|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
2-553 |
0e+00 |
|
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: 767.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKEllqtklkdivslvprlrh 81
Cdd:cd17639 25 LGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDGK------------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 iitvdgkpptwsefpkgvivhtmaavqalgvkanvekkahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:cd17639 87 --------------------------------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIP-RLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADqssKIKKGSKGDTSVLKPTLMAAVPEIMDRIYK 240
Cdd:cd17639 123 RVPeLLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGCKGDLTEFKPTLMVGVPAIWDTIRK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 241 NVMNKVNEMSAFQRNLFILAYNYKMEQISKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNIcFCCPVG 320
Cdd:cd17639 200 GVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLNI-VLCPVI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 321 QGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFnTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfe 400
Cdd:cd17639 279 QGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYS-TDKPPPRGEILIRGPNVFKGYYKNPEKTKEAF-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 401 deNGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKEL 480
Cdd:cd17639 356 --DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHL 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209977076 481 TELARTKGFK-GTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKEL 553
Cdd:cd17639 434 TKLAEKHGVInSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1-565 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 732.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 1 MLGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIIT-SKELlqTKLKDIVSLVPRL 79
Cdd:PLN02387 125 ALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICdSKQL--KKLIDISSQLETV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 80 RHIITVDGKPPTWSEFPKGV---IVHTMAAVQALGVKANVEKkahSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASI 156
Cdd:PLN02387 203 KRVIYMDDEGVDSDSSLSGSsnwTVSSFSEVEKLGKENPVDP---DLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 157 TGMARRIPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSVLKPTLMAAVPEIMD 236
Cdd:PLN02387 280 AGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTLMTAVPAILD 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 237 RIYKNVMNKVNEMSAFQRNLFILAYNYKMEQI------SKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRF 310
Cdd:PLN02387 360 RVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIegswfgAWGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRF 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 311 MNICFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKN 390
Cdd:PLN02387 440 INICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKN 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 391 EAKTKTDFFEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVI 470
Cdd:PLN02387 520 QEKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCV 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 471 GFVVPNQKELTELARTKGFK-GTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLK 549
Cdd:PLN02387 600 ALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLK 679
|
570
....*....|....*.
gi 209977076 550 RKELKTHYQADIERMY 565
Cdd:PLN02387 680 REQIRKKFKDDLKKLY 695
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
4-565 |
9.46e-177 |
|
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: 510.22 E-value: 9.46e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 4 QKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTniitskellqtklkdivslvprlrhII 83
Cdd:cd05927 29 PAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS-------------------------IV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 84 TVDgkpptwsefpKGVIVHTMAAVQALGVKAnveKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGM---A 160
Cdd:cd05927 84 FCD----------AGVKVYSLEEFEKLGKKN---KVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkiL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 161 RRIPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSS--PQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDRI 238
Cdd:cd05927 151 EILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD-----------DIKALKPTVFPGVPRVLNRI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 239 YKNVMNKVNEMSAFQRNLFILAYNYKMEQISKG--CSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFC 316
Cdd:cd05927 220 YDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 317 CPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDkPHPRGEILIGGQNVTMGYYKNEAKTKT 396
Cdd:cd05927 300 CPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKD-PNPRGEVCIRGPNVFSGYYKDPEKTAE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 397 DFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPN 476
Cdd:cd05927 379 AL--DEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 477 QKELTELARTK-GFKGTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKT 555
Cdd:cd05927 455 PDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKK 534
|
570
....*....|
gi 209977076 556 HYQADIERMY 565
Cdd:cd05927 535 YYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-568 |
1.32e-142 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 425.28 E-value: 1.32e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSLVPRLRH 81
Cdd:COG1022 60 LGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRH 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IITVDGKPPtwsefPKGVIVHTMAAVQALGVKANVE---KKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITG 158
Cdd:COG1022 140 IVVLDPRGL-----RDDPRLLSLDELLALGREVADPaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 159 MARRIPrLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYS-SPQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDR 237
Cdd:COG1022 215 LLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------DLREVKPTFMLAVPRVWEK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 238 IYKNVMNKVNEMSAFQRNLFILAYN--YKM-EQISKGCSTP--------LCDRFVFRNVRRLLGGNIRLLLCGGAPLSAT 306
Cdd:COG1022 283 VYAGIQAKAEEAGGLKRKLFRWALAvgRRYaRARLAGKSPSlllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALGPE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 307 TQRF---MNIcfccPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLknweeggyfntdkpHPRGEILIGGQNV 383
Cdd:COG1022 363 LARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI--------------AEDGEILVRGPNV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 384 TMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYAN 463
Cdd:COG1022 425 MKGYYKNPEATAEAFDADG----WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGD 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 464 SyHSYVIGFVVPNQKELTELARTKGFK-GTWEELCNSSEMENEVLKVLseAAISASLEKFEIPLKIRLSPDPWTPETGLV 542
Cdd:COG1022 501 G-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEV--DRANAGLSRAEQIKRFRLLPKEFTIENGEL 577
|
570 580
....*....|....*....|....*.
gi 209977076 543 TDAFKLKRKELKTHYQADIERMYGRK 568
Cdd:COG1022 578 TPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2-565 |
9.32e-139 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 416.81 E-value: 9.32e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIvSLVPRLRH 81
Cdd:PLN02736 98 HGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCL-SEIPSVRL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IITVDGKPPTWSEFPK--GVIVHTMAAVQALGvkaNVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGM 159
Cdd:PLN02736 177 IVVVGGADEPLPSLPSgtGVEIVTYSKLLAQG---RSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 160 ARRIPrLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLadqsskikkGSKGDTSVLKPTLMAAVPEIMDRIY 239
Cdd:PLN02736 254 SLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNL---------KLMDDLAALRPTIFCSVPRLYNRIY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 240 KNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCS-TPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCP 318
Cdd:PLN02736 324 DGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGR 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 319 VGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDF 398
Cdd:PLN02736 404 VLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVI 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 399 feDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQK 478
Cdd:PLN02736 484 --DEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPE 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 479 ELTELARTKGFK-GTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHY 557
Cdd:PLN02736 560 VLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYF 639
|
....*...
gi 209977076 558 QADIERMY 565
Cdd:PLN02736 640 AKAISDMY 647
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
2-565 |
3.67e-137 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 414.37 E-value: 3.67e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKEllqtKLKDIVSLVP--RL 79
Cdd:PTZ00216 141 LGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK----NVPNLLRLMKsgGM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 80 RH--IITVDGKPPtwSEFPKGVIVHTMAAVQALGvkaNVEKKAHSKPLPS---DIAVIMYTSGSTGIPKGVMISHSNIIA 154
Cdd:PTZ00216 217 PNttIIYLDSLPA--SVDTEGCRLVAWTDVVAKG---HSAGSHHPLNIPEnndDLALIMYTSGTTGDPKGVMHTHGSLTA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 155 SITGMARRIPRL----GEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKikkgSKGDTSVLKPTLMAA 230
Cdd:PTZ00216 292 GILALEDRLNDLigppEEDETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFAR----PHGDLTEFRPVFLIG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 231 VPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRF 310
Cdd:PTZ00216 368 VPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEF 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 311 MNICFcCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEggYFNTDKPHPRGEILIGGQNVTMGYYKN 390
Cdd:PTZ00216 448 VNVVF-GMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEE--YKHTDTPEPRGEILLRGPFLFKGYYKQ 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 391 EAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSY 468
Cdd:PTZ00216 525 EELTREVL--DEDG--WFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngVCVLVHPARSY 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 469 VIGFVVPNQKELTELARTKGFKGTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKL 548
Cdd:PTZ00216 601 ICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKL 680
|
570
....*....|....*..
gi 209977076 549 KRKELKTHYQADIERMY 565
Cdd:PTZ00216 681 KRRVIDERYADLIKELF 697
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2-553 |
3.34e-134 |
|
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: 398.51 E-value: 3.34e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKellqtklkdivslvprlrh 81
Cdd:cd05907 25 LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 iitvdgkpptwsefpkgvivhtmaavqalgvkanvekkahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:cd05907 86 --------------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIPrLGEEDVYIGYLPLAHVLE-LSAELVCLSHGCRIGY-SSPQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDRIY 239
Cdd:cd05907 122 RLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFaSSAETLLD-----------DLSEVRPTVFLAVPRVWEKVY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 240 KNVmnKVNEMSAFQRNLFILAYnykmeqiskgcstplcdrfvfrnvrrllGGNIRLLLCGGAPLSATTQRFMNIcFCCPV 319
Cdd:cd05907 190 AAI--KVKAVPGLKRKLFDLAV----------------------------GGRLRFAASGGAPLPAELLHFFRA-LGIPV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 320 GQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLknweeggyfntdkpHPRGEILIGGQNVTMGYYKNEAKTKTDFF 399
Cdd:cd05907 239 YEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRI--------------ADDGEILVRGPNVMLGYYKNPEATAEALD 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 400 EDengqRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSyHSYVIGFVVPNQKE 479
Cdd:cd05907 305 AD----GWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-RPFLVALIVPDPEA 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209977076 480 LTELARTKGFKG-TWEELCNSSEMENEVLKVLSEAaiSASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKEL 553
Cdd:cd05907 380 LEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAA--NARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
2-565 |
1.56e-115 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 357.20 E-value: 1.56e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITS----KELLQ------TKLKD 71
Cdd:PLN02430 96 SGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQdkkiKELLEpdcksaKRLKA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 72 IVSLVPRLRHIIT----VDGKPPTWSEFpkgvivhtmaavqalgVKANVEKKAH-SKPLPSDIAVIMYTSGSTGIPKGVM 146
Cdd:PLN02430 176 IVSFTSVTEEESDkasqIGVKTYSWIDF----------------LHMGKENPSEtNPPKPLDICTIMYTSGTSGDPKGVV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 147 ISHSNIIASITG----MARRIPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAdqsskikkgSKGDTSV 222
Cdd:PLN02430 240 LTHEAVATFVRGvdlfMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNA---------LRDDLME 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 223 LKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCS----TPLCDRFVFRNVRRLLGGNIRLLLC 298
Cdd:PLN02430 311 LKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLAFRKVKAKLGGRLRLLIS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 299 GGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNT-GRVGAPLVCCEIKLKNWEEGGYFNTDKPhPRGEIL 377
Cdd:PLN02430 391 GGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYDPLGEP-PRGEIC 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 378 IGGQNVTMGYYKNEAKTktdffEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDN 457
Cdd:PLN02430 470 VRGKCLFSGYYKNPELT-----EEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVED 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 458 ICAYANSYHSYVIGFVVPNQKELTELARTKGFKGTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTP 537
Cdd:PLN02430 545 IWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDV 624
|
570 580
....*....|....*....|....*...
gi 209977076 538 ETGLVTDAFKLKRKELKTHYQADIERMY 565
Cdd:PLN02430 625 ERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
3-565 |
1.73e-113 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 352.40 E-value: 1.73e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 3 GQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSLVPRLRHI 82
Cdd:PLN02614 100 GVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 83 ITVDGKPPTWSEFPK--GVIVHTMAAVQALGvkanvEKKAHSKPL--PSDIAVIMYTSGSTGIPKGVMISHSNIIASITG 158
Cdd:PLN02614 180 VSFGGVSREQKEEAEtfGLVIYAWDEFLKLG-----EGKQYDLPIkkKSDICTIMYTSGTTGDPKGVMISNESIVTLIAG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 159 MARRI----PRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSpqtlADQSSKIKkgskgDTSVLKPTLMAAVPEI 234
Cdd:PLN02614 255 VIRLLksanAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR----GDVKLLIE-----DLGELKPTIFCAVPRV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 235 MDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCS----TPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATTQRF 310
Cdd:PLN02614 326 LDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESF 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 311 MNICFCCPVGQGYGLTESTgAGTITEVWDY--NTGRVGAPLVCCEIKLKNWEEGGYfNTDKPHPRGEILIGGQNVTMGYY 388
Cdd:PLN02614 406 LRVVACCHVLQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVDIRLESVPEMEY-DALASTPRGEICIRGKTLFSGYY 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 389 KNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSY 468
Cdd:PLN02614 484 KREDLTKEVLIDG-----WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESF 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 469 VIGFVVPNQKELTELARTKGFKGTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKL 548
Cdd:PLN02614 559 LVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKK 638
|
570
....*....|....*..
gi 209977076 549 KRKELKTHYQADIERMY 565
Cdd:PLN02614 639 KRPQLLKYYQSVIDEMY 655
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
2-435 |
6.56e-107 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 326.96 E-value: 6.56e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSLVPRLRH 81
Cdd:pfam00501 41 LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IITVDGKPPTWSEfpkgvivhtmaAVQALGVKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:pfam00501 121 VLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 ---RIPRLGEEDVYIGYLPLAHVLELSAE-LVCLSHGCRIGYSSPQTLADQsskikKGSKGDTSVLKPTLMAAVPEIMDR 237
Cdd:pfam00501 190 vrpRGFGLGPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGFPALDP-----AALLELIERYKVTVLYGVPTLLNM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 238 IYKNvmnkvnemsafqrnlfilaynykmeqiskgcstplcdrfvfRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCC 317
Cdd:pfam00501 265 LLEA-----------------------------------------GAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 318 PVGQGYGLTESTGAGT--ITEVWDYNT-GRVGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKT 394
Cdd:pfam00501 304 ALVNGYGLTETTGVVTtpLPLDEDLRSlGSVGRPLPGTEVKIVDDETGEPVPPGEP---GELCVRGPGVMKGYLNDPELT 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 209977076 395 KTDFFEDengqRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQ 435
Cdd:pfam00501 381 AEAFDED----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
2-565 |
6.27e-105 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 329.88 E-value: 6.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSkellQTKLKDIVSLVPR--- 78
Cdd:PLN02861 97 RGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ----ESKISSILSCLPKcss 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 79 -LRHIITVDGKPPTWSEFPK--GVIVHTMAAVQALGvKANVEKKAHSKplpSDIAVIMYTSGSTGIPKGVMISHSNIIA- 154
Cdd:PLN02861 173 nLKTIVSFGDVSSEQKEEAEelGVSCFSWEEFSLMG-SLDCELPPKQK---TDICTIMYTSGTTGEPKGVILTNRAIIAe 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 155 --SITGMARRIPRL-GEEDVYIGYLPLAHVLELSAELVCLSHGCRIGY--SSPQTLADqsskikkgskgDTSVLKPTLMA 229
Cdd:PLN02861 249 vlSTDHLLKVTDRVaTEEDSYFSYLPLAHVYDQVIETYCISKGASIGFwqGDIRYLME-----------DVQALKPTIFC 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 230 AVPEIMDRIYKNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCS----TPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSA 305
Cdd:PLN02861 318 GVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRLVFDKIKEGLGGRVRLLLSGAAPLPR 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 306 TTQRFMNICFCCPVGQGYGLTESTGaGTITEVWDYNT--GRVGAPLVCCEIKLKNWEEGGYfNTDKPHPRGEILIGGQNV 383
Cdd:PLN02861 398 HVEEFLRVTSCSVLSQGYGLTESCG-GCFTSIANVFSmvGTVGVPMTTIEARLESVPEMGY-DALSDVPRGEICLRGNTL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 384 TMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYAN 463
Cdd:PLN02861 476 FSGYHKRQDLTEEVLIDG-----WFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGN 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 464 SYHSYVIGFVVPNQKELTELARTKGFKGTWEELCNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVT 543
Cdd:PLN02861 551 SFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLIT 630
|
570 580
....*....|....*....|..
gi 209977076 544 DAFKLKRKELKTHYQADIERMY 565
Cdd:PLN02861 631 PTFKLKRPQLLKYYKDCIDQLY 652
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
2-550 |
7.96e-65 |
|
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: 219.15 E-value: 7.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMynfqlvtlyatLGGPAIVHGlnetevtNIITSKELLQTklkdivslvprLRH 81
Cdd:cd17640 25 LGVKAGEKVALFADNSPRWLIADQGIMA-----------LGAVDVVRG-------SDSSVEELLYI-----------LNH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 iitvdgkpptwSEfPKGVIVHTMaavqalgvkanvekkahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:cd17640 76 -----------SE-SVALVVEND---------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIPrLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLadqsskikkgsKGDTSVLKPTLMAAVPEIMDRIYKN 241
Cdd:cd17640 123 IVP-PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTL-----------KDDLKRVKPHYIVSVPRLWESLYSG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 242 VMNKVNEMSAFQRNLFILAynykmeqiskgcstplcdrfvfrnvrrLLGGNIRLLLCGGAPLSATTQRFMNIcFCCPVGQ 321
Cdd:cd17640 191 IQKQVSKSSPIKQFLFLFF---------------------------LSGGIFKFGISGGGALPPHVDTFFEA-IGIEVLN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 322 GYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNwEEGGyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeD 401
Cdd:cd17640 243 GYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVD-PEGN--VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL--D 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 402 ENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNIcayansyhsYVIG--------FV 473
Cdd:cd17640 318 SDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQI---------MVVGqdqkrlgaLI 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 474 VPNQKELTELARTKGFKGTWEELCNSSEME------NEVLKVLSEAAISASLEKFeipLKIRLSPDPWTpETGLVTDAFK 547
Cdd:cd17640 387 VPNFEELEKWAKESGVKLANDRSQLLASKKvlklykNEIKDEISNRPGFKSFEQI---APFALLEEPFI-ENGEMTQTMK 462
|
...
gi 209977076 548 LKR 550
Cdd:cd17640 463 IKR 465
|
|
| carboxyl_red |
NF041592 |
carboxylic acid reductase; |
52-565 |
2.12e-59 |
|
carboxylic acid reductase;
Pssm-ID: 469476 [Multi-domain] Cd Length: 1161 Bit Score: 213.65 E-value: 2.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 52 ETEVTNIITSKELLQtklkDIVSLV---PRLRHIITVDGKPPT-------------WSEFPkGVIVHTMAAVQALGVkan 115
Cdd:NF041592 147 ETEPRVLAASVDLLD----DAVELVltgPAPRRLVVFDYHPEVddhrealeaararLADAG-PVVVETLAEVLERGR--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 116 vEKKAHSKPLPSD---IAVIMYTSGSTGIPKGVMISHSNIiasiTGMARRIPRLGEED-----VYIGYLPLAHVLELSAE 187
Cdd:NF041592 219 -ALPAAPPPASDDddpLALLIYTSGSTGAPKGAMYTERLV----ANMWRGSARAGWGPravpsITLNFMPMSHVMGRGTL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 188 LVCLSHGcRIGYSSPQtlADQSSKIKkgskgDTSVLKPTLMAAVPEIMDRIYKNVMnkvnemSAFQRnlfilaynykmeQ 267
Cdd:NF041592 294 YGTLARG-GTAYFAAR--SDLSTLLE-----DLALVRPTELNFVPRVWDMLFQEYQ------SELDR------------R 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 268 ISKGCSTPLCDRFVFRNVRR-LLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEstgAGTITevwdyNTGRVG 346
Cdd:NF041592 348 AADGADRAAAEAAVKAELREdLLGGRFVSAMTGSAPISAEMKAFVESLLDLHLHDGYGSTE---AGGVF-----IDGRVR 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 347 APLVCcEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDI-GEFDPDGcLKII 425
Cdd:NF041592 420 RPPVL-DYKLVDVPELGYFGTDRPHPRGELLVKTTTMFPGYYKRPEVTAEVF--DEDG--FYRTGDIvAELGPDQ-LVYV 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 426 DRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPnqkelTE--LARTKgfkgtweelcNSSEME 503
Cdd:NF041592 494 DRRNNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYVYGNSARAYLLAVVVP-----TEeaLARHG----------DAAELK 558
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977076 504 NEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMY 565
Cdd:NF041592 559 ALIAESLQRVAREAGLQSYEIPRDFLIETTPFTLENGLLTGIRKLARPKLKERYGERLEQLY 620
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
128-533 |
6.36e-58 |
|
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: 196.74 E-value: 6.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAD 207
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASG-GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 208 QSSKIKKgskgdtsvLKPTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfilaynykmeqiskgcstPLCDRFVFRNVRR 287
Cdd:cd04433 80 ALELIER--------EKVTILLGVPTLLARLLKA---------------------------------PESAGYDLSSLRA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 288 LLggnirlllCGGAPLS-ATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDYNTGR--VGAPLVCCEIKLKNwEEGGy 364
Cdd:cd04433 119 LV--------SGGAPLPpELLERFEEA-PGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPVPGVEVRIVD-PDGG- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 365 fnTDKPHPRGEILIGGQNVTMGYYKNEAKTktdFFEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGK 444
Cdd:cd04433 188 --ELPPGEIGELVVRGPSVMKGYWNNPEAT---AAVDEDG--WYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVYPAE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 445 VEAALKNLPLIDnicayansyHSYVIGfvVPNQKELTELArtkgfkgTWEELCNSSEMENEVLKvlseAAISASLEKFEI 524
Cdd:cd04433 260 VEAVLLGHPGVA---------EAAVVG--VPDPEWGERVV-------AVVVLRPGADLDAEELR----AHVRERLAPYKV 317
|
....*....
gi 209977076 525 PLKIRLSPD 533
Cdd:cd04433 318 PRRVVFVDA 326
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
2-557 |
1.72e-57 |
|
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: 200.39 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEvtniitSKELLQTKLKDIVSLVPrlrh 81
Cdd:cd05932 26 LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSE------SKALFVGKLDDWKAMAP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 iiTVDGKPPTWSEFPKGVIvHTMAAVQALGVKANVEKKAhSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:cd05932 96 --GVPEGLISISLPPPSAA-NCQYQWDDLIAQHPPLEER-PTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIpRLGEEDVYIGYLPLAHVLELSA-ELVCLSHGCRIGYssPQTLADQSSKIKKGskgdtsvlKPTLMAAVPEIMDRIYK 240
Cdd:cd05932 172 HI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAF--AESLDTFVEDVQRA--------RPTLFFSVPRLWTKFQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 241 NVMNKVNEmSAFQRNLFIlaynykmeqiskgcstPLCDRFVFRNVRRLLGGN-IRLLLCGGAPLS-ATTQRFMNICFccP 318
Cdd:cd05932 241 GVQDKIPQ-QKLNLLLKI----------------PVVNSLVKRKVLKGLGLDqCRLAGCGSAPVPpALLEWYRSLGL--N 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 319 VGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKnweeggyfntdkphPRGEILIGGQNVTMGYYKNEAKTKTDF 398
Cdd:cd05932 302 ILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRIS--------------EDGEILVRSPALMMGYYKDPEATAEAF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 399 FEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAyANSYHSYVIGFVVPNqk 478
Cdd:cd05932 368 TADG----FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCV-IGSGLPAPLALVVLS-- 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 479 eltELARTKGFKGTWEELcnssemENEVLKVLseAAISASLEKFEIPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHY 557
Cdd:cd05932 441 ---EEARLRADAFARAEL------EASLRAHL--ARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2-482 |
1.67e-55 |
|
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: 194.74 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMynfqlvtlyatLGGPA-----------IVHGLNETEVTNIITSKELLQtKLK 70
Cdd:cd05911 30 LGLKKGDVVGIISPNSTYYPPVFLGCLF-----------AGGIFsaanpiytadeLAHQLKISKPKVIFTDPDGLE-KVK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 71 DIVSLVPRLRHIITVDGKPPTWSEFPKGVIVHTMAAVQALgvkanvekKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHS 150
Cdd:cd05911 98 EAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDL--------PPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 151 NIIASITGMARRIPR-LGEEDVYIGYLPLAHVLELSAELVCLSHGCRIgYSSPqtladqsskikkgsKGDTSVL------ 223
Cdd:cd05911 170 NLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLNGATV-IIMP--------------KFDSELFldliek 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 224 -KPTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfilaynykmeqiskgcstPLCDRFVFRNVRRLLggnirlllCGGAP 302
Cdd:cd05911 235 yKITFLYLVPPIAAALAKS---------------------------------PLLDKYDLSSLRVIL--------SGGAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 303 LSATTQRFMNICFC-CPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGgyfNTDKPHPRGEILIGGQ 381
Cdd:cd05911 274 LSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGK---DSLGPNEPGEICVRGP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 382 NVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICay 461
Cdd:cd05911 351 QVMKGYYNNPEATKETFDED----GWLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVAPAELEAVLLEHPGVADAA-- 423
|
490 500 510
....*....|....*....|....*....|....
gi 209977076 462 ansyhsyVIG------------FVVPNQ-KELTE 482
Cdd:cd05911 424 -------VIGipdevsgelpraYVVRKPgEKLTE 450
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
2-560 |
3.70e-55 |
|
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: 192.72 E-value: 3.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEvtniitskellqtklkdivslvprlrh 81
Cdd:COG0318 44 LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSG--------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 iitvdgkpptwsefPKGVIVhtmaavqalgvkanvekkahskplpsdiAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:COG0318 97 --------------ARALVT----------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIpRLGEEDVYIGYLPLAHVLELSAE-LVCLSHGCRI---GYSSPQTLADQsskIKKGskgdtsvlKPTLMAAVPEIMDR 237
Cdd:COG0318 135 AL-GLTPGDVVLVALPLFHVFGLTVGlLAPLLAGATLvllPRFDPERVLEL---IERE--------RVTVLFGVPTMLAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 238 IyknvmnkvnemsafqrnlfilaynykmeqiskgCSTPLCDRFVFRNVRrllggnirLLLCGGAPLSATT-QRFMNiCFC 316
Cdd:COG0318 203 L---------------------------------LRHPEFARYDLSSLR--------LVVSGGAPLPPELlERFEE-RFG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 317 CPVGQGYGLTESTGAGTIT--EVWDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKT 394
Cdd:COG0318 241 VRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVD-EDG---RELPPGEVGEIVVRGPNVMKGYWNDPEAT 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 395 KTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIG 471
Cdd:COG0318 317 AEAF---RDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAHPGVAEAAVVGvpdEKWGERVVA 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 472 FVVPNQ-KELTElartkgfkgtwEELcnssemenevlkvlsEAAISASLEKFEIPLKIRLSPD-PWTPeTGlvtdafKLK 549
Cdd:COG0318 391 FVVLRPgAELDA-----------EEL---------------RAFLRERLARYKVPRRVEFVDElPRTA-SG------KID 437
|
570
....*....|.
gi 209977076 550 RKELKTHYQAD 560
Cdd:COG0318 438 RRALRERYAAG 448
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
94-543 |
1.26e-53 |
|
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: 191.90 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 94 EFPKGVIVHTMAAVQALGVKAnvekKAHSKPLPSD--IAVIMYTSGSTGIPKGVMISHSNI----IASITGMARRIPrlg 167
Cdd:cd17632 192 AVGIPVTTLTLIAVRGRDLPP----APLFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLVatfwLKVSSIQDIRPP--- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 168 eEDVYIGYLPLAHVLELSAELVCLSHGcRIGYSSPQtlADQSSKIKkgskgDTSVLKPTLMAAVPEIMDRIYKNVMNKVN 247
Cdd:cd17632 265 -ASITLNFMPMSHIAGRISLYGTLARG-GTAYFAAA--SDMSTLFD-----DLALVRPTELFLVPRVCDMLFQRYQAELD 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 248 EMSAFQRNLFILAYNYKMEqiskgcstplcdrfvFRNvrRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTE 327
Cdd:cd17632 336 RRSVAGADAETLAERVKAE---------------LRE--RVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 328 stgAGTITEvwdynTGRVGAPLVCcEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrW 407
Cdd:cd17632 399 ---AGAVIL-----DGVIVRPPVL-DYKLVDVPELGYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAEVF--DEDG--F 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 408 LCTGDI-GEFDPDGcLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSYVIGFVVPNQKELTEL--A 484
Cdd:cd17632 466 YRTGDVmAELGPDR-LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEdtA 544
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 485 RTKGfkgtweelcnssemenEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGLVT 543
Cdd:cd17632 545 RLRA----------------ALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
18-457 |
6.65e-52 |
|
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: 187.18 E-value: 6.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 18 AEWMIAAQACFMYNFQLVTLYATlGGPAIVHGLNETEVTNII---TSKELlqTKLKDIVSLVPRLRHIITVDGKPP---- 90
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTT-NSPEACQYVAETSEANILvveNQKQL--QKILQIQDKLPHLKAIIQYKEPLKekep 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 91 ---TWSEFPKgvivhtmaavQALGVKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNI----IASITGMARRI 163
Cdd:cd05933 121 nlySWDEFME----------LGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 164 PRLGEEDVyIGYLPLAHVlelSAEL----VCLSHGCRIGYSSPQTLadqsskikKGSKGDT-SVLKPTLMAAVPEIMDRI 238
Cdd:cd05933 191 ATVGQESV-VSYLPLSHI---AAQIldiwLPIKVGGQVYFAQPDAL--------KGTLVKTlREVRPTAFMGVPRVWEKI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 239 YKNVMNKVNEMSAFQRNLFILAYNYKMEQISK---GCSTP-----LCDRFVFRNVRRLLG-GNIRLLLCGGAPLSATTQR 309
Cdd:cd05933 259 QEKMKAVGAKSGTLKRKIASWAKGVGLETNLKlmgGESPSplfyrLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 310 F---MNIcfccPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGYfntdkphprGEILIGGQNVTMG 386
Cdd:cd05933 339 FflsLNI----PIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGI---------GEICFWGRHVFMG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977076 387 YYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKN-LPLIDN 457
Cdd:cd05933 406 YLNMEDKTEEAI--DEDG--WLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKeLPIISN 473
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-455 |
1.52e-50 |
|
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: 180.72 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 121 HSKPL------PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMaRRIPRLGEEDVYIGYLPLAHVLELSAELVC-LSH 193
Cdd:cd05914 77 HSEAKaifvsdEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGV-KEVVLLGKGDKILSILPLHHIYPLTFTLLLpLLN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 194 GCRIGY----SSPQTLADQSSKIkkgskgdtsvlKPTLMAAVPEIMDRIYKNV-MNKVNemsaFQRNLFILAYNYKMEQI 268
Cdd:cd05914 156 GAHVVFldkiPSAKIIALAFAQV-----------TPTLGVPVPLVIEKIFKMDiIPKLT----LKKFKFKLAKKINNRKI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 269 SKgcstplcdrFVFRNVRRLLGGNIRLLLCGGAPLSATTQRF---MNICFCcpvgQGYGLTEsTGAGTITEVWD-YNTGR 344
Cdd:cd05914 221 RK---------LAFKKVHEAFGGNIKEFVIGGAKINPDVEEFlrtIGFPYT----IGYGMTE-TAPIISYSPPNrIRLGS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 345 VGAPLVCCEIKlknweeggyfnTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGC 421
Cdd:cd05914 287 AGKVIDGVEVR-----------IDSPDPAtgeGEIIVRGPNVMKGYYKNPEATAEAF--DKDG--WFHTGDLGKIDAEGY 351
|
330 340 350
....*....|....*....|....*....|....
gi 209977076 422 LKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLI 455
Cdd:cd05914 352 LYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
2-449 |
1.75e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 168.06 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTkLKDIVSLVPRLRH 81
Cdd:PRK06187 51 LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPL-LAAILPQLPTVRT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IITVDGKP-----PTWSEFpkgvivHTMAAVQAlgvkanvEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASI 156
Cdd:PRK06187 130 VIVEGDGPaaplaPEVGEY------EELLAAAS-------DTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 157 TGMARRIpRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYS---SPQTLADQsskIKKgskgdtsvLKPTLMAAVPE 233
Cdd:PRK06187 197 LAVCAWL-KLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 234 IMDriyknvmnkvnemsafqrnlFILAYnykmeqiskgcstPLCDrfvFRNVRRLlggniRLLLCGGAPLSATT-QRFMN 312
Cdd:PRK06187 265 IWQ--------------------MLLKA-------------PRAY---FVDFSSL-----RLVIYGGAALPPALlREFKE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 313 IcFCCPVGQGYGLTESTGAGTI-------TEVWDY--NTGRVgAPLVccEIKLKNwEEGgyfntdKPHPR-----GEILI 378
Cdd:PRK06187 304 K-FGIDLVQGYGMTETSPVVSVlppedqlPGQWTKrrSAGRP-LPGV--EARIVD-DDG------DELPPdggevGEIIV 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209977076 379 GGQNVTMGYYKNEAKTKtDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAAL 449
Cdd:PRK06187 373 RGPWLMQGYWNRPEATA-ETIDGG----WLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELEDAL 437
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
2-455 |
9.92e-45 |
|
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: 166.83 E-value: 9.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEW---MIAAQACFMYNfqlVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSLVPR 78
Cdd:cd17641 31 LGVGRGDVVAILGDNRPEWvwaELAAQAIGALS---LGIYQDSMAEEVAYLLNYTGARVVIAEDEEQVDKLLEIADRIPS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 79 LRHIITVDgkpptwsefPKGVIVHT---MAAVQALGVKANVEKKAHSKPL--------PSDIAVIMYTSGSTGIPKGVMI 147
Cdd:cd17641 108 VRYVIYCD---------PRGMRKYDdprLISFEDVVALGRALDRRDPGLYerevaagkGEDVAVLCTTSGTTGKPKLAML 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 148 SHSNIIASITGMARRIPRlGEEDVYIGYLPLAHVLE----LSAELVClshGCRIGY-SSPQTLadqsskikkgsKGDTSV 222
Cdd:cd17641 179 SHGNFLGHCAAYLAADPL-GPGDEYVSVLPLPWIGEqmysVGQALVC---GFIVNFpEEPETM-----------MEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 223 LKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLF---------ILAYNYKMEQISKGCSTP--LCDRFVFRNVRRLLG- 290
Cdd:cd17641 244 IGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFelgmklglrALDRGKRGRPVSLWLRLAswLADALLFRPLRDRLGf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 291 GNIRLLLCGGAPLSATTQRF---MNIcfccPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNweeggyfnt 367
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE--------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 368 dkphpRGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVSLGKVEA 447
Cdd:cd17641 391 -----VGEILVRSPGVFVGYYKNPEATAEDFDEDG----WLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIEN 461
|
....*...
gi 209977076 448 ALKNLPLI 455
Cdd:cd17641 462 KLKFSPYI 469
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
126-463 |
1.44e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 159.88 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLG-EEDVYIGYLPLAHVLELSAELVCLSHGCRIgysspqt 204
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKyNPKTHLSYLPISHIYERVIAYLSFMLGGTI------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 205 laDQSSK-IKKGSKgDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLF--ILA-----YNYKMEQISKGCSTpl 276
Cdd:PTZ00342 376 --NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVkkILSlrksnNNGGFSKFLEGITH-- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 277 cdrfVFRNVRRLLGGNIRLLLCGGAPLSATTQR----FMNICFCcpvgQGYGLTESTGAGTITEVWDYNTGRVGAPLV-C 351
Cdd:PTZ00342 451 ----ISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYGLTETTGPIFVQHADDNNTESIGGPISpN 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 CEIKLKNWEEggYFNTDKPhPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGEFDPDGCLKIIDRKKDL 431
Cdd:PTZ00342 523 TKYKVRTWET--YKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTED----GYFKTGDIVQINKNGSLTFLDRSKGL 595
|
330 340 350
....*....|....*....|....*....|..
gi 209977076 432 VKLQAGEYVSLGKVEAALKNLPLIDNICAYAN 463
Cdd:PTZ00342 596 VKLSQGEYIETDMLNNLYSQISFINFCVVYGD 627
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
126-455 |
3.50e-38 |
|
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: 147.00 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITG-MARRIPRLGEEDVYIGYLPLAHVLELSAELVCLSH-GCRI----GY 199
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQfVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRlGATVvvmpRF 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 SSPQTL-ADQSSKIkkgskgdtsvlkpTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfilaynykmeqiskgcstPLCD 278
Cdd:cd05904 237 DLEELLaAIERYKV-------------THLPVVPPIVLALVKS---------------------------------PIVD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 279 RFVFRNVRRLLggnirlllCGGAPLSATT-----QRFMNicfcCPVGQGYGLTESTGAGTITEVWDYNTGRVG-----AP 348
Cdd:cd05904 271 KYDLSSLRQIM--------SGAAPLGKELieafrAKFPN----VDLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 349 LVccEIKLKNWEEGgyfntdKPHP---RGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKII 425
Cdd:cd05904 339 NV--EAKIVDPETG------ESLPpnqTGELWIRGPSIMKGYLNNPEATAATI--DKEG--WLHTGDLCYIDEDGYLFIV 406
|
330 340 350
....*....|....*....|....*....|
gi 209977076 426 DRKKDLVKLQaGEYVSLGKVEAALKNLPLI 455
Cdd:cd05904 407 DRLKELIKYK-GFQVAPAELEALLLSHPEI 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
126-432 |
3.56e-38 |
|
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: 146.55 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGE-EDVYIGYLPLAHVLELSaelVCLSHGCRIGYsspqt 204
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEgDDVVLAALPLFHVFGLT---VALLLPLALGA----- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 205 ladqsskikkgskgdTSVLKPTLMAavpeimdriyKNVMNkvnEMSAFQRNLFILA---YNYKMEqiskgcstplcdrfv 281
Cdd:cd05936 196 ---------------TIVLIPRFRP----------IGVLK---EIRKHRVTIFPGVptmYIALLN--------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 282 FRNVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYN-TGRVGAPLVCCEIKLKNwE 360
Cdd:cd05936 233 APEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-D 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977076 361 EGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:cd05936 312 DG---EELPPGEVGELWVRGPQVMKGYWNRPEETAEAF---VDG--WLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
122-455 |
8.33e-34 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 132.86 E-value: 8.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 122 SKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiprLG--EEDVYIGYLPLAHVLELSAELVCLSHGCRIgY 199
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALN---LGltEDDNWLCALPLFHISGLSILMRSVIYGMTV-Y 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 SSPQTLADQSSKIKKGSKGdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrnlfilaynykMEQISKGCSTplcdr 279
Cdd:cd05912 148 LVDKFDAEQVLHLINSGKV-------TIISVVPTMLQRL--------------------------LEILGEGYPN----- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 280 fvfrnvrrllggNIRLLLCGGAPLSATT-----QRfmNIcfccPVGQGYGLTEsTGAGTITEVWDY---NTGRVGAPLVC 351
Cdd:cd05912 190 ------------NLRCILLGGGPAPKPLleqckEK--GI----PVYQSYGMTE-TCSQIVTLSPEDalnKIGSAGKPLFP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 CEIKLKNweeggyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDL 431
Cdd:cd05912 251 VELKIED-------DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF---ENG--WFKTGDIGYLDEEGFLYVLDRRSDL 318
|
330 340
....*....|....*....|....
gi 209977076 432 VkLQAGEYVSLGKVEAALKNLPLI 455
Cdd:cd05912 319 I-ISGGENIYPAEIEEVLLSHPAI 341
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
122-482 |
1.25e-33 |
|
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: 133.12 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 122 SKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIAS--ITGMARRIprlGEEDVYIGYLPLAHVLELSaelvclshgcriGY 199
Cdd:cd17631 93 AKVLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNavNALAALDL---GPDDVLLVVAPLFHIGGLG------------VF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 SSPQTLADQSSKIKKGSKGDTsVL------KPTLMAAVPEIMdriyknvmnkvnemsafqrnlfilaynYKMEQiskgcs 273
Cdd:cd17631 158 TLPTLLRGGTVVILRKFDPET-VLdlierhRVTSFFLVPTMI---------------------------QALLQ------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 274 tplCDRFVFRNVRRLlggniRLLLCGGAPLSATTQRFMnICFCCPVGQGYGLTESTGAGTITEVWDYNT--GRVGAPLVC 351
Cdd:cd17631 204 ---HPRFATTDLSSL-----RAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 CEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDL 431
Cdd:cd17631 275 VEVRIVD-PDG---REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF---RDG--WFHTGDLGRLDEDGYLYIVDRKKDM 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209977076 432 VKlQAGEYVSLGKVEAALKNLPLIDNiCAyansyhsyVIG------------FVVPNQK-ELTE 482
Cdd:cd17631 346 II-SGGENVYPAEVEDVLYEHPAVAE-VA--------VIGvpdekwgeavvaVVVPRPGaELDE 399
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
126-490 |
5.03e-33 |
|
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: 131.60 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAHVLELSAELVCLSHGcrigysspQTL 205
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGPGDVFLNQAPFSFDLSVMDLYPALASG--------ATL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 AdqsskikkgskgdtsvlkptlmaAVPEimdriyknvmnkvnEMSAFQRNLFilAYNYKMeQISKGCSTP----LCDRFV 281
Cdd:cd05945 167 V-----------------------PVPR--------------DATADPKQLF--RFLAEH-GITVWVSTPsfaaMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 282 FRNVRRLlgGNIRL-LLCGGAPLSATTQRFMNiCF-CCPVGQGYGLTESTGAGTITEV-----WDYNTGRVGAPLVCCEI 354
Cdd:cd05945 207 TFTPESL--PSLRHfLFCGEVLPHKTARALQQ-RFpDARIYNTYGPTEATVAVTYIEVtpevlDGYDRLPIGYAKPGAKL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 355 KLknWEEGGyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDEnGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKL 434
Cdd:cd05945 284 VI--LDEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-GQRAYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 435 QaGEYVSLGKVEAALKNLPLIDNICA---YANSYHSYVIGFVVPnqKELTELARTKGFK 490
Cdd:cd05945 359 N-GYRIELEEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVP--KPGAEAGLTKAIK 414
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
109-462 |
1.22e-31 |
|
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: 128.20 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 109 ALGVKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSAel 188
Cdd:cd05926 131 SNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTY-KLTPDDRTLVVMPLFHVHGLVA-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 189 VCLShgcrigysspqTLADQSSKIK----KGSK--GDTSVLKPTLMAAVPEIMDRIYKNVM-NKVNEMSAFqrnlfilay 261
Cdd:cd05926 208 SLLS-----------TLAAGGSVVLpprfSASTfwPDVRDYNATWYTAVPTIHQILLNRPEpNPESPPPKL--------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 262 nykmeqiskgcstplcdRFvfrnvrrllggnIRlllCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTIT--EVWD 339
Cdd:cd05926 268 -----------------RF------------IR---SCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 340 YNTGRVGAPlVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGEFDPD 419
Cdd:cd05926 316 RKPGSVGKP-VGVEVRILD-EDG---EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD----GWFRTGDLGYLDAD 386
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 209977076 420 GCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAYA 462
Cdd:cd05926 387 GYLFLTGRIKELIN-RGGEKISPLEVDGVLLSHPAVLEAVAFG 428
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2-432 |
4.61e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 126.56 E-value: 4.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTkLKDIVSLVPRLRH 81
Cdd:PRK07656 50 LGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGV-DYSATTRLPALEH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IITVdgkpPTWSEFPKGVIVHTMAAVQALGVKANVEKKAHskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAr 161
Cdd:PRK07656 129 VVIC----ETEEDDPHTEKMKTFTDFLAAGDPAERAPEVD----PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWA- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIPRLGEEDVYIGYLPLAHVLELSAELV-CLSHGCRI----GYSSPQTLAdqssKIKKGskgdtsvlKPTLMAAVPEImd 236
Cdd:PRK07656 200 EYLGLTEGDRYLAANPFFHVFGYKAGVNaPLMRGATIlplpVFDPDEVFR----LIETE--------RITVLPGPPTM-- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 237 riyknvmnkvnemsafqrnlfilaYNYkMEQISKGCSTPLcdrfvfrnvrrllgGNIRLLLCGGA--PLsATTQRFMNIC 314
Cdd:PRK07656 266 ------------------------YNS-LLQHPDRSAEDL--------------SSLRLAVTGAAsmPV-ALLERFESEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 315 FCCPVGQGYGLTESTGAGTIT---EVWDYNTGRVGAPLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNE 391
Cdd:PRK07656 306 GVDIVLTGYGLSEASGVTTFNrldDDRKTVAGTIGTAIAGVENKIVN-ELGEEVPVGEV---GELLVRGPNVMKGYYDDP 381
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 209977076 392 AKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK07656 382 EATAAAI--DADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
80-460 |
5.37e-31 |
|
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: 125.07 E-value: 5.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 80 RHIITVDGKPPTWSEFPKGVIVHTMAAVQALGvKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGM 159
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALD-DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 160 ARRIPrLGEEDVYIGYLPLAH---VLELsaeLVCLSHGCRIgysspqtladqsskikkgskgdtsvlkptlmAAVPEIMD 236
Cdd:TIGR01733 153 ARRYG-LDPDDRVLQFASLSFdasVEEI---FGALLAGATL-------------------------------VVPPEDEE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 237 RiyknvmnkvnemsAFQRNLFILAYNYKmeqISKGCSTP-LCDRFVFRNVRRLLGgnIRLLLCGGAPLSATT-----QRF 310
Cdd:TIGR01733 198 R-------------DDAALLAALIAEHP---VTVLNLTPsLLALLAAALPPALAS--LRLVILGGEALTPALvdrwrARG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 311 MNICFCcpvgQGYGLTESTGAGTITEVWDYNTGR-----VGAPLVCCEIKLKNweeggyfNTDKPHPR---GEILIGGQN 382
Cdd:TIGR01733 260 PGARLI----NLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRLYVLD-------DDLRPVPVgvvGELYIGGPG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 383 VTMGYYKNEAKTKTDFFED----ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNI 458
Cdd:TIGR01733 329 VARGYLNRPELTAERFVPDpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLRHPGVREA 407
|
..
gi 209977076 459 CA 460
Cdd:TIGR01733 408 VV 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
124-462 |
7.36e-31 |
|
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: 125.19 E-value: 7.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 124 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAHVlelsaelvclshgcrIGYSSPQ 203
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG-LGPGDVFLVASPMAHQ---------------TGFVYGF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 204 TLAdqsskikkgskgdtsvlkptLMAAVPEIMDRIYKnvMNKVNEMSAFQRNLFILAYNYKMEQI---SKGCSTPLCDrf 280
Cdd:cd05903 154 TLP--------------------LLLGAPVVLQDIWD--PDKALALMREHGVTFMMGATPFLTDLlnaVEEAGEPLSR-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 vfrnvrrllggnIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWD-----YNTGRVGAPLvccEIK 355
Cdd:cd05903 210 ------------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrlYTDGRPLPGV---EIK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 356 LKNweegGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQ 435
Cdd:cd05903 275 VVD----DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-----WFRTGDLARLDEDGYLRITGRSKDII-IR 344
|
330 340
....*....|....*....|....*..
gi 209977076 436 AGEYVSLGKVEAALKNLPLIDNICAYA 462
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
29-460 |
1.93e-29 |
|
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: 121.67 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 29 MYNFqlvtlyaTLGGPAIVHGLNETEVTNIITSKELLQtKLK-----------DIVSLvPRLRHIITVDGK--------- 88
Cdd:cd05909 60 MLNY-------TAGLRELRACIKLAGIKTVLTSKQFIE-KLKlhhlfdveydaRIVYL-EDLRAKISKADKckaflagkf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 89 PPTWSEFPKGVivhtmaavqalgvkanvekkahSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGE 168
Cdd:cd05909 131 PPKWLLRIFGV----------------------APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIF-DPNP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 169 EDVYIGYLPLAHVLELSAELVclshgcrigysSPQTladqsskikkgsKGDTSVLKPTLMAA--VPEImdrIYKNvmnKV 246
Cdd:cd05909 188 EDVVFGALPFFHSFGLTGCLW-----------LPLL------------SGIKVVFHPNPLDYkkIPEL---IYDK---KA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 247 NemsafqrnlfILaynykmeqiskgCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLSATT-QRFMNIcFCCPVGQGYGL 325
Cdd:cd05909 239 T----------IL------------LGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLrQEFQEK-FGIRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 326 TESTGAGTITEVW-DYNTGRVGAPLVCCEIKLKNWEeggyfnTDKPHPRGE---ILIGGQNVTMGYYKNEAKTKTDFfed 401
Cdd:cd05909 296 TECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVE------THEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF--- 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 402 enGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNICA 460
Cdd:cd05909 367 --GDGWYDTGDIGKIDGEGFLTITGRLSRFAKI-AGEMVSLEAIEDILSEILPEDNEVA 422
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
126-479 |
1.55e-28 |
|
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: 118.40 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLA---HVLEL------SAELVCLSHGCR 196
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSfdvSVWEIfgallaGATLVVLPEEVR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 197 igySSPQTLAD--QSSKIkkgskgdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrnlfiLAYNYkmeqiskgcst 274
Cdd:cd05930 171 ---KDPEALADllAEEGI-------------TVLHLTPSLLRLL--------------------LQELE----------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 275 plcdrfvFRNVRRLlggniRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESTGAGTITEV----WDYNTGRVGAPL 349
Cdd:cd05930 204 -------LAALPSL-----RLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATYYRVppddEEDGRVPIGRPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 350 VCCEIKLKNweEGGyfntdKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED-ENGQRWLC-TGDIGEFDPDGCLKI 424
Cdd:cd05930 272 PNTRVYVLD--ENL-----RPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPNpFGPGERMYrTGDLVRWLPDGNLEF 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 209977076 425 IDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDN---ICAYANSYHSYVIGFVVPNQKE 479
Cdd:cd05930 345 LGRIDDQVKI-RGYRIELGEIEAALLAHPGVREaavVAREDGDGEKRLVAYVVPDEGG 401
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
128-455 |
1.84e-28 |
|
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: 118.16 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSAELVC-LSHGcrigySSPQTLA 206
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW-RWTEDDVLLHVLPLHHVHGLVNALLCpLFAG-----ASVEFLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 207 DQSSKIKKGSKGDTSVlkpTLMAAVPEIMDRIyknvmnkvneMSAFQRNLfilaynYKMEQISKGCStplcdrfvfrnvr 286
Cdd:cd05941 164 KFDPKEVAISRLMPSI---TVFMGVPTIYTRL----------LQYYEAHF------TDPQFARAAAA------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 287 rllgGNIRLLLCGGAPLSATT-QRFMNIcfccpVGQG----YGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEE 361
Cdd:cd05941 212 ----ERLRLMVSGSAALPVPTlEEWEAI-----TGHTllerYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEET 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 362 GGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFFEDengqRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAGEYVS 441
Cdd:cd05941 283 GEPLPRGEV---GEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVS 355
|
330
....*....|....
gi 209977076 442 LGKVEAALKNLPLI 455
Cdd:cd05941 356 ALEIERVLLAHPGV 369
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
128-462 |
3.16e-28 |
|
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: 117.01 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAHV--LELSAeLVCLSHGCRIgysspqTL 205
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG-LGEDDVYLTVLPLFHInaQAVSV-LAALSVGATL------VL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 ADQSS------KIKKgsKGDT-----SVLKPTLMAAVPEIMDRiyknvMNKVnemsafqrnlfilaynykmeqiskgcst 274
Cdd:cd05934 154 LPRFSasrfwsDVRR--YGATvtnylGAMLSYLLAQPPSPDDR-----AHRL---------------------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 275 plcdRFVFrnvrrllggnirlllcGGAPLSATTQRFMNIcFCCPVGQGYGLTEsTGAGTITEVWDYN-TGRVGAPLVCCE 353
Cdd:cd05934 199 ----RAAY----------------GAPNPPELHEEFEER-FGVRLLEGYGMTE-TIVGVIGPRDEPRrPGSIGRPAPGYE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 354 IKLKNWEeggyfntDKPHPR---GEILI---GGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDR 427
Cdd:cd05934 257 VRIVDDD-------GQELPAgepGELVIrglRGWGFFKGYYNMPEATAEAM---RNG--WFHTGDLGYRDADGFFYFVDR 324
|
330 340 350
....*....|....*....|....*....|....*
gi 209977076 428 KKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAYA 462
Cdd:cd05934 325 KKDMIR-RRGENISSAEVERAILRHPAVREAAVVA 358
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
21-449 |
6.59e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 119.26 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 21 MIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQT-KLKDIVSLVPRLRHIITVDGKPPTWSEFPKgv 99
Cdd:PRK08633 679 ALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKlKNKGFDLELPENVKVIYLEDLKAKISKVDK-- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 100 iVHTMAAVQALGvKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMaRRIPRLGEEDVYIGYLPLA 179
Cdd:PRK08633 757 -LTALLAARLLP-ARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQI-SDVFNLRNDDVILSSLPFF 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 180 HVLELSAEL-VCLSHGCRIGYSSPQTLADQSSK-IKKgskgdtsvLKPTLMAAVPEIMdRIY-KNvmNKVN-EMsaFQRN 255
Cdd:PRK08633 834 HSFGLTVTLwLPLLEGIKVVYHPDPTDALGIAKlVAK--------HRATILLGTPTFL-RLYlRN--KKLHpLM--FASL 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 256 LFILAYNYKMEQiskgcstPLCDRFVFRNvrrllggNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESTGAGT-- 333
Cdd:PRK08633 901 RLVVAGAEKLKP-------EVADAFEEKF-------GIRIL------------------------EGYGATETSPVASvn 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 334 -----ITEVW---DYNTGRVGAPLVCCEIKLKNWEeggyfnTDKPHPRGE---ILIGGQNVTMGYYKNEAKTKtDFFEDE 402
Cdd:PRK08633 943 lpdvlAADFKrqtGSKEGSVGMPLPGVAVRIVDPE------TFEELPPGEdglILIGGPQVMKGYLGDPEKTA-EVIKDI 1015
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 209977076 403 NGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAAL 449
Cdd:PRK08633 1016 DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
127-458 |
7.58e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.99 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 127 SDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiprLG--EEDVYIGYLPLAHVLELSAELVCLSHGCRIgYSSPQT 204
Cdd:PRK03640 141 DEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALN---LGltEDDCWLAAVPIFHISGLSILMRSVIYGMRV-VLVEKF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 205 LADQSSKIKKGSKGdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrnlfilaynykMEQISKGcSTPlcdrfvfrn 284
Cdd:PRK03640 217 DAEKINKLLQTGGV-------TIISVVSTMLQRL--------------------------LERLGEG-TYP--------- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 285 vrrllgGNIRLLLCGGAPLSATT-----QRfmNIcfccPVGQGYGLTEsTGAGTITEVWDY---NTGRVGAPLVCCEIKL 356
Cdd:PRK03640 254 ------SSFRCMLLGGGPAPKPLleqckEK--GI----PVYQSYGMTE-TASQIVTLSPEDaltKLGSAGKPLFPCELKI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 -KNWEEGgyfntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQ 435
Cdd:PRK03640 321 eKDGVVV------PPFEEGEIVVKGPNVTKGYLNREDATRETF---QDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-IS 388
|
330 340
....*....|....*....|...
gi 209977076 436 AGEYVSLGKVEAALKNLPLIDNI 458
Cdd:PRK03640 389 GGENIYPAEIEEVLLSHPGVAEA 411
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
46-455 |
2.41e-27 |
|
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: 116.09 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 46 IVHGLNETEVTNIITSKELLQtKLKDIVSLVPRLRHIITVDGKPP--TWSEFPKGVIVHTMAAVQALGVKANVEKKahsk 123
Cdd:cd17642 108 LDHSLNISKPTIVFCSKKGLQ-KVLNVQKKLKIIKTIIILDSKEDykGYQCLYTFITQNLPPGFNEYDFKPPSFDR---- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 124 plPSDIAVIMYTSGSTGIPKGVMISHSNIIASITgmARRIPRLG----EEDVYIGYLPLAHVLELSAELVCLSHGCRIGY 199
Cdd:cd17642 183 --DEQVALIMNSSGSTGLPKGVQLTHKNIVARFS--HARDPIFGnqiiPDTAILTVIPFHHGFGMFTTLGYLICGFRVVL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 SSP-------QTLADQsskikkgsKGDTSVLKPTLMAAVPEimdriyknvmnkvnemsafqrnlfilaynykmeqiskgc 272
Cdd:cd17642 259 MYKfeeelflRSLQDY--------KVQSALLVPTLFAFFAK--------------------------------------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 273 sTPLCDRFVFrnvrrllgGNIRLLLCGGAPLSATTQRFMNICFCCP-VGQGYGLTESTGAGTITEVWDYNTGRVGAPLVC 351
Cdd:cd17642 292 -STLVDKYDL--------SNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 CEIKLKNWEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTdfFEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDL 431
Cdd:cd17642 363 FYAKVVDLDTG---KTLGPNERGELCVKGPMIMKGYVNNPEATKA--LIDKDG--WLHSGDIAYYDEDGHFFIVDRLKSL 435
|
410 420
....*....|....*....|....
gi 209977076 432 VKLQaGEYVSLGKVEAALKNLPLI 455
Cdd:cd17642 436 IKYK-GYQVPPAELESILLQHPKI 458
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
36-432 |
2.20e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 113.51 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 36 TLYATLGG---------------PAIVHGLNETEVTNIITSKELLQT----KLKDIVSLVPRLRHIITVDGKPPTWSefP 96
Cdd:PRK07529 96 THFALWGGeaagianpinpllepEQIAELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVDLARYLPG--P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 97 KGVIVHTM---AAVQALGVKANVEKK------AHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASiTGMARRIPRLG 167
Cdd:PRK07529 174 KRLAVPLIrrkAHARILDFDAELARQpgdrlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLGALLLGLG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 168 EEDVYIGYLPLAHVLELSAE-LVCLSHGCRIGYSSPQtladqsskikkGSKGdtsvlkptlmaavPEIMDRIYKNVMN-K 245
Cdd:PRK07529 253 PGDTVFCGLPLFHVNALLVTgLAPLARGAHVVLATPQ-----------GYRG-------------PGVIANFWKIVERyR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 246 VNEMSAFQRnlfilAYNYKMEQISKGcstplcdrfvfRNVRRLlggniRLLLCGGAPLS-ATTQRFMN---IcfccPVGQ 321
Cdd:PRK07529 309 INFLSGVPT-----VYAALLQVPVDG-----------HDISSL-----RYALCGAAPLPvEVFRRFEAatgV----RIVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 322 GYGLTESTGAGTITEV-WDYNTGRVGAPLVCCEIK-LKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYkNEAKTKTDFF 399
Cdd:PRK07529 364 GYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRvVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL 442
|
410 420 430
....*....|....*....|....*....|...
gi 209977076 400 EDengqRWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK07529 443 ED----GWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
121-457 |
3.94e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 112.40 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 121 HSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITgMARR-IPRLGEED-VYIGYLPLAHVLELSaelVCLSHGCRIG 198
Cdd:PRK05605 213 HPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA-QGKAwVPGLGDGPeRVLAALPMFHAYGLT---LCLTLAVSIG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 199 -----YSSPQtlADQSSKIKKGSKgdtsvlkPTLMAAVPEIMDRIYKnvmnkvnemSAFQRNLFIlaynykmeqisKGcs 273
Cdd:PRK05605 289 gelvlLPAPD--IDLILDAMKKHP-------PTWLPGVPPLYEKIAE---------AAEERGVDL-----------SG-- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 274 tplcdrfvfrnvrrllggnIRLLLCGGAPLSATTqrfmnicfccpVGQ-----------GYGLTEST---GAGTITEvwD 339
Cdd:PRK05605 338 -------------------VRNAFSGAMALPVST-----------VELwekltggllveGYGLTETSpiiVGNPMSD--D 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 340 YNTGRVGAPLVCCEIKLKNWEeggyfNTDKPHP---RGEILIGGQNVTMGYYKNEAKTKtDFFEDEngqrWLCTGDIGEF 416
Cdd:PRK05605 386 RRPGYVGVPFPDTEVRIVDPE-----DPDETMPdgeEGELLVRGPQVFKGYWNRPEETA-KSFLDG----WFRTGDVVVM 455
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 209977076 417 DPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDN 457
Cdd:PRK05605 456 EEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
128-478 |
6.62e-25 |
|
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: 105.81 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNII-ASITGMArrIPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCR---IGYSSPQ 203
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANLQLIH--AMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 204 TLAD--QSSKIkkgskgdtsvlkpTLMAAVPEIMDRIyknvmnkvnemsafqrnlfilaynykMEQISKGCSTPLCDRFV 281
Cdd:cd17637 79 EALEliEEEKV-------------TLMGSFPPILSNL--------------------------LDAAEKSGVDLSSLRHV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 282 FrnvrrllggnirlllcgGAPLSATTQRFMNIC---FCCpvgqGYGLTESTGAGTITEVWDyNTGRVGAPLVCCEIKLKN 358
Cdd:cd17637 120 L-----------------GLDAPETIQRFEETTgatFWS----LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 359 weeggyfNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRK--KDLVK 433
Cdd:cd17637 178 -------DNDRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTF---RNG--WHHTGDLGRFDEDGYLWYAGRKpeKELIK 245
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 209977076 434 lQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIGfvVPNQK 478
Cdd:cd17637 246 -PGGENVYPAEVEKVILEHPAIAEVC---------VIG--VPDPK 278
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
2-461 |
6.75e-25 |
|
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: 108.33 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQtKLKDIVSLVPRLRH 81
Cdd:TIGR03098 45 LGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSSERLD-LLHPALPGCHDLRT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IITVDGKPPTwSEFPKGVIVHTMAAVQALGVKAnvekkAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:TIGR03098 124 LIIVGDPAHA-SEGHPGEEPASWPKLLALGDAD-----PPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVAT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIpRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRI---GYSSPQTLADqsSKIKKGSKGdtsvlkptlMAAVPEIMDRi 238
Cdd:TIGR03098 198 YL-ENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhDYLLPRDVLK--ALEKHGITG---------LAAVPPLWAQ- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 239 yknvmnkvnemsafqrnLFILAYnykmeqiskgcstPLCDrfvFRNVRRLLGGnirlllcGGAPLSATTQRFMNICFCCP 318
Cdd:TIGR03098 265 -----------------LAQLDW-------------PESA---APSLRYLTNS-------GGAMPRATLSRLRSFLPNAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 319 VGQGYGLTESTGAGTI-TEVWDYNTGRVGAPLVCCEIKLKNwEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTD 397
Cdd:TIGR03098 305 LFLMYGLTEAFRSTYLpPEEVDRRPDSIGKAIPNAEVLVLR-EDGSEC---APGEEGELVHRGALVAMGYWNDPEKTAER 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209977076 398 F-----FEDEN--GQRWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAY 461
Cdd:TIGR03098 381 FrplppFPGELhlPELAVWSGDTVRRDEEGFLYFVGRRDEMIK-TSGYRVSPTEVEEVAYATGLVAEAVAF 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
122-475 |
7.42e-25 |
|
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: 107.74 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 122 SKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAH---------VLELSAELVCLS 192
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRF-AVGPDDRVLALSSLSFdlsvydifgALSAGATLVLPD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 193 HGCRigySSPQTLAD--QSSKIkkgskgdtsvlkpTLMAAVPEIMdriyknvmnkvnEMsafqrnlfilaynykmeqisk 270
Cdd:cd12114 200 EARR---RDPAHWAEliERHGV-------------TLWNSVPALL------------EM--------------------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 271 gcstpLCDrfVFRNVRRLLGGnIRLLLCGG--APLS---ATTQRFMNicfCCPVGQGyGLTESTGAGTITEVWDYNTGRV 345
Cdd:cd12114 231 -----LLD--VLEAAQALLPS-LRLVLLSGdwIPLDlpaRLRALAPD---ARLISLG-GATEASIWSIYHPIDEVPPDWR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 346 ----GAPLvcceiklknweEGGYFNTDKPHPR-------GEILIGGQNVTMGYYKNEAKTKTDFFEDENGQRWLCTGDIG 414
Cdd:cd12114 299 sipyGRPL-----------ANQRYRVLDPRGRdcpdwvpGELWIGGRGVALGYLGDPELTAARFVTHPDGERLYRTGDLG 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209977076 415 EFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICA--YANSYHSYVIGFVVP 475
Cdd:cd12114 368 RYRPDGTLEFLGRRDGQVKVR-GYRIELGEIEAALQAHPGVARAVVvvLGDPGGKRLAAFVVP 429
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
126-485 |
5.22e-23 |
|
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: 104.17 E-value: 5.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAH---VLELsaeLVCLSHGCRI----- 197
Cdd:COG1020 616 PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG-LGPGDRVLQFASLSFdasVWEI---FGALLSGATLvlapp 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 -GYSSPQTLAD--QSSKIkkgskgdtsvlkpTLMAAVPeimdriyknvmnkvnemSAFQrnLFIlaynykmEQISKGCST 274
Cdd:COG1020 692 eARRDPAALAEllARHRV-------------TVLNLTP-----------------SLLR--ALL-------DAAPEALPS 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 275 PlcdrfvfrnvrrllggniRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGR----VGAPL 349
Cdd:COG1020 733 L------------------RLVLVGGEALPPELvRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsvpIGRPI 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 350 VcceiklknweeggyfNT-----DK---PHP---RGEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGE 415
Cdd:COG1020 795 A---------------NTrvyvlDAhlqPVPvgvPGELYIGGAGLARGYLNRPELTAERFVADpfgFPGARLYRTGDLAR 859
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209977076 416 FDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVPNQKELTELAR 485
Cdd:COG1020 860 WLPDGNLEFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAredAPGDKRLVAYVVPEAGAAAAAAL 931
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-438 |
5.24e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 102.93 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSK--------ELLQTKLKDIV 73
Cdd:PRK12583 65 LGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsdyhAMLQELLPGLA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 74 SL---------VPRLRHIITVDGKPP----TWSEF---PKGVIVHTMAAVQAlgvkanvekkahsKPLPSDIAVIMYTSG 137
Cdd:PRK12583 145 EGqpgalacerLPELRGVVSLAPAPPpgflAWHELqarGETVSREALAERQA-------------SLDRDDPINIQYTSG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 138 STGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAH----VLelsAELVCLSHGCRIGYssPQTLADQSSKIK 213
Cdd:PRK12583 212 TTGFPKGATLSHHNILNNGYFVAESL-GLTEHDRLCVPVPLYHcfgmVL---ANLGCMTVGACLVY--PNEAFDPLATLQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 214 KGSKGdtsvlKPTLMAAVPEIMdriyknvmnkVNEMSAFQRNLFILAynykmeqiskgcstplcdrfvfrnvrrllggNI 293
Cdd:PRK12583 286 AVEEE-----RCTALYGVPTMF----------IAELDHPQRGNFDLS-------------------------------SL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 294 RLLLCGGAP-LSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGR---VGAPLVCCEIKLKNwEEGgyfNTDK 369
Cdd:PRK12583 320 RTGIMAGAPcPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRvetVGRTQPHLEVKVVD-PDG---ATVP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 370 PHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGE 438
Cdd:PRK12583 396 RGEIGELCTRGYSVMKGYWNNPEATAESI--DEDG--WMHTGDLATMDEQGYVRIVGRSKDMI-IRGGE 459
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
124-457 |
8.66e-23 |
|
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: 101.60 E-value: 8.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 124 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiPRLGEEDVYIGYLPLA---HVLELsaeLVCLSHGCRIGYS 200
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAVTTYAfdiSLLEL---LLPLLAGARVVIA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 201 SPQTLADqsskiKKGSKGDTSVLKPTLMAAVPeimdriyknvmnkvnemsAFQRNLFilaynykmeqiSKGcstplcdrf 280
Cdd:cd12116 199 PRETQRD-----PEALARLIEAHSITVMQATP------------------ATWRMLL-----------DAG--------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 vFRNVRRLlggnirLLLCGGAPLSATTQRFmnicFCCPVGQG---YGLTESTGAGTITEVWDYNTG-RVGAPLVcceikl 356
Cdd:cd12116 236 -WQGRAGL------TALCGGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAAAGPiPIGRPLA------ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 knweeggyfNTD--------KPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCL 422
Cdd:cd12116 299 ---------NTQvyvldaalRPVPPgvpGELYIGGDGVAQGYLGRPALTAERFVPDpfaGPGSRLYRTGDLVRRRADGRL 369
|
330 340 350
....*....|....*....|....*....|....*
gi 209977076 423 KIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN 457
Cdd:cd12116 370 EYLGRADGQVKIR-GHRIELGEIEAALAAHPGVAQ 403
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
128-557 |
1.58e-22 |
|
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: 98.56 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAHV---------LELSAELVCLSHgcrig 198
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVgglailvrsLLAGAELVLLER----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 199 ysspqtlaDQSSKIKKGSKGDTSV-LKPTlmaavpeimdriyknvmnkvnemsAFQRnlfILAynykmeqiSKGCSTPLc 277
Cdd:cd17630 75 --------NQALAEDLAPPGVTHVsLVPT------------------------QLQR---LLD--------SGQGPAAL- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 278 drfvfrnvrrllgGNIRLLLCGGAPLS------ATTQRFmnicfccPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVC 351
Cdd:cd17630 111 -------------KSLRAVLLGGAPIPpellerAADRGI-------PLYTTYGMTETASQVATKRPDGFGRGGVGVLLPG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 CEIKLknweeggyfntdkpHPRGEILIGGQNVTMGYYKNEakTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDL 431
Cdd:cd17630 171 RELRI--------------VEDGEIWVGGASLAMGYLRGQ--LVPEFNEDG----WFTTKDLGELHADGRLTVLGRADNM 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 432 VkLQAGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVPNQKELTelartkgfkgtwEELcnssemenevlk 508
Cdd:cd17630 231 I-ISGGENIQPEEIEAALAAHPAVRDAFVVGvpdEELGQRPVAVIVGRGPADP------------AEL------------ 285
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 209977076 509 vlsEAAISASLEKFEIPlkIRLSPDPWTPETGLVtdafKLKRKELKTHY 557
Cdd:cd17630 286 ---RAWLKDKLARFKLP--KRIYPVPELPRTGGG----KVDRRALRAWL 325
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
26-441 |
3.50e-22 |
|
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: 100.01 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 26 ACFMYNFQ--LVTLYATLGGPAIVHGLN---------------ETEVtnIITSKELLQtKLKDIVSLVPRLRHIITVDGK 88
Cdd:cd12119 54 ATLAWNTHrhLELYYAVPGMGAVLHTINprlfpeqiayiinhaEDRV--VFVDRDFLP-LLEAIAPRLPTVEHVVVMTDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 89 PPTWSEFPKGVIVHTMAAVQALGVKANVEKKAHskplpsDIAVIMYTSGSTGIPKGVMISH-SNIIASITGMARRIPRLG 167
Cdd:cd12119 131 AAMPEPAGVGVLAYEELLAAESPEYDWPDFDEN------TAAAICYTSGTTGNPKGVVYSHrSLVLHAMAALLTDGLGLS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 168 EEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKgdtsvlkPTLMAAVPEIMdriyknvmnkvn 247
Cdd:cd12119 205 ESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDPASLAELIEREG-------VTFAAGVPTVW------------ 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 248 emsafqrnLFILAYnykmeqiskgcstplcdrfVFRNVRRLLGGniRLLLCGGA--PLS---ATTQRFMNICfccpvgQG 322
Cdd:cd12119 266 --------QGLLDH-------------------LEANGRDLSSL--RRVVIGGSavPRSlieAFEERGVRVI------HA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 323 YGLTESTGAGTI------------TEVWDY--NTGRVgAPLVccEIKLKNwEEGGyfntDKPH---PRGEILIGGQNVTM 385
Cdd:cd12119 311 WGMTETSPLGTVarppsehsnlseDEQLALraKQGRP-VPGV--ELRIVD-DDGR----ELPWdgkAVGELQVRGPWVTK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 209977076 386 GYYKNEAKTKtdfFEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVS 441
Cdd:cd12119 383 SYYKNDEESE---ALTEDG--WLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWIS 432
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
128-455 |
4.10e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 100.30 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR----RIPRLGEEDVYIGYLPLAHVLELSAELV-CLSHGCRIGYSSP 202
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDNVYLAALPMFHIYGLSLFVVgLLSLGSTIVVMRR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 203 QTLADQSSKIKKGSKGDTSVLKPTLMAAVpeimdriyknvmnkvnemsafqrnlfilaynykmeQISKG-CSTPLcdrfv 281
Cdd:PLN02574 279 FDASDMVKVIDRFKVTHFPVVPPILMALT-----------------------------------KKAKGvCGEVL----- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 282 frnvrrllgGNIRLLLCGGAPLSA-TTQRFMNICFCCPVGQGYGLTESTGAGT----ITEVWDYNTGRVGAPLVccEIKL 356
Cdd:PLN02574 319 ---------KSLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTrgfnTEKLSKYSSVGLLAPNM--QAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 KNWEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLQa 436
Cdd:PLN02574 388 VDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG----WLRTGDIAYFDEDGYLYIVDRLKEIIKYK- 459
|
330
....*....|....*....
gi 209977076 437 GEYVSLGKVEAALKNLPLI 455
Cdd:PLN02574 460 GFQIAPADLEAVLISHPEI 478
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
126-478 |
4.50e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 97.73 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNII--ASITGMARRiprLGEEDVYIGYLPLAHVLELS-AELVCLSHGCRIGYssP 202
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGERLG---LTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVF--P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 203 QTLADQSSKIKKGSKGdtsvlKPTLMAAVPEImdriyknvmnkvnemsafqrnlFILAYNykmeqiskgcsTPLCDRFVF 282
Cdd:cd05917 76 SPSFDPLAVLEAIEKE-----KCTALHGVPTM----------------------FIAELE-----------HPDFDKFDL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 283 RNVRrllGGNIrlllcGGAPL-SATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWD-----YNTgrVGAPLVCCEIKL 356
Cdd:cd05917 118 SSLR---TGIM-----AGAPCpPELMKRVIEVMNMKDVTIAYGMTETSPVSTQTRTDDsiekrVNT--VGRIMPHTEAKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 KNwEEGGyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKtdffEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVkLQA 436
Cdd:cd05917 188 VD-PEGG--IVPPVGVPGELCIRGYSVMKGYWNDPEKTA----EAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRG 259
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 209977076 437 GEYVSLGKVEAALKNLPLIDNICayansyhsyVIGfvVPNQK 478
Cdd:cd05917 260 GENIYPREIEEFLHTHPKVSDVQ---------VVG--VPDER 290
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
75-453 |
4.58e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 96.76 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 75 LVPR--LRHIITV---DGKPPTWSEFPKGVIVHTMAAVQAL----GVKAN-VEKKAHSKPL------PSDIAVIMYTSGS 138
Cdd:PRK05677 139 VLPKtgVKHVIVTevaDMLPPLKRLLINAVVKHVKKMVPAYhlpqAVKFNdALAKGAGQPVteanpqADDVAVLQYTGGT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 139 TGIPKGVMISHSNIIASITGMARRI-PRLGE-EDVYIGYLPLAHVLELS----AELVCLSHGCRIgySSPQtlaDQSSKI 212
Cdd:PRK05677 219 TGVAKGAMLTHRNLVANMLQCRALMgSNLNEgCEILIAPLPLYHIYAFTfhcmAMMLIGNHNILI--SNPR---DLPAMV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 213 KKGSKgdtsvlkptlmaavpeimdriyknvmnkvNEMSAF--QRNLFIlaynykmeqiskgcstPLCDRFVFRNvrrLLG 290
Cdd:PRK05677 294 KELGK-----------------------------WKFSGFvgLNTLFV----------------ALCNNEAFRK---LDF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 291 GNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNwEEGGYFNTDK 369
Cdd:PRK05677 326 SALKLTLSGGMALqLATAERWKEVT-GCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 370 PhprGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAAL 449
Cdd:PRK05677 404 V---GELCVKGPQVMKGYWQRPEATDEIL--DSDG--WLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDVL 475
|
....
gi 209977076 450 KNLP 453
Cdd:PRK05677 476 AALP 479
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
134-453 |
5.29e-21 |
|
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: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 134 YTSGSTGIPKGVMISH--------SNIIASitgmarripRLGEEDVYIGYLPLAHvlelsaelvclshgCRiGYSSPQTL 205
Cdd:cd12118 140 YTSGTTGRPKGVVYHHrgaylnalANILEW---------EMKQHPVYLWTLPMFH--------------CN-GWCFPWTV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 AdqsskikkgSKGDTSVLKPTLMAavPEIMDRIYKNvmnKVNEMSAFQRNLFILAyNYKmeqiskgcstplcdrfvfRNV 285
Cdd:cd12118 196 A---------AVGGTNVCLRKVDA--KAIYDLIEKH---KVTHFCGAPTVLNMLA-NAP------------------PSD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 286 RRLLGGNIRLLLCGGAPLSATTQRFMNICFCcpVGQGYGLTESTGAGTITEvW--DYNT----------GRVGAPLVcce 353
Cdd:cd12118 243 ARPLPHRVHVMTAGAPPPAAVLAKMEELGFD--VTHVYGLTETYGPATVCA-WkpEWDElpteerarlkARQGVRYV--- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 354 ikLKNWEEGGYFNTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRK 428
Cdd:cd12118 317 --GLEEVDVLDPETMKPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAF---RGG--WFHSGDLAVIHPDGYIEIKDRS 389
|
330 340
....*....|....*....|....*
gi 209977076 429 KDLVkLQAGEYVSLGKVEAALKNLP 453
Cdd:cd12118 390 KDII-ISGGENISSVEVEGVLYKHP 413
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
126-559 |
9.83e-21 |
|
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: 95.30 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDvyigylplaHVLELSAelvclshgcrigYSSpqtl 205
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG-LTSES---------RVLQFAS------------YTF---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 adqsskikkgskgDTSVLK--PTLMA----AVPEIMDRiyknvMNKVNE-MSAFQRNLFILaynykmeqiskgcsTPlcd 278
Cdd:cd05918 159 -------------DVSILEifTTLAAggclCIPSEEDR-----LNDLAGfINRLRVTWAFL--------------TP--- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 279 rfvfrNVRRLLG----GNIRLLLCGGAPLSATTQ-------RFMNicfccpvgqGYGLTESTGAGTITEVWDYNTGR-VG 346
Cdd:cd05918 204 -----SVARLLDpedvPSLRTLVLGGEALTQSDVdtwadrvRLIN---------AYGPAECTIAATVSPVVPSTDPRnIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 347 APL-VCCEIKLKNweeggyfNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDengQRWLC------------T 410
Cdd:cd05918 270 RPLgATCWVVDPD-------NHDRLVPIgavGELLIEGPILARGYLNDPEKTAAAFIED---PAWLKqegsgrgrrlyrT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 411 GDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKN-LPLIDNICAYA-----NSYHSYVIGFVVPNQKELTELA 484
Cdd:cd05918 340 GDLVRYNPDGSLEYVGRKDTQVKIR-GQRVELGEIEHHLRQsLPGAKEVVVEVvkpkdGSSSPQLVAFVVLDGSSSGSGD 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209977076 485 RTKGFkgtweeLCNSSEMENEVLKVlsEAAISASLEKFEIP-LKIRLSPDPWTPeTGlvtdafKLKRKELKTHYQA 559
Cdd:cd05918 419 GDSLF------LEPSDEFRALVAEL--RSKLRQRLPSYMVPsVFLPLSHLPLTA-SG------KIDRRALRELAES 479
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
126-455 |
1.22e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 95.43 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASItgmARRI----PRLG--EEDVYIGYLPLAHVLELSAELVClshGCRIGy 199
Cdd:PLN02246 178 PDDVVALPYSSGTTGLPKGVMLTHKGLVTSV---AQQVdgenPNLYfhSDDVILCVLPMFHIYSLNSVLLC---GLRVG- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 sspqtladqsSKIKKGSKGDTSVL-------KPTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfilaynykmeqiskgc 272
Cdd:PLN02246 251 ----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKS------------------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 273 stPLCDRFVFrnvrrllgGNIRLLLCGGAPL-----SATTQRFMNICFccpvGQGYGLTEstgAGTI--------TEVWD 339
Cdd:PLN02246 290 --PVVEKYDL--------SSIRMVLSGAAPLgkeleDAFRAKLPNAVL----GQGYGMTE---AGPVlamclafaKEPFP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 340 YNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYKN-EAKTKTDffeDENGqrWLCTGDIGEFDP 418
Cdd:PLN02246 353 VKSGSCGTVVRNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDpEATANTI---DKDG--WLHTGDIGYIDD 424
|
330 340 350
....*....|....*....|....*....|....*..
gi 209977076 419 DGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI 455
Cdd:PLN02246 425 DDELFIVDRLKELIKYK-GFQVAPAELEALLISHPSI 460
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
128-459 |
1.28e-20 |
|
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: 94.47 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSAelvclshgcrigysspqtlad 207
Cdd:cd05935 85 DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWT-GLTPSDVILACLPLFHVTGFVG--------------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 208 qsskikkgskgdtsvlkpTLMAAVpeimdriykNVMNKVNEMSAFQRNLFILAYNYKMEQISKGCSTPLCDRFVFRNVRR 287
Cdd:cd05935 143 ------------------SLNTAV---------YVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 288 LLGGNIRLLLCGGAPL-SATTQRFMNIcFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFN 366
Cdd:cd05935 196 RDLSSLKVLTGGGAPMpPAVAEKLLKL-TGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 367 tdkPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDeNGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVE 446
Cdd:cd05935 275 ---PNEVGEIVVRGPQIFKGYWNRPEETEESFIEI-KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVE 349
|
330
....*....|...
gi 209977076 447 AALKNLPLIDNIC 459
Cdd:cd05935 350 AKLYKHPAI*EVC 362
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
77-455 |
2.64e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 94.35 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 77 PRLRHIITVDGK----------PPTWSEFPkgvivhtmAAVQALgvkanvekkAHSKPLPSDIAVIMYTSGSTGIPKGVM 146
Cdd:PRK13295 154 PALRHVVVVGGDgadsfealliTPAWEQEP--------DAPAIL---------ARLRPGPDDVTQLIYTSGTTGEPKGVM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 147 ISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHvlelsaeLVCLSHGCRIGYSSPQT--LADQSSKIKKGSKGDTSVLK 224
Cdd:PRK13295 217 HTANTLMANIVPYAERL-GLGADDVILMASPMAH-------QTGFMYGLMMPVMLGATavLQDIWDPARAAELIRTEGVT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 225 PTlMAAVPEIMDriyknvMNKVNEMSAfqrnlfilaynykmeqiskgcstplcdrfvfRNVRRLlggniRLLLCGGAPLS 304
Cdd:PRK13295 289 FT-MASTPFLTD------LTRAVKESG-------------------------------RPVSSL-----RTFLCAGAPIP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 305 ATTQRFMNICFCCPVGQGYGLTEsTGAGTITEVWDYN---TGRVGAPLVCCEIKLKNweeggyfNTDKPHPRGEI---LI 378
Cdd:PRK13295 326 GALVERARAALGAKIVSAWGMTE-NGAVTLTKLDDPDeraSTTDGCPLPGVEVRVVD-------ADGAPLPAGQIgrlQV 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977076 379 GGQNVTMGYYKNEAKTKTDFfedengQRWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLI 455
Cdd:PRK13295 398 RGCSNFGGYLKRPQLNGTDA------DGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAI 467
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
126-475 |
6.92e-20 |
|
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: 92.37 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASI--------TGMARRIPRLgeedVYIGYLPLAHVLelsaeLVCLSHGCRI 197
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVsqpparldVGPGSRVAQV----LSIAFDACIGEI-----FSTLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 GYSSP-QTLADQSSKIkkgskgDTSVLKPTLMAAVPeimDRIYKNVmnkvnemsafqrnlfilaynykmEQISKG---CS 273
Cdd:cd17653 175 VLADPsDPFAHVARTV------DALMSTPSILSTLS---PQDFPNL-----------------------KTIFLGgeaVP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 274 TPLCDRFVFRnvRRLLggnirlllcggaplsattqrfmnicfccpvgQGYGLTESTGAGTITEVWDYNTGRVGAPL--VC 351
Cdd:cd17653 223 PSLLDRWSPG--RRLY-------------------------------NAYGPTECTISSTMTELLPGQPVTIGKPIpnST 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 CEIKLKNWEEggyfntdKPHPR-GEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRK 428
Cdd:cd17653 270 CYILDADLQP-------VPEGVvGEICISGVQVARGYLGNPALTASKFVPDpfWPGSRMYRTGDYGRWTEDGGLEFLGRE 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 209977076 429 KDLVKLQaGEYVSLGKVEA-ALKNLPLIDNicAYANSYHSYVIGFVVP 475
Cdd:cd17653 343 DNQVKVR-GFRINLEEIEEvVLQSQPEVTQ--AAAIVVNGRLVAFVTP 387
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
108-478 |
7.06e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 93.35 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 108 QALGVKANVEKKAHS--KPLP---SDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEE---------DVYI 173
Cdd:PRK12492 183 QAVPFKQALRQGRGLslKPVPvglDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqEVMI 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 174 GYLPLAHVLELSAELVCL----SHGCRIgySSPQtlaDQSSKIKKGSKGDTSVL--KPTLMAAvpeimdriyknvmnkvn 247
Cdd:PRK12492 263 APLPLYHIYAFTANCMCMmvsgNHNVLI--TNPR---DIPGFIKELGKWRFSALlgLNTLFVA----------------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 248 emsafqrnlfilaynykmeqiskgcstpLCDRFVFRNVRRllgGNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLT 326
Cdd:PRK12492 321 ----------------------------LMDHPGFKDLDF---SALKLTNSGGTALvKATAERWEQLT-GCTIVEGYGLT 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 327 ESTGAGTITEvwdYNT----GRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKtdffEDE 402
Cdd:PRK12492 369 ETSPVASTNP---YGElarlGTVGIPVPGTALKVID-DDG---NELPLGERGELCIKGPQVMKGYWQQPEATA----EAL 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209977076 403 NGQRWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNiCAyansyhsyVIGfvVPNQK 478
Cdd:PRK12492 438 DAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVAN-CA--------AIG--VPDER 501
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
134-453 |
1.06e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 92.77 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 134 YTSGSTGIPKGVMISHS----NIIASITGMarripRLGEEDVYIGYLPLAHvlelsaelvclshgCRiGYSSPQTLAdqs 209
Cdd:PLN03102 193 YTSGTTADPKGVVISHRgaylSTLSAIIGW-----EMGTCPVYLWTLPMFH--------------CN-GWTFTWGTA--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 210 skikkgSKGDTSVLKPTLMAavPEimdrIYKNV-MNKVNEMSAFQRNLFILAynykmeqisKGCSTPLCDRfvfrnvrrl 288
Cdd:PLN03102 250 ------ARGGTSVCMRHVTA--PE----IYKNIeMHNVTHMCCVPTVFNILL---------KGNSLDLSPR--------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 289 lGGNIRLLLCGGAPLSATTQRFMNICFccPVGQGYGLTESTGAGTITEVWD-YN----------TGRVGAP-LVCCEIKL 356
Cdd:PLN03102 300 -SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEWQDeWNrlpenqqmelKARQGVSiLGLADVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 KNWEeggyfnTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDL 431
Cdd:PLN03102 377 KNKE------TQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF---KHG--WLNTGDVGVIHPDGHVEIKDRSKDI 445
|
330 340
....*....|....*....|..
gi 209977076 432 VkLQAGEYVSLGKVEAALKNLP 453
Cdd:PLN03102 446 I-ISGGENISSVEVENVLYKYP 466
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
3-495 |
1.39e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 92.12 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 3 GQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKD-IVSL---VPR 78
Cdd:PRK06087 70 GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDlILPLqnqLPQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 79 LRHIITVDGKPPTWSEFpkgvivhTMAAVQALGVKANVEKKAHSkplpSDIAVIMYTSGSTGIPKGVMISHSNIIASITG 158
Cdd:PRK06087 150 LQQIVGVDKLAPATSSL-------SLSQIIADYEPLTTAITTHG----DELAAVLFTSGTEGLPKGVMLTHNNILASERA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 159 MARRIpRLGEEDVYIGYLPLAHvlelsaelvclSHGCRIGYSSPQTLadqsskikkgskGDTSVL----KPT-------- 226
Cdd:PRK06087 219 YCARL-NLTWQDVFMMPAPLGH-----------ATGFLHGVTAPFLI------------GARSVLldifTPDaclalleq 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 227 -----LMAAVPEIMDrIYKNVMNKVNEMSAfqrnlfilaynykmeqiskgcstplcdrfvfrnvrrllggnIRLLLCGGA 301
Cdd:PRK06087 275 qrctcMLGATPFIYD-LLNLLEKQPADLSA-----------------------------------------LRFFLCGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 302 PLSATT-----QRFMNICFCcpvgqgYGLTESTGAGTITEvwDYNTGRVGA----PLVCCEIKLKNweegGYFNTDKPHP 372
Cdd:PRK06087 313 TIPKKVarecqQRGIKLLSV------YGSTESSPHAVVNL--DDPLSRFMHtdgyAAAGVEIKVVD----EARKTLPPGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 373 RGEILIGGQNVTMGYYKNeaKTKTDFFEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNL 452
Cdd:PRK06087 381 EGEEASRGPNVFMGYLDE--PELTARALDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQH 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209977076 453 PLI--------------DNICAYA---NSYHSyvigfvvPNQKELTE-LARTKGFKGTWEE 495
Cdd:PRK06087 456 PKIhdacvvampderlgERSCAYVvlkAPHHS-------LTLEEVVAfFSRKRVAKYKYPE 509
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
126-460 |
3.43e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 91.09 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGE----EDVYIGYLPLAHVLELSAE-LVCLS-HGCRIGY 199
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTANgLVFMKiGGCNHLI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 SSPQTLadqsskikkgsKGDTSVLKPTLMAAVPEImDRIYKNVMNkvnemsafqrnlfilaynykmeqiskgcsTPLCDR 279
Cdd:PRK08751 287 SNPRDM-----------PGFVKELKKTRFTAFTGV-NTLFNGLLN-----------------------------TPGFDQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 280 FVFRNVRRLLGGnirlllcGGAPLSATTQRFMNICfCCPVGQGYGLTESTGAGTIT--EVWDYNtGRVGAPLVCCEIKLK 357
Cdd:PRK08751 326 IDFSSLKMTLGG-------GMAVQRSVAERWKQVT-GLTLVEAYGLTETSPAACINplTLKEYN-GSIGLPIPSTDACIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 358 NweeggyfNTDKPHPRGEI---LIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkL 434
Cdd:PRK08751 397 D-------DAGTVLAIGEIgelCIKGPQVMKGYWKRPEETAKVM--DADG--WLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340
....*....|....*....|....*.
gi 209977076 435 QAGEYVSLGKVEAALKNLPLIDNICA 460
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEVAA 490
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
126-554 |
9.18e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.86 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIA-SITGMArrIPRLGEEDVYIGYLPLAHVLELSAELVCLSHG-CRIGYSspq 203
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVqSLAKIA--IVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGaCHVLLP--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 204 tladqsskiKKGSKGDTSVLKP---TLMAAVPEIM-DriyknvmnkvnemsafqrnlfILAYNyKMEQISKGcstplcdr 279
Cdd:PLN02860 246 ---------KFDAKAALQAIKQhnvTSMITVPAMMaD---------------------LISLT-RKSMTWKV-------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 280 fvFRNVRRLL--GGNIRLLLcggapLSATTQRFMnicfCCPVGQGYGLTES---------------TGAGTITEVWDYNT 342
Cdd:PLN02860 287 --FPSVRKILngGGSLSSRL-----LPDAKKLFP----NAKLFSAYGMTEAcssltfmtlhdptleSPKQTLQTVNQTKS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 343 GRVGAPLVCC--------EIKLKnweeggyfnTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIG 414
Cdd:PLN02860 356 SSVHQPQGVCvgkpaphvELKIG---------LDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDG----WLDTGDIG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 415 EFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNicayansyhSYVIGfvVPNQKeLTELA----RTKGfK 490
Cdd:PLN02860 423 WIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVAS---------VVVVG--VPDSR-LTEMVvacvRLRD-G 488
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209977076 491 GTWEELCNSSEMENEVL--KVLSEAAISASLEKFEIPLKIRLSPDPWTpetglVTDAFKLKRKELK 554
Cdd:PLN02860 489 WIWSDNEKENAKKNLTLssETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
126-432 |
1.44e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 88.92 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGM------ARRIPRLGEEDVYIGYLPLAHVLELSaelVCLSHGCRigy 199
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawlqpAFEKKPRPDQLNFVCALPLYHIFALT---VCGLLGMR--- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 sspqtladqsskikkgsKGDTSVLKPTlmaavPeimdriyKNVMNKVNEMSAFQRNLFI---LAYNYKMeqiskgcSTPL 276
Cdd:PRK07059 277 -----------------TGGRNILIPN-----P-------RDIPGFIKELKKYQVHIFPavnTLYNALL-------NNPD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 277 CDRFVFRNVRRLLGGnirlllcGGAPLSATTQRFMNICfCCPVGQGYGLTESTGAGTI--TEVWDYnTGRVGAPLVCCEI 354
Cdd:PRK07059 321 FDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCnpVDATEF-SGTIGLPLPSTEV 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209977076 355 KLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK07059 392 SIRD-DDGNDLPLGEP---GEICIRGPQVMAGYWNRPDETAKVMTADG----FFRTGDVGVMDERGYTKIVDRKKDMI 461
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
127-432 |
1.54e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 88.94 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 127 SDIAVIMYTSGSTGIPKGVMISHSNIIA-SITGMARRIPRLGEEDVYIGYLPLAHVLELSAELvclshgcrigysspqtl 205
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSnTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVM----------------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 adqsskikkgskgDTSVLKPTLMAAVPEI-MDRIYKNVMNKVNEMSAFQRNLFILAYNykmeqiskgcsTPLCDRFVFrn 284
Cdd:PRK06710 269 -------------NLSIMQGYKMVLIPKFdMKMVFEAIKKHKVTLFPGAPTIYIALLN-----------SPLLKEYDI-- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 285 vrrllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNT-GRVGAPLVCCEIKLKNWEEGG 363
Cdd:PRK06710 323 ------SSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSLETGE 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 364 YFntdKPHPRGEILIGGQNVTMGYYkNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK06710 397 AL---PPGEIGEIVVKGPQIMKGYW-NKPEETAAVLQDG----WLHTGDVGYMDEDGFFYVKDRKKDMI 457
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
126-455 |
1.74e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 88.40 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASitgMARRIPRLG--EEDVYIGYLPLAHV--LELSAeLVCLSHGCRIgyss 201
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNLHWK---SIDHVIALGltASERLLVVGPLYHVgaFDLPG-IAVLWVGGTL---- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 202 pqtladqssKIKKGSKGDTsvlkptLMAAVPEimDRIYKNVMNKVnemsafqrnlfilaynykmeQISKGCSTPLCDRFV 281
Cdd:PRK06145 220 ---------RIHREFDPEA------VLAAIER--HRLTCAWMAPV--------------------MLSRVLTVPDRDRFD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 282 FRNVRRLLGGNIRlllcggAP---LSATTQRFMNICFCcpvgQGYGLTESTGAGTITEVWDY--NTGRVGAPLVCCEIKL 356
Cdd:PRK06145 263 LDSLAWCIGGGEK------TPesrIRDFTRVFTRARYI----DAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 KNwEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQA 436
Cdd:PRK06145 333 AD-GAGRWL---PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----WFRSGDVGYLDEEGFLYLTDRKKDMI-ISG 402
|
330
....*....|....*....
gi 209977076 437 GEYVSLGKVEAALKNLPLI 455
Cdd:PRK06145 403 GENIASSEVERVIYELPEV 421
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
29-452 |
2.35e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 89.25 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 29 MYNFqlvtlyaTLGGPAIVHGLNETEVTNIITSKELL-QTKLKDIVSLVPRLRHIITVDgkpptwsEFPKGVivHTMAAV 107
Cdd:PRK06814 711 MINF-------SAGIANILSACKAAQVKTVLTSRAFIeKARLGPLIEALEFGIRIIYLE-------DVRAQI--GLADKI 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 108 QAL--GVKANVEKKAHSkplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAHVLELS 185
Cdd:PRK06814 775 KGLlaGRFPLVYFCNRD---PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLT 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 186 AELVC-LSHGCRIG-YSSPQTladqsskikkgskgdtsvlkptlMAAVPEImdrIYknvmnKVNEMSAFQRNLFILAY-N 262
Cdd:PRK06814 851 GGLVLpLLSGVKVFlYPSPLH-----------------------YRIIPEL---IY-----DTNATILFGTDTFLNGYaR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 263 YkmeqiskgcstplCDRFVFRnvrrllggNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEStgagtiTEVWDYNT 342
Cdd:PRK06814 900 Y-------------AHPYDFR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTET------APVIALNT 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 343 ------GRVGAPLVCCEIKLK---NWEEGgyfntdkphprGEILIGGQNVTMGYYKNEAKTKTDffEDENGqrWLCTGDI 413
Cdd:PRK06814 953 pmhnkaGTVGRLLPGIEYRLEpvpGIDEG-----------GRLFVRGPNVMLGYLRAENPGVLE--PPADG--WYDTGDI 1017
|
410 420 430
....*....|....*....|....*....|....*....
gi 209977076 414 GEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNL 452
Cdd:PRK06814 1018 VTIDEEGFITIKGRAKRFAKI-AGEMISLAAVEELAAEL 1055
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
117-458 |
2.81e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 88.11 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 117 EKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRI-PRLGEEDVYIGYLPLAHVLELSAelVCLShgc 195
Cdd:PLN02330 174 DTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVgPEMIGQVVTLGLIPFFHIYGITG--ICCA--- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 196 rigysspqTLADQSsKIKKGSKGDTSVLKPTLMAA-------VPEIMDRIYKNvmnkvnemsafqrnlfilaynykmeqi 268
Cdd:PLN02330 249 --------TLRNKG-KVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKN--------------------------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 269 skgcstPLCDRFVFRNVRrllggnIRLLLCGGAPL-----SATTQRFMNIcfccPVGQGYGLTESTGAgTITEvWDYNTG 343
Cdd:PLN02330 293 ------PIVEEFDLSKLK------LQAIMTAAAPLapellTAFEAKFPGV----QVQEAYGLTEHSCI-TLTH-GDPEKG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 344 R-------VGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYKNeaKTKTDFFEDENGqrWLCTGDIGEF 416
Cdd:PLN02330 355 HgiakknsVGFILPNLEVKFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYNN--KEETDRTIDEDG--WLHTGDIGYI 427
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 209977076 417 DPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNI 458
Cdd:PLN02330 428 DDDGDIFIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDA 468
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
126-432 |
4.20e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 87.24 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIiASITGMARRIPRLGEEDVYIGYLPLAHVlelsaelvclsHGCRIgySSPQTL 205
Cdd:PRK07514 155 ADDLAAILYTSGTTGRSKGAMLSHGNL-LSNALTLVDYWRFTPDDVLIHALPIFHT-----------HGLFV--ATNVAL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 ADQSSKIKKgSKGDTSVL-----KPTLMAAVPEIMDRIYKNvmnkvnemsafqrnlfilaynykmeqiskgcstplcDRF 280
Cdd:PRK07514 221 LAGASMIFL-PKFDPDAVlalmpRATVMMGVPTFYTRLLQE------------------------------------PRL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 VfrnvrRLLGGNIRLLLCGGAPLSATTQRfmniCFCCPVGQG----YGLTEsTG------------AGTitevwdyntgr 344
Cdd:PRK07514 264 T-----REAAAHMRLFISGSAPLLAETHR----EFQERTGHAilerYGMTE-TNmntsnpydgerrAGT----------- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 345 VGAPLVCCEIKLKNWEEGgyfntdKPHPRGE---ILIGGQNVTMGYYKNEAKTKTDFFEDenGqrWLCTGDIGEFDPDGC 421
Cdd:PRK07514 323 VGFPLPGVSLRVTDPETG------AELPPGEigmIEVKGPNVFKGYWRMPEKTAEEFRAD--G--FFITGDLGKIDERGY 392
|
330
....*....|.
gi 209977076 422 LKIIDRKKDLV 432
Cdd:PRK07514 393 VHIVGRGKDLI 403
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
124-475 |
4.60e-18 |
|
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: 87.33 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 124 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLA---HVLELsaeLVCLSHGCRIGYS 200
Cdd:cd17646 135 PRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYP-LGPGDRVLQKTPLSfdvSVWEL---FWPLVAGARLVVA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 201 SPQTLADqsskikkgskgdtsvlkptlMAAVPEIMDRIYKNVMNKVNEMSAfqrnLFIlaynykmEQISKGCSTPLcdrf 280
Cdd:cd17646 211 RPGGHRD--------------------PAYLAALIREHGVTTCHFVPSMLR----VFL-------AEPAAGSCASL---- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 vfrnvrrllggniRLLLCGGAPLSA-TTQRFMNIcFCCPVGQGYGLTESTgagtITEVWDYNTGRVGAPLVccEIKLKNW 359
Cdd:cd17646 256 -------------RRVFCSGEALPPeLAARFLAL-PGAELHNLYGPTEAA----IDVTHWPVRGPAETPSV--PIGRPVP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 360 EEGGYFNTD--KPHPRG---EILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:cd17646 316 NTRLYVLDDalRPVPVGvpgELYLGGVQLARGYLGRPALTAERFVPDpfGPGSRMYRTGDLARWRPDGALEFLGRSDDQV 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 209977076 433 KLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 475
Cdd:cd17646 396 KIR-GFRVEPGEIEAALAAHPAVTHAVVVAraaPAGAARLVGYVVP 440
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
126-487 |
5.10e-18 |
|
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: 86.59 E-value: 5.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGmARRIPRLGEEDVYIGY-------------LPLAHvlelSAELVCLS 192
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDDVWTLFhsyafdfsvweiwGALLH----GGRLVVVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 193 HGCRigySSPQTLADQsskIKKGskgdtsvlKPTLMAAVPeimdriyknvmnkvnemSAFQRnlFILAynykmeqiskgc 272
Cdd:cd17643 167 YEVA---RSPEDFARL---LRDE--------GVTVLNQTP-----------------SAFYQ--LVEA------------ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 273 stplcdrfVFRNVRRLLggNIRLLLCGGAPLSATTQRFMNICFCCPVGQ---GYGLTESTGAGTITEV-----WDYNTGR 344
Cdd:cd17643 202 --------ADRDGRDPL--ALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETTVHVTFRPLdaadlPAAAASP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 345 VGAPLVCCEIKLKNweeggyfNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDEN---GQRWLCTGDIGEFDP 418
Cdd:cd17643 272 IGRPLPGLRVYVLD-------ADGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpGSRMYRTGDLARRLP 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209977076 419 DGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYANSYH---SYVIGFVVPNQK------ELTELARTK 487
Cdd:cd17643 345 DGELEYLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDEpgdTRLVAYVVADDGaaadiaELRALLKEL 421
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-477 |
7.18e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTL 205
Cdd:PRK12467 655 PDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCA 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 ADQSSKIKKGSKGDTSVLKptlmaAVPeimdriyknvmnkvnemSAFQRNLfilaynykmeqiSKGCSTPlcdrfvfrnV 285
Cdd:PRK12467 734 RDAEAFAALMADQGVTVLK-----IVP-----------------SHLQALL------------QASRVAL---------P 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 286 RRLlggniRLLLCGGAPLS-ATTQRFMNICFCCPVGQGYGLTESTGAGTITEV----WDYNTGRVGAPLVCCEIKLKNwe 360
Cdd:PRK12467 771 RPQ-----RALVCGGEALQvDLLARVRALGPGARLINHYGPTETTVGVSTYELsdeeRDFGNVPIGQPLANLGLYILD-- 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 361 egGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaG 437
Cdd:PRK12467 844 --HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIR-G 920
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 209977076 438 EYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPNQ 477
Cdd:PRK12467 921 FRIELGEIEARLLAQPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
124-462 |
7.59e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 86.34 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 124 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSaelVCLSHgcrigysspq 203
Cdd:cd05922 114 VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL-GITADDRALTVLPLSYDYGLS---VLNTH---------- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 204 TLADQSSKIKKGSKGDTSVLKP------TLMAAVP---EIMDRIyknvmnkvnemsafqrnlfilaynykmeqISKGCST 274
Cdd:cd05922 180 LLRGATLVLTNDGVLDDAFWEDlrehgaTGLAGVPstyAMLTRL-----------------------------GFDPAKL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 275 PlcdrfvfrnvrrllggNIRLLLCGGAPLSATT-QRFmnicfcCPVGQG------YGLTESTGAGTI--TEVWDYNTGRV 345
Cdd:cd05922 231 P----------------SLRYLTQAGGRLPQETiARL------RELLPGaqvyvmYGQTEATRRMTYlpPERILEKPGSI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 346 GAPLVCCEIKLKNwEEGGYFNTDKPhprGEILIGGQNVTMGYYKNEA-KTKTDFFEDEngqrwLCTGDIGEFDPDGCLKI 424
Cdd:cd05922 289 GLAIPGGEFEILD-DDGTPTPPGEP---GEIVHRGPNVMKGYWNDPPyRRKEGRGGGV-----LHTGDLARRDEDGFLFI 359
|
330 340 350
....*....|....*....|....*....|....*...
gi 209977076 425 IDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNICAYA 462
Cdd:cd05922 360 VGRRDRMIKL-FGNRISPTEIEAAARSIGLIIEAAAVG 396
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
77-432 |
7.74e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.79 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 77 PRLRHIITVDGKPP----TWSEfpkgvivhtmaaVQALGVKANVEK-KAHSKPLPSDIAV-IMYTSGSTGIPKGVMISHS 150
Cdd:PRK08315 155 PELRRVIFLGDEKHpgmlNFDE------------LLALGRAVDDAElAARQATLDPDDPInIQYTSGTTGFPKGATLTHR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 151 NII--ASITGMARRiprLGEED-----VyigylPLAH----VLelsAELVCLSHGCRIGYSSP--------QTLADQSSK 211
Cdd:PRK08315 223 NILnnGYFIGEAMK---LTEEDrlcipV-----PLYHcfgmVL---GNLACVTHGATMVYPGEgfdplatlAAVEEERCT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 212 IKKG--------------SKGDTSVLKPTLMAAVP---EIMdriyKNVMNKVNemsafqrnlfilaynykMEQISkgcst 274
Cdd:PRK08315 292 ALYGvptmfiaeldhpdfARFDLSSLRTGIMAGSPcpiEVM----KRVIDKMH-----------------MSEVT----- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 275 plcdrfvfrnvrrllggnirlllcggaplsattqrfmnICfccpvgqgYGLTESTGAGTITEVWD---YNTGRVGAPLVC 351
Cdd:PRK08315 346 --------------------------------------IA--------YGMTETSPVSTQTRTDDpleKRVTTVGRALPH 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 CEIKLKNWEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKtdffE--DENGqrWLCTGDIGEFDPDGCLKIIDRKK 429
Cdd:PRK08315 380 LEVKIVDPETG---ETVPRGEQGELCTRGYSVMKGYWNDPEKTA----EaiDADG--WMHTGDLAVMDEEGYVNIVGRIK 450
|
...
gi 209977076 430 DLV 432
Cdd:PRK08315 451 DMI 453
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
126-482 |
1.34e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.88 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASI---TGMARRIPRLGEEDVYIGyLPLAHVLELSAELVCLSHgcrigyssp 202
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqaKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFIE--------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 203 qtladqsskikkgsKGDTSVL--KPTLMAAVPEIMDRIYKNVMNKVNemsafqrNLFILAYNYKmeqiskgcstplcdrf 280
Cdd:PRK08974 275 --------------LGGQNLLitNPRDIPGFVKELKKYPFTAITGVN-------TLFNALLNNE---------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 vfrNVRRLLGGNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLTESTG--AGTITEVWDYNtGRVGAPLVCCEIKLK 357
Cdd:PRK08974 318 ---EFQELDFSSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTECSPlvSVNPYDLDYYS-GSIGLPVPSTEIKLV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 358 NwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKtDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAG 437
Cdd:PRK08974 393 D-DDG---NEVPPGEPGELWVKGPQVMLGYWQRPEATD-EVIKDG----WLATGDIAVMDEEGFLRIVDRKKDMI-LVSG 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 209977076 438 EYVSLGKVEAALKNLPLIDNICAYANSYHS---YVIGFVVPNQKELTE 482
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLTE 510
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
126-432 |
1.82e-17 |
|
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: 85.75 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAH----VLELsaeLVCLSHGCRIGYSS 201
Cdd:cd05931 148 PDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYHdmglIGGL---LTPLYSGGPSVLMS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 202 PQT-LADQSSKIKKGSKGdtsvlKPTLMAAvPeimdriykNvmnkvnemsaFqrnlfilAYNYkmeqiskgCstplCDRF 280
Cdd:cd05931 224 PAAfLRRPLRWLRLISRY-----RATISAA-P--------N----------F-------AYDL--------C----VRRV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 VFRNVRRLLGGNIRLLLCGGAPLSATT-QRFMNiCFcCPVG-------QGYGLTEST--------GAGTITEVWDY---- 340
Cdd:cd05931 261 RDEDLEGLDLSSWRVALNGAEPVRPATlRRFAE-AF-APFGfrpeafrPSYGLAEATlfvsggppGTGPVVLRVDRdala 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 341 NTGRVGAP-------LVCC-------EIKLKNWEeggyfnTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFF---- 399
Cdd:cd05931 339 GRAVAVAAddpaareLVSCgrplpdqEVRIVDPE------TGRELPDgevGEIWVRGPSVASGYWGRPEATAETFGalaa 412
|
330 340 350
....*....|....*....|....*....|...
gi 209977076 400 EDENGqrWLCTGDIGeFDPDGCLKIIDRKKDLV 432
Cdd:cd05931 413 TDEGG--WLRTGDLG-FLHDGELYITGRLKDLI 442
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
58-449 |
4.52e-17 |
|
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: 84.34 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 58 IITSKELLQTKLKDIVSLVPRLRHIITVDGKPPtwsEFPKGVIVHTMAAVQALGVKANVEkkahskplPSDIAVIMYTSG 137
Cdd:cd05959 105 VVVSGELAPVLAAALTKSEHTLVVLIVSGGAGP---EAGALLLAELVAAEAEQLKPAATH--------ADDPAFWLYSSG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 138 STGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGYLPLAHVLELSAELVC-LSHGCRI----GYSSPQTLADqssKI 212
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFpLSVGATTvlmpERPTPAAVFK---RI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 213 KKGskgdtsvlKPTLMAAVPEimdrIYkNVMNKVNEMSafQRNLfilaynykmeqiskgcstplcdrfvfrnvrrllgGN 292
Cdd:cd05959 251 RRY--------RPTVFFGVPT----LY-AAMLAAPNLP--SRDL----------------------------------SS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 293 IRLLLCGGAPLSATT-QRFMNIcFCCPVGQGYGLTE------STGAGTItevwDYNTgrVGAPLVCCEIKLKNwEEGGYF 365
Cdd:cd05959 282 LRLCVSAGEALPAEVgERWKAR-FGLDILDGIGSTEmlhiflSNRPGRV----RYGT--TGKPVPGYEVELRD-EDGGDV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 366 NTDKPhprGEILIGGQNVTMGYYKNEAKTKTDfFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKV 445
Cdd:cd05959 354 ADGEP---GELYVRGPSSATMYWNNRDKTRDT-FQGE----WTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEV 424
|
....
gi 209977076 446 EAAL 449
Cdd:cd05959 425 ESAL 428
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
124-486 |
5.51e-17 |
|
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: 83.87 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 124 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGmARRIPRLGEEDVYIGYLPLAHV---LELSAELVCLshGCR-IGY 199
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFLNWVPLDHVgglVELHLRAVYL--GCQqVHV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 SSPQTLADqsskikkgskgdtsvlkPTLMAavpEIMDRIYKNVmnkvnemsAFQRNlFILAYnykmeqiskgcstpLCDR 279
Cdd:cd05906 241 PTEEILAD-----------------PLRWL---DLIDRYRVTI--------TWAPN-FAFAL--------------LNDL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 280 FVFRNVRRLLGGNIRLLLCGGAPLSA-TTQRFMNICFCCPVGQ-----GYGLTEsTGAGTItevWD-----YNTGR---- 344
Cdd:cd05906 278 LEEIEDGTWDLSSLRYLVNAGEAVVAkTIRRLLRLLEPYGLPPdairpAFGMTE-TCSGVI---YSrsfptYDHSQalef 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 345 --VGAPLVCCEIKLKNWEEGGyfntdKPHPR-GEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGeFDPDGC 421
Cdd:cd05906 354 vsLGRPIPGVSMRIVDDEGQL-----LPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDG----WFRTGDLG-FLDNGN 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977076 422 LKIIDRKKDLVKLQAGEYvSLGKVEAALKNLPLIDN--ICAYA-----NSYHSYVIgFVVPNQKELTELART 486
Cdd:cd05906 424 LTITGRTKDTIIVNGVNY-YSHEIEAAVEEVPGVEPsfTAAFAvrdpgAETEELAI-FFVPEYDLQDALSET 493
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
125-478 |
5.75e-17 |
|
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: 83.67 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 125 LPSDIAVIMYTSGSTGIPKGVMISHSNIIAS------ITGMARRIPRLGEE-----DVYIGylPLAHVLELSAELVCLSH 193
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAahawrrEYELDSFPVRLLQMasfsfDVFAG--DFARSLLNGGTLVICPD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 194 GCRIgysSPQTLADqsskIKKGSKGDTSVLKPTLMAAVpeiMDRIYKNvmnkvnEMSAFQRNLFILAynykmeqiSKGCs 273
Cdd:cd17650 169 EVKL---DPAALYD----LILKSRITLMESTPALIRPV---MAYVYRN------GLDLSAMRLLIVG--------SDGC- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 274 tPLCDrfvFRNVRRLLGGNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESTGAGTITEVWDYNTGR-----VGAP 348
Cdd:cd17650 224 -KAQD---FKTLAARFGQGMRII------------------------NSYGVTEATIDSTYYEEGRDPLGDsanvpIGRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 349 LVCCEIKLKNweeggyfNTDKPHP---RGEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLK 423
Cdd:cd17650 276 LPNTAMYVLD-------ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVENpfAPGERMYRTGDLARWRADGNVE 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 209977076 424 IIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVPNQK 478
Cdd:cd17650 349 LLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVVAVredKGGEARLCAYVVAAAT 405
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
104-455 |
1.04e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 82.93 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 104 MAAVQALGVKANVEKKAHSKPLPSD-IAVIMYTSGSTGIPKGVMISHSNIIASITGMARrIPRLGEEDVYIGYLPLAHVL 182
Cdd:PRK09088 111 VEDLAAFIASADALEPADTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGV-LGRVDAHSSFLCDAPMFHII 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 183 ELSAEL-VCLSHGCRI----GYSSPQTLadqsskikkGSKGDTSvLKPTLMAAVPEIMDRIYknvmnkvnemsafqrnlf 257
Cdd:PRK09088 190 GLITSVrPVLAVGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAFR------------------ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 258 ilaynykmeqiskgcSTPlcdRFVFRNVRRLLGgnirlLLCGGAPLSATTQRFMnICFCCPVGQGYGLTEstgAGTI--- 334
Cdd:PRK09088 242 ---------------AQP---GFDAAALRHLTA-----LFTGGAPHAAEDILGW-LDDGIPMVDGFGMSE---AGTVfgm 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 335 ---TEVWDYNTGRVGAPLVCCEIKLKNWEEggyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTG 411
Cdd:PRK09088 295 svdCDVIRAKAGAAGIPTPTVQTRVVDDQG----NDCPAGVPGELLLRGPNLSPGYWRRPQATARAF--TGDG--WFRTG 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 209977076 412 DIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLI 455
Cdd:PRK09088 367 DIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
78-453 |
1.07e-16 |
|
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: 83.02 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 78 RLRHIITvDGKPP---TWSEFPKGVIVHTMAAVQALGVKANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIA 154
Cdd:cd12117 85 RLAFMLA-DAGAKvllTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 155 SITGmaRRIPRLGEEDVYIGYLPL---AHVLELsaeLVCLSHGCRIGYSSPQTLADQSSkikkgskgdtsvlkptLMAAV 231
Cdd:cd12117 164 LVKN--TNYVTLGPDDRVLQTSPLafdASTFEI---WGALLNGARLVLAPKGTLLDPDA----------------LGALI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 232 PEimdriyknvmNKVNEM---SAfqrnLF-ILAynykmeQISKGCstplcdrfvFRNVRRLL-GGN------IRLLLCGG 300
Cdd:cd12117 223 AE----------EGVTVLwltAA----LFnQLA------DEDPEC---------FAGLRELLtGGEvvspphVRRVLAAC 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 301 APLsattqRFMNicfccpvgqGYGLTESTGAGT---ITEVwDYNTGRV--GAPLVcceiklknweeggyfNTD------- 368
Cdd:cd12117 274 PGL-----RLVN---------GYGPTENTTFTTshvVTEL-DEVAGSIpiGRPIA---------------NTRvyvlded 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 369 -KPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSL 442
Cdd:cd12117 324 gRPVPPgvpGELYVGGDGLALGYLNRPALTAERFVADpfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIR-GFRIEL 402
|
410
....*....|.
gi 209977076 443 GKVEAALKNLP 453
Cdd:cd12117 403 GEIEAALRAHP 413
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
128-449 |
1.31e-16 |
|
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: 82.12 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDV-------YIGYlplahvlelsaelvCLSHGCRIGYS 200
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRvfssakmFFGY--------------GLGNSLWFPLA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 201 SpqtladqsskikkgskGDTSVLKPTlmAAVPEimdriykNVMNKvneMSAFQRNLFIlaynykmeqiskgcSTPLcdrf 280
Cdd:cd05919 158 V----------------GASAVLNPG--WPTAE-------RVLAT---LARFRPTVLY--------------GVPT---- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 VFRNVRRLLGG------NIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEI 354
Cdd:cd05919 192 FYANLLDSCAGspdalrSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 355 KLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVKL 434
Cdd:cd05919 272 RLVD-EEG---HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-----WYRTGDKFCRDADGWYTHAGRADDMLKV 342
|
330
....*....|....*
gi 209977076 435 qAGEYVSLGKVEAAL 449
Cdd:cd05919 343 -GGQWVSPVEVESLI 356
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
96-566 |
1.57e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 83.00 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 96 PKGVIVHTMAAVQALGVKANVEKkAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEED-VYIG 174
Cdd:PRK08180 179 VPGRAATPFAALLATPPTAAVDA-AHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpVLVD 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 175 YLPLAHVLELSAEL-VCLSHGcriGysspqTLAdqsskIKKGskgdtsvlKPT--LMAA----VPEIMDRIYKNVmNKVN 247
Cdd:PRK08180 258 WLPWNHTFGGNHNLgIVLYNG---G-----TLY-----IDDG--------KPTpgGFDEtlrnLREISPTVYFNV-PKGW 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 248 EMsafqrnlfILAYnykMEQiskgcSTPLCDRFvFRNVRrllggnirLLLCGGAPLSATT----QRF-MNIC-----FCC 317
Cdd:PRK08180 316 EM--------LVPA---LER-----DAALRRRF-FSRLK--------LLFYAGAALSQDVwdrlDRVaEATCgerirMMT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 318 pvgqGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKnwEEGGYFntdkphprgEILIGGQNVTMGYYKNEAKTKTD 397
Cdd:PRK08180 371 ----GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLV--PVGGKL---------EVRVKGPNVTPGYWRAPELTAEA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 398 FfeDENGqrWLCTGDIGEF-DPDgclkiiDRKKDLV---------KLQAGEYVSLGKVEAALKNL--PLIDNICAyANSY 465
Cdd:PRK08180 436 F--DEEG--YYRSGDAVRFvDPA------DPERGLMfdgriaedfKLSSGTWVSVGPLRARAVSAgaPLVQDVVI-TGHD 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 466 HSYVIGFVVPNQKELTELARTKGFkGTWEELCNSSEMEN---EVLKVLSEAAISASLEkfeiPLKIRLSPDPWTPETGLV 542
Cdd:PRK08180 505 RDEIGLLVFPNLDACRRLAGLLAD-ASLAEVLAHPAVRAafrERLARLNAQATGSSTR----VARALLLDEPPSLDAGEI 579
|
490 500
....*....|....*....|....
gi 209977076 543 TDAFKLKRKELKTHYQADIERMYG 566
Cdd:PRK08180 580 TDKGYINQRAVLARRAALVEALYA 603
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2-459 |
3.14e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 81.54 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDIVSLvpRLRH 81
Cdd:PRK08314 56 CGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNL--RLRH 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 II--------TVDG--KPPTWSEFPKGVIVHTMAAVQAL--GVKANVEKKAHSkPLPSDIAVIMYTSGSTGIPKGVMISH 149
Cdd:PRK08314 134 VIvaqysdylPAEPeiAVPAWLRAEPPLQALAPGGVVAWkeALAAGLAPPPHT-AGPDDLAVLPYTSGTTGVPKGCMHTH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 150 SNIIASITGMARRIpRLGEEDVYIGYLPLAHVLelsaelvclshGCRIGYSSPqtladqsskIKKGSkgdTSVLKPTL-M 228
Cdd:PRK08314 213 RTVMANAVGSVLWS-NSTPESVVLAVLPLFHVT-----------GMVHSMNAP---------IYAGA---TVVLMPRWdR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 229 AAVPEIMDRiYKnVMNKVNeMSAFQRNLFilaynykmeqiskgcSTPLCDRFVFRNVrRLLGGnirlllcGGAPL-SATT 307
Cdd:PRK08314 269 EAAARLIER-YR-VTHWTN-IPTMVVDFL---------------ASPGLAERDLSSL-RYIGG-------GGAAMpEAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 308 QRFM---NICFCcpvgQGYGLTEsTGAGTITEVWDyntgrvgAP-LVCCEIKLknweeggyFNTD---------KPHPR- 373
Cdd:PRK08314 323 ERLKeltGLDYV----EGYGLTE-TMAQTHSNPPD-------RPkLQCLGIPT--------FGVDarvidpetlEELPPg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 374 --GEILIGGQNVTMGYYKNEAKTKTDFFEDEnGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKN 451
Cdd:PRK08314 383 evGEIVVHGPQVFKGYWNRPEATAEAFIEID-GKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYK 460
|
....*...
gi 209977076 452 LPLIDNIC 459
Cdd:PRK08314 461 HPAIQEAC 468
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
120-449 |
3.17e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 81.19 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 120 AHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEeDVYIGYLPLAHVlelsaelvclsHGC---- 195
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHV-----------HGLvlgv 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 196 ----RIGYS-------SPQTLADQSSkikkgskgdtsvLKPTLMAAVPEIMDRIYKNvmnkvnEMSAfqrnlfilaynyk 264
Cdd:PRK07787 189 lgplRIGNRfvhtgrpTPEAYAQALS------------EGGTLYFGVPTVWSRIAAD------PEAA------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 265 meqiskgcstplcdrfvfrnvrRLLGGnIRLLLCGGAPLSATT-QRFMNICFCCPVgQGYGLTE-----STGA-Gtitev 337
Cdd:PRK07787 238 ----------------------RALRG-ARLLVSGSAALPVPVfDRLAALTGHRPV-ERYGMTEtlitlSTRAdG----- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 338 wDYNTGRVGAPLVCCEIKLKnwEEGGyfnTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIG 414
Cdd:PRK07787 289 -ERRPGWVGLPLAGVETRLV--DEDG---GPVPHDGetvGELQVRGPTLFDGYLNRPDATAAAFTADG----WFRTGDVA 358
|
330 340 350
....*....|....*....|....*....|....*..
gi 209977076 415 EFDPDGCLKIIDRKK-DLVKlqAGEY-VSLGKVEAAL 449
Cdd:PRK07787 359 VVDPDGMHRIVGREStDLIK--SGGYrIGAGEIETAL 393
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
123-432 |
5.46e-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: 80.61 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 123 KPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSA-ELVCLSHGCRigyss 201
Cdd:cd05908 102 CELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST-EWKTKDRILSWMPLTHDMGLIAfHLAPLIAGMN----- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 202 pQTLADQSSKIKkgskgdtsvlKPTLMaavpeimdrIYKNVMNKVNEMSA--FQRNLFI------LAYNYKMEQI----- 268
Cdd:cd05908 176 -QYLMPTRLFIR----------RPILW---------LKKASEHKATIVSSpnFGYKYFLktlkpeKANDWDLSSIrmiln 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 269 -SKGCSTPLCDRFVFRNVRRLLGGNIRLLLCGGAPLS-ATTQRFMNICFCCPVGQGYGLTESTGAGTI--TEVWDYNTGR 344
Cdd:cd05908 236 gAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASvGASLPKAQSPFKTITLGRRHVTHGEPEPEVdkKDSECLTFVE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 345 VGAPLVCCEIKLKNWE----EGGYFntdkphprGEILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGeFDPDG 420
Cdd:cd05908 316 VGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEATAKVFTDDG----WLKTGDLG-FIRNG 382
|
330
....*....|..
gi 209977076 421 CLKIIDRKKDLV 432
Cdd:cd05908 383 RLVITGREKDII 394
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
2-453 |
5.96e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 80.67 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQTKLKdivslvprLRH 81
Cdd:PRK06839 48 LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALS--------MQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IITVdgKPPTWSEFPKGVIVHTmaavqalgvKANVEKKAHSKPLpsdiaVIMYTSGSTGIPKGVMISHSNIIASITGMAR 161
Cdd:PRK06839 120 VSYV--QRVISITSLKEIEDRK---------IDNFVEKNESASF-----IICYTSGTTGKPKGAVLTQENMFWNALNNTF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 162 RIPrLGEEDVYIGYLPLAHV--LELSAeLVCLSHGCRIgysspqTLADQSSKIKKGSKGDTSvlKPTLMAAVPEIMDRIY 239
Cdd:PRK06839 184 AID-LTMHDRSIVLLPLFHIggIGLFA-FPTLFAGGVI------IVPRKFEPTKALSMIEKH--KVTVVMGVPTIHQALI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 240 KnvmnkvnemsafqrnlfilaynykmeqiskgcstplCDRFVFRNVRrllggNIRLLLCGGAPLSAT-TQRFMNICFccP 318
Cdd:PRK06839 254 N------------------------------------CSKFETTNLQ-----SVRWFYNGGAPCPEElMREFIDRGF--L 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 319 VGQGYGLTESTGAGTITEVWDY--NTGRVGAPLVCCEIKL-----KNWEEGGYfntdkphprGEILIGGQNVTMGYYKNE 391
Cdd:PRK06839 291 FGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELidenkNKVEVGEV---------GELLIRGPNVMKEYWNRP 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977076 392 AKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 453
Cdd:PRK06839 362 DATEETI---QDG--WLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLS 417
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
126-453 |
9.42e-16 |
|
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: 79.06 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARrIPRLGEEDVYIGYLPLAHVLELSAELVC-LSHGCRIGYSSPQt 204
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLAL-NSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAGPA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 205 ladqsskikkGSKGDTSV---------LKPTLMAAVPEIMdriyknvmnkvnemsafqrnlfilaynykmeqiskgcsTP 275
Cdd:cd05944 79 ----------GYRNPGLFdnfwklverYRITSLSTVPTVY--------------------------------------AA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 276 LCDRFVFRNVrrllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTIT-EVWDYNTGRVGAPLVCCEI 354
Cdd:cd05944 111 LLQVPVNADI-----SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNpPDGPKRPGSVGLRLPYARV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 355 KLKNWE-EGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKtKTDFFEDengqRWLCTGDIGEFDPDGCLKIIDRKKDLVk 433
Cdd:cd05944 186 RIKVLDgVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGN-KNAFVAD----GWLNTGDLGRLDADGYLFITGRAKDLI- 259
|
330 340
....*....|....*....|
gi 209977076 434 LQAGEYVSLGKVEAALKNLP 453
Cdd:cd05944 260 IRGGHNIDPALIEEALLRHP 279
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
126-475 |
1.14e-15 |
|
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: 79.28 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrlGEEdvyigylpLAHVL-------ELSA-ELVC-LSHGCR 196
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFS--AEE--------LAGVLastsicfDLSVfELFGpLATGGK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 197 IgysspqTLADQS-SKIKKGSKGDTSVLK--PTLMAAVPEiMDRIYKNV--MNKVNEmsAFQRNLfiLAYNYKMEQIskg 271
Cdd:cd12115 174 V------VLADNVlALPDLPAAAEVTLINtvPSAAAELLR-HDALPASVrvVNLAGE--PLPRDL--VQRLYARLQV--- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 272 cstplcdrfvfRNVRRLLGgnirlllcggaPLSATTQRFMnicfcCPVGQGYGLTESTG---AGTITEVWDyntgRVGAP 348
Cdd:cd12115 240 -----------ERVVNLYG-----------PSEDTTYSTV-----APVPPGASGEVSIGrplANTQAYVLD----RALQP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 349 LvcceiklknweeggyfntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIID 426
Cdd:cd12115 289 V-------------------PLGVPGELYIGGAGVARGYLGRPGLTAERFLPDpfGPGARLYRTGDLVRWRPDGLLEFLG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 209977076 427 RKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 475
Cdd:cd12115 350 RADNQVKVR-GFRIELGEIEAALRSIPGVREAVVVAigdAAGERRLVAYIVA 400
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
126-486 |
1.40e-15 |
|
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: 79.29 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPL---AHVLELSAELVClSHGCRIgyssp 202
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIsfdASVTEIFASLLS-GNTLYI----- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 203 qtladqsskIKKGSKGDtsvlkptlmaaVPEIMDRIYKnvmNKVNEMSAFQRNLFILAYNykmeQISKGCStplcdrfvf 282
Cdd:cd17655 209 ---------VRKETVLD-----------GQALTQYIRQ---NRITIIDLTPAHLKLLDAA----DDSEGLS--------- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 283 rnvrrllggnIRLLLCGGAPLSATTQRFMNICFC--CPVGQGYGLTESTGAGTI--TEVWDYNTGRV--GAPLVCCEIKL 356
Cdd:cd17655 253 ----------LKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 KNwEEGgyfntdKPHP---RGEILIGGQNVTMGYYKNEAKTKTDFFEDE--NGQRWLCTGDIGEFDPDGCLKIIDRKKDL 431
Cdd:cd17655 323 LD-QYG------RPQPvgvAGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209977076 432 VKLQaGEYVSLGKVEAALKNLPLIDNICAYANSYHS---YVIGFVVPNqKELT------ELART 486
Cdd:cd17655 396 VKIR-GYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnYLCAYIVSE-KELPvaqlreFLARE 457
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
67-566 |
1.44e-15 |
|
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: 79.78 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 67 TKLKDIVSLV-PRL----------RHIITV--DGKPPTWS-EFPKGVIVHTMAAVQALGVKANVEKkAHSKPLPSDIAVI 132
Cdd:cd05921 92 AKLKHLFELLkPGLvfaqdaapfaRALAAIfpLGTPLVVSrNAVAGRGAISFAELAATPPTAAVDA-AFAAVGPDTVAKF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 133 MYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEED-VYIGYLPLAHVLELSA--ELVCLSHGcrigysspqTLADQS 209
Cdd:cd05921 171 LFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNHTFGGNHnfNLVLYNGG---------TLYIDD 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 210 SKIKKGSKGDTsvlkptlMAAVPEIMDRIYKNVMNKVNEMSAFQRNlfilaynykmeqiskgcSTPLCDRFvFRNVrrll 289
Cdd:cd05921 242 GKPMPGGFEET-------LRNLREISPTVYFNVPAGWEMLVAALEK-----------------DEALRRRF-FKRL---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 290 ggniRLLLCGGAPLS------------ATTQRFMnicfccPVGQGYGLTESTGAGTITeVWDYN-TGRVGAPLVCCEIKL 356
Cdd:cd05921 293 ----KLMFYAGAGLSqdvwdrlqalavATVGERI------PMMAGLGATETAPTATFT-HWPTErSGLIGLPAPGTELKL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 KnwEEGGYFntdkphprgEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEF-DPDgclkiiDRKKDLV--- 432
Cdd:cd05921 362 V--PSGGKY---------EVRVKGPNVTPGYWRQPELTAQAF--DEEG--FYCLGDAAKLaDPD------DPAKGLVfdg 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 433 ------KLQAGEYVSLGKVEAALKNL--PLIDN--ICAYANSYhsyvIGF-VVPNQKELTELARTKGFKgtweelcnsse 501
Cdd:cd05921 421 rvaedfKLASGTWVSVGPLRARAVAAcaPLVHDavVAGEDRAE----VGAlVFPDLLACRRLVGLQEAS----------- 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209977076 502 mENEVLKVLS-EAAISASLEKFE--------IPLKIRLSPDPWTPETGLVTDAFKLKRKELKTHYQADIERMYG 566
Cdd:cd05921 486 -DAEVLRHAKvRAAFRDRLAALNgeatgsssRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYA 558
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
125-487 |
1.80e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 79.16 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 125 LPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSAELVC-LSHGCRI-----G 198
Cdd:PRK05852 174 LRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYHGHGLIAALLAtLASGGAVllparG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 199 YSSPQTLADqsskikkgskgDTSVLKPTLMAAVPEIMDriyknvmnkvnemsafqrnlfILAYNYKMEQISKGcstplcd 278
Cdd:PRK05852 253 RFSAHTFWD-----------DIKAVGATWYTAVPTIHQ---------------------ILLERAATEPSGRK------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 279 RFVFRNVRRllggnirlllCGgAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEV-WDYNT----------GRVGA 347
Cdd:PRK05852 294 PAALRFIRS----------CS-APLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIeGIGQTenpvvstglvGRSTG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 348 PlvccEIKLKNwEEGGYFntdKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDR 427
Cdd:PRK05852 363 A----QIRIVG-SDGLPL---PAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG-----WLRTGDLGSLSAAGDLSIRGR 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 428 KKDLVKlQAGEYVSLGKVEAALKNLPLIDNICAYANSYHSY---VIGFVVPNQ------KELTELARTK 487
Cdd:PRK05852 430 IKELIN-RGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPREsapptaEELVQFCRER 497
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
68-447 |
1.96e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 79.32 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 68 KLKDIVSLV-PRL----------RHIITVDGKPPTW---SEFPKGVIVHTMAAVQALGVKANVEKkAHSKPLPSDIAVIM 133
Cdd:PRK12582 148 KLKHLFDLVkPRVvfaqsgapfaRALAALDLLDVTVvhvTGPGEGIASIAFADLAATPPTAAVAA-AIAAITPDTVAKYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 134 YTSGSTGIPKGVMISHSNIIASITGMA--RRIPRLGEEDVYIGYLPLAHVLELSAELvclsHGCRIGYSspqTLADQSSK 211
Cdd:PRK12582 227 FTSGSTGMPKAVINTQRMMCANIAMQEqlRPREPDPPPPVSLDWMPWNHTMGGNANF----NGLLWGGG---TLYIDDGK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 212 IKKGSKGDTsvlkptlMAAVPEIMDRIYKNVMnkvnemsafqrnlfiLAYNYKMEQISKgcSTPLCDRFvFRNvrrllgg 291
Cdd:PRK12582 300 PLPGMFEET-------IRNLREISPTVYGNVP---------------AGYAMLAEAMEK--DDALRRSF-FKN------- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 292 nIRLLLCGGAPLS-------------ATTQRFmnicfccPVGQGYGLTEStgAGTITEV-WDYN-TGRVGAPLVCCEIKL 356
Cdd:PRK12582 348 -LRLMAYGGATLSddlyermqalavrTTGHRI-------PFYTGYGATET--APTTTGThWDTErVGLIGLPLPGVELKL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 357 KnweeggyfntdkphPRG---EILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEF-DPDGCLK--IID-RKK 429
Cdd:PRK12582 418 A--------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAF--DEEG--FYRLGDAARFvDPDDPEKglIFDgRVA 479
|
410
....*....|....*...
gi 209977076 430 DLVKLQAGEYVSLGKVEA 447
Cdd:PRK12582 480 EDFKLSTGTWVSVGTLRP 497
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
10-487 |
4.30e-15 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 78.23 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 10 IAIFCETRAEWMIAAQACFmynfQL----VTLYATLGGPAIVHGLNETEVTNIITSKEL--------LQTKLKDIVSLVP 77
Cdd:COG0365 67 VAIYLPNIPEAVIAMLACA----RIgavhSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidLKEKVDEALEELP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 78 RLRHIITVD--GKPPTWSEfpkgviVHTMAAVQAlgvkaNVEKKAHSKPLPS-DIAVIMYTSGSTGIPKGVMISHSNIIA 154
Cdd:COG0365 143 SLEHVIVVGrtGADVPMEG------DLDWDELLA-----AASAEFEPEPTDAdDPLFILYTSGTTGKPKGVVHTHGGYLV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 155 SITGMARRIPRLGEEDVYIGYLPLAHVLELSAELV-CLSHGC-------RIGYSSPQTLADQSSKikkgskgdtsvLKPT 226
Cdd:COG0365 212 HAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYgPLLNGAtvvlyegRPDFPDPGRLWELIEK-----------YGVT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 227 LMAAVPeimdRIYKNVMNKVNEMSAfQRNLfilaynykmeqiskgcSTplcdrfvfrnvrrllggnIRLLLCGGAPLSAT 306
Cdd:COG0365 281 VFFTAP----TAIRALMKAGDEPLK-KYDL----------------SS------------------LRLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 307 TQRFMNICFCCPVGQGYGLTESTGA-GT---ITEVWDyntGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQN 382
Cdd:COG0365 322 VWEWWYEAVGVPIVDGWGQTETGGIfISnlpGLPVKP---GSMGKPVPGYDVAVVD-EDG---NPVPPGEEGELVIKGPW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 383 VTM--GYYKNEAKTKTDFFEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLIDNiCA 460
Cdd:COG0365 395 PGMfrGYWNDPERYRETYFGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINV-SGHRIGTAEIESALVSHPAVAE-AA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 209977076 461 yansyhsyVIG------------FVVPNQ---------KELTELARTK 487
Cdd:COG0365 471 --------VVGvpdeirgqvvkaFVVLKPgvepsdelaKELQAHVREE 510
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
58-449 |
5.34e-15 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 77.57 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 58 IITSKELLQTkLKDIVSLVPRLRHIITVDGKPPTWSEFpkgvivhtmaaVQALGVKANVEKKAHSKPlpSDIAVIMYTSG 137
Cdd:TIGR02262 106 VFVSGALLPV-IKAALGKSPHLEHRVVVGRPEAGEVQL-----------AELLATESEQFKPAATQA--DDPAFWLYSSG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 138 STGIPKGVMISHSNIIASITGMARRIPRLGEEDVYigylplahvleLSAELVCLSHGCRIGYSSPQTLadqsskikkgsk 217
Cdd:TIGR02262 172 STGMPKGVVHTHSNPYWTAELYARNTLGIREDDVC-----------FSAAKLFFAYGLGNALTFPMSV------------ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 218 GDTSVL---KPTlMAAVPEIMDRiyknvmnkvnemsaFQRNLFIlaynykmeqiskGCSTPLCDRFVFRNVRRLLGGNIR 294
Cdd:TIGR02262 229 GATTVLmgeRPT-PDAVFDRLRR--------------HQPTIFY------------GVPTLYAAMLADPNLPSEDQVRLR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 295 LLLCGGAPLSATTQRFMNICFCCPVGQGYGLTE------STGAGtitevwDYNTGRVGAPLVCCEIKLKNwEEGGYFNTD 368
Cdd:TIGR02262 282 LCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEmlhiflSNLPG------DVRYGTSGKPVPGYRLRLVG-DGGQDVADG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 369 KPhprGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAA 448
Cdd:TIGR02262 355 EP---GELLISGPSSATMYWNNRAKSRDTFQGE-----WTRSGDKYVRNDDGSYTYAGRTDDMLKV-SGIYVSPFEIESA 425
|
.
gi 209977076 449 L 449
Cdd:TIGR02262 426 L 426
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
78-496 |
7.95e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 77.24 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 78 RLRHIITVdGKPP---TWSEFP---KGVIVHTMAAVQALGVKANVEKKAHS-KPlpSDIAVIMYTSGSTGIPKGVMISHS 150
Cdd:PRK04813 90 RIEMIIEV-AKPSliiATEELPleiLGIPVITLDELKDIFATGNPYDFDHAvKG--DDNYYIIFTSGTTGKPKGVQISHD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 151 NIIaSITGMARRIPRLGEEDVYIGYLP---------LAHVLELSAELVCLSHgcrigysspqtlaDQSSKIKkgskgdts 221
Cdd:PRK04813 167 NLV-SFTNWMLEDFALPEGPQFLNQAPysfdlsvmdLYPTLASGGTLVALPK-------------DMTANFK-------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 222 vlkpTLMAAVPEImdriyknvmnKVN---------EMSafqrnlfILAYNYKMEQIskgcstPLCDRFVFrnvrrllggn 292
Cdd:PRK04813 225 ----QLFETLPQL----------PINvwvstpsfaDMC-------LLDPSFNEEHL------PNLTHFLF---------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 293 irlllCGGApLSATT-----QRF-----MNIcfccpvgqgYGLTESTGAGT---IT-EVWD-YNTGRVGAPLVCCEIKLK 357
Cdd:PRK04813 268 -----CGEE-LPHKTakkllERFpsatiYNT---------YGPTEATVAVTsieITdEMLDqYKRLPIGYAKPDSPLLII 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 358 NWEEGGYFNTDKphprGEILIGGQNVTMGYYKNEAKTKTDFFEdENGQRWLCTGDIGEFDpDGCLKIIDRKKDLVKLqAG 437
Cdd:PRK04813 333 DEEGTKLPDGEQ----GEIVISGPSVSKGYLNNPEKTAEAFFT-FDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKL-NG 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209977076 438 EYVSLGKVEAALKNLPLIDNICA---YANSYHSYVIGFVVPNQKELT-ELARTKGFKgtwEEL 496
Cdd:PRK04813 406 YRIELEEIEQNLRQSSYVESAVVvpyNKDHKVQYLIAYVVPKEEDFErEFELTKAIK---KEL 465
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
126-475 |
9.92e-15 |
|
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: 76.44 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIAsitgmarriprlgeedvyigylplahvlelsaelVCLSHGCRIGYsspqTL 205
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVN----------------------------------LCEWHRPYFGV----TP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 ADQSSKIKkGSKGDTSVLK--PTLMA-AVPEIMDRIYKNVMNKVNEMsaFQRNLFILAYnykmeqiskgCSTPLCDRFVf 282
Cdd:cd17645 145 ADKSLVYA-SFSFDASAWEifPHLTAgAALHVVPSERRLDLDALNDY--FNQEGITISF----------LPTGAAEQFM- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 283 rnvrRLLGGNIRLLLCGGAPLSATTQRFMNICfccpvgQGYGLTESTGAGTITEV-WDYNTGRVGAPLVCCEIKLKNweE 361
Cdd:cd17645 211 ----QLDNQSLRVLLTGGDKLKKIERKGYKLV------NNYGPTENTVVATSFEIdKPYANIPIGKPIDNTRVYILD--E 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 362 GgyfNTDKPH-PRGEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGE 438
Cdd:cd17645 279 A---LQLQPIgVAGELCIAGEGLARGYLNRPELTAEKFIVHpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR-GY 354
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 209977076 439 YVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 475
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIELAAVLAkedADGRKYLVAYVTA 394
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
127-528 |
1.10e-14 |
|
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: 76.22 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 127 SDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIgylplahvlelsaelvclshgcrigysspqTLA 206
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWL-GLRPDDIHW------------------------------NIA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 207 DqsSKIKKGSKGdtSVLKPTLMAAVpeimdriykNVMNKVNEMSAfqRNLFILAYNYKmeqISKGCSTPLcdrfVFRNVR 286
Cdd:cd05972 130 D--PGWAKGAWS--SFFGPWLLGAT---------VFVYEGPRFDA--ERILELLERYG---VTSFCGPPT----AYRMLI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 287 RLLG-----GNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNwEE 361
Cdd:cd05972 188 KQDLssykfSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 362 GgyfNTDKPHPRGEILIGGQNVTM--GYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEY 439
Cdd:cd05972 267 G---RELPPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD-----YYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 440 VSLGKVEAALKNLPLIdNICAYANS----YHSYVIGFVVpnqkeltelaRTKGFKGTwEELCNssEMENEVLKVLSEAAI 515
Cdd:cd05972 338 IGPFEVESALLEHPAV-AEAAVVGSpdpvRGEVVKAFVV----------LTSGYEPS-EELAE--ELQGHVKKVLAPYKY 403
|
410
....*....|....*
gi 209977076 516 SASLEkF--EIPLKI 528
Cdd:cd05972 404 PREIE-FveELPKTI 417
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
127-474 |
1.86e-14 |
|
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: 74.99 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 127 SDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLA 206
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 207 DQSSKIKKGSKGDTSVLKPTLMAAVPEimdrIYKNVMNKVNEMsafqrnlfilaynykmeqiskgcstplcdrfvfrnvr 286
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVS----ELKSANATVPSL------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 287 rllggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDY-NTGRVGAPLVCCEIKLKNWEEGGYF 365
Cdd:cd17635 120 -------RLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSiEINAVGRPYPGVDVYLAATDGIAGP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 366 NTDKphprGEILIGGQNVTMGYYKNEAKTKTDFFEDengqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKV 445
Cdd:cd17635 193 SASF----GTIWIKSPANMLGYWNNPERTAEVLIDG-----WVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDEV 262
|
330 340 350
....*....|....*....|....*....|..
gi 209977076 446 EAALKNLPLIDNICAYA---NSYHSYVIGFVV 474
Cdd:cd17635 263 ERIAEGVSGVQECACYEisdEEFGELVGLAVV 294
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
126-482 |
2.46e-14 |
|
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: 75.51 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGYLPlAHVLELSAELVCLShgcrigYSSPQTL 205
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFS-NYVFDFFVEQMTLA------LLNGQKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 adqsskikkgskgdtsVLKPTLMAAVPeimDRIYKnVMNKvnemsafqrnlfilaynykmEQISKGCSTP-LCDRFVFRN 284
Cdd:cd17648 166 ----------------VVPPDEMRFDP---DRFYA-YINR--------------------EKVTYLSGTPsVLQQYDLAR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 285 VRRLlggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEvwdYNTGR-----VGAPL--VCCEIklk 357
Cdd:cd17648 206 LPHL-----KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRF---FPGDQrfdksLGRPVrnTKCYV--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 358 nweeggyFNTD-KPHP---RGEILIGGQNVTMGYYKNEAKTKTDF----FEDE------NGQRWLCTGDIGEFDPDGCLK 423
Cdd:cd17648 275 -------LNDAmKRVPvgaVGELYLGGDGVARGYLNRPELTAERFlpnpFQTEqerargRNARLYKTGDLVRWLPSGELE 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209977076 424 IIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI---------DNICAYANSyHSYVIGFVVPNQKELTE 482
Cdd:cd17648 348 YLGRNDFQVKIR-GQRIEPGEVEAALASYPGVrecavvakeDASQAQSRI-QKYLVGYYLPEPGHVPE 413
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
128-453 |
2.98e-14 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 74.07 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARrIPRLGEEDVYIGYLPLAHVLELSAE-LVCLSHGCRIgysSPQTLA 206
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFHTFGYKAGiVACLLTGATV---VPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 207 DQSSKIKKGSKGDTSVL--KPTLmaavpeimdriyknvmnkvnemsaFQRNLfilaynykmeqiskgcSTPLCDRFVFrn 284
Cdd:cd17638 77 DVDAILEAIERERITVLpgPPTL------------------------FQSLL----------------DHPGRKKFDL-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 285 vrrllgGNIRLLLCGGAPLSATTQR-------FMNicfccpVGQGYGLTEStGAGTITEVWDYNT---GRVGAPLVCCEI 354
Cdd:cd17638 115 ------SSLRAAVTGAATVPVELVRrmrselgFET------VLTAYGLTEA-GVATMCRPGDDAEtvaTTCGRACPGFEV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 355 KLKNweeggyfntdkphpRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkL 434
Cdd:cd17638 182 RIAD--------------DGEVLVRGYNVMQGYLDDPEATAEAI--DADG--WLHTGDVGELDERGYLRITDRLKDMY-I 242
|
330
....*....|....*....
gi 209977076 435 QAGEYVSLGKVEAALKNLP 453
Cdd:cd17638 243 VGGFNVYPAEVEGALAEHP 261
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
126-453 |
1.71e-13 |
|
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: 72.79 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPL---AHVLELSAELVClshGCRIGYSSP 202
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERY-GLTPGDRELQFASFnfdGAHEQLLPPLIC---GACVVLRPD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 203 QTLADQsskikkgskgdtsvlkptlmAAVPEIMDRIYKNVMNkvnemsafqrnlFILAYNYKMEQiskgcstplcdrfVF 282
Cdd:cd17649 169 ELWASA--------------------DELAEMVRELGVTVLD------------LPPAYLQQLAE-------------EA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 283 RNVRRLLGGNIRLLLCGGAPLSATTQR--FMNICFCCpvgQGYGLTEstgaGTITE-VWDYNTGR--------VGAPLvc 351
Cdd:cd17649 204 DRTGDGRPPSLRLYIFGGEALSPELLRrwLKAPVRLF---NAYGPTE----ATVTPlVWKCEAGAaragasmpIGRPL-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 352 ceiklknweeGGY----FNTD-KPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDG 420
Cdd:cd17649 275 ----------GGRsayiLDADlNPVPVgvtGELYIGGEGLARGYLGRPELTAERFVPDpfgAPGSRLYRTGDLARWRDDG 344
|
330 340 350
....*....|....*....|....*....|...
gi 209977076 421 CLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 453
Cdd:cd17649 345 VIEYLGRVDHQVKIR-GFRIELGEIEAALLEHP 376
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-565 |
1.86e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.84 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 105 AAVQALGVKANVEKKAHSKP----LPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAH 180
Cdd:PRK12316 3170 QGVQVLDLDRGDENYAEANPairtMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG-LGVGDRVLQFTTFSF 3248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 181 VLELSAELVCLSHGCRIGYSSPQTLADQsskikkgskgdtsvlkptlmAAVPEIMDRIYKNVMNKVNEMsafqrnlfila 260
Cdd:PRK12316 3249 DVFVEELFWPLMSGARVVLAGPEDWRDP--------------------ALLVELINSEGVDVLHAYPSM----------- 3297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 261 ynykmeqiskgcstpLCDRFVFRNVRRLlgGNIRLLLCGGAPLSATTQRFMNICFccPVGQGYGLTESTGAGTITEVWDY 340
Cdd:PRK12316 3298 ---------------LQAFLEEEDAHRC--TSLKRIVCGGEALPADLQQQVFAGL--PLYNLYGPTEATITVTHWQCVEE 3358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 341 NTGR--VGAPLVCCEIKLKNweegGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEF 416
Cdd:PRK12316 3359 GKDAvpIGRPIANRACYILD----GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDpfVPGERLYRTGDLARY 3434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 417 DPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYANSYHSyVIGFVVPNQKEltelartkgfkGTWEel 496
Cdd:PRK12316 3435 RADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDEA-----------GDLR-- 3499
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 497 cnssemenEVLKvlseAAISASLEKFEIPLK-IRLSPDPWTPETglvtdafKLKRKELKTHYQADIERMY 565
Cdd:PRK12316 3500 --------EALK----AHLKASLPEYMVPAHlLFLERMPLTPNG-------KLDRKALPRPDAALLQQDY 3550
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-553 |
2.65e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRiPRLGEEDVYIGYLPLA---HVLELSAELVClshGCRI----- 197
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFSfdgSHEGLYHPLIN---GASVvirdd 4768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 GYSSPQTLADQSSKikkgskgdtsvLKPTLMAAVPeimdriyknvmnkvnemSAFQrnlfilaynykmeQISKGCStplc 277
Cdd:PRK12316 4769 SLWDPERLYAEIHE-----------HRVTVLVFPP-----------------VYLQ-------------QLAEHAE---- 4803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 278 drfvfrnvRRLLGGNIRLLLCGGAPLSATTQRFMnICFCCPVG--QGYGLTESTGAGTITEVWDYNT-GRVGAPLvccEI 354
Cdd:PRK12316 4804 --------RDGEPPSLRVYCFGGEAVAQASYDLA-WRALKPVYlfNGYGPTETTVTVLLWKARDGDAcGAAYMPI---GT 4871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 355 KLKNweEGGYFNTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIID 426
Cdd:PRK12316 4872 PLGN--RSGYVLDGQLNPLpvgvaGELYLGGEGVARGYLERPALTAERFVPDpfgAPGGRLYRTGDLARYRADGVIDYLG 4949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 427 RKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPNQKELTElartkgfkgtweelcnSSEMEN 504
Cdd:PRK12316 4950 RVDHQVKIR-GFRIELGEIEARLREHPAVREavVIAQEGAVGKQLVGYVVPQDPALAD----------------ADEAQA 5012
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 209977076 505 EVLKVLsEAAISASLEKFEIPLK-IRLSPDPWTPETglvtdafKLKRKEL 553
Cdd:PRK12316 5013 ELRDEL-KAALRERLPEYMVPAHlVFLARMPLTPNG-------KLDRKAL 5054
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-553 |
4.55e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.68 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTL 205
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 ADqsskikkgskgdtsvlkptlMAAVPEIMDRIYKNVMNKVNEM-SAFQRNLFIlaynykmeqiskgcstPLCDrfvfrn 284
Cdd:PRK12316 733 RD--------------------PAKLVELINREGVDTLHFVPSMlQAFLQDEDV----------------ASCT------ 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 285 vrrllggNIRLLLCGGAPLSATTQ-RFMNICFCCPVGQGYGLTESTGAGT----ITEVWDynTGRVGAPL--VCCEIKLK 357
Cdd:PRK12316 771 -------SLRRIVCSGEALPADAQeQVFAKLPQAGLYNLYGPTEAAIDVThwtcVEEGGD--SVPIGRPIanLACYILDA 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 358 NWEeggyfntdkPHP---RGEILIGGQNVTMGYYKNEAKTKTDFFEDE--NGQRWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK12316 842 NLE---------PVPvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQV 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 433 KLQaGEYVSLGKVEAALKNLPLIDNICAYANSYHSYViGFVVPnqkeltelartkgfkgtweelcnssEMENEVLKVLSE 512
Cdd:PRK12316 913 KLR-GLRIELGEIEARLLEHPWVREAAVLAVDGKQLV-GYVVL-------------------------ESEGGDWREALK 965
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 209977076 513 AAISASLEKFEIPLKI-RLSPDPWTPETglvtdafKLKRKEL 553
Cdd:PRK12316 966 AHLAASLPEYMVPAQWlALERLPLTPNG-------KLDRKAL 1000
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
3-462 |
5.14e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 71.71 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 3 GQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLQtKLKDIVSLVPRLRHI 82
Cdd:PRK06155 67 GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLA-ALEAADPGDLPLPAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 83 ITVDGkPPTWSeFPKGVIVHTMAAVQALGVKANVEkkahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARR 162
Cdd:PRK06155 146 WLLDA-PASVS-VPAGWSTAPLPPLDAPAPAAAVQ--------PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAED 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 163 IpRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIgysspqtladqsskikkgskgdtsVLKPTLMAAvpeimdRIYknv 242
Cdd:PRK06155 216 L-EIGADDVLYTTLPLFHTNALNAFFQALLAGATY------------------------VLEPRFSAS------GFW--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 243 mnkvnemSAFQRNLFILAYnYKMEQISKGCSTPLCDRFVFRNVRRLLGGnirlllcGGAP--LSATTQRfmnicFCCPVG 320
Cdd:PRK06155 262 -------PAVRRHGATVTY-LLGAMVSILLSQPARESDRAHRVRVALGP-------GVPAalHAAFRER-----FGVDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 321 QGYGLTESTG--AGTITEVWDYNTGRVgAPLVccEIKLKNwEEGGYFNTDKPhprGEILIGGQN---VTMGYYKNEAKTK 395
Cdd:PRK06155 322 DGYGSTETNFviAVTHGSQRPGSMGRL-APGF--EARVVD-EHDQELPDGEP---GELLLRADEpfaFATGYFGMPEKTV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977076 396 TDFfedenGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA 462
Cdd:PRK06155 395 EAW-----RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRR-GENISSFEVEQVLLSHPAVAAAAVFP 455
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
40-446 |
5.65e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 71.66 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 40 TLGGPAIVHGLNETEVTNIITSKELLQT-KLKDIVSLVPRLRHIITVDGKPPTWSEFPKGVIVHTMAAVQALgvkanVEK 118
Cdd:PRK08043 288 TAGVKGLTSAITAAEIKTIFTSRQFLDKgKLWHLPEQLTQVRWVYLEDLKDDVTTADKLWIFAHLLMPRLAQ-----VKQ 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 119 KahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMaRRIPRLGEEDVYIGYLPLAHVLELSAELVC-LSHGCRI 197
Cdd:PRK08043 363 Q------PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQI-KTIADFTPNDRFMSALPLFHSFGLTVGLFTpLLTGAEV 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 G-YSSPQTladqsskikkgskgdtsvlkptlMAAVPEIMdriyknvmnkvnemsaFQRNLFILAynykmeqiskGCSTPL 276
Cdd:PRK08043 436 FlYPSPLH-----------------------YRIVPELV----------------YDRNCTVLF----------GTSTFL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 277 --CDRFVF-RNVRRLlggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCE 353
Cdd:PRK08043 467 gnYARFANpYDFARL-----RYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 354 ---IKLKNWEEGgyfntdkphprGEILIGGQNVTMGYYKNEA--KTKTDFFEDENGQR---WLCTGDIGEFDPDGCLKII 425
Cdd:PRK08043 542 arlLSVPGIEQG-----------GRLQLKGPNIMNGYLRVEKpgVLEVPTAENARGEMergWYDTGDIVRFDEQGFVQIQ 610
|
410 420
....*....|....*....|.
gi 209977076 426 DRKKDLVKLqAGEYVSLGKVE 446
Cdd:PRK08043 611 GRAKRFAKI-AGEMVSLEMVE 630
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-475 |
2.51e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.37 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAhvLELSAE--LVCLSHGCRI-----G 198
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS--FDGAHEqwFHPLLNGARVlirddE 2221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 199 YSSPQTLADQSSKikkgsKGDTSVLKPTLMaavpeimdriyknvmnkvnemsafqrnlfilaynykMEQISKGCStplcd 278
Cdd:PRK12316 2222 LWDPEQLYDEMER-----HGVTILDFPPVY------------------------------------LQQLAEHAE----- 2255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 279 rfvfRNVRRLlggNIRLLLCGGAPLSAT----------TQRFMNicfccpvgqGYGLTESTGAGTI-TEVWDYNTGRVGA 347
Cdd:PRK12316 2256 ----RDGRPP---AVRVYCFGGEAVPAAslrlawealrPVYLFN---------GYGPTEAVVTPLLwKCRPQDPCGAAYV 2319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 348 PLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKI 424
Cdd:PRK12316 2320 PIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDpfsASGERLYRTGDLARYRADGVVEY 2399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 209977076 425 IDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVP 475
Cdd:PRK12316 2400 LGRIDHQVKIR-GFRIELGEIEARLQAHPAVREavVVAQDGASGKQLVAYVVP 2451
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
34-449 |
6.57e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 68.05 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 34 LVTLYATLGGPAIVHGLNETEVTNIITSKELLQTkLKDIVSLVPRLrHIITVDGKPPtwsEFPKGVIVHTMAAVQALgvk 113
Cdd:PRK08162 95 LNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEV-AREALALLPGP-KPLVIDVDDP---EYPGGRFIGALDYEAFL--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 114 anvekkAHSKP-----LPSD----IAvIMYTSGSTGIPKGVMISH--------SNIIAsiTGMARRiprlgeeDVYIGYL 176
Cdd:PRK08162 167 ------ASGDPdfawtLPADewdaIA-LNYTSGTTGNPKGVVYHHrgaylnalSNILA--WGMPKH-------PVYLWTL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 177 PLAHvlelsaelvclshgCRiGYSSPQTLAdqsskikkgskgdtsvlkptLMAAVpeimdriykNV-MNKVNEMSAFQrn 255
Cdd:PRK08162 231 PMFH--------------CN-GWCFPWTVA--------------------ARAGT---------NVcLRKVDPKLIFD-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 256 lFIlaynyKMEQISKGCSTPLCDRFVFR---NVRRLLGGNIRLLLCGGAPLSATTQRFMNICFCcpVGQGYGLTESTGAG 332
Cdd:PRK08162 265 -LI-----REHGVTHYCGAPIVLSALINapaEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFD--LTHVYGLTETYGPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 333 TIT---EVWD--------YNTGRVGAPLVCCE-IKLKNWEeggyfnTDKPHPR-----GEILIGGqNVTM-GYYKNEAKT 394
Cdd:PRK08162 337 TVCawqPEWDalplderaQLKARQGVRYPLQEgVTVLDPD------TMQPVPAdgetiGEIMFRG-NIVMkGYLKNPKAT 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 209977076 395 KTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAAL 449
Cdd:PRK08162 410 EEAF---AGG--WFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVL 458
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
128-460 |
8.61e-12 |
|
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: 67.50 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAD 207
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 208 QSSKIkkgskgdTSVLKPTLMAAVPeimdriyknvmnkvNEMSAfqrnlfILAYNYKMEQiskgcstplcdrfvfrnvrr 287
Cdd:cd05958 178 LLLSA-------IARYKPTVLFTAP--------------TAYRA------MLAHPDAAGP-------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 288 lLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEVWDYNTGRVGAPLVCCEIKLKNwEEGgyfnt 367
Cdd:cd05958 211 -DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEG----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 368 dKPHPRGEilIGGQNVT--MGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKV 445
Cdd:cd05958 284 -NPVPDGT--IGRLAVRgpTGCRYLADKRQRTYVQGG----WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEV 355
|
330
....*....|....*
gi 209977076 446 EAALKNLPLIDNiCA 460
Cdd:cd05958 356 EDVLLQHPAVAE-CA 369
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
79-455 |
1.08e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 67.23 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 79 LRHIITVDGKpptwsEFPKGVIVHTMAAVQALGVKANVEKKahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASIT- 157
Cdd:PRK09274 137 VRRLVTVGGR-----LLWGGTTLATLLRDGAAAPFPMADLA------PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEa 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 158 -----GMARriprlGEEDvyigyLPLAHVLELSAelVCLshgcrigysspqtladqsskikkgskGDTSVLkPTLMAAVP 232
Cdd:PRK09274 206 lredyGIEP-----GEID-----LPTFPLFALFG--PAL--------------------------GMTSVI-PDMDPTRP 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 233 EIMD--RIYKnvmnkvnemsAFQR----NLFIL-AYnykMEQISKGCSTplcDRFVFRNVRRLLggnirlllCGGAPLSA 305
Cdd:PRK09274 247 ATVDpaKLFA----------AIERygvtNLFGSpAL---LERLGRYGEA---NGIKLPSLRRVI--------SAGAPVPI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 306 TT-QRF---MNicfccPVGQ---GYGLTESTGAGTI---------TEVWDYNTGR-VGAPLVCCEIKL--------KNWE 360
Cdd:PRK09274 303 AViERFramLP-----PDAEiltPYGATEALPISSIesreilfatRAATDNGAGIcVGRPVDGVEVRIiaisdapiPEWD 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 361 EggyfntDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQAG 437
Cdd:PRK09274 378 D------ALRLATgeiGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGG 451
|
410
....*....|....*...
gi 209977076 438 EYVSLgKVEAALKNLPLI 455
Cdd:PRK09274 452 TLYTI-PCERIFNTHPGV 468
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
126-453 |
1.21e-11 |
|
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: 66.89 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNiIASITGMARRIPRLGEEDVYIGYLPL---AHVLELSAELvcLSHGC-----RI 197
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQFASPsfdASVWELLMAL--LAGATlvlapAE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 GYSSPQTLAD--QSSKIkkgskgDTSVLKPTLMAAVP--EIMDRiyknvmnkvnemsafqRNLfilaynykmeqISKG-- 271
Cdd:cd17652 169 ELLPGEPLADllREHRI------THVTLPPAALAALPpdDLPDL----------------RTL-----------VVAGea 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 272 CSTPLCDRFvfrnvrrllggnirlllcggaplsATTQRFMNicfccpvgqGYGLTESTGAGTITEVW-DYNTGRVGAPLV 350
Cdd:cd17652 216 CPAELVDRW------------------------APGRRMIN---------AYGPTETTVCATMAGPLpGGGVPPIGRPVP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 351 CCEIklknweeggYFNTDKPHP-----RGEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCL 422
Cdd:cd17652 263 GTRV---------YVLDARLRPvppgvPGELYIAGAGLARGYLNRPGLTAERFVADpfgAPGSRMYRTGDLARWRADGQL 333
|
330 340 350
....*....|....*....|....*....|.
gi 209977076 423 KIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 453
Cdd:cd17652 334 EFLGRADDQVKIR-GFRIELGEVEAALTEHP 363
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
126-475 |
1.59e-11 |
|
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: 66.69 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDvyigylplaHVLELSAelvclshgcrIGYsspqtl 205
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY-GITSSD---------RVLQFAS----------IAF------ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 aDQSSK--IKKGSKGDTSVLKPTLMAAVPEIM-DRIYKNvmnkvnemsafQRNLFILAYNYKMEQISKGcSTPLCDrfvf 282
Cdd:cd17644 159 -DVAAEeiYVTLLSGATLVLRPEEMRSSLEDFvQYIQQW-----------QLTVLSLPPAYWHLLVLEL-LLSTID---- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 283 rnvrrlLGGNIRLLLCGG-APLSATTQRFMNIcfccpVGQ------GYGLTESTGAGTITEVWDYNTGRVGAPLVCCEI- 354
Cdd:cd17644 222 ------LPSSLRLVIVGGeAVQPELVRQWQKN-----VGNfiqlinVYGPTEATIAATVCRLTQLTERNITSVPIGRPIa 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 355 KLKNWEEGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDF----FEDENGQRWLCTGDIGEFDPDGCLKIIDRKKD 430
Cdd:cd17644 291 NTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFishpFNSSESERLYKTGDLARYLPDGNIEYLGRIDN 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 209977076 431 LVKLQaGEYVSLGKVEAALKNLPLIDNICAYA---NSYHSYVIGFVVP 475
Cdd:cd17644 371 QVKIR-GFRIELGEIEAVLSQHNDVKTAVVIVredQPGNKRLVAYIVP 417
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
126-453 |
1.68e-11 |
|
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: 66.60 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLgeedvyigylPLAHVLELSAelvclshgcrIGYsspqtl 205
Cdd:cd17651 135 ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLG----------PGARTLQFAG----------LGF------ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 adqsskikkgskgDTSVLK--PTLMAA-----VPEimdriykNVMNKVNEMSAF---QRNLFILAYNYKMEQISKGcSTP 275
Cdd:cd17651 189 -------------DVSVQEifSTLCAGatlvlPPE-------EVRTDPPALAAWldeQRISRVFLPTVALRALAEH-GRP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 276 LCDRfvfrnvrrllGGNIRLLLCGGAPLSAT--------TQRFMNICFccpvgqGYGLTEST--GAGTITEVWDYNTGR- 344
Cdd:cd17651 248 LGVR----------LAALRYLLTGGEQLVLTedlrefcaGLPGLRLHN------HYGPTETHvvTALSLPGDPAAWPAPp 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 345 -VGAPLVCCEIK-LKNWeeggyfntDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFEDE--NGQRWLCTGDIGEFD 417
Cdd:cd17651 312 pIGRPIDNTRVYvLDAA--------LRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPfvPGARMYRTGDLARWL 383
|
330 340 350
....*....|....*....|....*....|....*.
gi 209977076 418 PDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 453
Cdd:cd17651 384 PDGELEFLGRADDQVKIR-GFRIELGEIEAALARHP 418
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3-453 |
1.82e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.45 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 3 GQKPKANIAIFCETRAEWMIAAQACFM---------YNF---QLVTLYATLGGPAIVHglnETEvtniitskelLQTKLK 70
Cdd:PRK07798 49 GLGPGDHVGIYARNRIEYVEAMLGAFKaravpvnvnYRYvedELRYLLDDSDAVALVY---ERE----------FAPRVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 71 DIVSLVPRLRHIITVDGkpPTWSEFPKGVIVHTMAAVQALGVKANVEkkahskPLPSDIaVIMYTSGSTGIPKGVMISHS 150
Cdd:PRK07798 116 EVLPRLPKLRTLVVVED--GSGNDLLPGAVDYEDALAAGSPERDFGE------RSPDDL-YLLYTGGTTGMPKGVMWRQE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 151 NIIASitGMARRIPRLGE--EDVYigylplAHVLELSAEL------VC-LSHGcrigysspqtlADQSSKIKKGSKGDTS 221
Cdd:PRK07798 187 DIFRV--LLGGRDFATGEpiEDEE------ELAKRAAAGPgmrrfpAPpLMHG-----------AGQWAAFAALFSGQTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 222 VLKPTLM---AAVPEIMDRiyknvmNKVNEMS----AFQRnlfilaynykmeqiskgcstPLCDRFVFRnvRRLLGGNIR 294
Cdd:PRK07798 248 VLLPDVRfdaDEVWRTIER------EKVNVITivgdAMAR--------------------PLLDALEAR--GPYDLSSLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 295 LLLCGGAPLSATT-QRFM----NICfccpVGQGYGLTEsTGAGTITEVWDYNTGRvGAPLV-----CCEIklknwEEGGY 364
Cdd:PRK07798 300 AIASGGALFSPSVkEALLellpNVV----LTDSIGSSE-TGFGGSGTVAKGAVHT-GGPRFtigprTVVL-----DEDGN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 365 FNTDKPHPRGEILIGGqNVTMGYYKNEAKTKTDFFEdENGQRWLCTGDIGEFDPDGCLKIIDRkKDLVKLQAGEYVSLGK 444
Cdd:PRK07798 369 PVEPGSGEIGWIARRG-HIPLGYYKDPEKTAETFPT-IDGVRYAIPGDRARVEADGTITLLGR-GSVCINTGGEKVFPEE 445
|
....*....
gi 209977076 445 VEAALKNLP 453
Cdd:PRK07798 446 VEEALKAHP 454
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
97-432 |
1.87e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.56 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 97 KGVIVHTMAAVQALGVKANVEKKahskplPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGYL 176
Cdd:PRK07768 128 KGIRVLTVADLLAADPIDPVETG------EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 177 PLAHVLELSAEL-VCLSHGCRIGYSSP-QTLADqsskikkgskgdtsvlkPTLMaavPEIMDRiYKNVMnkvnemsafqr 254
Cdd:PRK07768 202 PLFHDMGMVGFLtVPMYFGAELVKVTPmDFLRD-----------------PLLW---AELISK-YRGTM----------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 255 nlfILAYNYKMEQISkgcstplcdrfvfrnvRRLLGG---------NIRLLLCGGAPLS-ATTQRFmnicfcCPVGQG-- 322
Cdd:PRK07768 250 ---TAAPNFAYALLA----------------RRLRRQakpgafdlsSLRFALNGAEPIDpADVEDL------LDAGARfg 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 323 ---------YGLTESTGAGTItevwdyntGRVGAPLVCCEIKLKNWEEGGYF-NTDKPHPR------------------- 373
Cdd:PRK07768 305 lrpeailpaYGMAEATLAVSF--------SPCGAGLVVDEVDADLLAALRRAvPATKGNTRrlatlgpplpglevrvvde 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977076 374 ----------GEILIGGQNVTMGYykneakTKTDFFE---DENGqrWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK07768 377 dgqvlpprgvGVIELRGESVTPGY------LTMDGFIpaqDADG--WLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
50-482 |
1.88e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 66.63 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 50 LNETEVTNIITSKELLqtklkdivslvPRLRHIITVDGKPPtwsefpKGVIVHTMAAVQALGVKANVEKKA-------HS 122
Cdd:PRK08008 105 LQNSQASLLVTSAQFY-----------PMYRQIQQEDATPL------RHICLTRVALPADDGVSSFTQLKAqqpatlcYA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 123 KPLPS-DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHV-LELSAELVCLSHGCRI--- 197
Cdd:PRK08008 168 PPLSTdDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQC-ALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFvll 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 -GYSSpQTLADQSSKIKkgskgdtsvlkptlmAAVPEIMDRIYKNVMnkVNEMSAFQRN------LFILAynykmeqISK 270
Cdd:PRK08008 247 eKYSA-RAFWGQVCKYR---------------ATITECIPMMIRTLM--VQPPSANDRQhclrevMFYLN-------LSD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 271 GCSTPLCDRFvfrnvrrllggNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESTGaGTITevwDYNTGR-----V 345
Cdd:PRK08008 302 QEKDAFEERF-----------GVRLL------------------------TSYGMTETIV-GIIG---DRPGDKrrwpsI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 346 GAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGG---QNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCL 422
Cdd:PRK08008 343 GRPGFCYEAEIRD-DHN---RPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADG----WLHTGDTGYVDEEGFF 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209977076 423 KIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIG------------FVVPNQKE-LTE 482
Cdd:PRK08008 415 YFVDRRCNMIK-RGGENVSCVELENIIATHPKIQDIV---------VVGikdsirdeaikaFVVLNEGEtLSE 477
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
120-481 |
3.27e-11 |
|
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: 65.81 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 120 AHSKPlpsDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARrIPRLGEEDVYIGYLPLAHVLELSAE--LVCLSHGCRI 197
Cdd:cd05920 135 AESIP---EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAE-VCGLDQDTVYLAVLPAAHNFPLACPgvLGTLLAGGRV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 GYS---SPQT---LADQSskikkgskgdtsvlKPTLMAAVPEImdriyknVMNKVNEMSAFQRNLfilaynykmeqiskg 271
Cdd:cd05920 211 VLApdpSPDAafpLIERE--------------GVTVTALVPAL-------VSLWLDAAASRRADL--------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 272 cstplcdrfvfrnvrrllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEstGAGTIT------EVWDYNTGRV 345
Cdd:cd05920 255 -------------------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTrlddpdEVIIHTQGRP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 346 GAPLVccEIKLknWEEGGyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKII 425
Cdd:cd05920 314 MSPDD--EIRV--VDEEG--NPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVE 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 426 DRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNiCAYANSYHSY----VIGFVVPNQKELT 481
Cdd:cd05920 384 GRIKDQIN-RGGEKIAAEEVENLLLRHPAVHD-AAVVAMPDELlgerSCAFVVLRDPPPS 441
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
128-478 |
6.41e-11 |
|
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: 64.80 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIAsitgmarripRLGEEDVYIGYLPLAHVLELSAelvclshgcrigYSSPQTLAD 207
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNMVN----------LLHFEREKTNINFSDKVLQFAT------------CSFDVCYQE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 208 QSSKIKKGskGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFILaYNYKmeqiskgcstplcDRFvFRNVRR 287
Cdd:cd17656 187 IFSTLLSG--GTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-REFI-------------NRF-PTCVKH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 288 LLGGNIRLLLcggaplSATTQRFMNiCFCCPVGQGYGLTESTGAGTIT-----EVWDYNTgrVGAPLVCCEIKLKNWEEg 362
Cdd:cd17656 250 IITAGEQLVI------TNEFKEMLH-EHNVHLHNHYGPSETHVVTTYTinpeaEIPELPP--IGKPISNTWIYILDQEQ- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 363 gyfntdKPHPRG---EILIGGQNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaG 437
Cdd:cd17656 320 ------QLQPQGivgELYISGASVARGYLNRQELTAEKFFPDpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR-G 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 209977076 438 EYVSLGKVEAALKNLPLIDN--ICAYANSY-HSYVIGFVVPNQK 478
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
125-455 |
9.03e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 64.41 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 125 LPSDI-AVIMYTSGSTGIPKGVMISHSNIIA-SITGM-ARRIPRlgEEDVYIGYLPLAHVLELSAELVCLSHGCRI---- 197
Cdd:PRK07786 171 IPNDSpALIMYTSGTTGRPKGAVLTHANLTGqAMTCLrTNGADI--NSDVGFVGVPLFHIAGIGSMLPGLLLGAPTviyp 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 -GYSSPQTLADqsskIKKGSKGDTSVLKPTLMAAVpeimdriyknvmnkVNEMSAFQRNLfilaynykmeqiskgcstpl 276
Cdd:PRK07786 249 lGAFDPGQLLD----VLEAEKVTGIFLVPAQWQAV--------------CAEQQARPRDL-------------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 277 cdrfvfrnvrrllggNIRLLLCGGAPLSATTQRFMNICFccPVGQ---GYGLTESTgagTITEVWD-----YNTGRVGAP 348
Cdd:PRK07786 291 ---------------ALRVLSWGAAPASDTLLRQMAATF--PEAQilaAFGQTEMS---PVTCMLLgedaiRKLGSVGKV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 349 LVCCEIKLKNWEeggyFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRK 428
Cdd:PRK07786 351 IPTVAARVVDEN----MNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---AGG--WFHSGDLVRQDEEGYVWVVDRK 421
|
330 340
....*....|....*....|....*..
gi 209977076 429 KDLVkLQAGEYVSLGKVEAALKNLPLI 455
Cdd:PRK07786 422 KDMI-ISGGENIYCAEVENVLASHPDI 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-482 |
2.28e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.03 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLA---HVLELSAELVclsHGCRIGYSSP 202
Cdd:PRK12467 1717 PQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAfdvSVWELFWPLI---NGARLVIAPP 1792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 203 QTLADQSSKIkkgskgdtsvlkptlmaavpEIMDRIYKNVMNKVNemSAFQRNLfilaynyKMEQISKGCSTplcdrfvf 282
Cdd:PRK12467 1793 GAHRDPEQLI--------------------QLIERQQVTTLHFVP--SMLQQLL-------QMDEQVEHPLS-------- 1835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 283 rnvrrllggnIRLLLCGGAPLSATTQRFMNICFCcPVG--QGYGLTEST---GAGTITEVWDynTGRVGAPLvccEIKLK 357
Cdd:PRK12467 1836 ----------LRRVVCGGEALEVEALRPWLERLP-DTGlfNLYGPTETAvdvTHWTCRRKDL--EGRDSVPI---GQPIA 1899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 358 NWeeGGYF--NTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKK 429
Cdd:PRK12467 1900 NL--STYIldASLNPVPIgvaGELYLGGVGLARGYLNRPALTAERFVADpfgTVGSRLYRTGDLARYRADGVIEYLGRID 1977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 209977076 430 DLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPNQKELTE 482
Cdd:PRK12467 1978 HQVKIR-GFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVD 2031
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
114-554 |
3.67e-10 |
|
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: 62.06 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 114 ANVEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSniiasitgmarriprlgeedVYIGYLPlahvlelsaelvclsh 193
Cdd:cd05971 75 SNSGASALVTDGSDDPALIIYTSGTTGPPKGALHAHR--------------------VLLGHLP---------------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 194 gcriGYSSPQTLADQSSKIKKGSK------GDTSVLKPTLMAAVPEIMDRiyknvMNKVNEMSAFQ-------RNLFILA 260
Cdd:cd05971 119 ----GVQFPFNLFPRDGDLYWTPAdwawigGLLDVLLPSLYFGVPVLAHR-----MTKFDPKAALDlmsrygvTTAFLPP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 261 YNYKMeqiskgcstplcdrfvFRNV---RRLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGA-GTITE 336
Cdd:cd05971 190 TALKM----------------MRQQgeqLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLViGNCSA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 337 VWDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQN-VTM-GYYKNEAKTKTDFFEDengqrWLCTGDIG 414
Cdd:cd05971 254 LFPIKPGSMGKPIPGHRVAIVD-DNG---TPLPPGEVGEIAVELPDpVAFlGYWNNPSATEKKMAGD-----WLLTGDLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 415 EFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIGfvVPNQkeltelARTKGFKGtWE 494
Cdd:cd05971 325 RKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEECLLKHPAVLMAA---------VVG--IPDP------IRGEIVKA-FV 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 495 ELcNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDPWTPETGlvtdafKLKRKELK 554
Cdd:cd05971 386 VL-NPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATG------KIRRRELR 438
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
2-432 |
4.07e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 62.31 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAE-WMIAAQACFMyNFQLVTLYAtLGGPA-IVHGLNETEVTNIITSKELLQTKLKDIVSLVPRL 79
Cdd:PRK06188 57 LGLGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHP-LGSLDdHAYVLEDAGISTLIVDPAPFVERALALLARVPSL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 80 RHIITVDgkpptwsEFPKGVIVHTMAAVQAlgvkanvEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSniiaSITGM 159
Cdd:PRK06188 135 KHVLTLG-------PVPDGVDLLAAAAKFG-------PAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHR----SIATM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 160 A------RRIPrlgEEDVYIGYLPLAHVlelSAELVClshgcrigyssPqTLAdqsskikkgsKGDTSVLKP-----TLM 228
Cdd:PRK06188 197 AqiqlaeWEWP---ADPRFLMCTPLSHA---GGAFFL-----------P-TLL----------RGGTVIVLAkfdpaEVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 229 AAVPEimDRIykNVMNKVNEMsafqrnLFILaynykMEqiskgcstplCDRFVFRNVRRLlggniRLLLCGGAPLSAT-- 306
Cdd:PRK06188 249 RAIEE--QRI--TATFLVPTM------IYAL-----LD----------HPDLRTRDLSSL-----ETVYYGASPMSPVrl 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 307 ---TQRFMNIcfccpVGQGYGLTESTGAGTITEVWDYNTGRV------GAPLVCCEIKLKNwEEGGYFNTDKPhprGEIL 377
Cdd:PRK06188 299 aeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQGEV---GEIC 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 209977076 378 IGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK06188 370 VRGPLVMDGYWNRPEETAEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKDMI 419
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
128-432 |
5.64e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 62.05 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIpRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAD 207
Cdd:PRK07769 181 TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDAL-EGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 208 QSSK-IKKgskgdtsvlkptlMAAVPEIMDRIYKNVMNKVNEMSAfQRNLfilaynykmeqiSKGCSTPLcDRfvfrnvr 286
Cdd:PRK07769 260 RPGRwIRE-------------LARKPGGTGGTFSAAPNFAFEHAA-ARGL------------PKDGEPPL-DL------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 287 rllgGNIRLLLCGGAPLSATTQRFMNICFcCPVG-------QGYGLTEST----------------------GAGTITEV 337
Cdd:PRK07769 306 ----SNVKGLLNGSEPVSPASMRKFNEAF-APYGlpptaikPSYGMAEATlfvsttpmdeeptviyvdrdelNAGRFVEV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 338 WDYNTGRVgAPLVCCEIKLKNWEEGGYFNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFFE-------------D 401
Cdd:PRK07769 381 PADAPNAV-AQVSAGKVGVSEWAVIVDPETASELPDgqiGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshaegA 459
|
330 340 350
....*....|....*....|....*....|.
gi 209977076 402 ENGQRWLCTGDIGEFdPDGCLKIIDRKKDLV 432
Cdd:PRK07769 460 PDDALWVRTGDYGVY-FDGELYITGRVKDLV 489
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-432 |
1.25e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASiTGMARR---IPrLGEEDVYIGYLPLAHVLELsaelvclshgcrIGyssp 202
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVAN-EQLIRHgfgID-LNPDDVIVSWLPLYHDMGL------------IG---- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 203 qtladqsskikkgskgdtSVLKPtLMAAVPEIMdriyknvmnkvneMSAfqrNLFILAYNYKMEQISKGCST----P--- 275
Cdd:PRK05691 227 ------------------GLLQP-IFSGVPCVL-------------MSP---AYFLERPLRWLEAISEYGGTisggPdfa 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 276 --LC-DRFVFRNVRRLLGGNIRLLLCGGAP-----LSATTQRFMNiC-------FCCpvgqgYGLTEST--------GAG 332
Cdd:PRK05691 272 yrLCsERVSESALERLDLSRWRVAYSGSEPirqdsLERFAEKFAA-CgfdpdsfFAS-----YGLAEATlfvsggrrGQG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 333 -TITEVWDYNTGR------VGAPLVCC-------EIKLKNWEEGGYFNTDKPhprGEILIGGQNVTMGYYKN-EAKTKTd 397
Cdd:PRK05691 346 iPALELDAEALARnraepgTGSVLMSCgrsqpghAVLIVDPQSLEVLGDNRV---GEIWASGPSIAHGYWRNpEASAKT- 421
|
330 340 350
....*....|....*....|....*....|....*
gi 209977076 398 fFEDENGQRWLCTGDIGeFDPDGCLKIIDRKKDLV 432
Cdd:PRK05691 422 -FVEHDGRTWLRTGDLG-FLRDGELFVTGRLKDML 454
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
130-441 |
1.31e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 60.92 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 130 AVIMYTSGSTGIPKGVMISH-SNIIASITGMARRIPRLGEEDVYIGYLPLAHvlelsaelvclSHGCRIGYSSPQTLADQ 208
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVLHALMANNGDALGTSAADTMLPVVPLFH-----------ANSWGIAFSAPSMGTKL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 209 sskIKKGSKGD-TSVL------KPTLMAAVPEIMdriyknvmnkvnemsafqrnLFILAYnykMEQisKGCSTPlcdrfv 281
Cdd:PRK06018 249 ---VMPGAKLDgASVYelldteKVTFTAGVPTVW--------------------LMLLQY---MEK--EGLKLP------ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 282 frnvrrllggNIRLLLCGGAPL-SATTQRFMNicFCCPVGQGYGLTESTGAGTITEV---WDYNTG--------RVGAPL 349
Cdd:PRK06018 295 ----------HLKMVVCGGSAMpRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAALkppFSKLPGdarldvlqKQGYPP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 350 VCCEIKLKNweeggyfNTDKPHPR-----GEILIGGQNVTMGYYKNEAKTKtdffeDENGqrWLCTGDIGEFDPDGCLKI 424
Cdd:PRK06018 363 FGVEMKITD-------DAGKELPWdgktfGRLKVRGPAVAAAYYRVDGEIL-----DDDG--FFDTGDVATIDAYGYMRI 428
|
330
....*....|....*..
gi 209977076 425 IDRKKDLVKlQAGEYVS 441
Cdd:PRK06018 429 TDRSKDVIK-SGGEWIS 444
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
10-192 |
2.33e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 59.89 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 10 IAIFCETRAEWMIAAQA-------CFMYNFQLVtlyatlgGPAIVHGLNETEVTNIITSKELLQTklkdIVSLVPrlrhi 82
Cdd:PRK08279 90 VALLMENRPEYLAAWLGlaklgavVALLNTQQR-------GAVLAHSLNLVDAKHLIVGEELVEA----FEEARA----- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 83 iTVDGKPPTWSEFPK-GVIVHTMAAVQALGVKANVEKKAHSKPLPS-DIAVIMYTSGSTGIPKGVMISHSNIIASITGMA 160
Cdd:PRK08279 154 -DLARPPRLWVAGGDtLDDPEGYEDLAAAAAGAPTTNPASRSGVTAkDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFG 232
|
170 180 190
....*....|....*....|....*....|..
gi 209977076 161 RRIpRLGEEDVYIGYLPLAHVlelSAELVCLS 192
Cdd:PRK08279 233 GLL-RLTPDDVLYCCLPLYHN---TGGTVAWS 260
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
2-453 |
4.09e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 59.17 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHGLNETEVTNIITSKELLqTKLKDIVSLVPRLRH 81
Cdd:PRK07788 94 LGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFT-DLLSALPPDLGRLRA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 82 IIT-VDGKPPTWSEFPkgvivhTMAAVqalgVKANVEKKAHSKPLPSDIaVIMyTSGSTGIPKGVMISHSNIIASITGMA 160
Cdd:PRK07788 173 WGGnPDDDEPSGSTDE------TLDDL----IAGSSTAPLPKPPKPGGI-VIL-TSGTTGTPKGAPRPEPSPLAPLAGLL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 161 RRIPRLGEEDVYIGyLPLAHVLELSAELVCLSHGCRI----GYSSPQTLADqsskIKKgskgdtsvLKPTLMAAVPeimd 236
Cdd:PRK07788 241 SRVPFRAGETTLLP-APMFHATGWAHLTLAMALGSTVvlrrRFDPEATLED----IAK--------HKATALVVVP---- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 237 riyknVMnkvnemsaFQRNLFILAynykmEQISK-GCStplcdrfvfrnvrrllggNIRLLLCGGAPLSATT-QRFMN-- 312
Cdd:PRK07788 304 -----VM--------LSRILDLGP-----EVLAKyDTS------------------SLKIIFVSGSALSPELaTRALEaf 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 313 ---ICfccpvgQGYGLTESTGAgTIT--EVWDYNTGRVGAPLVCCEIKLknweeggYFNTDKPHPRGE---ILIGGqNVT 384
Cdd:PRK07788 348 gpvLY------NLYGSTEVAFA-TIAtpEDLAEAPGTVGRPPKGVTVKI-------LDENGNEVPRGVvgrIFVGN-GFP 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209977076 385 MGYYKNeAKTKtdffEDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 453
Cdd:PRK07788 413 FEGYTD-GRDK----QIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHP 473
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
46-455 |
5.19e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 58.90 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 46 IVHGLNETEVTNIITSKELLqtKLKDIVSLVPRLRHIITV---DGKPPTWS-EFPKGV---------IVHTMAAVQALGV 112
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA--PVVEQVRAETSLRHVIVTslaDVLPAEPTlPLPDSLraprlaaagAIDLLPALRACTA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 113 KANVEKkahskPLPSDIAVIMYTSGSTGIPKGVMISHSNII---ASITGMARRiprLGEEDVYIGYLP----------LA 179
Cdd:PRK06178 200 PVPLPP-----PALDALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVAVV---GGEDSVFLSFLPefwiagenfgLL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 180 HVLELSAELVCLShgcrigysspqtladqsskikkgsKGDTSvlkpTLMAAVPE----IMDRIYKNVMNKVNEMSAFQRN 255
Cdd:PRK06178 272 FPLFSGATLVLLA------------------------RWDAV----AFMAAVERyrvtRTVMLVDNAVELMDHPRFAEYD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 256 LFILaynykmeqiskgcSTPLCDRFVfrnvrRLLGGNIRlllcggaplsattQRFMNICFCCPVGQGYGLTESTGAGTIT 335
Cdd:PRK06178 324 LSSL-------------RQVRVVSFV-----KKLNPDYR-------------QRWRALTGSVLAEAAWGMTETHTCDTFT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 336 ---EVWDYN-TGR---VGAPLVCCEIKLKNweeggyFNTDKPHP---RGEILIGGQNVTMGYYKNEAKTKTDFfedENGq 405
Cdd:PRK06178 373 agfQDDDFDlLSQpvfVGLPVPGTEFKICD------FETGELLPlgaEGEIVVRTPSLLKGYWNKPEATAEAL---RDG- 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 209977076 406 rWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLI 455
Cdd:PRK06178 443 -WLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAV 490
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
126-555 |
9.14e-09 |
|
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: 57.83 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISH------SNIIASITGMArriprlgEEDVYIGYLPLAH-VLELSAELVCLSHGCRIG 198
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWrrtlvtSNLLSHDLNLK-------NGDRTYTCMPLYHgTAAFLGACNCLMSGGTLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 199 YSS--------PQTLADQSSKIKKGSKgdtsvLKPTLMAAVPEIMDRiyknvMNKVnemsafqrnlfILAYnykmeqiSK 270
Cdd:cd05937 159 LSRkfsasqfwKDVRDSGATIIQYVGE-----LCRYLLSTPPSPYDR-----DHKV-----------RVAW-------GN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 271 GCSTPLCDRFvfrnvrrllggnirlllcggaplsatTQRFmNIcfccP-VGQGYGLTESTGAgtiteVWDYNTGRVGAPL 349
Cdd:cd05937 211 GLRPDIWERF--------------------------RERF-NV----PeIGEFYAATEGVFA-----LTNHNVGDFGAGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 350 VCCEIKLKNWE-EGGYF------NTDKPHPR--------------GEIL--IGGQNVTM--GYYKNEAKTKTDFFED--E 402
Cdd:cd05937 255 IGHHGLIRRWKfENQVVlvkmdpETDDPIRDpktgfcvrapvgepGEMLgrVPFKNREAfqGYLHNEDATESKLVRDvfR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 403 NGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEaalknlpliDNICAYANSYHSYVIGFVVPNQKeltE 482
Cdd:cd05937 335 KGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHPDIAEANVYGVKVPGHD---G 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209977076 483 LARTKGFKGTweelcNSSEMENEVLKVLSEAAISASLEKFEIPLKIRLSPDpwtpetGLVTDAFKLKRKELKT 555
Cdd:cd05937 402 RAGCAAITLE-----ESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VATTDNHKQQKGVLRD 463
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
255-482 |
1.22e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 57.31 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 255 NLFILayNYKMEQISKGCSTPLCDRF---VFRNVRRLLGGNI------RLLLCGGAP----LsATTQRFMNIcfccPVGQ 321
Cdd:PRK07445 187 KLVIL--PYKRLKSGQELPPNPSDFFlslVPTQLQRLLQLRPqwlaqfRTILLGGAPawpsL-LEQARQLQL----RLAP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 322 GYGLTEStgAGTIT-----EVWDYNTGrVGAPLVCCEIKLKNweeggyfntdkpHPRGEILIGGQNVTMGYYKNEaktkt 396
Cdd:PRK07445 260 TYGMTET--ASQIAtlkpdDFLAGNNS-SGQVLPHAQITIPA------------NQTGNITIQAQSLALGYYPQI----- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 397 dffedENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLIDNICAY--ANSY-HSYVIGFV 473
Cdd:PRK07445 320 -----LDSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLglPDPHwGEVVTAIY 393
|
....*....
gi 209977076 474 VPNQKELTE 482
Cdd:PRK07445 394 VPKDPSISL 402
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
77-462 |
1.53e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 57.75 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 77 PRLrhIITVDGKPPTWSEFPKGVIVhTMAAVQALGvkanvEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASI 156
Cdd:PRK10252 556 PSL--LITTADQLPRFADVPDLTSL-CYNAPLAPQ-----GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 157 TGMARRIPrLGEEDVYIGYLPLA---HVLELSAELVClshGCRIGYSSPQTLADqsskikkgskgdtsvlkPTLMAAvpe 233
Cdd:PRK10252 628 LWMQNHYP-LTADDVVLQKTPCSfdvSVWEFFWPFIA---GAKLVMAEPEAHRD-----------------PLAMQQ--- 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 234 IMDRIYKNVMNKVNEM-SAFQRNLfilaynyKMEQISKGCSTplcdrfvfrnvrrllggnIRLLLCGGAPLSATTQRFMN 312
Cdd:PRK10252 684 FFAEYGVTTTHFVPSMlAAFVASL-------TPEGARQSCAS------------------LRQVFCSGEALPADLCREWQ 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 313 ICFCCPVGQGYGLTES----TGAGTITEVWDYNTGR---VGAPLvcceiklknWEEGGYFNTDKPHP-----RGEILIGG 380
Cdd:PRK10252 739 QLTGAPLHNLYGPTEAavdvSWYPAFGEELAAVRGSsvpIGYPV---------WNTGLRILDARMRPvppgvAGDLYLTG 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 381 QNVTMGYYKNEAKTKTDFFED--ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNI 458
Cdd:PRK10252 810 IQLAQGYLGRPDLTASRFIADpfAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIR-GQRIELGEIDRAMQALPDVEQA 888
|
....
gi 209977076 459 CAYA 462
Cdd:PRK10252 889 VTHA 892
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
96-437 |
1.75e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.08 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 96 PKGVIVHTMAAVQALGVKANVEKKAHSKPlpsdiAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGY 175
Cdd:PRK05851 126 DSSVTVHDLATAAHTNRSASLTPPDSGGP-----AVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSW 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 176 LPLAHVLELSAELVCLSHGCRIgYSSPqTLADQSSKIKKGSKGDTSvlKPTLMAAvPEimdriyknvmnkvnemsafqrn 255
Cdd:PRK05851 201 LPLYHDMGLAFLLTAALAGAPL-WLAP-TTAFSASPFRWLSWLSDS--RATLTAA-PN---------------------- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 256 lfiLAYNykmeqiskgcstplcdrFVFRNVRRLLG---GNIRLLLCGGAPLS-ATTQRFMNIcfCCPVG-------QGYG 324
Cdd:PRK05851 254 ---FAYN-----------------LIGKYARRVSDvdlGALRVALNGGEPVDcDGFERFATA--MAPFGfdagaaaPSYG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 325 LTESTGAGT---------ITEVWDYNTG------RVGAPLVCCEIKLKNWEEGGYFNTdkpHPRGEILIGGQNvTMGYYK 389
Cdd:PRK05851 312 LAESTCAVTvpvpgiglrVDEVTTDDGSgarrhaVLGNPIPGMEVRISPGDGAAGVAG---REIGEIEIRGAS-MMSGYL 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 209977076 390 NEAKTKTDffedengqRWLCTGDIGEFdPDGCLKIIDRKKDLVKLqAG 437
Cdd:PRK05851 388 GQAPIDPD--------DWFPTGDLGYL-VDGGLVVCGRAKELITV-AG 425
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
126-449 |
2.09e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.75 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLgEEDVYIGYLPLAHVLEL-SAELVCLSHGCRIGYSS--- 201
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK-EDDVMMSFLPPFHAYGFnSCTLFPLLSGVPVVFAYnpl 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 202 -PQTLADQSSKIKKgskgdtsvlkpTLMAAVPEIMDRIYKNVMNKVNEMSAFqrnlfilaynykmeqiskgcstplcdRF 280
Cdd:PRK06334 261 yPKKIVEMIDEAKV-----------TFLGSTPVFFDYILKTAKKQESCLPSL--------------------------RF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 281 VfrnvrrLLGGNIRlllcgGAPLSATTQR-FMNICfccpVGQGYGLTESTGAGTITEVwdyNTGR----VGAPLVCCEIK 355
Cdd:PRK06334 304 V------VIGGDAF-----KDSLYQEALKtFPHIQ----LRQGYGTTECSPVITINTV---NSPKhescVGMPIRGMDVL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 356 LKNWEeggyfnTDKPHPRGE---ILIGGQNVTMGYYKNEaktKTDFFEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK06334 366 IVSEE------TKVPVSSGEtglVLTRGTSLFSGYLGED---FGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFV 436
|
330
....*....|....*..
gi 209977076 433 KLqAGEYVSLGKVEAAL 449
Cdd:PRK06334 437 KI-GAEMVSLEALESIL 452
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
132-453 |
2.77e-08 |
|
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: 55.85 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 132 IMYTSGSTGIPKGVMISHSNIIASITGMArriPRLGEEDVYIGYLPLAHVlelSAElvclshGCRIGYSSPQTLADQSSK 211
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGGA---DFGTGEFTPSEDAHKAAA---AAA------GTVMFPAPPLMHGTGSWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 212 IKKGSKGDTSVLKPTLMAAVPEIMDRIYKNvmnKVNEMS----AFQRNLfilaynykMEQISKGCSTPLcdrfvfrnvrr 287
Cdd:cd05924 76 AFGGLLGGQTVVLPDDRFDPEEVWRTIEKH---KVTSMTivgdAMARPL--------IDALRDAGPYDL----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 288 llgGNIRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESTGAGTItevwdYNTGRV--GAPLVCCEIKLKNWEEGGY 364
Cdd:cd05924 134 ---SSLFAISSGGALLSPEVkQGLLELVPNITLVDAFGSSETGFTGSG-----HSAGSGpeTGPFTRANPDTVVLDDDGR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 365 FNTDKPHPRGEILIGGqNVTMGYYKNEAKTKTDFFEdENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGK 444
Cdd:cd05924 206 VVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETFPE-VDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-TGGEKVFPEE 282
|
....*....
gi 209977076 445 VEAALKNLP 453
Cdd:cd05924 283 VEEALKSHP 291
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
64-504 |
3.13e-08 |
|
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: 56.36 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 64 LLQTKLK--DIVSLVPR--LRHIITVDGKPPTWSEFPKGVIVHTMAAVQALGVKANVEKKAHSKPL-PSDIAVIMYTSGS 138
Cdd:cd05923 82 LINPRLKaaELAELIERgeMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPRePEQPAFVFYTSGT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 139 TGIPKGVMISHSNIIASITGMARRIP-RLGEEDVYIGYLPLAHVLELSAELV-CLSHG---CRIGYSSPQTLADQSSKik 213
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQAGlRHGRHNVVLGLMPLYHVIGFFAVLVaALALDgtyVVVEEFDPADALKLIEQ-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 214 kgskgdtsvLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRNLFilaynykmeqisKGCSTPlcdRFVFRNVRRLLGGni 293
Cdd:cd05923 240 ---------ERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTF------------AGATMP---DAVLERVNQHLPG-- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 294 rlllcggaplsattqRFMNIcfccpvgqgYGLTEstgAGTITEVWDYNTGRVGAPLVCCEIKLKNWeEGGYFNTDKPHPR 373
Cdd:cd05923 294 ---------------EKVNI---------YGTTE---AMNSLYMRDARTGTEMRPGFFSEVRIVRI-GGSPDEALANGEE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 374 GEILI--GGQNVTMGYYKNEAKTKTDFFEdengqRWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKN 451
Cdd:cd05923 346 GELIVaaAADAAFTGYLNQPEATAKKLQD-----GWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSR 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 209977076 452 LPLIDNICAYA---NSYHSYVIGFVVPNQKELTELArtkgfkgtWEELCNSSEMEN 504
Cdd:cd05923 420 HPGVTEVVVIGvadERWGQSVTACVVPREGTLSADE--------LDQFCRASELAD 467
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
128-453 |
3.22e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 56.09 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIAS-----ITGmarripRLGEEDVYIGYLPLAHvlelSAEL-VCLShgcrigyss 201
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEyvsciVAG------DMSADDIPLHALPLYH----CAQLdVFLG--------- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 202 PQTLAdqsskikkgskGDTSVLKPTlmAAVPEIMDRIYKNvmnKVnemsafqRNLFI-------LAynykmeqiskgcST 274
Cdd:PRK08316 233 PYLYV-----------GATNVILDA--PDPELILRTIEAE---RI-------TSFFApptvwisLL------------RH 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 275 PLCDRfvfRNVRRLLGGnirlllCGGA------PLSATTQRFMNICF--CcpvgqgYGLTESTGAGTI--TEVWDYNTGR 344
Cdd:PRK08316 278 PDFDT---RDLSSLRKG------YYGAsimpveVLKELRERLPGLRFynC------YGQTEIAPLATVlgPEEHLRRPGS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 345 VGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKI 424
Cdd:PRK08316 343 AGRPVLNVETRVVD-DDG---NDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF---RGG--WFHSGDLGVMDEEGYITV 413
|
330 340
....*....|....*....|....*....
gi 209977076 425 IDRKKDLVKlQAGEYVSLGKVEAALKNLP 453
Cdd:PRK08316 414 VDRKKDMIK-TGGENVASREVEEALYTHP 441
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
134-443 |
3.25e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 56.20 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 134 YTSGSTGIPKGVMISHSNIIASITG-MARRIPRLGEEDVYIGYLPLahvlelsaelvclSHGCRIgysspQTLAdQSSKi 212
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFVITNhLADLMPGTTEQDASLVVAPL-------------SHGAGI-----HQLC-QVAR- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 213 kkgskGDTSVLKPTLMAAVPEIMDRIYKNvmnKVNemsafqrNLFILAYNYKM--EQiskgcstPLCDRFVFrnvrrllg 290
Cdd:PRK07470 230 -----GAATVLLPSERFDPAEVWALVERH---RVT-------NLFTVPTILKMlvEH-------PAVDRYDH-------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 291 GNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTIT-----EVWDYNTGRVGaplvCC-------EIKLKN 358
Cdd:PRK07470 280 SSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLppalhDAEDGPDARIG----TCgfertgmEVQIQD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 359 wEEGgyfNTDKPHPRGEILIGGQNVTMGYYKN-EAKTKTdfFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLvklqag 437
Cdd:PRK07470 356 -DEG---RELPPGETGEICVIGPAVFAGYYNNpEANAKA--FRDG----WFRTGDLGHLDARGFLYITGRASDM------ 419
|
....*.
gi 209977076 438 eYVSLG 443
Cdd:PRK07470 420 -YISGG 424
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
90-455 |
6.73e-08 |
|
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: 55.20 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 90 PTWSEFPKGVIVHTMAAVQALGVKANVEKKahSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIAS-ITGmaRRIPRLGE 168
Cdd:cd05969 54 PLFSAFGPEAIRDRLENSEAKVLITTEELY--ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYyFTG--KYVLDLHP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 169 EDVYIGYLPLAHVLELSAELVC-LSHGCrigysspQTLADQSSKIKKGSKGDTSVLKPTLMAAVPEIMDRIyknvMNKVN 247
Cdd:cd05969 130 DDIYWCTADPGWVTGTVYGIWApWLNGV-------TNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRML----MKEGD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 248 EMSAfqrnlfilayNYKMEqiskgcstplcdrfvfrnvrrllggNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTE 327
Cdd:cd05969 199 ELAR----------KYDLS-------------------------SLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 328 sTGAGTITEV--WDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTM--GYYKNEAKTKTDFFedeN 403
Cdd:cd05969 244 -TGSIMIANYpcMPIKPGSMGKPLPGVKAAVVD-ENG---NELPPGTKGILALKPGWPSMfrGIWNDEERYKNSFI---D 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 209977076 404 GqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLI 455
Cdd:cd05969 316 G--WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAV 364
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
71-485 |
7.90e-08 |
|
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: 55.15 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 71 DIVSLVPRLRHIItVDGKPPTWSEFPkgvivhTMAAVQALGVKANVEkkahskplPSDIAVIMYTSGSTGIPKGVMISHS 150
Cdd:COG1021 143 ELQAEVPSLRHVL-VVGDAGEFTSLD------ALLAAPADLSEPRPD--------PDDVAFFQLSGGTTGLPKLIPRTHD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 151 NIIASITGMARrIPRLGEEDVYIGYLPLAHVLELSAE--LVCLSHGCRI---GYSSPQT---LADQSskikkgskgdtsv 222
Cdd:COG1021 208 DYLYSVRASAE-ICGLDADTVYLAALPAAHNFPLSSPgvLGVLYAGGTVvlaPDPSPDTafpLIERE------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 223 lKPTLMAAVPEImdriyknVMNKVNEMSAFQRNLfilaynykmeqiskgcstplcdrfvfrnvrrllgGNIRLLLCGGAP 302
Cdd:COG1021 274 -RVTVTALVPPL-------ALLWLDAAERSRYDL----------------------------------SSLRVLQVGGAK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 303 LSATTQRFMNICFCCPVGQGYGLTEstGAGTITEVWD-----YNTgrVGAPLvcC---EIKLKNwEEGgyfntdKPHPRG 374
Cdd:COG1021 312 LSPELARRVRPALGCTLQQVFGMAE--GLVNYTRLDDpeeviLTT--QGRPI--SpddEVRIVD-EDG------NPVPPG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 375 EIligGQNVTMG------YYKNEAKTKTDFfeDENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAA 448
Cdd:COG1021 379 EV---GELLTRGpytirgYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEEVENL 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 209977076 449 LKNLPLIDN--------------ICAyansyhsyvigFVVPNQKELT--ELAR 485
Cdd:COG1021 451 LLAHPAVHDaavvampdeylgerSCA-----------FVVPRGEPLTlaELRR 492
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
124-456 |
1.27e-07 |
|
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: 54.39 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 124 PLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRI-PRLGEEDVyIGYLPLA---HVLELSAELVCLSHgCRIGY 199
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYgIRPGEVDL-ATFPLFAlfgPALGLTSVIPDMDP-TRPAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 SSPQTLADQSSKikkgskgdtsvLKPTLMAAVPEIMDRIYKNVMNKVNEMSAFQRnlfilaynykmeQISKGCSTP--LC 277
Cdd:cd05910 160 ADPQKLVGAIRQ-----------YGVSIVFGSPALLERVARYCAQHGITLPSLRR------------VLSAGAPVPiaLA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 278 DRFvfrnvRRLLGGNIRLLLCGGA----PLSATTQRfmnicfccPVGQGYGLTESTGAGTItevwdyntgrVGAPLVCCE 353
Cdd:cd05910 217 ARL-----RKMLSDEAEILTPYGAtealPVSSIGSR--------ELLATTTAATSGGAGTC----------VGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 354 IKLKNWEEGGYFNTDKPH--PR---GEILIGGQNVTMGYYKNEAKTKTDFFEDENGQRWLCTGDIGEFDPDGCLKIIDRK 428
Cdd:cd05910 274 VRIIEIDDEPIAEWDDTLelPRgeiGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRK 353
|
330 340
....*....|....*....|....*...
gi 209977076 429 KDLVKLQAGEYVSLgKVEAALKNLPLID 456
Cdd:cd05910 354 AHRVITTGGTLYTE-PVERVFNTHPGVR 380
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
128-453 |
1.34e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.79 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMaRRIPRLGEEDVYIGYLPLA---HVLELSAELVClshGCRIGYSSPQT 204
Cdd:PRK05691 1274 NLAYVIYTSGSTGQPKGVGNTHAALAERLQWM-QATYALDDSDVLMQKAPISfdvSVWECFWPLIT---GCRLVLAGPGE 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 205 LADQSSKIKKGSKGDTSVLKptlmaAVPEIMdriyknvmnkvnemsafqrNLFIlaynykMEQISKGCSTplcdrfvfrn 284
Cdd:PRK05691 1350 HRDPQRIAELVQQYGVTTLH-----FVPPLL-------------------QLFI------DEPLAAACTS---------- 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 285 vrrllggnIRLLLCGGAPLSATTQ-RFMNICFCCPVGQGYGLTEStgAGTIT----EVWDYNTGRVGAPL--VCCEIKlk 357
Cdd:PRK05691 1390 --------LRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTET--AINVThwqcQAEDGERSPIGRPLgnVLCRVL-- 1457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 358 nweeGGYFNTDKPHPRGEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKL 434
Cdd:PRK05691 1458 ----DAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDplgEDGARLYRTGDRARWNADGALEYLGRLDQQVKL 1533
|
330
....*....|....*....
gi 209977076 435 QaGEYVSLGKVEAALKNLP 453
Cdd:PRK05691 1534 R-GFRVEPEEIQARLLAQP 1551
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
116-476 |
2.56e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 53.45 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 116 VEKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASiTGMArRIPRLGEEDVYIGYLPLAHVlelSAELVCLsHGC 195
Cdd:cd05938 133 VPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQC-SGFL-SLCGVTADDVIYITLPLYHS---SGFLLGI-GGC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 196 rigysspqtladqsskIKKGSkgdTSVLKPTLMAAvpEIMDRIYK-NVmnkvnemSAFQrnlfilaynYKMEQISKGCST 274
Cdd:cd05938 207 ----------------IELGA---TCVLKPKFSAS--QFWDDCRKhNV-------TVIQ---------YIGELLRYLCNQ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 275 PLCDRFVFRNVRRLLGGNIRlllcggaplsATT-----QRFMNICFCcpvgQGYGLTESTgAGTItevwDYnTGRVGA-P 348
Cdd:cd05938 250 PQSPNDRDHKVRLAIGNGLR----------ADVwreflRRFGPIRIR----EFYGSTEGN-IGFF----NY-TGKIGAvG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 349 LVCCEIKLKNWEEGGYFNTDKPHP------------RGE--ILIG---GQNVTMGYYKNEAKTKTDFFED--ENGQRWLC 409
Cdd:cd05938 310 RVSYLYKLLFPFELIKFDVEKEEPvrdaqgfcipvaKGEpgLLVAkitQQSPFLGYAGDKEQTEKKLLRDvfKKGDVYFN 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977076 410 TGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNicayANSYhsyviGFVVPN 476
Cdd:cd05938 390 TGDLLVQDQQNFLYFHDRVGDTFRWK-GENVATTEVADVLGLLDFLQE----VNVY-----GVTVPG 446
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
367-455 |
3.27e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 53.31 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 367 TDKPHPR-----GEILIGGQNVTMGYYKNEAKTKTDFfedENGqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVS 441
Cdd:PLN02479 391 TMKPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF---ANG--WFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENIS 464
|
90
....*....|....
gi 209977076 442 LGKVEAALKNLPLI 455
Cdd:PLN02479 465 SLEVENVVYTHPAV 478
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
122-432 |
6.96e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 51.93 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 122 SKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGYLPLAHVLELSaelvclshGCRIgysS 201
Cdd:PRK09192 171 PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGLV--------GFLL---T 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 202 PqtLADQSSkikkgskgdTSVLKPTLMAAVPEI-MDRIyknvmnkvnemsafQRNLFILAYN----YKmeqiskgcstpL 276
Cdd:PRK09192 240 P--VATQLS---------VDYLPTRDFARRPLQwLDLI--------------SRNRGTISYSppfgYE-----------L 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 277 CDRFVfrNVRRLLGGNI---RLLLCGGAPLSA-TTQRFMNiCFcCPVG-------QGYGLTEST--------GAGTITEV 337
Cdd:PRK09192 284 CARRV--NSKDLAELDLscwRVAGIGADMIRPdVLHQFAE-AF-APAGfddkafmPSYGLAEATlavsfsplGSGIVVEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 338 WD--------------YNTGRV------GAPLVCCEIKLKNweEGGyfnTDKPHPR-GEILIGGQNVTMGYYKNEAKTKT 396
Cdd:PRK09192 360 VDrdrleyqgkavapgAETRRVrtfvncGKALPGHEIEIRN--EAG---MPLPERVvGHICVRGPSLMSGYFRDEESQDV 434
|
330 340 350
....*....|....*....|....*....|....*.
gi 209977076 397 dffEDENGqrWLCTGDIGeFDPDGCLKIIDRKKDLV 432
Cdd:PRK09192 435 ---LAADG--WLDTGDLG-YLLDGYLYITGRAKDLI 464
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
85-459 |
7.39e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 51.58 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 85 VDGKPPTWSEFPKGVIVHTMAAVQALGVkanvekkahSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARrip 164
Cdd:PRK07824 2 LAGRAPALLPVPAQDERRAALLRDALRV---------GEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHD--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 165 RLGEEDVYIGYLPLAHVLELSAELVCLSHGcrigySSPQTLaDQSskikkgskgdTSVLKPTLMAAVPEI-MDRIYKNVM 243
Cdd:PRK07824 70 RLGGPGQWLLALPAHHIAGLQVLVRSVIAG-----SEPVEL-DVS----------AGFDPTALPRAVAELgGGRRYTSLV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 244 NKvnemsafqrnlfilaynykmeQISKGCSTPlcdrfvfRNVRRLlggniRLL---LCGGAPLSATTQRF---MNIcfcc 317
Cdd:PRK07824 134 PM---------------------QLAKALDDP-------AATAAL-----AELdavLVGGGPAPAPVLDAaaaAGI---- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 318 PVGQGYGLTESTGAGtiteVWDyntgrvGAPLVCCEIKLKNweeggyfntdkphprGEILIGGQNVTMGYYKNEaktKTD 397
Cdd:PRK07824 177 NVVRTYGMSETSGGC----VYD------GVPLDGVRVRVED---------------GRIALGGPTLAKGYRNPV---DPD 228
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209977076 398 FFEDENgqrWLCTGDIGEFDpDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNIC 459
Cdd:PRK07824 229 PFAEPG---WFRTDDLGALD-DGVLTVLGRADDAIS-TGGLTVLPQVVEAALATHPAVADCA 285
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
128-555 |
7.46e-07 |
|
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: 51.59 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIaSITGMARRIPRLGEEDVYIGYLPLAHVlelSAELVCLsHGCRIGysspqtlad 207
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFAGSGGALPSDVLYTCLPLYHS---TALIVGW-SACLAS--------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 208 qsskikkgskGDTSVLKPTLMAavpeimdriyknvmnkvnemSAFQRNlfILAYNYKMEQ-ISKGC----STPLCDRFVF 282
Cdd:cd05940 148 ----------GATLVIRKKFSA--------------------SNFWDD--IRKYQATIFQyIGELCryllNQPPKPTERK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 283 RNVRRLLGGNIRlllcgGAPLSATTQRFMNICFCcpvgQGYGLTESTGA--------GTITEVWDYNTGRVGAPLVCCEI 354
Cdd:cd05940 196 HKVRMIFGNGLR-----PDIWEEFKERFGVPRIA----EFYAATEGNSGfinffgkpGAIGRNPSLLRKVAPLALVKYDL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 355 K----LKNweEGGYFntdKPHPRGE--ILIG----GQNVTmGYYKN---EAKTKTDFFEDenGQRWLCTGDIGEFDPDGC 421
Cdd:cd05940 267 EsgepIRD--AEGRC---IKVPRGEpgLLISrinpLEPFD-GYTDPaatEKKILRDVFKK--GDAWFNTGDLMRLDGEGF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 422 LKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNicayANSYhsyviGFVVPNqkeltelarTKGFKGTweELCNSSE 501
Cdd:cd05940 339 WYFVDRLGDTFRWK-GENVSTTEVAAVLGAFPGVEE----ANVY-----GVQVPG---------TDGRAGM--AAIVLQP 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 209977076 502 MENEVLKVLSeAAISASLEKFEIPLKIRLSPDPWTPETglvtdaFKLKRKELKT 555
Cdd:cd05940 398 NEEFDLSALA-AHLEKNLPGYARPLFLRLQPEMEITGT------FKQQKVDLRN 444
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
37-172 |
1.46e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 51.05 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 37 LYATLGGPAIVHGLNETEVTNIITSKELLQTKLKDivsLVPRLRHIITVDG----KPPTWSeFPKgvivhtmaavqalgv 112
Cdd:PRK04319 128 LFEAFMEEAVRDRLEDSEAKVLITTPALLERKPAD---DLPSLKHVLLVGEdveeGPGTLD-FNA--------------- 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977076 113 kanvEKKAHSKPL------PSDIAVIMYTSGSTGIPKGVMISHSNIIA-SITGmaRRIPRLGEEDVY 172
Cdd:PRK04319 189 ----LMEQASDEFdiewtdREDGAILHYTSGSTGKPKGVLHVHNAMLQhYQTG--KYVLDLHEDDVY 249
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
117-455 |
1.47e-06 |
|
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: 50.93 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 117 EKKAHSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGmARRIPRLGEEDVYIGYLPLA---HVLELSAELvcLSH 193
Cdd:cd17654 108 EHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQH-FRSLFNITSEDILFLTSPLTfdpSVVEIFLSL--SSG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 194 GCRIgySSPQTLADQSSKIkkgSKGDTSVLKPTLMAAVPEIMDRIYKNVMNKVNeMSAFQrnlfilaynykmeqiskgcs 273
Cdd:cd17654 185 ATLL--IVPTSVKVLPSKL---ADILFKRHRITVLQATPTLFRRFGSQSIKSTV-LSATS-------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 274 tplcdrfvfrnvrrllggNIRLLLCGGAP------LSATTQRFMNICFCcpvgQGYGLTESTGAGTITEVWDYNTG-RVG 346
Cdd:cd17654 239 ------------------SLRVLALGGEPfpslviLSSWRGKGNRTRIF----NIYGITEVSCWALAYKVPEEDSPvQLG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 347 APLV--CCEIKLKNWEEGgyfntdkphpRGEILIGGQNvtMGYYKNEAKTKTdffedeNGQrWLCTGDIGEFDpDGCLKI 424
Cdd:cd17654 297 SPLLgtVIEVRDQNGSEG----------TGQVFLGGLN--RVCILDDEVTVP------KGT-MRATGDFVTVK-DGELFF 356
|
330 340 350
....*....|....*....|....*....|..
gi 209977076 425 IDRKKDLVKlQAGEYVSLGKVE-AALKNLPLI 455
Cdd:cd17654 357 LGRKDSQIK-RRGKRINLDLIQqVIESCLGVE 387
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
374-446 |
2.01e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 50.48 E-value: 2.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209977076 374 GEILIGGQNVTMGYYKNEAKTKTDffedengqRWLCTGDIGEFDPDGCLKIIDRKKDLVKlQAGEYVSLGKVE 446
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASPLVD--------GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
106-202 |
2.07e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 50.71 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 106 AVQALGVKANVEKKAHSKPLPSdIAVIMYTSGSTGIPKGVMISHSNIIASITGMAR-------RIPRLGEEDVyiGYLPL 178
Cdd:PRK05850 140 EVDLLDLDSPRGSDARPRDLPS-TAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSdyfgdtgGVPPPDTTVV--SWLPF 216
|
90 100
....*....|....*....|....*...
gi 209977076 179 AH----VLELSAELVClshGCRIGYSSP 202
Cdd:PRK05850 217 YHdmglVLGVCAPILG---GCPAVLTSP 241
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
297-475 |
2.39e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 50.26 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 297 LCGGA--PLSATTQ-RFMNI-CFCcpvgqGYGLTEStgAGTITEVWDYNTGRVGAPLVCCEIKLKNweeggyfntdkphp 372
Cdd:PRK09029 246 LLGGAaiPVELTEQaEQQGIrCWC-----GYGLTEM--ASTVCAKRADGLAGVGSPLPGREVKLVD-------------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 373 rGEILIGGQNVTMGYYKNEAKTKtdfFEDENGqrWLCTGDIGEFDpDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNL 452
Cdd:PRK09029 305 -GEIWLRGASLALGYWRQGQLVP---LVNDEG--WFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQH 376
|
170 180
....*....|....*....|...
gi 209977076 453 PLIDNIcayansyhsyvigFVVP 475
Cdd:PRK09029 377 PLVQQV-------------FVVP 386
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
293-563 |
2.61e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 50.08 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 293 IRLLLCGGAPLSATTQRFMnICFCCPV-GQGYGLTEStgaGTIT----EVWDYNTGRVGAPLVCCEIKLKNwEEGgyfnt 367
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAM-IEWWGPViYEYYGSTES---GAVTfatsEDALSHPGTVGKAAPGAELRFVD-EDG----- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 368 dKPHPRGEI------LIGGQNVTmgyYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVkLQAGEYVS 441
Cdd:PRK12406 343 -RPLPQGEIgeiysrIAGNPDFT---YHNKPEKRAEIDRGG----FITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIY 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 442 LGKVEAALKNLPLIDNiCAYansyhsyvigFVVPNQkeltELArtkgfkgtwEELCNSSEMENEVlkVLSEAAISASLE- 520
Cdd:PRK12406 414 PAEIEAVLHAVPGVHD-CAV----------FGIPDA----EFG---------EALMAVVEPQPGA--TLDEADIRAQLKa 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 209977076 521 ---KFEIPLKIRLSPDpwTPEtglvTDAFKLKRKELKTHYQADIER 563
Cdd:PRK12406 468 rlaGYKVPKHIEIMAE--LPR----EDSGKIFKRRLRDPYWANAGR 507
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
46-478 |
2.89e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 50.17 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 46 IVHGLNETEVTNIITSKELLQtKLKDIVSLVPRLRHIITVDGKPPTWSEfpkgviVHTMAAVQALGVKANVEKKAHSKPL 125
Cdd:PRK05620 103 IVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIGPSDADSAA------AHMPEGIKVYSYEALLDGRSTVYDW 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 P----SDIAVIMYTSGSTGIPKGVMISHSNIIASITGMaRRIPRLGEED--VYIGYLPLAHVLELSAELVCLSHGcrigy 199
Cdd:PRK05620 176 PeldeTTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSL-RTTDSLAVTHgeSFLCCVPIYHVLSWGVPLAAFMSG----- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 200 sSPQTLADQSskikkgskgdtsVLKPTLMAAVPEIMDRIYKNVmnkvnemSAFQRNLFILAYNYKMEQISkgcstplcdr 279
Cdd:PRK05620 250 -TPLVFPGPD------------LSAPTLAKIIATAMPRVAHGV-------PTLWIQLMVHYLKNPPERMS---------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 280 fvfrnvrrllggnIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESTGAGTITEV---------WDY--NTGRVGAP 348
Cdd:PRK05620 300 -------------LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPpsgvsgearWAYrvSQGRFPAS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 349 LvccEIKLKNweEGGYFNTdkpHPR--GEILIGGQNVTMGYYKNEAKTKT--------DFFEDENGQ----RWLCTGDIG 414
Cdd:PRK05620 367 L---EYRIVN--DGQVMES---TDRneGEIQVRGNWVTASYYHSPTEEGGgaastfrgEDVEDANDRftadGWLRTGDVG 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209977076 415 EFDPDGCLKIIDRKKDLVKlQAGEYVslgkVEAALKNLplidnICAYANSYHSYVIGFvvPNQK 478
Cdd:PRK05620 439 SVTRDGFLTIHDRARDVIR-SGGEWI----YSAQLENY-----IMAAPEVVECAVIGY--PDDK 490
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
131-476 |
5.83e-06 |
|
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: 48.45 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 131 VIMYTSGSTGIPKGVMISHSNIIASITGMARrIPRLGEEDVYIGYLPLAHVLEL-------------------SAELVC- 190
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAV-LQAIDEGTVFLNSGPLFHIGTLmftlatfhaggtnvfvrrvDAEEVLe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 191 --LSHGCRIGYSSPQTLaDQSSKIKKGSKGDTSVLKPTlmAAVPEimdriyknvmnkvnemsafqrnlfilaynykmeqi 268
Cdd:cd17636 83 liEAERCTHAFLLPPTI-DQIVELNADGLYDLSSLRSS--PAAPE----------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 269 SKGCSTPLCDRFvfrnvRRLLGGnirlllcggaplsattqrfmnicfccpvgqgYGLTESTGAGTITEVWDYNTGRVGAP 348
Cdd:cd17636 125 WNDMATVDTSPW-----GRKPGG-------------------------------YGQTEVMGLATFAALGGGAIGGAGRP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 349 LVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQNVTMGYYKNEaktktdffeDENGQR----WLCTGDIGEFDPDGCLKI 424
Cdd:cd17636 169 SPLVQVRILD-EDG---REVPDGEVGEIVARGPTVMAGYWNRP---------EVNARRtrggWHHTNDLGRREPDGSLSF 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 209977076 425 IDRKKDLVKlQAGEYVSLGKVEAALKNLPLIDNICayansyhsyVIGfvVPN 476
Cdd:cd17636 236 VGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAA---------VIG--VPD 275
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
128-432 |
8.55e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.58 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPRLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAD 207
Cdd:PRK12476 194 DVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 208 QSSK-IKKGSKGDTSVlkPTLMAAvPeimdriyknvmNKVNEMSAfQRNLfilaynykmeqiskgcsTPLCDRFVFRNVr 286
Cdd:PRK12476 274 RPQRwIKALSEGSRTG--RVVTAA-P-----------NFAYEWAA-QRGL-----------------PAEGDDIDLSNV- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 287 rllggnirLLLCGGAPLSATTQRFMNICFcCPVG-------QGYGLTEST----------------------GAGTITEV 337
Cdd:PRK12476 321 --------VLIIGSEPVSIDAVTTFNKAF-APYGlprtafkPSYGIAEATlfvatiapdaepsvvyldreqlGAGRAVRV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 338 wDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPR---GEILIGGQNVTMGYYKNEAKTKTDFF--------------E 400
Cdd:PRK12476 392 -AADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDgevGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegshadG 470
|
330 340 350
....*....|....*....|....*....|..
gi 209977076 401 DENGQRWLCTGDIGeFDPDGCLKIIDRKKDLV 432
Cdd:PRK12476 471 AADDGTWLRTGDLG-VYLDGELYITGRIADLI 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-476 |
1.33e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 48.62 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 126 PSDIAVIMYTSGSTGIPKGVMISHSniiasitgmarriprlgeedvyigylPLAHVLELSAELVCLSHGCRIGYSSPQTL 205
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHG--------------------------ALANHLCWIAEAYELDANDRVLLFMSFSF 3289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 206 adqsskikkgskgDTSV--LKPTLMAAVPEIMdriyknvmnKVNEMSAFQRNLFILAYnykmEQISKGCSTP--LCDRFV 281
Cdd:PRK12467 3290 -------------DGAQerFLWTLICGGCLVV---------RDNDLWDPEELWQAIHA----HRISIACFPPayLQQFAE 3343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 282 FRNVRRllGGNIRLLLCGG--APLSATTQRFMNICfccPVG--QGYGLTESTGAGTI-TEVWDYNTGRVGAPL------V 350
Cdd:PRK12467 3344 DAGGAD--CASLDIYVFGGeaVPPAAFEQVKRKLK---PRGltNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIgrpvagR 3418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 351 CCEIKLKNWEeggyfntdkPHPRG---EILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKI 424
Cdd:PRK12467 3419 SIYVLDGQLN---------PVPVGvagELYIGGVGLARGYHQRPSLTAERFVADpfsGSGGRLYRTGDLARYRADGVIEY 3489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 209977076 425 IDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDN--ICAYANSYHSYVIGFVVPN 476
Cdd:PRK12467 3490 LGRIDHQVKIR-GFRIELGEIEARLLQHPSVREavVLARDGAGGKQLVAYVVPA 3542
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
323-432 |
2.13e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 47.21 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 323 YGLTESTGAGTIT-EVWDYNTGRVGAPLVCceiKLKNWEEGGyfntdKPHPRGEI-LI----GGQNVTmgYYKNEAKTKt 396
Cdd:PRK08276 294 YASSEGGGVTVITsEDWLAHPGSVGKAVLG---EVRILDEDG-----NELPPGEIgTVyfemDGYPFE--YHNDPEKTA- 362
|
90 100 110
....*....|....*....|....*....|....*.
gi 209977076 397 dffEDENGQRWLCTGDIGEFDPDGCLKIIDRKKDLV 432
Cdd:PRK08276 363 ---AARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI 395
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
10-206 |
1.12e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 45.12 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 10 IAIFCETRAEWMIAAQACfmynfqlvtlyATLGgpAIVHGLN----ETEVTNIITSKE----LLQTKLKDI--------- 72
Cdd:PRK06164 63 VAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHILGRGRarwlVVWPGFKGIdfaailaav 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 73 -VSLVPRLRHIITVDGKPPTWSEFPKGVIV-----HTMAAVQALGVKANVekkahskplPSDIAVIMYTSGSTGIPKGVM 146
Cdd:PRK06164 130 pPDALPPLRAIAVVDDAADATPAPAPGARVqlfalPDPAPPAAAGERAAD---------PDAGALLFTTSGTTSGPKLVL 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209977076 147 ISHSNIIASitgmARRIPR---LGEEDVYIGYLPLAHVLELSAELVCLSHG----CRIGYSSPQTLA 206
Cdd:PRK06164 201 HRQATLLRH----ARAIARaygYDPGAVLLAALPFCGVFGFSTLLGALAGGaplvCEPVFDAARTAR 263
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
376-455 |
4.54e-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: 42.80 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 376 ILIGGQNVTMGYYKNEAKTKTDFFEDEngqrWLCTGDIGEFDPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLI 455
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDG----FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLENALMGHPKV 437
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
374-485 |
5.45e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 374 GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALK 450
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAERFVADpfaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIR-GFRIELGEIESRLL 2611
|
90 100 110
....*....|....*....|....*....|....*..
gi 209977076 451 NLPLIDN--ICAYANSYHSYVIGFVVPNQKELTELAR 485
Cdd:PRK05691 2612 EHPAVREavVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
121-462 |
6.17e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 42.75 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 121 HSKPLPSDIAVIMYTSGSTGIPKGVMISHSNIIASITGMARRIPrLGEEDVYIGYLPLAH---VleLSAELVCLSHGCRI 197
Cdd:PRK07867 146 FRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFG-LGPDDVCYVSMPLFHsnaV--MAGWAVALAAGASI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 198 G----YSSPQTLADqsskIKK-GSKGDTSVLKPtlmaavpeimdriyknvmnkvnemsafqrnlfiLAYNYKMEQISKGC 272
Cdd:PRK07867 223 AlrrkFSASGFLPD----VRRyGATYANYVGKP---------------------------------LSYVLATPERPDDA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 273 STPLcdrfvfrnvrRLLGGNirlllcGGAPlsATTQRFMNIcFCCPVGQGYGLTE---------STGAGTI------TEV 337
Cdd:PRK07867 266 DNPL----------RIVYGN------EGAP--GDIARFARR-FGCVVVDGFGSTEggvaitrtpDTPPGALgplppgVAI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 338 WDYNTGRVGAPLVcceiklknWEEGGYFNTDKphPRGEIL-IGGQNVTMGYYKNEAKTKTDFfedENGQRWlcTGDIGEF 416
Cdd:PRK07867 327 VDPDTGTECPPAE--------DADGRLLNADE--AIGELVnTAGPGGFEGYYNDPEADAERM---RGGVYW--SGDLAYR 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 209977076 417 DPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLIDNICAYA 462
Cdd:PRK07867 392 DADGYAYFAGRLGDWMRVD-GENLGTAPIERILLRYPDATEVAVYA 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
125-152 |
6.68e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 6.68e-04
10 20
....*....|....*....|....*...
gi 209977076 125 LPSDIAVIMYTSGSTGIPKGVMISHSNI 152
Cdd:PRK05691 2331 LPQHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-147 |
1.47e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 1.47e-03
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
2-194 |
2.21e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 40.83 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 2 LGQKPKANIAIFCETRA---EWMIAAQACFMYnFQLVTLYATLGGPAIVhgLNETEVTNIITSKELLqtklkDIVSL--- 75
Cdd:PRK13391 44 LGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAAYI--VDDSGARALITSAAKL-----DVARAllk 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 76 -VPRLRHIITVD--GKPPTWSEFPkgvivhtmAAVQALGvkanvekkahSKPLPSDI--AVIMYTSGSTGIPKGVM--IS 148
Cdd:PRK13391 116 qCPGVRHRLVLDgdGELEGFVGYA--------EAVAGLP----------ATPIADESlgTDMLYSSGTTGRPKGIKrpLP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 209977076 149 HSNIIA--SITGMARRIPRLGEEDVYIGYLPLAHVLELSAELVCLSHG 194
Cdd:PRK13391 178 EQPPDTplPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLG 225
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
374-490 |
2.54e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.92 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209977076 374 GEILIGGQNVTMGYYKNEAKTKTDFFED---ENGQRWLCTGDIGEFDPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALK 450
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFVPHpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIR-GYRIELGEIEARLH 4145
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90 100 110 120
....*....|....*....|....*....|....*....|..
gi 209977076 451 NLPLIDN--ICAYANSYHSYVIGFVVPNQKELTELARTKGFK 490
Cdd:PRK05691 4146 EQAEVREaaVAVQEGVNGKHLVGYLVPHQTVLAQGALLERIK 4187
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| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
128-180 |
3.91e-03 |
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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: 40.10 E-value: 3.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 209977076 128 DIAVIMYTSGSTGIPKGVMISHSNIIaSITGMARRIPRLGEEDVYIGYLPLAH 180
Cdd:cd05939 105 DKLFYIYTSGTTGLPKAAVIVHSRYY-RIAAGAYYAFGMRPEDVVYDCLPLYH 156
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