cdd:PRK07059 355 ITEGYGLSETSpVATcnpvDATEFS-----GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRpdetaK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 635 ALSAEKFiicrlpymaaeerlYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV-ESACVVARSQP 713
Cdd:PRK07059 430 VMTADGF--------------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVlEVAAVGVPDEH 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 714 SGKILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK07059 496 SGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1446-1734 |
4.34e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 71.30 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1446 PAAADaLPIPADdtLAYIMYTSGSTGNPKGVMITHGNLnnftndfVGRLA--------LSARD---KVLSLTSIsfdifg 1514
Cdd:PLN02387 241 PVDPD-LPSPND--IAVIMYTSGSTGLPKGVMMTHGNI-------VATVAgvmtvvpkLGKNDvylAYLPLAHI------ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1515 LELF---------CSLAGGAHVTLCP----------------RETAMDPV-----------------------KLYHFIE 1546
Cdd:PLN02387 305 LELAaesvmaavgAAIGYGSPLTLTDtsnkikkgtkgdasalKPTLMTAVpaildrvrdgvrkkvdakgglakKLFDIAY 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1547 RQQPSVIQAT--------PTVWSTIVHHLPAA--SQRPLTVLCGGEkmPAALLTQlRRI----ATRVLQVYGPTEttiws 1612
Cdd:PLN02387 385 KRRLAAIEGSwfgawgleKLLWDALVFKKIRAvlGGRIRFMLSGGA--PLSGDTQ-RFIniclGAPIGQGYGLTE----- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1613 TCADLTHEGASDC----IGTPIQATEV-LVMDQAGN------PLPSgafGELWLGGAGVSPGYWRNPTLSDKVFLRRqaf 1681
Cdd:PLN02387 457 TCAGATFSEWDDTsvgrVGPPLPCCYVkLVSWEEGGylisdkPMPR---GEIVIGGPSVTLGYFKNQEKTDEVYKVD--- 530
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 1682 gaERYM--YRTGDIVRFNRQGQLEYLGRNDHQVKIR-GHRIELSEIDLSLSS---LDNI 1734
Cdd:PLN02387 531 --ERGMrwFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVspyVDNI 587
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1436-1803 |
5.45e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 70.62 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1436 AVGFDSLVSHPAAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITHGNLnnFTNDFVGRLALSARDK------------- 1501
Cdd:PRK12492 184 AVPFKQALRQGRGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNL--VANMLQVRACLSQLGPdgqplmkegqevm 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1502 VLSLTSISFDIFGLELFCSLAGGAHVTLCpretaMDPVKLYHFIE---RQQPSVIQATPTVWSTIVHHlPAASQRPLTVL 1578
Cdd:PRK12492 262 IAPLPLYHIYAFTANCMCMMVSGNHNVLI-----TNPRDIPGFIKelgKWRFSALLGLNTLFVALMDH-PGFKDLDFSAL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1579 ----CGGEKMPAALLTQLRRI-ATRVLQVYGPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGEL 1653
Cdd:PRK12492 336 kltnSGGTALVKATAERWEQLtGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1654 WLGGAGVSPGYWRNPTLSDkvflrrQAFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEID---LSLSS 1730
Cdd:PRK12492 416 CIKGPQVMKGYWQQPEATA------EALDAEGW-FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEdvvMAHPK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1731 LDNI-------ERSlslivGEGQQARIVSYLQLTSGEELnekavRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK12492 489 VANCaaigvpdERS-----GEAVKLFVVARDPGLSVEEL-----KAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
314-770 |
5.50e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALIL 393
Cdd:PRK13390 22 GEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 ADSPLHSGDAPCIAPSSI------------DYRSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMigreglSNVAQNHR 461
Cdd:PRK13390 102 ASAALDGLAAKVGADLPLrlsfggeidgfgSFEAALAGAGPRLTEQPCGAVMLYSSGTTGFPKGIQ------PDLPGRDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 462 DfiglAQGSRVLAIASLGFDAFGWDVYgalVSGATLY-LAP----SELHT-----------DVGALHDYLTQHDIGHITI 525
Cdd:PRK13390 176 D----APGDPIVAIARAFYDISESDIY---YSSAPIYhAAPlrwcSMVHAlggtvvlakrfDAQATLGHVERYRITVTQM 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 526 TPAIL--------ELLPREMWPGLRTMIVMGDAPPADV----VAWWAerTRLCNGYGPTEAS----IATSLCEYRPGvpw 589
Cdd:PRK13390 249 VPTMFvrllkldaDVRTRYDVSSLRAVIHAAAPCPVDVkhamIDWLG--PIVYEYYSSTEAHgmtfIDSPDWLAHPG--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 590 nCIGKPLKNyRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHqealSAEKFIICRLPymaAEERLYRTGDIAKWDEQGN 669
Cdd:PRK13390 324 -SVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLN----DPEKTAAAQHP---AHPFWTTVGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 670 IIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQ-----PASPELTIDALRHALVTLLH 743
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEmGEQVKAVIQlvegiRGSDELARELIDYTRSRIAH 474
|
490 500
....*....|....*....|....*..
gi 1725075560 744 PAAiPSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK13390 475 YKA-PRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1340-1805 |
1.36e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.46 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1340 AVSCERQQY---SYRQLWAQSERVAhalLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPI-------------- 1401
Cdd:PRK06334 35 ATVCWDEQLgklSYNQVRKAVIALA---TKVSKYPDQhIGIMMPASAGAYIAYFATLLSGKIPVMInwsqglrevtacan 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1402 -----------------------DVHYPADRVsYMiENAQARLLVtdgepeqgWASPAVGFDSLVSHPAAADALPIPADD 1458
Cdd:PRK06334 112 lvgvthvltskqlmqhlaqthgeDAEYPFSLI-YM-EEVRKELSF--------WEKCRIGIYMSIPFEWLMRWFGVSDKD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1459 T--LAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLSLTSiSFDIFGLE---LFCSLAGgAHVTLCprE 1533
Cdd:PRK06334 182 PedVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLP-PFHAYGFNsctLFPLLSG-VPVVFA--Y 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1534 TAMDPVKLYHFIERQQPSVIQATPTVWSTIvhhLPAASQRPLT------VLCGGEKMPAALLTQLRR----IATRvlQVY 1603
Cdd:PRK06334 258 NPLYPKKIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESClpslrfVVIGGDAFKDSLYQEALKtfphIQLR--QGY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1604 GPTETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGN-PLPSGAFGELWLGGAGVSPGYWRN-PTLSdkvFLRrqaF 1681
Cdd:PRK06334 333 GTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEdFGQG---FVE---L 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1682 GAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLS---SLDNIERSLSLIVG--EGQQARIVSYLQL 1756
Cdd:PRK06334 407 GGETW-YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMegfGQNAADHAGPLVVCglPGEKVRLCLFTTF 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 1757 -TSGEELNE--KAVRTAlkarlpNIMIPSGFVVLSAFPLTNNNKIDIRRLPA 1805
Cdd:PRK06334 486 pTSISEVNDilKNSKTS------SILKISYHHQVESIPMLGTGKPDYCSLNA 531
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
428-765 |
1.48e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.99 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIG-REGLSNVAQ-NHRdfIGLAQGSRVLAIASLgFDAFGWDVyGA---LVSGATLYLAPS 502
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLShRNLLANRAQvAAR--IDFSPEDKVFNALPV-FHSFGLTG-GLvlpLLSGVKVFLYPS 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 503 ELHT--------DVGAlhdyltqhdighiTI---TPAILELLPREMWP----GLRtMIVMGDAPPADVV-AWWAER--TR 564
Cdd:PRK06814 869 PLHYriipeliyDTNA-------------TIlfgTDTFLNGYARYAHPydfrSLR-YVFAGAEKVKEETrQTWMEKfgIR 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 565 LCNGYGPTEAS--IATSLCEY-RPGVpwncIGK--PLKNYRchiLDlhhnPLPvGFE--GELCIAGSGLAHGYLHQEAls 637
Cdd:PRK06814 935 ILEGYGVTETApvIALNTPMHnKAGT----VGRllPGIEYR---LE----PVP-GIDegGRLFVRGPNVMLGYLRAEN-- 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 638 aekfiicrlPYM--AAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVES-AVRSHPLVESACVvarSQPS 714
Cdd:PRK06814 1001 ---------PGVlePPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEElAAELWPDALHAAV---SIPD 1068
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 715 GK-----ILAAFVQPASPELTIDALRHALVTLLHpaaIPSVFIFLPALPLTINGKI 765
Cdd:PRK06814 1069 ARkgeriILLTTASDATRAAFLAHAKAAGASELM---VPAEIITIDEIPLLGTGKI 1121
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
653-771 |
1.81e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 68.52 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 653 ERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-SGKILAAFVQpASPELTI 731
Cdd:PRK08308 290 DKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGERVKAKVI-SHEEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1725075560 732 DALRHALVTLLHPAAIPSVFIFLPALPLTINGKIARQQLE 771
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1456-1728 |
1.84e-11 |
|
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: 68.36 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 ADDTLaYIMYTSGSTGNPKGVMITH-----GNLNnfTNDFVGrlaLSARDKVLSLTSISFDIFGLE-LFCSLAGGAHVTL 1529
Cdd:cd05974 84 ADDPM-LLYFTSGTTSKPKLVEHTHrsypvGHLS--TMYWIG---LKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1530 CpRETAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPLTVLCG-GEKMPAALLTQLRRIATRVLQV-YGPTE 1607
Cdd:cd05974 158 F-NYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGaGEPLNPEVIEQVRRAWGLTIRDgYGQTE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1608 TT--IWSTCADLTHEGAsdcIGTPIQATEVLVMDQAGNPLPSGAFGeLWLGG---AGVSPGYWRNPTlsdkvflrRQAFG 1682
Cdd:cd05974 237 TTalVGNSPGQPVKAGS---MGRPLPGYRVALLDPDGAPATEGEVA-LDLGDtrpVGLMKGYAGDPD--------KTAHA 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1725075560 1683 AERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd05974 305 MRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
388-772 |
2.09e-11 |
|
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: 68.85 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 388 QPaLILADSPLHSGDAPCIAPSSIDYRSLNIHAEQLPQSRDALAYVC---------YTSGTTGKPKGVMigreglsnvaQ 458
Cdd:cd05906 119 SP-VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSrpddlallmLTSGSTGFPKAVP----------L 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 459 NHRDFIGLAQGsrvlAIASLGFDA----FGW---DVYGALV---------SGATLYLAPSELHTDVGALHDYLTQHdigH 522
Cdd:cd05906 188 THRNILARSAG----KIQHNGLTPqdvfLNWvplDHVGGLVelhlravylGCQQVHVPTEEILADPLRWLDLIDRY---R 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 523 ITITPA-------ILELLPRE---MW--PGLRTMIVMGDAppadVVAWWAER-TRLCNGYG-PTEASIAT-SLCEYRPGV 587
Cdd:cd05906 261 VTITWApnfafalLNDLLEEIedgTWdlSSLRYLVNAGEA----VVAKTIRRlLRLLEPYGlPPDAIRPAfGMTETCSGV 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 588 PWN---------------CIGKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAE 652
Cdd:cd05906 337 IYSrsfptydhsqalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF---------TE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 653 ERLYRTGDIAkWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVES---ACVVARSQPSGKILAAFVqpASPEL 729
Cdd:cd05906 408 DGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAIF--FVPEY 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1725075560 730 TIDALRHALV-----TLLHPAAI-PSVFIFLP--ALPLTINGKIARQQLEK 772
Cdd:cd05906 485 DLQDALSETLrairsVVSREVGVsPAYLIPLPkeEIPKTSLGKIQRSKLKA 535
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
318-768 |
3.21e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 67.99 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 318 SYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQPALILADSP 397
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 398 LHSGDAPCIAP-----------SSIDYRSLNIH---------AEQLPQS-RDALAYVCYTSGTTGKPKGVMIGReglSNV 456
Cdd:PRK05852 125 GPHDRAEPTTRwwpltvnvggdSGPSGGTLSVHldaateptpATSTPEGlRPDDAMIMFTGGTTGLPKMVPWTH---ANI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 457 AQNHRDFI---GLAQGSRVLAIASLgFDAFGW--DVYGALVSGATLYL---APSELHT---DVGALHD--YLTQHDIGHI 523
Cdd:PRK05852 202 ASSVRAIItgyRLSPRDATVAVMPL-YHGHGLiaALLATLASGGAVLLparGRFSAHTfwdDIKAVGAtwYTAVPTIHQI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 524 TITPAILELLPREMwPGLRtMIVMGDAPPADVVAWWAERT----RLCnGYGPTEAS-------IATSLCEYRPGVPWNCI 592
Cdd:PRK05852 281 LLERAATEPSGRKP-AALR-FIRSCSAPLTAETAQALQTEfaapVVC-AFGMTEAThqvtttqIEGIGQTENPVVSTGLV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 593 GKPlKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaeERLYRTGDIAKWDEQGNIIF 672
Cdd:PRK05852 358 GRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT----------DGWLRTGDLGSLSAAGDLSI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 673 VGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVAR-SQPSGKILAAFVQP-ASPELTIDALRHALVTLLHPAAIPSV 750
Cdd:PRK05852 427 RGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVpDQLYGEAVAAVIVPrESAPPTAEELVQFCRERLAAFEIPAS 506
|
490
....*....|....*...
gi 1725075560 751 FIFLPALPLTINGKIARQ 768
Cdd:PRK05852 507 FQEASGLPHTAKGSLDRR 524
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
874-1288 |
3.84e-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: 67.28 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 874 APLSPQQNllWYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETDG--VAYQLAEPHTPIRLa 951
Cdd:cd19534 2 VPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGgwQQRIRGDVEELFRL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 952 dHWVDGQTLSAEKWVRQLCA---TPFDITARPPLVLRLVQYHQQHHVLIWVKHNIITDAWSEQLILNDLWQRYNELDdhH 1028
Cdd:cd19534 79 -EVVDLSSLAQAAAIEALAAeaqSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQAL--A 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1029 GLDAPQPQ---IQT-----IDIVNSGIASPapaDVAYWQQQL---------------QDCRELDFPLDKPRP---LMPTH 1082
Cdd:cd19534 156 GEPIPLPSktsFQTwaellAEYAQSPALLE---ELAYWRELPaadywglpkdpeqtyGDARTVSFTLDEEETealLQEAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1083 AGerihYQLQP-DVagLLASRGKALGatpfallcaalslllsRYTQQQDIVI-----GtaiaaRDNLDQTQ-----VSGF 1151
Cdd:cd19534 233 AA----YRTEInDL--LLAALALAFQ----------------DWTGRAPPAIfleghG-----REEIDPGLdlsrtVGWF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1152 HVNTvPLRIQLSEQDTLAGLIGNMMEtCIGAYQHQQLSFD--RILHQIEYERMSNKNPlfqiMAILQN-AGDVcQQNLRD 1228
Cdd:cd19534 286 TSMY-PVVLDLEASEDLGDTLKRVKE-QLRRIPNKGIGYGilRYLTPEGTKRLAFHPQ----PEISFNyLGQF-DQGERD 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1229 CTLHRLPLSSG----------FSMFDMtwNFSVEQDAVTIELDYASELFYPASMQMLLDNYQQTLRQLLT 1288
Cdd:cd19534 359 DALFVSAVGGGgsdigpdtprFALLDI--NAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
603-773 |
4.42e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 67.71 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 603 ILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKI 682
Cdd:PRK10946 367 VADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF---------DANGFYCSGDLVSIDPDGYITVVGREKDQINR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 683 RGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPELTIDALRHALVTLLHPAAIPSVFIFLPALPLTI 761
Cdd:PRK10946 438 GGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEKSCAFLVVKEPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTA 517
|
170
....*....|..
gi 1725075560 762 NGKIARQQLEKW 773
Cdd:PRK10946 518 VGKVDKKQLRQW 529
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
567-730 |
8.16e-11 |
|
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: 66.85 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 567 NGYGPTE---ASIATSLCEYRPGvpwnCIGKPLKNYRCHILD------LHHNPLPvgfEGELCIAGSGLAHGYLHQEALS 637
Cdd:cd17639 279 QGYGLTEtcaGGTVQDPGDLETG----RVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKT 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 638 AEKFiicrlpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIR-GVRIEMGEVESAVRSHPLVESACVVARSQPSgK 716
Cdd:cd17639 352 KEAF---------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKS-Y 421
|
170
....*....|....
gi 1725075560 717 ILaAFVQPASPELT 730
Cdd:cd17639 422 PV-AIVVPNEKHLT 434
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
875-1212 |
1.09e-10 |
|
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: 65.67 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSP--QQNLLWYLSALNPddCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTRFTETD-GVAYQLAEPHTPIRLA 951
Cdd:cd19537 3 ALSPieREWWHKYQLSTGT--SSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDgGLRRSYSSSPPRVQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 952 DHwVDgqtlsaekwVRQLCATPFDItARPPLVLRLVqyhQQHHVLIWVKHnIITDAWSEQLILNDLWQRYnelddhHGLD 1031
Cdd:cd19537 81 DT-LD---------VWKEINRPFDL-EREDPIRVFI---SPDTLLVVMSH-IICDLTTLQLLLREVSAAY------NGKL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1032 APQPQIQTIDIvnSGIASPAPADV-AYWQQQLQDCRELDFPldkPRPLMPTHAGERIHYQLQPDVAGLLASRGKALGATP 1110
Cdd:cd19537 140 LPPVRREYLDS--TAWSRPASPEDlDFWSEYLSGLPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1111 fallcaalslllsrytQQ----------------QDIVIGTAIAARDNLDQTQVSGFHVNTVPLRIQLSEQ--DTLAGLI 1172
Cdd:cd19537 215 ----------------HQlalaavalalqdlsdrTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSSsdASAADFL 278
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1725075560 1173 GNMMETCIGAYQHqQLSFDRILHQIEYERMSNKNPLFQIM 1212
Cdd:cd19537 279 RAVRRSSQAALAH-AIPWHQLLEHLGLPPDSPNHPLFDVM 317
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
314-774 |
1.23e-10 |
|
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: 65.92 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLL-EHSGAASSVVAVSMDKSATLLIVLLGILKSNKtyvlldpqAPAARNQSILDDvqpALI 392
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGA--------APAFINYNLSGD---PLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 393 ladsplHsgdapCIAPSSidyrslnihAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRV 472
Cdd:cd05937 72 ------H-----CLKLSG---------SRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 473 L--------AIASLGFDAfgwdvygALVSGATLYLAP--------SELHTD-------VGALHDYLTqhdigHITITPAI 529
Cdd:cd05937 132 YtcmplyhgTAAFLGACN-------CLMSGGTLALSRkfsasqfwKDVRDSgatiiqyVGELCRYLL-----STPPSPYD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 530 LELLPREMW-PGLRTMIvmgdappadvvaWWAERTR-----LCNGYGPTEAsIATSLCEYRPGVPWNCIGK--PLKNYRC 601
Cdd:cd05937 200 RDHKVRVAWgNGLRPDI------------WERFRERfnvpeIGEFYAATEG-VFALTNHNVGDFGAGAIGHhgLIRRWKF 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 602 H----ILDLHHNP--------------LPVGFEGELCIA----GSGLAHGYLHQEALSAEKFI--ICRlpymaAEERLYR 657
Cdd:cd05937 267 EnqvvLVKMDPETddpirdpktgfcvrAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVrdVFR-----KGDIYFR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 658 TGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS--GKILAAFVQPASPELTIDALR 735
Cdd:cd05937 342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGhdGRAGCAAITLEESSAVPTEFT 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1725075560 736 HALVTLLHPAAIPS----VFI-FLPALPLTINGKIARQQL--EKWP 774
Cdd:cd05937 422 KSLLASLARKNLPSyavpLFLrLTEEVATTDNHKQQKGVLrdEGVD 467
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
384-773 |
1.64e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 65.74 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 384 LDDVQPALILADSPLHSGDAPciaPSSIDYRSLNIH-----AEQLPQSR-DALAyVCYTSGTTGKPKGVMIGREG----- 452
Cdd:PRK08162 136 LPGPKPLVIDVDDPEYPGGRF---IGALDYEAFLASgdpdfAWTLPADEwDAIA-LNYTSGTTGNPKGVVYHHRGaylna 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 453 LSNVAQnhrdfIGLAQGSRVLAIASL----GFdAFGWDVygALVSGATLYLApselHTDVGALHDYLTQHDIGHITITPA 528
Cdd:PRK08162 212 LSNILA-----WGMPKHPVYLWTLPMfhcnGW-CFPWTV--AARAGTNVCLR----KVDPKLIFDLIREHGVTHYCGAPI 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 529 ILELL---PREMWPGLR---TMIVMGDAPPADVVAWWAER-TRLCNGYGPTEASIATSLCEYRPGvpWNCIG-------K 594
Cdd:PRK08162 280 VLSALinaPAEWRAGIDhpvHAMVAGAAPPAAVIAKMEEIgFDLTHVYGLTETYGPATVCAWQPE--WDALPlderaqlK 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 595 PLKNYRCHILD----LHHN---PLPVGFE--GELCIAGSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWD 665
Cdd:PRK08162 358 ARQGVRYPLQEgvtvLDPDtmqPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF----------AGGWFHTGDLAVLH 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 666 EQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQ-----PASPELTIDALRhalv 739
Cdd:PRK08162 428 PDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKwGEVPCAFVElkdgaSATEEEIIAHCR---- 503
|
410 420 430
....*....|....*....|....*....|....
gi 1725075560 740 TLLHPAAIPSVFIFLPaLPLTINGKIARQQLEKW 773
Cdd:PRK08162 504 EHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQ 536
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1455-1803 |
1.94e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 64.68 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1455 PADDTLAYIMYTSGSTGNPKGVMITHGNLN---NFTNDFVG-----RLALSARD----KVLsLTSIsfdIFGLE-LFCSL 1521
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTasaDATHDRLGgpgqwLLALPAHHiaglQVL-VRSV---IAGSEpVELDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1522 AGGAHVTLCPRETA-MDPVKLYhfierqqpsvIQATPTVWSTIVHHLPA-ASQRPL-TVLCGGEKMPAALLTQLRRIATR 1598
Cdd:PRK07824 108 SAGFDPTALPRAVAeLGGGRRY----------TSLVPMQLAKALDDPAAtAALAELdAVLVGGGPAPAPVLDAAAAAGIN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1599 VLQVYGPTETtiwstcadlthegASDCI--GTPIQATEVLVMDqagnplpsgafGELWLGGAGVSPGYwRNPTLSDkvfl 1676
Cdd:PRK07824 178 VVRTYGMSET-------------SGGCVydGVPLDGVRVRVED-----------GRIALGGPTLAKGY-RNPVDPD---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1677 rrqAFgAERYMYRTGDIVRFNrQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIVGE---GQqaRIVSY 1753
Cdd:PRK07824 229 ---PF-AEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDdrlGQ--RVVAA 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1754 LQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:PRK07824 302 VVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1447-1707 |
3.00e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 65.38 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1447 AAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITHGNLnnftndFVGRLALSARdkvlsLTsisfDIFG----LELFCS- 1520
Cdd:PTZ00216 252 GSHHPLNIPENnDDLALIMYTSGTTGDPKGVMHTHGSL------TAGILALEDR-----LN----DLIGppeeDETYCSy 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1521 ---------------LAGGAHVTLC-PReTAMDPVKLYH--FIERqQPSVIQATPTVWSTI---VH-HLPA--------- 1569
Cdd:PTZ00216 317 lplahimefgvtnifLARGALIGFGsPR-TLTDTFARPHgdLTEF-RPVFLIGVPRIFDTIkkaVEaKLPPvgslkrrvf 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1570 --ASQRPL-----------------------------TVLCGGEKMPAAllTQ--LRRIATRVLQVYGPTETTIWST--- 1613
Cdd:PTZ00216 395 dhAYQSRLralkegkdtpywnekvfsapravlggrvrAMLSGGGPLSAA--TQefVNVVFGMVIQGWGLTETVCCGGiqr 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1614 CADLThegaSDCIGTPIQATEVLVMDQAG-----NPLPSgafGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYmY 1688
Cdd:PTZ00216 473 TGDLE----PNAVGQLLKGVEMKLLDTEEykhtdTPEPR---GEILLRGPFLFKGYYKQEELT------REVLDEDGW-F 538
|
330
....*....|....*....
gi 1725075560 1689 RTGDIVRFNRQGQLEYLGR 1707
Cdd:PTZ00216 539 HTGDVGSIAANGTLRIIGR 557
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1327-1729 |
3.31e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 64.82 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1327 HIG----RLAHTQPDS-LAVSCERQQySYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVP 1400
Cdd:PLN02860 8 HICqcltRLATLRGNAvVTISGNRRR-TGHEFVDGVLSLAAGLLRLGLRNGDvVAIAALNSDLYLEWLLAVACAGGIVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1401 IDVHYPADRVSYMIENAQARLLVTDgEPEQGWASPA-------------VGFDSLVSHPAAADALPIP------------ 1455
Cdd:PLN02860 87 LNYRWSFEEAKSAMLLVRPVMLVTD-ETCSSWYEELqndrlpslmwqvfLESPSSSVFIFLNSFLTTEmlkqralgttel 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 ----ADDTLAYIMYTSGSTGNPKGVMITHgnlNNFTNDFVGRLALSA--RDKVLSLTSISFDIFGLE--LFCSLAGGAHV 1527
Cdd:PLN02860 166 dyawAPDDAVLICFTSGTTGRPKGVTISH---SALIVQSLAKIAIVGygEDDVYLHTAPLCHIGGLSsaLAMLMVGACHV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1528 TLcPR---ETAMDPVKLYHFIerqqpSVIqATPTVWSTIVHhlPAAS-------QRPLTVLCGGEKMPAALLTQLRRI-- 1595
Cdd:PLN02860 243 LL-PKfdaKAALQAIKQHNVT-----SMI-TVPAMMADLIS--LTRKsmtwkvfPSVRKILNGGGSLSSRLLPDAKKLfp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1596 ATRVLQVYGPTET----------------------TIWSTCADLTHEGASDCIGTPIQATEVLV-MDQagnplpSGAFGE 1652
Cdd:PLN02860 314 NAKLFSAYGMTEAcssltfmtlhdptlespkqtlqTVNQTKSSSVHQPQGVCVGKPAPHVELKIgLDE------SSRVGR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1653 LWLGGAGVSPGYWRNPTLSDKVflrRQAFGaeryMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLS 1729
Cdd:PLN02860 388 ILTRGPHVMLGYWGQNSETASV---LSNDG----WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLS 457
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1349-1664 |
3.85e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.63 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRIDSRPFS-VGVMMEKSCHVAVLLLGVLRAGKHYVPidVHYPADR------------VSYMIE 1415
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDaVAVLAGAPVEIAPTAQGLWMRGASLTM--LHQPTPRtdlavwaedtlrVIGMIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1416 naqARLLVTdGEPEQGwASP-----AVGFDSLVSHPAAADALPIPA-DDTLAYIMYTSGSTGNPKGVMITHGNLnnFTND 1489
Cdd:PRK07768 109 ---AKAVVV-GEPFLA-AAPvleekGIRVLTVADLLAADPIDPVETgEDDLALMQLTSGSTGSPKAVQITHGNL--YANA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1490 FVGRLALSAR---DKVLSLTSISFDIfGLELFCSL---AGGAHVTLCPRETAMDPVKLYHFIERQQPSVIQATPTVWSTI 1563
Cdd:PRK07768 182 EAMFVAAEFDvetDVMVSWLPLFHDM-GMVGFLTVpmyFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1564 VHHLPAASQRP---LT----VLCGGEKM-PAA---LLTQLRRIATR---VLQVYGPTETTIWST-------------CAD 1616
Cdd:PRK07768 261 ARRLRRQAKPGafdLSslrfALNGAEPIdPADvedLLDAGARFGLRpeaILPAYGMAEATLAVSfspcgaglvvdevDAD 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1617 L---------THEGASD---CIGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGY 1664
Cdd:PRK07768 341 LlaalrravpATKGNTRrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY 400
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
552-763 |
5.20e-10 |
|
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: 63.09 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 552 PADVVAWwaerTRLCNGYGPTEASIATSLCEY---------RPGvPWncigkplknYRCHILDLHHNPLPVGFEGELCIA 622
Cdd:cd17636 130 TVDTSPW----GRKPGGYGQTEVMGLATFAALgggaiggagRPS-PL---------VQVRILDEDGREVPDGEVGEIVAR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 623 GSGLAHGYLHQEALSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV 702
Cdd:cd17636 196 GPTVMAGYWNRPEVNARRT----------RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAV 265
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 703 ESACVVARSQPS-GKILAAFVQP-----ASPELTIDALRHALVTLLHPAAIpsvfIFLPALPLTING 763
Cdd:cd17636 266 ADAAVIGVPDPRwAQSVKAIVVLkpgasVTEAELIEHCRARIASYKKPKSV----EFADALPRTAGG 328
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
314-764 |
5.55e-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: 63.91 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 314 GQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQApaaRNQSILDDVQPAlil 393
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNL---RGESLAHCLNVS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 394 adSPLHsgdapCIApssidyrslnihaeqlpqsrDALAYVcYTSGTTGKPKGVMIgreglsnvaQNHR--------DFIG 465
Cdd:cd05940 75 --SAKH-----LVV--------------------DAALYI-YTSGTTGLPKAAII---------SHRRawrggaffAGSG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 466 LAQGSRVLAI------ASLGFDAFGwdvyGALVSGATLYLA----PSELHTDVGAlhdyltqhdiGHITITPAILELL-- 533
Cdd:cd05940 118 GALPSDVLYTclplyhSTALIVGWS----ACLASGATLVIRkkfsASNFWDDIRK----------YQATIFQYIGELCry 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 534 -----PREMWPGLRTMIVMGDAPPADVvawWAERT------RLCNGYGPTEASIATSLCEYRPGVpwncIGK----PLKN 598
Cdd:cd05940 184 llnqpPKPTERKHKVRMIFGNGLRPDI---WEEFKerfgvpRIAEFYAATEGNSGFINFFGKPGA----IGRnpslLRKV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 599 YRCHILDLHHN-------------PLPVGFEGELCIAGSGLAH--GYLHQEAlsAEKFIICRLpyMAAEERLYRTGDIAK 663
Cdd:cd05940 257 APLALVKYDLEsgepirdaegrciKVPRGEPGLLISRINPLEPfdGYTDPAA--TEKKILRDV--FKKGDAWFNTGDLMR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 664 WDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS--GKI-LAAFVQPASPELTIDALRHALVT 740
Cdd:cd05940 333 LDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGtdGRAgMAAIVLQPNEEFDLSALAAHLEK 412
|
490 500
....*....|....*....|....*
gi 1725075560 741 LLHPAAIPsVFI-FLPALPLTINGK 764
Cdd:cd05940 413 NLPGYARP-LFLrLQPEMEITGTFK 436
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1332-1667 |
6.67e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 63.74 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1332 AHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLRIDSRPFSvGVMMEKSCHVAVLL--LGVLRAGKHYVPIDVHYPADR 1409
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGS-GVALRGKNSPETLLayLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1410 VSYMIENAQARLLVTDgepeqgwaSPAVGFDSLVSHPAAADALPIPAD---DTLAYIMYTSGSTGNPKGVMITHGNlnnf 1486
Cdd:PRK09029 92 LEELLPSLTLDFALVL--------EGENTFSALTSLHLQLVEGAHAVAwqpQRLATMTLTSGSTGLPKAAVHTAQA---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1487 tndfvgRLAlSARDkVLSLtsISFD-----IFGLELF-CS--------LAGGAHVTLcpreTAMDPvkLYHfierqqpSV 1552
Cdd:PRK09029 160 ------HLA-SAEG-VLSL--MPFTaqdswLLSLPLFhVSgqgivwrwLYAGATLVV----RDKQP--LEQ-------AL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1553 IQAT-----PT-VWstivhHLPAASQRPLT---VLCGGEKMPAALLTQLRRIATRVLQVYGPTETTiwST-CADLThEGA 1622
Cdd:PRK09029 217 AGCThaslvPTqLW-----RLLDNRSEPLSlkaVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMA--STvCAKRA-DGL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1725075560 1623 SDcigtpiqatevlvmdqAGNPLPSGAF----GELWLGGAGVSPGYWRN 1667
Cdd:PRK09029 289 AG----------------VGSPLPGREVklvdGEIWLRGASLALGYWRQ 321
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1316-1500 |
7.25e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 64.13 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1316 ADAGSRDSLLMHIGRLAHTQPDSLAVSCERQQYSYRQLWAQSERVAHALLridSRPFS----VGVMMEKSCHVAVLLLGV 1391
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAA---ARGVGkgdvVALLMENRPEYLAAWLGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1392 LRAGKHYVPIDVHYPADRVSYMIENAQARLLVTDGE---------------PEQGWASPAV-----GFDSLVSHPAAADA 1451
Cdd:PRK08279 108 AKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEElveafeearadlarpPRLWVAGGDTlddpeGYEDLAAAAAGAPT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 1452 LP------IPADDTLAYImYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARD 1500
Cdd:PRK08279 188 TNpasrsgVTAKDTAFYI-YTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDD 241
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1348-1668 |
1.04e-09 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 63.46 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1348 YSYRQLWAQSERVAHALLRIDSRPFSVgVM--MEKSCHVAVLLLGVLRAGK-------HYVPIDVHYPA----------- 1407
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDV-VMllLPNCPEFVLAFLGASRRGAvtttanpFYTPAEIAKQAkasgakliitq 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1408 ----DRVSYMIENAQARLLVTDGEPEQgwaspAVGFDSLV-SHPAAADALPIPADDTLAyIMYTSGSTGNPKGVMITHGN 1482
Cdd:PLN02246 130 scyvDKLKGLAEDDGVTVVTIDDPPEG-----CLHFSELTqADENELPEVEISPDDVVA-LPYSSGTTGLPKGVMLTHKG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1483 LNNFTNDFVG----RLALSARDKVLSLTSIsFDIFGLE--LFCSLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQAT 1556
Cdd:PLN02246 204 LVTSVAQQVDgenpNLYFHSDDVILCVLPM-FHIYSLNsvLLCGLRVGAAILIMPK---FEIGALLELIQRHKVTIAPFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1557 PTVW-----STIVHHLPAASQRplTVLCGGEKMPAALLTQLR-RIATRVL-QVYGPTET-TIWSTCADLTHE------GA 1622
Cdd:PLN02246 280 PPIVlaiakSPVVEKYDLSSIR--MVLSGAAPLGKELEDAFRaKLPNAVLgQGYGMTEAgPVLAMCLAFAKEpfpvksGS 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1725075560 1623 sdCiGTPIQATEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNP 1668
Cdd:PLN02246 358 --C-GTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDP 401
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
312-770 |
1.27e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 62.79 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 312 ADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP-A 390
Cdd:PRK13391 20 STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGArA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 391 LI-----LADSPLHSGDAPCIAP--------SSIDYRSLNIHAEQLPQSR--------DALayvcYTSGTTGKPKGVMig 449
Cdd:PRK13391 100 LItsaakLDVARALLKQCPGVRHrlvldgdgELEGFVGYAEAVAGLPATPiadeslgtDML----YSSGTTGRPKGIK-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 450 REglsnvaqnhrdfIGLAQGSRVLAIASLGFDAFGWDVYGALVSGATLY----LAPSELHTDVGALH---------DYLT 516
Cdd:PRK13391 174 RP------------LPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYhsapQRAVMLVIRLGGTVivmehfdaeQYLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 517 ---QHDIGHITITPA----ILELlPREM-----WPGLRTMIvMGDAP-PADV----VAWWaertrlcnG------YGPTE 573
Cdd:PRK13391 242 lieEYGVTHTQLVPTmfsrMLKL-PEEVrdkydLSSLEVAI-HAAAPcPPQVkeqmIDWW--------GpiiheyYAATE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 574 ASIATSLCEY----RPGVpwncIGKPLKNyRCHILDLHHNPLPVGFEGELCIAGsGLAHGYLHQEALSAEKfiicrlpyM 649
Cdd:PRK13391 312 GLGFTACDSEewlaHPGT----VGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEA--------R 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 650 AAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASPE 728
Cdd:PRK13391 378 HPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEEVKAVVQPVDGV 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1725075560 729 LTIDALRHALVTLL--HPAAI--PSVFIFLPALPLTINGKIARQQL 770
Cdd:PRK13391 458 DPGPALAAELIAFCrqRLSRQkcPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
424-707 |
1.59e-09 |
|
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: 62.62 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 424 PQSRDALAYVCYTSGTTGKPKGVMIgreglsnvaqNHRDFIglAQGSRVLAIASLGFDAFGWDVY--------------- 488
Cdd:cd05927 110 PPKPEDLATICYTSGTTGNPKGVML----------THGNIV--SNVAGVFKILEILNKINPTDVYisylplahifervve 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 489 -GALVSGATL-YLA--PSELHTDVGAL---------------HDYLTQHDI-----------------------GHITIT 526
Cdd:cd05927 178 aLFLYHGAKIgFYSgdIRLLLDDIKALkptvfpgvprvlnriYDKIFNKVQakgplkrklfnfalnyklaelrsGVVRAS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 527 P----AILELLPREMWPGLRTMIVmGDAP-PADVVawwaERTR------LCNGYGPTEASIATSLC---EYRPGvpwnCI 592
Cdd:cd05927 258 PfwdkLVFNKIKQALGGNVRLMLT-GSAPlSPEVL----EFLRvalgcpVLEGYGQTECTAGATLTlpgDTSVG----HV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 593 GKPLKNYRCHILDL--------HHNPlpvgfEGELCIAGSGLAHGYLHQEALSAEKFiicrlpymaAEERLYRTGDIAKW 664
Cdd:cd05927 329 GGPLPCAEVKLVDVpemnydakDPNP-----RGEVCIRGPNVFSGYYKDPEKTAEAL---------DEDGWLHTGDIGEW 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1725075560 665 DEQGNIIFVGRRDHQVKI-RGVRIEMGEVESAVRSHPLVESACV 707
Cdd:cd05927 395 LPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1635-1898 |
1.77e-09 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 61.30 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1635 VLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPtlsDKVFLRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKI 1714
Cdd:COG3433 32 LIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAA---RAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1715 R---GHRIELSEIDLSLSSLDNIERSLSLIVGEGQQARIVSYLQLTSGEElnekAVRTALKARLPNIMIPSGFVVLSAFP 1791
Cdd:COG3433 109 RaerGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAA----AAALAALDKVPPDVVAASAVVALDAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1792 LTNNNKIDIRRLPAPETRYSASEADY---TPAANEAESAMQHIWQQVLSQT--QISVCDSFFSLGGNSLQIPQLLHAIRQ 1866
Cdd:COG3433 185 LLLALKVVARAAPALAAAEALLAAASpapALETALTEEELRADVAELLGVDpeEIDPDDNLFDLGLDSIRLMQLVERWRK 264
|
250 260 270
....*....|....*....|....*....|..
gi 1725075560 1867 QmGVSLTIREFIMHSQIRELTALALSKTAEVA 1898
Cdd:COG3433 265 A-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
435-777 |
1.85e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 62.35 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGV-----MIGREGLSNVAQ--NHRDFIG-----LAQGSRVLAiaslgfdafGWDVygALVSGATLYLAP- 501
Cdd:PRK13388 157 FTSGTTGAPKAVrcshgRLAFAGRALTERfgLTRDDVCyvsmpLFHSNAVMA---------GWAP--AVASGAAVALPAk 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 502 ---SELHTDV---GAlhDYLTQ--HDIGHITITPAilelLPREMWPGLRtmIVMG-DAPPADVvAWWAER--TRLCNGYG 570
Cdd:PRK13388 226 fsaSGFLDDVrryGA--TYFNYvgKPLAYILATPE----RPDDADNPLR--VAFGnEASPRDI-AEFSRRfgCQVEDGYG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 571 PTEASIATSLceyRPGVPWNCIGKPLKNYRchILDLH------------HNPLPVGFE--GELC-IAGSGLAHGYLHQEA 635
Cdd:PRK13388 297 SSEGAVIVVR---EPGTPPGSIGRGAPGVA--IYNPEtltecavarfdaHGALLNADEaiGELVnTAGAGFFEGYYNNPE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 636 LSAEKFiicrlpymaaEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQP-S 714
Cdd:PRK13388 372 ATAERM----------RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErV 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 715 G-KILAAFVQPASPELTIDALRHALVTL--LHPAAIPSVFIFLPALPLTINGKIARQQL--EKWPLDE 777
Cdd:PRK13388 442 GdQVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELiaQGWATGD 509
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1439-1730 |
2.52e-09 |
|
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: 62.33 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1439 FDSLVSHPAAADALPIPADDTLaYIMYTSGSTGNPKGVMITHG--------NLNNFTNDFVGRLALSARDkVLSLTSISF 1510
Cdd:cd05967 212 WSELLAKAEPVDCVPVAATDPL-YILYTSGTTGKPKGVVRDNGghavalnwSMRNIYGIKPGDVWWAASD-VGWVVGHSY 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1511 DIFG-LelfcsLAGGAHVTLCPRETAM-DPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAAS---QRPLTVL----CGG 1581
Cdd:cd05967 290 IVYGpL-----LHGATTVLYEGKPVGTpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKyikKYDLSSLrtlfLAG 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1582 EKMPAALLTQLRRIATR-VLQVYGPTETTiWSTCADL----THEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLG 1656
Cdd:cd05967 365 ERLDPPTLEWAENTLGVpVIDHWWQTETG-WPITANPvglePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1657 G---AGVSPGYWRNPTLsdkvfLRRQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSS 1730
Cdd:cd05967 444 LplpPGCLLTLWKNDER-----FKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLS 515
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1452-1799 |
2.57e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 62.42 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1452 LPIPADDTlAYIMYTSGSTGNPKGVMITHGNLnnFTN--------DFvgrlalSARDKVLSLTSIsFDIFGLE--LFCSL 1521
Cdd:PRK08043 360 VKQQPEDA-ALILFTSGSEGHPKGVVHSHKSL--LANveqiktiaDF------TPNDRFMSALPL-FHSFGLTvgLFTPL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1522 AGGAHVTL--CPRETAMDPVKLYHfierQQPSVIQATptvwSTIVHHL-----PAASQRPLTVLCGGEKmpaaLLTQLRR 1594
Cdd:PRK08043 430 LTGAEVFLypSPLHYRIVPELVYD----RNCTVLFGT----STFLGNYarfanPYDFARLRYVVAGAEK----LQESTKQ 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1595 I-----ATRVLQVYGPTEttiwstCADLThegasdCIGTPIQATEVLV------MDQAGNPLP---SGafGELWLGGAGV 1660
Cdd:PRK08043 498 LwqdkfGLRILEGYGVTE------CAPVV------SINVPMAAKPGTVgrilpgMDARLLSVPgieQG--GRLQLKGPNI 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1661 SPGYWR--NPtlsdKVFLRRQAFGAERYM----YRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIelseidlslsSLDNI 1734
Cdd:PRK08043 564 MNGYLRveKP----GVLEVPTAENARGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMV----------SLEMV 629
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1735 ERSLSLIVGEGQQARIV--------SYLQLTSGEELN-EKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKID 1799
Cdd:PRK08043 630 EQLALGVSPDKQHATAIksdaskgeALVLFTTDSELTrEKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1456-1801 |
2.57e-09 |
|
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: 61.24 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1456 ADDTlaYIMYTSGSTGNPKGVMITHGNL-------------NNFTNDFVGRLALSARDkvLSLTSISFDIFGLEL---FC 1519
Cdd:cd05924 3 ADDL--YILYTGGTTGMPKGVMWRQEDIfrmlmggadfgtgEFTPSEDAHKAAAAAAG--TVMFPAPPLMHGTGSwtaFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1520 SLAGGAhvTLCPRETAMDPVKLYHFIERQQPSVIQ------ATPtvwstIVHHLPAASQRPLTVL----CGG----EKMP 1585
Cdd:cd05924 79 GLLGGQ--TVVLPDDRFDPEEVWRTIEKHKVTSMTivgdamARP-----LIDALRDAGPYDLSSLfaisSGGallsPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1586 AALLTQLRRIAtrVLQVYGPTETTIWSTcadlTHEGASDCIGTPIQ--ATEVLVMDQAGNPLPSGAFGELWLGGAGVSP- 1662
Cdd:cd05924 152 QGLLELVPNIT--LVDAFGSSETGFTGS----GHSAGSGPETGPFTraNPDTVVLDDDGRVVPPGSGGVGWIARRGHIPl 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1663 GYWRNPTLSDKVFLRrqaFGAERYMYrTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIV 1742
Cdd:cd05924 226 GYYGDEAKTAETFPE---VDGVRYAV-PGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYD--VLVV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 1743 GE-----GQqaRIVSYLQLTSGEELNEKAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKIDIR 1801
Cdd:cd05924 300 GRpderwGQ--EVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
435-777 |
2.84e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 61.75 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMigregLS--NVAQNHRdFIGLAQG----SRVLAIASLgFDAFG--WDVYGALVSGATLyLAPSE--- 503
Cdd:PRK08315 206 YTSGTTGFPKGAT-----LThrNILNNGY-FIGEAMKlteeDRLCIPVPL-YHCFGmvLGNLACVTHGATM-VYPGEgfd 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 504 -LHT-------DVGALHdyltqhdiGHITITPAILELLPREMW--PGLRTMIVMGDAPPADVVAWWAER---TRLCNGYG 570
Cdd:PRK08315 278 pLATlaaveeeRCTALY--------GVPTMFIAELDHPDFARFdlSSLRTGIMAGSPCPIEVMKRVIDKmhmSEVTIAYG 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 571 PTEAS-------IATSLcEYRpgVpwNCIGKPLKNYRCHILDLH-HNPLPVGFEGELCIAGSGLAHGYLHQEALSAEkfI 642
Cdd:PRK08315 350 MTETSpvstqtrTDDPL-EKR--V--TTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--A 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 643 IcrlpymaAEERLYRTGDIAKWDEQGNIIFVGRrdhqVK---IRGvriemG------EVESAVRSHPLVESACVVArsQP 713
Cdd:PRK08315 423 I-------DADGWMHTGDLAVMDEEGYVNIVGR----IKdmiIRG-----GeniyprEIEEFLYTHPKIQDVQVVG--VP 484
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 714 S---GKILAAFVQPASPE-LTIDALRHALVTLLHPAAIPSVFIFLPALPLTINGKIA----RQQ-LEKWPLDE 777
Cdd:PRK08315 485 DekyGEEVCAWIILRPGAtLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQkfkmREMmIEELGLQA 557
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1346-1735 |
7.34e-09 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 60.76 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLRIDSRPFSVG-VMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVT 1424
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVvVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1425 DG---EPEQGWASP-----------AVGFDSLVShpaAADAlpipADDTLAY----------IMYTSGSTGNPKGVMITH 1480
Cdd:PLN02330 134 NDtnyGKVKGLGLPvivlgeekiegAVNWKELLE---AADR----AGDTSDNeeilqtdlcaLPFSSGTTGISKGVMLTH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1481 GNL--NNFTNDFVGRLALSARDKVLSLTSIsFDIFGLELFC--SLAGGAHVTLCPRetaMDPVKLYHFIERQQPSVIQAT 1556
Cdd:PLN02330 207 RNLvaNLCSSLFSVGPEMIGQVVTLGLIPF-FHIYGITGICcaTLRNKGKVVVMSR---FELRTFLNALITQEVSFAPIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1557 PTVWSTIVHHlPAASQRPLTVLCGGEKMPAA------LLTQLRRI--ATRVLQVYGPTEttiwSTCADLTHEGAS----- 1623
Cdd:PLN02330 283 PPIILNLVKN-PIVEEFDLSKLKLQAIMTAAaplapeLLTAFEAKfpGVQVQEAYGLTE----HSCITLTHGDPEkghgi 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1624 ---DCIGTPIQATEVLVMD-QAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKvflrrqAFGAERYMYrTGDIVRFNRQ 1699
Cdd:PLN02330 358 akkNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDR------TIDEDGWLH-TGDIGYIDDD 430
|
410 420 430
....*....|....*....|....*....|....*.
gi 1725075560 1700 GQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIE 1735
Cdd:PLN02330 431 GDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE 466
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1463-1706 |
9.21e-09 |
|
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: 59.24 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1463 IMYTSGSTGNPKGVMITHGNL----------NNFTNDFVgrlALSArdkvLSLTSISFDIFGLELFcsLAGGAHVTLcPR 1532
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALlaqalvlavlQAIDEGTV---FLNS----GPLFHIGTLMFTLATF--HAGGTNVFV-RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1533 etaMDPVKLYHFIERQQpsVIQA---TPTVWStiVHHLPAASQRPLTVLCGGEKMP--AALLTQLRRIATRVLQVYGPTE 1607
Cdd:cd17636 75 ---VDAEEVLELIEAER--CTHAfllPPTIDQ--IVELNADGLYDLSSLRSSPAAPewNDMATVDTSPWGRKPGGYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1608 TTIWSTCADLTHEGASDCiGTPIQATEVLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDkvflRRQAFGaeryM 1687
Cdd:cd17636 148 VMGLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNA----RRTRGG----W 218
|
250
....*....|....*....
gi 1725075560 1688 YRTGDIVRFNRQGQLEYLG 1706
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVG 237
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1396-1728 |
1.37e-08 |
|
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: 59.79 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1396 KHYVPIDVHYPA-DRVSYMIENAQARLLVTDgEPEQGWASpavgFDSLVSHpaAAD---ALPIPADDTLAyIMYTSGSTG 1471
Cdd:cd05928 116 KCIVTSDELAPEvDSVASECPSLKTKLLVSE-KSRDGWLN----FKELLNE--ASTehhCVETGSQEPMA-IYFTSGTTG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1472 NPKGVMITHGNLN-NFTNDfvGR--LALSARDKVLSLTSISFDIFGL-ELFCSLAGGAHVtlcpretamdpvkLYHFIER 1547
Cdd:cd05928 188 SPKMAEHSHSSLGlGLKVN--GRywLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACV-------------FVHHLPR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1548 QQPSVIQAT------------PTVWSTIVHHLPAASQRPLT--VLCGGEKMPAALLTQLR-RIATRVLQVYGPTETTIws 1612
Cdd:cd05928 253 FDPLVILKTlssypittfcgaPTVYRMLVQQDLSSYKFPSLqhCVTGGEPLNPEVLEKWKaQTGLDIYEGYGQTETGL-- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1613 TCADL-THEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELwlgGAGVSP--------GYWRNPTLSDKVFlrRQAFga 1683
Cdd:cd05928 331 ICANFkGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDI---GIRVKPirpfglfsGYVDNPEKTAATI--RGDF-- 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1725075560 1684 erymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:cd05928 404 ----YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESAL 444
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
428-775 |
1.43e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 59.77 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIGREglSNVAQ----NHRDFIGLAQGSRVLAIASLgFDAFGWDV-YGALVSGATLYLAPS 502
Cdd:PRK06018 177 NTAAGMCYTSGTTGDPKGVLYSHR--SNVLHalmaNNGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPGA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 503 ELhtDVGALHDYLTQHDIGHITITPAILELLPREM------WPGLRTMIVMGDAPPADVVAWWAER-TRLCNGYGPTEAS 575
Cdd:PRK06018 254 KL--DGASVYELLDTEKVTFTAGVPTVWLMLLQYMekeglkLPHLKMVVCGGSAMPRSMIKAFEDMgVEVRHAWGMTEMS 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 576 IATSLCEYRPgvpwncigkPLKNY----RCHILDLHHNPlPVGFE------------------GELCIAGSGLAHGYLH- 632
Cdd:PRK06018 332 PLGTLAALKP---------PFSKLpgdaRLDVLQKQGYP-PFGVEmkitddagkelpwdgktfGRLKVRGPAVAAAYYRv 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 633 -QEALSAEKFiicrlpymaaeerlYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARS 711
Cdd:PRK06018 402 dGEILDDDGF--------------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVY 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 712 QPS-GKILAAFVQPASPEltiDALRHALVTLLHPAA----IPSVFIFLPALPLTINGKIA----RQQLEKWPL 775
Cdd:PRK06018 468 HPKwDERPLLIVQLKPGE---TATREEILKYMDGKIakwwMPDDVAFVDAIPHTATGKILktalREQFKDYKL 537
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
432-772 |
1.48e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 59.91 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 432 YVCYTSGTTGKPKGVMIGREG-LSNVAQNHRDFIGLAQGSRVLAIASLGF-DAFGWDVYGALVSGATL------------ 497
Cdd:PLN02654 279 FLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWiTGHSYVTYGPMLNGATVlvfegapnypds 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 498 ---------------YLAPSELHTDVGALHDYLTQHDIGHITITPAILELLPREMWPGLRTmiVMGDA--PPADVvaWWA 560
Cdd:PLN02654 359 grcwdivdkykvtifYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFN--VVGDSrcPISDT--WWQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 561 ERTrlcNGYgpteasIATSLCEYRPGVPWNCIgKPLKNYRCHILDLHHNPLPVGFEGELCIAGSGlaHGYLHQEALSAEK 640
Cdd:PLN02654 435 TET---GGF------MITPLPGAWPQKPGSAT-FPFFGVQPVIVDEKGKEIEGECSGYLCVKKSW--PGAFRTLYGDHER 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 641 FiicRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVA-RSQPSGKILA 719
Cdd:PLN02654 503 Y---ETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGiEHEVKGQGIY 579
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 720 AFVQPASPELTIDALRHALVTLLHPA----AIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:PLN02654 580 AFVTLVEGVPYSEELRKSLILTVRNQigafAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
419-764 |
1.70e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 59.72 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 419 HAEQLPQSRDALAYVCYTSGTTGKPKGVMIGREG-LSNVAQnHRDFIGLAQGSRVLAIASLgFDAFGWDV--YGALVSGA 495
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSlLANVEQ-IKTIADFTPNDRFMSALPL-FHSFGLTVglFTPLLTGA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 496 TLYLAPSELHTDVgalhdyltqhdighititpaILELL-PREMWPGLRTMIVMGD----APPAD------VVA------- 557
Cdd:PRK08043 434 EVFLYPSPLHYRI--------------------VPELVyDRNCTVLFGTSTFLGNyarfANPYDfarlryVVAgaeklqe 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 558 ----WWAER--TRLCNGYGPTEASIATSLceyrpGVPWNC----IGKPLKNYRCHILdlhhnPLPvGFE--GELCIAGSG 625
Cdd:PRK08043 494 stkqLWQDKfgLRILEGYGVTECAPVVSI-----NVPMAAkpgtVGRILPGMDARLL-----SVP-GIEqgGRLQLKGPN 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 626 LAHGYLHQE------ALSAEKfiicrlPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRG--VRIEMGEvESAVR 697
Cdd:PRK08043 563 IMNGYLRVEkpgvleVPTAEN------ARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGemVSLEMVE-QLALG 635
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 698 SHPLVESAcVVARSQPS-GKILAAFVQPAspELTIDALRHALVTLLHPA-AIPSVFIFLPALPLTINGK 764
Cdd:PRK08043 636 VSPDKQHA-TAIKSDASkGEALVLFTTDS--ELTREKLQQYAREHGVPElAVPRDIRYLKQLPLLGSGK 701
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1344-1714 |
1.84e-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: 59.39 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1344 ERQQYSYRQLWAQSERVA---HALLRIDSRPFsVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIE----- 1415
Cdd:cd17632 64 RFETITYAELWERVGAVAaahDPEQPVRPGDF-VAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAetepr 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1416 -------------------NAQARLLVTDGEPE--------QGWASPAVGFDSLVSHPAAA-----DALPIPA------D 1457
Cdd:cd17632 143 llavsaehldlaveavlegGTPPRLVVFDHRPEvdahraalESARERLAAVGIPVTTLTLIavrgrDLPPAPLfrpepdD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1458 DTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVgrlALSARDKVLSLTsISF----DIFG-LELFCSLAGGAHVTLCPr 1532
Cdd:cd17632 223 DPLALLIYTSGSTGTPKGAMYTERLVATFWLKVS---SIQDIRPPASIT-LNFmpmsHIAGrISLYGTLARGGTAYFAA- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1533 etAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPLTVLCGGEKMPAALLTQLRRiatrvlQVYGPTETTIWS 1612
Cdd:cd17632 298 --ASDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRE------RVLGGRLLAAVC 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1613 TCADLTHEGAS---DCIGTPIQ----ATE---VLVMDQAGNP---------LPS-GAF--------GELWLGGAGVSPGY 1664
Cdd:cd17632 370 GSAPLSAEMKAfmeSLLDLDLHdgygSTEagaVILDGVIVRPpvldyklvdVPElGYFrtdrphprGELLVKTDTLFPGY 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1665 WRNPTLSDKVFlRRQAFgaerymYRTGDIVRFNRQGQLEYLGRNDHQVKI 1714
Cdd:cd17632 450 YKRPEVTAEVF-DEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKL 492
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1438-1803 |
2.30e-08 |
|
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: 59.08 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1438 GFDSLVSHPAAADAlpipaDDTLAYIMYTSGSTGNPKGVMITHGNLnnftndfVGRLAlSARDKVLS---------LTSI 1508
Cdd:cd17642 169 GFNEYDFKPPSFDR-----DEQVALIMNSSGSTGLPKGVQLTHKNI-------VARFS-HARDPIFGnqiipdtaiLTVI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1509 SF-DIFG-LELFCSLAGGAHVTLCPR-ETAMdpvklyhFIERQQPSVIQAT---PTVWSTIVHHlPAASQRPLT----VL 1578
Cdd:cd17642 236 PFhHGFGmFTTLGYLICGFRVVLMYKfEEEL-------FLRSLQDYKVQSAllvPTLFAFFAKS-TLVDKYDLSnlheIA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1579 CGGEKMPAALLTQL-RRIATR-VLQVYGPTETT--IWSTCADLTHEGASDCIgTPIQATEVLVMDqAGNPLPSGAFGELW 1654
Cdd:cd17642 308 SGGAPLSKEVGEAVaKRFKLPgIRQGYGLTETTsaILITPEGDDKPGAVGKV-VPFFYAKVVDLD-TGKTLGPNERGELC 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1655 LGGAGVSPGYWRNPTLSdkvflrrQAFGAERYMYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNI 1734
Cdd:cd17642 386 VKGPMIMKGYVNNPEAT-------KALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKI 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725075560 1735 ERSLSL-----IVGEGQQARIVsylqLTSGEELNEKAVRTALKARL-PNIMIPSGFVVLSAFPLTNNNKIDIRRL 1803
Cdd:cd17642 459 FDAGVAgipdeDAGELPAAVVV----LEAGKTMTEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1323-1707 |
4.47e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 58.20 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1323 SLLMHIGRLAHTQPDSLA-----VSCER----QQYSYRQLWAQSERVAHALLRIDSRPFSVGVMMEKSCHVAVLLLGVLR 1393
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAyrfldFSTERdgvaRDLTWSQFGARNRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1394 AGKHYVPI-DVHYP--ADRVSYMIENAQARLLVTDGEPEQG-----WASPA------VGFDSLVSHPAAADALPIPADDT 1459
Cdd:PRK07769 102 AGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGvrkffRARPAkerprvIAVDAVPDEVGATWVPPEANEDT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1460 LAYIMYTSGSTGNPKGVMITHGNLNnfTNDFVGRLALSARDKVLSLTSISF--DIFGLELFCSLAGGAHVTLcpretaMD 1537
Cdd:PRK07769 182 IAYLQYTSGSTRIPAGVQITHLNLP--TNVLQVIDALEGQEGDRGVSWLPFfhDMGLITVLLPALLGHYITF------MS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1538 PVKlyhFIER-------------QQPSVIQATPTVW--STIVHHLPAASQRPL------TVLCGGEKMPAAlltQLRRI- 1595
Cdd:PRK07769 254 PAA---FVRRpgrwirelarkpgGTGGTFSAAPNFAfeHAAARGLPKDGEPPLdlsnvkGLLNGSEPVSPA---SMRKFn 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1596 ---------ATRVLQVYGPTE------TTIWSTCADLTH------------EGASDCIGTPIQAT---------EVLVMD 1639
Cdd:PRK07769 328 eafapyglpPTAIKPSYGMAEatlfvsTTPMDEEPTVIYvdrdelnagrfvEVPADAPNAVAQVSagkvgvsewAVIVDP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1640 QAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLRR--------QAFGAE---RYMyRTGDI-VRFNrqGQLEYLGR 1707
Cdd:PRK07769 408 ETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNIlksrlsesHAEGAPddaLWV-RTGDYgVYFD--GELYITGR 484
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1349-1717 |
4.74e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.21 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRIDSRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPI---DVHYPADRVSYMIENAQARLLVTD 1425
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTVVLTT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1426 GEpeqgwASPAV-GFDSLVSHP--------------AAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITHGNLNnfTNd 1489
Cdd:PRK12476 150 TA-----AAEAVeGFLRNLPRLrrprviaidaipdsAGESFVPVELDtDDVSHLQYTSGSTRPPVGVEITHRAVG--TN- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1490 fVGRLALSARDKVLSLTSIS----FDIFGLEL--FCSLAGGaHVTLcpretaMDPVKlyhFIERQQ------------PS 1551
Cdd:PRK12476 222 -LVQMILSIDLLDRNTHGVSwlplYHDMGLSMigFPAVYGG-HSTL------MSPTA---FVRRPQrwikalsegsrtGR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1552 VIQATPTV---WsTIVHHLPAASQ----RPLTVLCGGEKMPAALLTQLRRI-------ATRVLQVYGPTETTIW-STCA- 1615
Cdd:PRK12476 291 VVTAAPNFayeW-AAQRGLPAEGDdidlSNVVLIIGSEPVSIDAVTTFNKAfapyglpRTAFKPSYGIAEATLFvATIAp 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1616 ---------DLTHEGASDCIGTPIQATE----------------VLVMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTL 1670
Cdd:PRK12476 370 daepsvvylDREQLGAGRAVRVAADAPNavahvscgqvarsqwaVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEE 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 1671 SDKVF---LRRQ------AFGAE--RYMYRTGDIvRFNRQGQLEYLGRNDHQVKIRGH 1717
Cdd:PRK12476 450 TERTFgakLQSRlaegshADGAAddGTWLRTGDL-GVYLDGELYITGRIADLIVIDGR 506
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
785-858 |
4.81e-08 |
|
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: 51.78 E-value: 4.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 785 PETETEAILERIVANAIGCPQADVTQE---FINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYIENK 858
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEEITPDdsfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
423-767 |
5.75e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.71 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 423 LPQ-SRDALAYVCYTSGTTGKPKGVMIG-REGLSNVAQNHRDFIGLAQGSRvlaiaslgfdAFGW-----DVygALVSga 495
Cdd:PRK09192 170 LPRpTPDDIAYLQYSSGSTRFPRGVIIThRALMANLRAISHDGLKVRPGDR----------CVSWlpfyhDM--GLVG-- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 496 tLYLAP--SELHTDVGALHDY---------LTQHDIGHITITPAI-LELLPREM------------WpglRTMIVMGDAP 551
Cdd:PRK09192 236 -FLLTPvaTQLSVDYLPTRDFarrplqwldLISRNRGTISYSPPFgYELCARRVnskdlaeldlscW---RVAGIGADMI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 552 PADVVAWWAERTRLCN--------GYGPTEASIATSLCE------------------------------YRPGVpwNCiG 593
Cdd:PRK09192 312 RPDVLHQFAEAFAPAGfddkafmpSYGLAEATLAVSFSPlgsgivveevdrdrleyqgkavapgaetrrVRTFV--NC-G 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 594 KPLKNYRCHILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALSAEkfiicrlpyMAAEERLyRTGDIAkWDEQGNIIFV 673
Cdd:PRK09192 389 KALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDV---------LAADGWL-DTGDLG-YLLDGYLYIT 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 674 GRRDHQVKIRGVRIEMGEVESAVRSHPLVES--ACVVARSQPSGKILAAFVQ-PASPELTIDALRHALVTLLHPA-AIPS 749
Cdd:PRK09192 458 GRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdAAAFSIAQENGEKIVLLVQcRISDEERRGQLIHALAALVRSEfGVEA 537
|
410 420
....*....|....*....|
gi 1725075560 750 VFIFLP--ALPLTINGKIAR 767
Cdd:PRK09192 538 AVELVPphSLPRTSSGKLSR 557
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1423-1798 |
6.51e-08 |
|
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: 57.67 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1423 VTDGEPEQGWASPAVGFDSLVSHPAAA--DALPIPADDTLaYIMYTSGSTGNPKGvmITHGnlnnftndfVGRLALsard 1500
Cdd:cd05943 213 VAAGQPDLSKIAKALTLEDFLATGAAGelEFEPLPFDHPL-YILYSSGTTGLPKC--IVHG---------AGGTLL---- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1501 KVLSLTSISFDI-FGLELFC--------------SLAGGAHVTL---CPreTAMDPVKLYHFIERQQPSVIQATPTvwst 1562
Cdd:cd05943 277 QHLKEHILHCDLrPGDRLFYyttcgwmmwnwlvsGLAVGATIVLydgSP--FYPDTNALWDLADEEGITVFGTSAK---- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1563 IVHHLPAASQRPLTVLCggekmpaalLTQLRriatrvlqvygptetTIWSTCADLTHEG---ASDCI-----------GT 1628
Cdd:cd05943 351 YLDALEKAGLKPAETHD---------LSSLR---------------TILSTGSPLKPESfdyVYDHIkpdvllasisgGT 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1629 ------------------PIQA----TEVLVMDQAGNPLPsGAFGELwlggAGVSP------GYWRNPtlsDKVFLRRQA 1680
Cdd:cd05943 407 diiscfvggnpllpvyrgEIQCrglgMAVEAFDEEGKPVW-GEKGEL----VCTKPfpsmpvGFWNDP---DGSRYRAAY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1681 FgaERY--MYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSLSSLDNIERslSLIVG---EGQQARIVSYLQ 1755
Cdd:cd05943 479 F--AKYpgVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVED--SLVVGqewKDGDERVILFVK 554
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1725075560 1756 LTSGEELNE---KAVRTALKARLPNIMIPSGFVVLSAFPLTNNNKI 1798
Cdd:cd05943 555 LREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
432-767 |
8.35e-08 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 57.27 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 432 YVCYTSGTTGKPKGVmigreglsnvaqnHRDFIGLAqgsrvLAIAS---LGFDA-----------FGWDV------YGAL 491
Cdd:PRK10524 237 YILYTSGTTGKPKGV-------------QRDTGGYA-----VALATsmdTIFGGkagetffcasdIGWVVghsyivYAPL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 492 VSG-ATLYLAPSELHTDVGALHDYLTQHDIGHITITP-AI-------LELLPREMWPGLRTMIVMG---DAPPADVVA-- 557
Cdd:PRK10524 299 LAGmATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPtAIrvlkkqdPALLRKHDLSSLRALFLAGeplDEPTASWISea 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 558 --------WWAERT-----RLCNGYGPTEAsiatslceyRPGVPwnciGKPLKNYRCHILD-LHHNPLPVGFEGELCIAG 623
Cdd:PRK10524 379 lgvpvidnYWQTETgwpilAIARGVEDRPT---------RLGSP----GVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEG 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 624 SgLAHGYLHQEALSAEKFIicRLPYMAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLV- 702
Cdd:PRK10524 446 P-LPPGCMQTVWGDDDRFV--KTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVa 522
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 703 ESACVVARSQPSGKILAAFVQPASPELTID-ALRHAL--------VTLLHPAAIPSVFIFLPALPLTINGKIAR 767
Cdd:PRK10524 523 EVAVVGVKDALKGQVAVAFVVPKDSDSLADrEARLALekeimalvDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
900-1064 |
1.01e-07 |
|
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: 56.73 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 900 LAIDIQGpLDLGRFEQAINFIYEKHESLRTRFTEtDGVAYQLAEPHTPiRLADHwvDGQTLSAEKWVRQLCAT------- 972
Cdd:cd19535 30 LEFDGED-LDPDRLERAWNKLIARHPMLRAVFLD-DGTQQILPEVPWY-GITVH--DLRGLSEEEAEAALEELrerlshr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 973 PFDITARPPLVLRLVQYHQQHHVLiwvkH----NIITDAWSEQLILNDLWQRYNelddHHGLDAPQPQIQTIDIVNSGIA 1048
Cdd:cd19535 105 VLDVERGPLFDIRLSLLPEGRTRL----HlsidLLVADALSLQILLRELAALYE----DPGEPLPPLELSFRDYLLAEQA 176
|
170
....*....|....*....
gi 1725075560 1049 SPAPA---DVAYWQQQLQD 1064
Cdd:cd19535 177 LRETAyerARAYWQERLPT 195
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1445-1707 |
1.46e-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: 56.28 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1445 HPAAADALPIPAD-DTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRLALSARDKVLS---LTSISFDIFGLELfcS 1520
Cdd:cd17641 144 DPGLYEREVAAGKgEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSvlpLPWIGEQMYSVGQ--A 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1521 LAGGAHVTlCPRE--TAMDPVKlyhfieRQQPSVIQATPTVWSTIV------------------HHLPAASQRPLTVLCG 1580
Cdd:cd17641 222 LVCGFIVN-FPEEpeTMMEDLR------EIGPTFVLLPPRVWEGIAadvrarmmdatpfkrfmfELGMKLGLRALDRGKR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1581 GEKMPAAL--------------------LTQLRRIAT-------------RVL-----QVYGPTETTIWSTcADLTHEGA 1622
Cdd:cd17641 295 GRPVSLWLrlaswladallfrplrdrlgFSRLRSAATggaalgpdtfrffHAIgvplkQLYGQTELAGAYT-VHRDGDVD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1623 SDCIGTPIQATEVLVMDQagnplpsgafGELWLGGAGVSPGYWRNPTLSdkvflrRQAFGAERYMyRTGDIVRFNRQGQL 1702
Cdd:cd17641 374 PDTVGVPFPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEAT------AEDFDEDGWL-HTGDAGYFKENGHL 436
|
....*
gi 1725075560 1703 EYLGR 1707
Cdd:cd17641 437 VVIDR 441
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
313-772 |
2.20e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 56.04 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 313 DGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQapaARNQSI---LDDVQP 389
Cdd:PRK08279 59 EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQ---QRGAVLahsLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADS----------------PLHSGDAPCIAPSSIDYRSLNIHAEQLP----------QSRDALAYVcYTSGTTGKP 443
Cdd:PRK08279 136 KHLIVGEelveafeearadlarpPRLWVAGGDTLDDPEGYEDLAAAAAGAPttnpasrsgvTAKDTAFYI-YTSGTTGLP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 444 KGV----------MIGREGLSNVAQNHRDFIGL----AQGSRVlaiaslgfdAFGwdvyGALVSGATLYLAP----SELH 505
Cdd:PRK08279 215 KAAvmshmrwlkaMGGFGGLLRLTPDDVLYCCLplyhNTGGTV---------AWS----SVLAAGATLALRRkfsaSRFW 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 506 TDVgalhdylTQHDIGHITitpAILELL---------PREMWPGLRTMIVMGDAPpaDVVAWWAERT---RLCNGYGPTE 573
Cdd:PRK08279 282 DDV-------RRYRATAFQ---YIGELCryllnqppkPTDRDHRLRLMIGNGLRP--DIWDEFQQRFgipRILEFYAASE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 574 ASIATSLCEYRPGVPWNCIGKPLKNYR---------CHILDLHHNPLPVGFeGE--LCIAGSGLAH---GYLHQEAlsAE 639
Cdd:PRK08279 350 GNVGFINVFNFDGTVGRVPLWLAHPYAivkydvdtgEPVRDADGRCIKVKP-GEvgLLIGRITDRGpfdGYTDPEA--SE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 640 KFIIcRLPYmAAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACV--VARSQPSGKI 717
Cdd:PRK08279 427 KKIL-RDVF-KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGTDGRA 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 718 -LAAFVQPASPELTIDALRHALVTLLHPAAIPsVFIFL-PALPLTINGKIARQQLEK 772
Cdd:PRK08279 505 gMAAIVLADGAEFDLAALAAHLYERLPAYAVP-LFVRLvPELETTGTFKYRKVDLRK 560
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1831-1885 |
5.63e-07 |
|
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: 48.33 E-value: 5.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1831 IWQQVL--SQTQISVCDSFFSLGGNSLQIPQLLHAIRQQMGVSLTIREFIMHSQIRE 1885
Cdd:pfam00550 6 LLAEVLgvPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1466-1775 |
8.50e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 53.61 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1466 TSGSTGNPKGVMITHGNLNNFTnDFVGRlALSA-----RDKVLSLtsisfdiFGLELFcslAGGAHVTLCPRE------- 1533
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWA-ELFAR-SLRAagvrpGDRVQNA-------FGYGLF---TGGLGLHYGAERlgatvip 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1534 -TAMDPVKLYHFIERQQPSVIQATPTVWSTIVHHLPAASQRPL-----TVLCGGEKMPAALLTQL-RRIATRVLQVYGPT 1606
Cdd:COG1541 159 aGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRdlslkKGIFGGEPWSEEMRKEIeERWGIKAYDIYGLT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1607 E--TTIWSTCADltHEGASdcigtpIQATEVLVM---DQAGNPLPSGAFGELwlggagvspgywrnptlsdkVF--LRRQ 1679
Cdd:COG1541 239 EvgPGVAYECEA--QDGLH------IWEDHFLVEiidPETGEPVPEGEEGEL--------------------VVttLTKE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1680 AfgaeryM----YRTGDIVRFN-------RQGQ-LEY-LGRNDHQVKIRGHRIELSEIDLSLSSLDNIERSLSLIV-GEG 1745
Cdd:COG1541 291 A------MplirYRTGDLTRLLpepcpcgRTHPrIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVdREG 364
|
330 340 350
....*....|....*....|....*....|..
gi 1725075560 1746 QQARIVSYLQLTSGEELN--EKAVRTALKARL 1775
Cdd:COG1541 365 GLDELTVRVELAPGASLEalAEAIAAALKAVL 396
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
433-729 |
2.11e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 52.72 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 433 VCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGS------------------RVLAI------ASLGFdafgW--D 486
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAltvkdvylsylplahifdRVIEEcfiqhgAAIGF----WrgD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 487 VYGALVSGATL---------------YLAPSELHTDVGALH----DYLTQHDIG-------HITITPAILELLPREMWPG 540
Cdd:PLN02614 304 VKLLIEDLGELkptifcavprvldrvYSGLQKKLSDGGFLKkfvfDSAFSYKFGnmkkgqsHVEASPLCDKLVFNKVKQG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 541 LR---TMIVMGDAPPADVVAWWAERTRLCN---GYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCH---ILDLHHNPL 611
Cdd:PLN02614 384 LGgnvRIILSGAAPLASHVESFLRVVACCHvlqGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRlesVPEMEYDAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 612 PVGFEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaeERLYRTGDIAKWDEQGNIIFVGRRDHQVKI-RGVRIEMG 690
Cdd:PLN02614 464 ASTPRGEICIRGKTLFSGYYKREDLTKEVLI----------DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVE 533
|
330 340 350
....*....|....*....|....*....|....*....
gi 1725075560 691 EVESAVRSHPLVESACVVARSQPSgkILAAFVQPASPEL 729
Cdd:PLN02614 534 NIENIYGEVQAVDSVWVYGNSFES--FLVAIANPNQQIL 570
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
310-773 |
2.82e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 52.18 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 310 LHADGQTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVLLDPQAPAARNQSILDDVQP 389
Cdd:PRK09029 22 LRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 390 ALILADSplHSGDAPCIAPSSIdyrSLNIHAEQLPQSRDALAYVCYTSGTTGKPKGVMigreglsNVAQNHRDFiglAQG 469
Cdd:PRK09029 102 DFALVLE--GENTFSALTSLHL---QLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAV-------HTAQAHLAS---AEG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 470 srVLAIasLGFDAfgWD----------------VYGALVSGATLYLAPSE-LHTDV-GALHDYL--TQ------HDIGHI 523
Cdd:PRK09029 167 --VLSL--MPFTA--QDswllslplfhvsgqgiVWRWLYAGATLVVRDKQpLEQALaGCTHASLvpTQlwrlldNRSEPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 524 TITpAIL--------ELLPREMWPGLRTmivmgdappadvvawWAertrlcnGYGPTEAsiATSLC----EYRPGVpwnc 591
Cdd:PRK09029 241 SLK-AVLlggaaipvELTEQAEQQGIRC---------------WC-------GYGLTEM--ASTVCakraDGLAGV---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 592 iGKPLKNYRCHILDlhhnplpvgfeGELCIAGSGLAHGYLHQEALsaekfiicrLPyMAAEERLYRTGDIAKWDeQGNII 671
Cdd:PRK09029 292 -GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQL---------VP-LVNDEGWFATRDRGEWQ-NGELT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 672 FVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQPASpELTIDALRHALVTLL----HPAA 746
Cdd:PRK09029 349 ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfGQRPVAVVESDS-EAAVVNLAEWLQDKLarfqQPVA 427
|
490 500 510
....*....|....*....|....*....|
gi 1725075560 747 ipsvfiFLPaLPLTI-NG--KIARQQLEKW 773
Cdd:PRK09029 428 ------YYL-LPPELkNGgiKISRQALKEW 450
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1455-1483 |
5.80e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 51.25 E-value: 5.80e-06
10 20
....*....|....*....|....*....
gi 1725075560 1455 PADDTLAYIMYTSGSTGNPKGVMITHGNL 1483
Cdd:PLN02736 218 PKPEDVATICYTSGTTGTPKGVVLTHGNL 246
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1452-1735 |
8.53e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 50.79 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1452 LPIPADDTLAYIMYTSGSTGNPKGVMITHGNLNNFTNDFVGRL-----ALSARDKVLSL-------------------TS 1507
Cdd:PLN02614 217 LPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksanaALTVKDVYLSYlplahifdrvieecfiqhgAA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1508 ISF----------DIFGLE--LFCS---------------LAGGAHVtlcpRETAMDPVKLYHF--IERQQpSVIQATP- 1557
Cdd:PLN02614 297 IGFwrgdvkllieDLGELKptIFCAvprvldrvysglqkkLSDGGFL----KKFVFDSAFSYKFgnMKKGQ-SHVEASPl 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1558 ---TVWSTIVHHLPAASQrplTVLCGGEKMPAALLTQLRRIA-TRVLQVYGPTETTIwSTCADLTHE-GASDCIGTPIQA 1632
Cdd:PLN02614 372 cdkLVFNKVKQGLGGNVR---IILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCA-GTFVSLPDElDMLGTVGPPVPN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1633 TEVL---VMDQAGNPLPSGAFGELWLGGAGVSPGYWRNPTLSDKVFLrrqafgaERYMYrTGDIVRFNRQGQLEYLGRND 1709
Cdd:PLN02614 448 VDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLH-TGDVGEWQPNGSMKIIDRKK 519
|
330 340
....*....|....*....|....*..
gi 1725075560 1710 HQVKI-RGHRIELSEIDLSLSSLDNIE 1735
Cdd:PLN02614 520 NIFKLsQGEYVAVENIENIYGEVQAVD 546
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1344-1480 |
1.40e-05 |
|
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: 49.98 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1344 ERQQYSYRQLWAQSERVAHALLRIDSrpfsvgvMMEKSChVAVLL----------LGVLRAGKHYVPIDVHYPADRVSYM 1413
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAG-------LRPGDT-VALLLgnepaflwiwLGLAKLGCPVAFLNTNIRSKSLLHC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1414 IENAQARLLVTDGE---------P---EQG---WA----SPAVGFDSLVSHPAAADALPIPAD--------DTLAYImYT 1466
Cdd:cd05938 74 FRCCGAKVLVVAPElqeaveevlPalrADGvsvWYlshtSNTEGVISLLDKVDAASDEPVPASlrahvtikSPALYI-YT 152
|
170
....*....|....
gi 1725075560 1467 SGSTGNPKGVMITH 1480
Cdd:cd05938 153 SGTTGLPKAARISH 166
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1462-1728 |
2.98e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 48.97 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1462 YIMYTSGSTGNPKGVMITHG-NLNNFTNDFVGRLALSARDKVLSLTSISFDIFGLELFCSLAGGAhvTLCPRETAMDPVK 1540
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGpHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGN--TFVMFEGGIIKNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1541 -----LYHFIERQQPSVIQATPTVWSTIVHHLPAASQ--------RPLTVLCGGEKMPAALLTQL-RRIATRVLQVYGPT 1606
Cdd:PTZ00237 336 hieddLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIirskydlsNLKEIWCGGEVIEESIPEYIeNKLKIKSSRGYGQT 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1607 ETTIWSTCADLTHEGASDCIGTPIQATEVLVMDQAGNPLPSGAFGELWLG---GAGVSPGYWRNPTLSDKVFLRRQAFga 1683
Cdd:PTZ00237 416 EIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKFPGY-- 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1725075560 1684 erymYRTGDIVRFNRQGQLEYLGRNDHQVKIRGHRIELSEIDLSL 1728
Cdd:PTZ00237 494 ----YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSI 534
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
436-704 |
3.27e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 48.61 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 436 TSGTTGKPKGVMIGREGLSNVAQNH-RDF--IGLAQGSRVLAIASLGFDAFGWDV-YGALVSGATLYLA---PSELHtdV 508
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFaRSLraAGVRPGDRVQNAFGYGLFTGGLGLhYGAERLGATVIPAgggNTERQ--L 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 509 GALHDYltQHDIghITITPAILELLPREM--------WPGLRTMIVMGDAppadvvawWAERTR----------LCNGYG 570
Cdd:COG1541 169 RLMQDF--GPTV--LVGTPSYLLYLAEVAeeegidprDLSLKKGIFGGEP--------WSEEMRkeieerwgikAYDIYG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 571 PTEASIATSL-CEYRPGvpwncigkplknyrCHILDLH----------HNPLPVGFEGELCIAGsglahgylhqeaLSAE 639
Cdd:COG1541 237 LTEVGPGVAYeCEAQDG--------------LHIWEDHflveiidpetGEPVPEGEEGELVVTT------------LTKE 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725075560 640 KFIICRlpymaaeerlYRTGDIAKWDEQ-----------GNIIfvGRRDHQVKIRGVRIEMGEVESAVRSHPLVES 704
Cdd:COG1541 291 AMPLIR----------YRTGDLTRLLPEpcpcgrthpriGRIL--GRADDMLIIRGVNVFPSQIEEVLLRIPEVGP 354
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
344-471 |
5.05e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 48.19 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 344 VAVSMDKSATLLIVLLGILKSNKTYV-LLDPQAP--AARNQSILDDVQPALILADSPLHSGDAPCIAPSSIDYRSLNIHA 420
Cdd:PRK07769 82 VAILAPQNLDYLIAFFGALYAGRIAVpLFDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERPRVIAV 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725075560 421 EQLPQS-----------RDALAYVCYTSGTTGKPKGVMIGREGL-SNVAQnHRDFIGLAQGSR 471
Cdd:PRK07769 162 DAVPDEvgatwvppeanEDTIAYLQYTSGSTRIPAGVQITHLNLpTNVLQ-VIDALEGQEGDR 223
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
379-465 |
5.70e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.01 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 379 RNQSILDDVQPALILADSP----------LHSGDApciAPSSIDYRSLNIHAEQ----LPQSRDALAYVCYTSGTTGKPK 444
Cdd:PRK05850 100 RVSAVLRDTSPSVVLTTSAvvddvteyvaPQPGQS---APPVIEVDLLDLDSPRgsdaRPRDLPSTAYLQYTSGSTRTPA 176
|
90 100
....*....|....*....|..
gi 1725075560 445 GVMIGREGL-SNVAQNHRDFIG 465
Cdd:PRK05850 177 GVMVSHRNViANFEQLMSDYFG 198
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
424-457 |
7.39e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.79 E-value: 7.39e-05
10 20 30
....*....|....*....|....*....|....*
gi 1725075560 424 PQSRDALAYVCYTSGTTGKPKGVMIGREGL-SNVA 457
Cdd:PLN02736 217 PPKPEDVATICYTSGTTGTPKGVVLTHGNLiANVA 251
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
428-722 |
7.55e-05 |
|
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: 47.80 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 428 DALAYVCYTSGTTGKPKGVMIGREGLSNVAQNHRDFIGLAQGSRVLAIASLGFdaFGWDVYG---ALVSGATLYLaPSEL 504
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW--IGEQMYSvgqALVCGFIVNF-PEEP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 505 HTdvgalhdylTQHDIGHITitPAILELLPReMWPGLRT--MIVMGDAPP----------------------------AD 554
Cdd:cd17641 235 ET---------MMEDLREIG--PTFVLLPPR-VWEGIAAdvRARMMDATPfkrfmfelgmklglraldrgkrgrpvslWL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 555 VVAWW--------AERTRL---------CNG---------------------YGPTEASIATSLceYRPG-VPWNCIGKP 595
Cdd:cd17641 303 RLASWladallfrPLRDRLgfsrlrsaaTGGaalgpdtfrffhaigvplkqlYGQTELAGAYTV--HRDGdVDPDTVGVP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 596 LKNYRCHILDlhhnplpvgfEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYRTGDIAKWDEQGNIIFVGR 675
Cdd:cd17641 381 FPGTEVRIDE----------VGEILVRSPGVFVGYYKNPEATAEDFD---------EDGWLHTGDAGYFKENGHLVVIDR 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1725075560 676 -RDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPsgkILAAFV 722
Cdd:cd17641 442 aKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRP---YLTAFI 486
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
423-707 |
7.73e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 47.66 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 423 LPQSRDALAYVCYTSGTTGKPKGVM--IGR--EGLSNVAQNHRDFIG-LAQGSRVLAIASLG--FDaFGWDVY----GAL 491
Cdd:PTZ00216 259 IPENNDDLALIMYTSGTTGDPKGVMhtHGSltAGILALEDRLNDLIGpPEEDETYCSYLPLAhiME-FGVTNIflarGAL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 492 V---SGATLYLAPSELHTD-----------------------------VGAL------HDYLTQ-------HDighitiT 526
Cdd:PTZ00216 338 IgfgSPRTLTDTFARPHGDltefrpvfligvprifdtikkaveaklppVGSLkrrvfdHAYQSRlralkegKD------T 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 527 PAILEL---LPREMWPG-LRTMiVMGDAPPAD-------VVAwwaerTRLCNGYGPTEasiatSLC---EYRPG-VPWNC 591
Cdd:PTZ00216 412 PYWNEKvfsAPRAVLGGrVRAM-LSGGGPLSAatqefvnVVF-----GMVIQGWGLTE-----TVCcggIQRTGdLEPNA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 592 IGKPLKNYRCHILDLHH-----NPLPvgfEGELCIAGSGLAHGYLHQEALSAEKFIicrlpymaaEERLYRTGDIAKWDE 666
Cdd:PTZ00216 481 VGQLLKGVEMKLLDTEEykhtdTPEP---RGEILLRGPFLFKGYYKQEELTREVLD---------EDGWFHTGDVGSIAA 548
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1725075560 667 QGNIIFVGRRDHQVK-IRGVRIEMGEVESAVRSHPLVESACV 707
Cdd:PTZ00216 549 NGTLRIIGRVKALAKnCLGEYIALEALEALYGQNELVVPNGV 590
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1330-1481 |
2.00e-04 |
|
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: 46.47 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1330 RLAHTQPDSLAVSCE------RQQYSYRQLWAQSERVAHALLRIDSRPF-SVGVMMEKSCHVAVLLLGVLRAG-KHYVpI 1401
Cdd:TIGR02188 65 RHLEARPDKVAIIWEgdepgeVRKITYRELHREVCRFANVLKSLGVKKGdRVAIYMPMIPEAAIAMLACARIGaIHSV-V 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1402 DVHYPADRVSYMIENAQARLLVT-DGEPEQGWASPA------------------------------------VGFDSLVS 1444
Cdd:TIGR02188 144 FGGFSAEALADRINDAGAKLVITaDEGLRGGKVIPLkaivdealekcpvsvehvlvvrrtgnpvvpwvegrdVWWHDLMA 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 1725075560 1445 H-PAAADALPIPADDTLaYIMYTSGSTGNPKGVMITHG 1481
Cdd:TIGR02188 224 KaSAYCEPEPMDSEDPL-FILYTSGSTGKPKGVLHTTG 260
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
435-772 |
2.15e-04 |
|
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: 45.88 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 435 YTSGTTGKPKGVMIGREG--LSNVAQNHRDFIGLAQGSRVLAIASLgFDAFGWDVYGALVSGATLYLAPSELHTDvGALH 512
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPM-FHVNAWCLPYAATLVGAKQVLPGPRLDP-ASLV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 513 DYLTQHDIGHITITPAILELLP------REMWPGLRTMIVMGDAPPADVVAWWA-ERTRLCNGYGPTEASIATSLCEYRP 585
Cdd:cd05915 238 ELFDGEGVTFTAGVPTVWLALAdylestGHRLKTLRRLVVGGSAAPRSLIARFErMGVEVRQGYGLTETSPVVVQNFVKS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 586 gvPWNCIGKP----LK-----NYRCHILD-LHHNPLPVGFEGE----LCIAGSGLAHGYLH-QEALSAEKFiicrlpyma 650
Cdd:cd05915 318 --HLESLSEEekltLKaktglPIPLVRLRvADEEGRPVPKDGKalgeVQLKGPWITGGYYGnEEATRSALT--------- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 651 aEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSHPLVESACVVARSQPS-GKILAAFVQ----PA 725
Cdd:cd05915 387 -PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKwQERPLAVVVprgeKP 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1725075560 726 SPELTIDALRHALVTLlhpAAIPSVFIFLPALPLTINGKIARQQLEK 772
Cdd:cd05915 466 TPEELNEHLLKAGFAK---WQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1822-1895 |
2.47e-04 |
|
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: 41.38 E-value: 2.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725075560 1822 NEAESAMQHIWQQVL--SQTQISVCDSFFS-LGGNSLQIPQLLHAIRQQMGVSLTIREFIMHSQIRELTALALSKTA 1895
Cdd:COG0236 4 EELEERLAEIIAEVLgvDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
315-675 |
2.56e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 46.03 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 315 QTYSYGEIDRASDQFACWLLEHSGAASSVVAVSMDKSATLLIVLLGILKSNKTYVlldPQAPA--------ARNQSILDD 386
Cdd:PRK08180 68 RRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYA---PVSPAyslvsqdfGKLRHVLEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 387 VQPALILADSP---------LHSGDAPCIAPSSIDYRSLNIHAEQLPQSR--------------DALAYVCYTSGTTGKP 443
Cdd:PRK08180 145 LTPGLVFADDGaafaralaaVVPADVEVVAVRGAVPGRAATPFAALLATPptaavdaahaavgpDTIAKFLFTSGSTGLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 444 KGV-----MIGreglSNVAQNHRDFIGLAQGSRVLaiaslgFDAFGWD-VYG-------ALVSGATLYL-----APSELH 505
Cdd:PRK08180 225 KAVinthrMLC----ANQQMLAQTFPFLAEEPPVL------VDWLPWNhTFGgnhnlgiVLYNGGTLYIddgkpTPGGFD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 506 TDVGALHD-----YLTQhDIGHITITPAiLE---LLPREMWPGLRTMIVMGDAPPADVvawWA-----------ERTRLC 566
Cdd:PRK08180 295 ETLRNLREisptvYFNV-PKGWEMLVPA-LErdaALRRRFFSRLKLLFYAGAALSQDV---WDrldrvaeatcgERIRMM 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 567 NGYGPTEASIATSLCEY---RPGvpwnCIGKPLknyrchildlhhnP------LPVGFEGELCIAGSGLAHGYLHQEALS 637
Cdd:PRK08180 370 TGLGMTETAPSATFTTGplsRAG----NIGLPA-------------PgcevklVPVGGKLEVRVKGPNVTPGYWRAPELT 432
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1725075560 638 AEKFiicrlpymaAEERLYRTGDIAKW-D----EQGnIIFVGR 675
Cdd:PRK08180 433 AEAF---------DEEGYYRSGDAVRFvDpadpERG-LMFDGR 465
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
793-849 |
3.07e-04 |
|
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: 40.62 E-value: 3.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 793 LERIVANAIGCPQADVT--QEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVR 849
Cdd:pfam00550 3 LRELLAEVLGVPAEEIDpdTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1601-1720 |
3.11e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 45.86 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1601 QVYGPTETT--IWSTCADLTHegaSDCIGTPIQA-TEVLVMD----QAGNPLPSGafgELWLGGAGVSPGYwrnptlsdk 1673
Cdd:PTZ00342 491 QGYGLTETTgpIFVQHADDNN---TESIGGPISPnTKYKVRTwetyKATDTLPKG---ELLIKSDSIFSGY--------- 555
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1725075560 1674 vFLRRQ----AFGAERYmYRTGDIVRFNRQGQLEYLGRNDHQVKI-RGHRIE 1720
Cdd:PTZ00342 556 -FLEKEqtknAFTEDGY-FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
784-855 |
4.90e-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: 40.70 E-value: 4.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725075560 784 PPETETEAILERI---VANAIGCPQA---DVTQEFINLGAHSLTMSKIVALVARDLCCHLSIADLFRHNTVRKLAEYI 855
Cdd:smart00823 5 PPAERRRLLLDLVreqVAAVLGHAAAeaiDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1453-1481 |
6.67e-04 |
|
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: 44.47 E-value: 6.67e-04
10 20
....*....|....*....|....*....
gi 1725075560 1453 PIPADDTLaYIMYTSGSTGNPKGVMITHG 1481
Cdd:cd05966 227 WMDSEDPL-FILYTSGSTGKPKGVVHTTG 254
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1346-1480 |
7.01e-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: 44.34 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1346 QQYSYRQLWAQSERVAHALLridSRPFSVG----VMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARL 1421
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQ---AQGYRSGdvvaLFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 1422 LVTDGEPEQGWASPavgfdslvSHPAAADalPIPADDTLAYImYTSGSTGNPKGVMITH 1480
Cdd:cd05939 79 LIFNLLDPLLTQSS--------TEPPSQD--DVNFRDKLFYI-YTSGTTGLPKAAVIVH 126
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
425-699 |
8.31e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 44.04 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 425 QSRDALAYVCYTSGTTGKPKGVMIGReglSNVAQNHR---DFIGLAQGSRVLAIASlGFDAFGWDVYG--ALVSGATLYL 499
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTH---ANLLANQRaclKFFSPKEDDVMMSFLP-PFHAYGFNSCTlfPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 500 APSELHTDvgalhDYLTQHDIGHITI---TPAILELLPR------EMWPGLRTMIVMGDAPpADVVAWWAERT----RLC 566
Cdd:PRK06334 256 AYNPLYPK-----KIVEMIDEAKVTFlgsTPVFFDYILKtakkqeSCLPSLRFVVIGGDAF-KDSLYQEALKTfphiQLR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 567 NGYGPTEASIATSLCEYRPGVPWNCIGKPLKNYRCHILDLH-HNPLPVGFEGELCIAGSGLAHGYLhqEALSAEKFIicR 645
Cdd:PRK06334 330 QGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEEtKVPVSSGETGLVLTRGTSLFSGYL--GEDFGQGFV--E 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1725075560 646 LpymaAEERLYRTGDIAKWDEQGNIIFVGRRDHQVKIRGVRIEMGEVESAVRSH 699
Cdd:PRK06334 406 L----GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1349-1483 |
1.50e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) 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. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It 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: 341256 [Multi-domain] Cd Length: 596 Bit Score: 43.50 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1349 SYRQLWAQSERVAHALLRID-SRPFSVGVMMEKSCHVAVLLLGVLRAGKHYVPIDVHYPADRVSYMIENAQARLLVTD-- 1425
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGlERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEnq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1426 ----------------------GEP---------------EQGWASPAVGFDSLVSHPAAadalpipadDTLAYIMYTSG 1468
Cdd:cd05933 90 kqlqkilqiqdklphlkaiiqyKEPlkekepnlyswdefmELGRSIPDEQLDAIISSQKP---------NQCCTLIYTSG 160
|
170
....*....|....*
gi 1725075560 1469 STGNPKGVMITHGNL 1483
Cdd:cd05933 161 TTGMPKGVMLSHDNI 175
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1453-1481 |
1.92e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.21 E-value: 1.92e-03
10 20
....*....|....*....|....*....
gi 1725075560 1453 PIPADDTLaYIMYTSGSTGNPKGVMITHG 1481
Cdd:PRK00174 241 PMDAEDPL-FILYTSGSTGKPKGVLHTTG 268
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
565-724 |
2.14e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 42.91 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 565 LCNGYGPTE--ASIATSLCEYRP-----GVPWNCIGKPLKNyrchILDLHHNPLPVGFEGELCIAGSGLAHGYLHQEALS 637
Cdd:PLN02861 411 LSQGYGLTEscGGCFTSIANVFSmvgtvGVPMTTIEARLES----VPEMGYDALSDVPRGEICLRGNTLFSGYHKRQDLT 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 638 AEKFIicrlpymaaeERLYRTGDIAKWDEQGNIIFVGRRDHQVKI-RGVRIEMGEVESAVRSHPLVESACVVARSQPSgk 716
Cdd:PLN02861 487 EEVLI----------DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIASIWVYGNSFES-- 554
|
....*...
gi 1725075560 717 ILAAFVQP 724
Cdd:PLN02861 555 FLVAVVVP 562
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1453-1486 |
3.92e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 42.11 E-value: 3.92e-03
10 20 30
....*....|....*....|....*....|....
gi 1725075560 1453 PIPADdtLAYIMYTSGSTGNPKGVMITHGNLNNF 1486
Cdd:PLN02430 217 PKPLD--ICTIMYTSGTSGDPKGVVLTHEAVATF 248
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1452-1483 |
6.35e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 41.37 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|..
gi 1725075560 1452 LPIPADDTLAYIMYTSGSTGNPKGVMITHGNL 1483
Cdd:PLN02861 214 LPPKQKTDICTIMYTSGTTGEPKGVILTNRAI 245
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1425-1481 |
7.09e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.32 E-value: 7.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1725075560 1425 DGEPEQGWASPAVGFDSLVSHPAAA--DALPIPADDTLaYIMYTSGSTGNPKGvmITHG 1481
Cdd:PRK03584 229 GPAAAAAALPGALLWEDFLAPAEAAelEFEPVPFDHPL-WILYSSGTTGLPKC--IVHG 284
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
875-1171 |
9.44e-03 |
|
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: 40.50 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 875 PLSP-QQNLLwYLSALNPDDCSYNLPLAIDIQGPLDLGRFEQAINFIYEKHESLRTrftetdGVAYQ-LAEP------HT 946
Cdd:cd19544 3 PLAPlQEGIL-FHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRT------AILWEgLSEPvqvvwrQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 947 PIRLadHWVD-GQTLSAEKWVRQLCA---TPFDITaRPPLvLRLVQYH---QQHHVLIWVKHNIITDAWSEQLILNDLwQ 1019
Cdd:cd19544 76 ELPV--EELTlDPGDDALAQLRARFDprrYRLDLR-QAPL-LRAHVAEdpaNGRWLLLLLFHHLISDHTSLELLLEEI-Q 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1020 RYnELDDHHGLDAPQP------QIQTidivnsgiASPAPADVAYWQQQLQDCRELDFPLDkprpLMPTHA-GERI---HY 1089
Cdd:cd19544 151 AI-LAGRAAALPPPVPyrnfvaQARL--------GASQAEHEAFFREMLGDVDEPTAPFG----LLDVQGdGSDIteaRL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725075560 1090 QLQPDVAGLLASRGKALGATPfallcaalslllsRYTQQQDIVIGT-------AIAARDnldqtQVSGFHVNTVPLRIQL 1162
Cdd:cd19544 218 ALDAELAQRLRAQARRLGVSPaslfhlawalvlaRCSGRDDVVFGTvlsgrmqGGAGAD-----RALGMFINTLPLRVRL 292
|
....*....
gi 1725075560 1163 SEQDTLAGL 1171
Cdd:cd19544 293 GGRSVREAV 301
|
|
| |
