|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
130-701 |
0e+00 |
|
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: 921.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 130 PYQWINYDEALLRAKNFGAGMLALGAR--PKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQ 207
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 208 VVIVEDdgkaamllekaprslkiivaikpirqttlerarsrGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTT 287
Cdd:cd05927 82 IVFCDA-----------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 288 GNPKGVMLTHGNVVAGVCSVILQMGDH-RIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKP 366
Cdd:cd05927 127 GNPKGVMLTHGNIVSNVAGVFKILEILnKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIKALKP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 367 TVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEIARGVLRRNGCWDKLVFKKVHQAFGGNLRLMVVGSAPL 445
Cdd:cd05927 207 TVFPGVPRVLNRIYDKIFNKVQAKGpLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 446 AGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFA--NQNTGEVCVRGSNVF 523
Cdd:cd05927 287 SPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIRGPNVF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 524 HGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSC 603
Cdd:cd05927 367 SGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSF 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 604 IIAVVVPDTDVLKQWATENN-VRGTLSVLCNNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFK 682
Cdd:cd05927 447 LVAIVVPDPDVLKEWAASKGgGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFK 526
|
570
....*....|....*....
gi 24666501 683 AKRPQLKSYFKPQLEDMYK 701
Cdd:cd05927 527 LKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
101-703 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 651.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 101 VRTLYQTFREGAYASNNGPCLGWR---ETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQG 177
Cdd:PLN02736 43 IGTLHDNFVYAVETFRDYKYLGTRirvDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 178 CYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAML--LEKAPrSLKIIVAIKPIRQTTLERARSRGIQIFSF 255
Cdd:PLN02736 123 CSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLscLSEIP-SVRLIVVVGGADEPLPSLPSGTGVEIVTY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 256 IDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILqmgDHRIRAGDVMVSFLPLAHMFERC 335
Cdd:PLN02736 202 SKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSL---STKFYPSDVHISYLPLAHIYERV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 336 CENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEIARGvlr 414
Cdd:PLN02736 279 NQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGgLKERLFNAAYNAKKQALENG--- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 415 RN--GCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVS 492
Cdd:PLN02736 356 KNpsPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 493 CNAVKLVDVPEMEYFANQNT---GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKL 569
Cdd:PLN02736 436 ACEVKLVDVPEMNYTSEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 570 SQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVR-GTLSVLCNNKNVKELIMNDMLNW 648
Cdd:PLN02736 516 AQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAV 595
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 24666501 649 GKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYKHL 703
Cdd:PLN02736 596 GREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
99-702 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 540.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 99 ENVRTLYQTFREGAYASNNGPCLGWRETltSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGC 178
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 179 YSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAMLLEKAPR--SLKIIVAIKPirqttleRARSRGIQIFSFI 256
Cdd:COG1022 86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDElpSLRHIVVLDP-------RGLRDDPRLLSLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 257 DVEKLGAKGNHPE------VPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAH 330
Cdd:COG1022 159 ELLALGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL---PLGPGDRTLSFLPLAH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 331 MFERCCENGMYYVGGCVGfYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDIS-ASGLKRGLFNMAMR-AKEKEI 408
Cdd:COG1022 236 VFERTVSYYALAAGATVA-FAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeAGGLKRKLFRWALAvGRRYAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 409 ARGVLRRNGCW--------DKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQG 480
Cdd:COG1022 315 ARLAGKSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLTETSPVITVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 481 DHVPNHVGPPVSCNAVKLVDvpemeyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRII 560
Cdd:COG1022 394 DNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRIT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 561 DRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKsCIIAVVVPDTDVLKQWATENNV-RGTLSVLCNNKNVKE 639
Cdd:COG1022 463 GRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLpYTSYAELAQDPEVRA 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666501 640 LIMN--DMLNwgkqSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYKH 702
Cdd:COG1022 542 LIQEevDRAN----AGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
88-701 |
1.09e-164 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 488.97 E-value: 1.09e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 88 SKNGKFVsyITENVRTLYQTFREGAYASNNGPCLGWRETLTS---PYQWINYDEALLRAKNFGAGMLALGARPKQLIGIY 164
Cdd:PLN02861 31 AKDGLLD--LPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSkvgPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 165 SQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAML--LEKAPRSLKIIVAIKPIRQTTL 242
Cdd:PLN02861 109 GSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILscLPKCSSNLKTIVSFGDVSSEQK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 243 ERARSRGIQIFSFIDVEKLGAKgnHPEVPPTAE-DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSV--ILQMGDHRIRAG 319
Cdd:PLN02861 189 EEAEELGVSCFSWEEFSLMGSL--DCELPPKQKtDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhLLKVTDRVATEE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 320 DVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFN 398
Cdd:PLN02861 267 DSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGmLRKKLFD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 399 MAMRAKEKEIARGVLRRNGC--WDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTE-CTGAIT 475
Cdd:PLN02861 347 FAYNYKLGNLRKGLKQEEASprLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFT 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 476 LTVQGDHVPNHVGPPVSCNAVKLVDVPEMEY--FANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLP 553
Cdd:PLN02861 427 SIANVFSMVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQP 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 554 NGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCN 633
Cdd:PLN02861 506 NGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCK 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666501 634 NKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYK 701
Cdd:PLN02861 586 NLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
99-701 |
3.21e-164 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 487.99 E-value: 3.21e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 99 ENVRTLYQTFREGAYASNNGPCLGWRETLTSP---YQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYE 175
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKpgkYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 176 QGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgKAAMLLEKAPRS---LKIIVAIKPIRQTTLERARSRGIQI 252
Cdd:PLN02614 122 EACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK-KISELFKTCPNSteyMKTVVSFGGVSREQKEEAETFGLVI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 253 FSFIDVEKLGaKGNHPEVP-PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVI--LQMGDHRIRAGDVMVSFLPLA 329
Cdd:PLN02614 201 YAWDEFLKLG-EGKQYDLPiKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrlLKSANAALTVKDVYLSYLPLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 330 HMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEI 408
Cdd:PLN02614 280 HIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGfLKKFVFDSAFSYKFGNM 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 409 ARGV--LRRNGCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTE-CTGAITLTVQGDHVPN 485
Cdd:PLN02614 360 KKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDMLG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 486 HVGPPVSCNAVKLVDVPEMEYFANQNT--GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRR 563
Cdd:PLN02614 440 TVGPPVPNVDIRLESVPEMEYDALASTprGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRK 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 564 KHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCNNKNVKELIMN 643
Cdd:PLN02614 519 KNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILG 598
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666501 644 DMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYK 701
Cdd:PLN02614 599 ELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
100-703 |
5.08e-163 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 484.70 E-value: 5.08e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 100 NVRTLYQTFREGA--YASNNgpCLGWRETL---TSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILY 174
Cdd:PLN02430 40 DITTAWDIFSKSVekYPDNK--MLGWRRIVdgkVGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 175 EQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgKAAMLLE---KAPRSLKIIVAIKPIRQTTLERARSRGIQ 251
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK-KIKELLEpdcKSAKRLKAIVSFTSVTEEESDKASQIGVK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 252 IFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMG--DHRIRAGDVMVSFLPLA 329
Cdd:PLN02430 197 TYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfEDKMTHDDVYLSFLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 330 HMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISA-SGLKRGLFNMAMRAKEKEI 408
Cdd:PLN02430 277 HILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQElNPRRRLIFNALYKYKLAWM 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 409 ARGVLRRNGC--WDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDH-VPN 485
Cdd:PLN02430 357 NRGYSHKKASpmADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMcMLG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 486 HVGPPVSCNAVKLVDVPEMEY--FANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRR 563
Cdd:PLN02430 437 TVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRK 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 564 KHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCNNKNVKELIMN 643
Cdd:PLN02430 516 KNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILS 595
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 644 DMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYKHL 703
Cdd:PLN02430 596 ELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
129-685 |
2.96e-160 |
|
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: 471.70 E-value: 2.96e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 129 SPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQV 208
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 209 VIVEddgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpPTAEDLCTVCYTSGTTG 288
Cdd:cd17639 81 IFTD-----------------------------------------------------------GKPDDLACIMYTSGSTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 289 NPKGVMLTHGNVVAGVCSVILQMGDHrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFysGDIKELTN--------D 360
Cdd:cd17639 102 NPKGVMLTHGNLVAGIAGLGDRVPEL-LGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrgckgD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 361 LKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEIARGVLrrNGCWDKLVFKKVHQAFGGNLRLMV 439
Cdd:cd17639 179 LTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGgLKRTLFWTAYQSKLKALKEGPG--TPLLDELVFKKVRAALGGRLRYML 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 440 VGSAPLAGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQ--NTGEVCV 517
Cdd:cd17639 257 SGGAPLSADTQEFLN-IVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKppPRGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 518 RGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 598 ESLKSCIIAVVVPDTDVLKQWATENNV-RGTLSVLCNNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGL 676
Cdd:cd17639 416 DPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPENGL 495
|
....*....
gi 24666501 677 LTPTFKAKR 685
Cdd:cd17639 496 VTAAQKLKR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
130-688 |
3.34e-143 |
|
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: 426.24 E-value: 3.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 130 PYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVV 209
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 210 IVEDdgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptAEDLCTVCYTSGTTGN 289
Cdd:cd05907 82 FVED------------------------------------------------------------PDDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFERCCenGMYYV---GGCVGFYSgDIKELTNDLKMLKP 366
Cdd:cd05907 102 PKGVMLSHRNILSNALALAERL---PATEGDRHLSFLPLAHVFERRA--GLYVPllaGARIYFAS-SAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 367 TVMPAVPRLLNRVYDKIQNDISaSGLKRGLFnmamrakekeiargvlrrngcwdklvfkkvHQAFGGNLRLMVVGSAPLA 446
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAV-PGLKRKLF------------------------------DLAVGGRLRFAASGGAPLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 447 GNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDvpemeyfanqnTGEVCVRGSNVFHGY 526
Cdd:cd05907 225 AELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 527 YKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKsCIIA 606
Cdd:cd05907 293 YKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP-FLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 607 VVVPDTDVLKQWATENNV-RGTLSVLCNNKNVKELI--MNDMLNwgkqSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKA 683
Cdd:cd05907 372 LIVPDPEALEAWAEEHGIaYTDVAELAANPAVRAEIeaAVEAAN----ARLSRYEQIKKFLLLPEPFTIENGELTPTLKL 447
|
....*
gi 24666501 684 KRPQL 688
Cdd:cd05907 448 KRPVI 452
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
99-700 |
3.66e-133 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 408.74 E-value: 3.66e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 99 ENVRTLYQTFREGAYASNNGPCLGWR-----ETLTSP------------YQWINYDEALLRAKNFGAGMLALGARPKQLI 161
Cdd:PLN02387 55 EGATTLAALFEQSCKKYSDKRLLGTRklisrEFETSSdgrkfeklhlgeYEWITYGQVFERVCNFASGLVALGHNKEERV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 162 GIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDG-KAAMLLEKAPRSLKIIVAIKPIRQ- 239
Cdd:PLN02387 135 AIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlKKLIDISSQLETVKRVIYMDDEGVd 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 240 TTLERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDhrIRAG 319
Cdd:PLN02387 215 SDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPK--LGKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 320 DVMVSFLPLAHMFERCCENGMYYVGGCVGF--------YSGDIKELTN-DLKMLKPTVMPAVPRLLNRVYDKIQNDISAS 390
Cdd:PLN02387 293 DVYLAYLPLAHILELAAESVMAAVGAAIGYgspltltdTSNKIKKGTKgDASALKPTLMTAVPAILDRVRDGVRKKVDAK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 391 G-LKRGLFNMAMRAKEKEI------ARGVLRRngCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLE 463
Cdd:PLN02387 373 GgLAKKLFDIAYKRRLAAIegswfgAWGLEKL--LWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQ 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 464 GYGQTE-CTGAiTLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNT---GEVCVRGSNVFHGYYKDPEKTAEA--I 537
Cdd:PLN02387 451 GYGLTEtCAGA-TFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVykV 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 538 DSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVL 615
Cdd:PLN02387 530 DERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQAL 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 616 KQWATENNVR-GTLSVLCNNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKP 694
Cdd:PLN02387 610 EKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKD 689
|
....*.
gi 24666501 695 QLEDMY 700
Cdd:PLN02387 690 DLKKLY 695
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
128-570 |
6.53e-121 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 367.41 E-value: 6.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 128 TSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQ 207
Cdd:pfam00501 16 VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 208 VVIVEDDGKAAMLLEKAPR----SLKIIVAIKPIRQTTLerarsrgiqifsFIDVEKLGAKGNHPEVPPTAEDLCTVCYT 283
Cdd:pfam00501 96 VLITDDALKLEELLEALGKlevvKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 284 SGTTGNPKGVMLTHGNVVAGVCSV-ILQMGDHRIRAGDVMVSFLPLAHMFERC-CENGMYYVGGCVGFYSG----DIKEL 357
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIkRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGfpalDPAAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 358 TNDLKMLKPTVMPAVPRLLNRVydkiqndISASGLKRGLFnmamrakekeiargvlrrngcwdklvfkkvhqafgGNLRL 437
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML-------LEAGAPKRALL-----------------------------------SSLRL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 438 MVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDH---VPNHVGPPVSCNAVKLVDVPEMEYFANQNTGE 514
Cdd:pfam00501 282 VLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGE 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666501 515 VCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLS 570
Cdd:pfam00501 362 LCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
132-685 |
1.81e-103 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 331.56 E-value: 1.81e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 132 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIV 211
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 212 edDGKA-AMLLEKAprSLKIIVAIKPIRQTTL-ERARSRGIQIFSFIDVEKLG--AKGNHPEVPPT-AEDLCTVCYTSGT 286
Cdd:PTZ00216 200 --NGKNvPNLLRLM--KSGGMPNTTIIYLDSLpASVDTEGCRLVAWTDVVAKGhsAGSHHPLNIPEnNDDLALIMYTSGT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 287 TGNPKGVMLTHGNVVAGVCSVilqmgDHRI-------RAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFysGDIKELTN 359
Cdd:PTZ00216 276 TGDPKGVMHTHGSLTAGILAL-----EDRLndligppEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 360 -------DLKMLKPTVMPAVPRllnrVYDKIQNDISAS-----GLKRGLFNMAMRAKEKEIargvlrRNGC----WDKLV 423
Cdd:PTZ00216 349 tfarphgDLTEFRPVFLIGVPR----IFDTIKKAVEAKlppvgSLKRRVFDHAYQSRLRAL------KEGKdtpyWNEKV 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 424 FKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVlEGYGQTE--CTGAITLTvqGDHVPNHVGPPVSCNAVKLVDV 501
Cdd:PTZ00216 419 FSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGMVI-QGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDT 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 502 PEmeyFANQNT----GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVP 577
Cdd:PTZ00216 496 EE---YKHTDTpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIAL 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 578 EKIENIYTLSQYV--NQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCNNKNVKELIMNDMLNWGKQSGLK 655
Cdd:PTZ00216 573 EALEALYGQNELVvpNGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRK 652
|
570 580 590
....*....|....*....|....*....|
gi 24666501 656 SFEQVKDIYLHPDPFSVQNGLLTPTFKAKR 685
Cdd:PTZ00216 653 SFEIVRHVRVLSDEWTPENGVLTAAMKLKR 682
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
130-686 |
5.04e-90 |
|
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: 288.87 E-value: 5.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 130 PYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVV 209
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 210 IVEDDGKaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaeDLCTVCYTSGTTGN 289
Cdd:cd17640 82 VVENDSD-----------------------------------------------------------DLATIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTHGNVVAGVCSvILQMGDhrIRAGDVMVSFLPLAHMFERCCEngmYYV--GGCVGFYSgDIKELTNDLKMLKPT 367
Cdd:cd17640 103 PKGVMLTHANLLHQIRS-LSDIVP--PQPGDRFLSILPIWHSYERSAE---YFIfaCGCSQAYT-SIRTLKDDLKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 368 VMPAVPRLLNRVYDKIQNDISASGLKRglfnmamrakeKEIARGVLrrngcwdklvfkkvhqaFGGNLRLMVVGSAPLAG 447
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPIK-----------QFLFLFFL-----------------SGGIFKFGISGGGALPP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 448 NVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYY 527
Cdd:cd17640 228 HVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 528 KDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKScIIAV 607
Cdd:cd17640 307 KNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKR-LGAL 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 608 VVPDTDVLKQWATENNVR--GTLSVLCNNKNVKELIMNDMLNW-GKQSGLKSFEQVKDIYLHPDPFsVQNGLLTPTFKAK 684
Cdd:cd17640 386 IVPNFEELEKWAKESGVKlaNDRSQLLASKKVLKLYKNEIKDEiSNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKIK 464
|
..
gi 24666501 685 RP 686
Cdd:cd17640 465 RN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
131-685 |
2.22e-75 |
|
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: 251.62 E-value: 2.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 131 YQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 210
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 211 VeddGKaamlLEKAPrSLKIIVAIKPIRQTTLERARSRgiqifSFIDVEKLGAKGN--HPEVPPTAEDLCTVCYTSGTTG 288
Cdd:cd05932 84 V---GK----LDDWK-AMAPGVPEGLISISLPPPSAAN-----CQYQWDDLIAQHPplEERPTRFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 289 NPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTV 368
Cdd:cd05932 151 QPKGVMLTFGSFAWAAQAGIEHIG---TEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 369 MPAVPRLLNRVYDKIQNDISASGLKRglfnmamrakekeiargvLRRNGCWDKLVFKKVHQAFGGN-LRLMVVGSAPLAG 447
Cdd:cd05932 228 FFSVPRLWTKFQQGVQDKIPQQKLNL------------------LLKIPVVNSLVKRKVLKGLGLDqCRLAGCGSAPVPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 448 NVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDvpemeyfanqnTGEVCVRGSNVFHGYY 527
Cdd:cd05932 290 ALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 528 KDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAV 607
Cdd:cd05932 358 KDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666501 608 VVPDTDVLKQWA-TENNVRGTLSVLCNNKNvkelimndmlnwgkqSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKR 685
Cdd:cd05932 438 VLSEEARLRADAfARAELEASLRAHLARVN---------------STLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
131-641 |
1.08e-74 |
|
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: 251.57 E-value: 1.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 131 YQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 210
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 211 VEDDGKAAMLLEKAPR--SLKIIVAIKPirqttlerarsRGIQIFS---FIDVEKLGAKGN-----HPEVPPTA------ 274
Cdd:cd17641 89 AEDEEQVDKLLEIADRipSVRYVIYCDP-----------RGMRKYDdprLISFEDVVALGRaldrrDPGLYEREvaagkg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVvAGVCSVILQMGDhrIRAGDVMVSFLPLAHMFERccengMYYVG------GCVG 348
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNF-LGHCAAYLAADP--LGPGDEYVSVLPLPWIGEQ-----MYSVGqalvcgFIVN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 FYSgDIKELTNDLKMLKPTVMPAVPRllnrVYDKIQNDIS-----ASGLKRGLFNMAMRAKEKEIARGV-LRRNGCW--- 419
Cdd:cd17641 230 FPE-EPETMMEDLREIGPTFVLLPPR----VWEGIAADVRarmmdATPFKRFMFELGMKLGLRALDRGKrGRPVSLWlrl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 420 -----DKLVFKKVHQAFG-GNLRLMVVGSAPLAGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSC 493
Cdd:cd17641 305 aswlaDALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 494 NAVKLvdvpemeyfanQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGE 573
Cdd:cd17641 384 TEVRI-----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGT 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666501 574 YIVPEKIENIYTLSQYVNQVYVYGESlKSCIIAVVVPDTDVLKQWATENNVR-GTLSVLCNNKNVKELI 641
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELI 520
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
124-678 |
3.18e-68 |
|
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: 234.66 E-value: 3.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 124 RETLTSPyQWINYDEALLRAKNFGAGmlalgARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQ 203
Cdd:cd17632 65 FETITYA-ELWERVGAVAAAHDPEQP-----VRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 204 TDMQVVIVE----DDGKAAMLLEKAPRSLKIIVAIKPIRQTT--LERARSRGIQIFSFIDVEKLGAKGNH-------PEV 270
Cdd:cd17632 139 TEPRLLAVSaehlDLAVEAVLEGGTPPRLVVFDHRPEVDAHRaaLESARERLAAVGIPVTTLTLIAVRGRdlppaplFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 271 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV-AGVCSVILQmgDHRIRAGdVMVSFLPLAHMFERCCENGMYYVGGCVGF 349
Cdd:cd17632 219 EPDDDPLALLIYTSGSTGTPKGAMYTERLVAtFWLKVSSIQ--DIRPPAS-ITLNFMPMSHIAGRISLYGTLARGGTAYF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 350 YS-GDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQndisaSGLKRGLFNMAMRAKEKEIARGVLRRngcwdklvfkkvh 428
Cdd:cd17632 296 AAaSDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQ-----AELDRRSVAGADAETLAERVKAELRE------------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 429 QAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLtvqgDHVPnhVGPPVScnAVKLVDVPEMEYFA 508
Cdd:cd17632 358 RVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE-AGAVIL----DGVI--VRPPVL--DYKLVDVPELGYFR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 509 NQNT---GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYT 585
Cdd:cd17632 429 TDRPhprGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 586 LSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATEnNVRGTLSvlcnnKNVKELimndmlnwGKQSGLKSFEQVKDIYL 665
Cdd:cd17632 509 ASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTA-RLRAALA-----ESLQRI--------AREAGLQSYEIPRDFLI 574
|
570
....*....|...
gi 24666501 666 HPDPFSVQNGLLT 678
Cdd:cd17632 575 ETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
134-685 |
2.58e-67 |
|
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: 228.87 E-value: 2.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaEDLCTVCYTSGTTGNPKGV 293
Cdd:cd05914 88 E------------------------------------------------------------DDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 294 MLTHGNVVAGV--CSVILQMGdhrirAGDVMVSFLPLAHMFErCCENGMY--YVGGCVGFYSGDIKELTNDLKMLKPTVM 369
Cdd:cd05914 108 MLTYRNIVSNVdgVKEVVLLG-----KGDKILSILPLHHIYP-LTFTLLLplLNGAHVVFLDKIPSAKIIALAFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 370 PAVPRLLnRVYDKIQND-ISASGLKRGLFNMAMRAKEKEIArgvlrrngcwdKLVFKKVHQAFGGNLRLMVVGSAPLAGN 448
Cdd:cd05914 182 LGVPVPL-VIEKIFKMDiIPKLTLKKFKFKLAKKINNRKIR-----------KLAFKKVHEAFGGNIKEFVIGGAKINPD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 449 VLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVscnavKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYK 528
Cdd:cd05914 250 VEEFLR-TIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI-----DGVEVRIDSPDPATGEGEIIVRGPNVMKGYYK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 529 DPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSciIAVV 608
Cdd:cd05914 324 NPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL--VALA 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666501 609 VPDTDVLKQWATennvrgtlsvlcNNKNVKELIMNDMLNWGKQSgLKSFEQVKDIYLHPDPFSVqngllTPTFKAKR 685
Cdd:cd05914 402 YIDPDFLDVKAL------------KQRNIIDAIKWEVRDKVNQK-VPNYKKISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
124-622 |
1.11e-66 |
|
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: 226.62 E-value: 1.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 124 RETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQ 203
Cdd:COG0318 15 RPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 204 TDMQVVIVeddgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaedlCTVCYT 283
Cdd:COG0318 95 SGARALVT------------------------------------------------------------------ALILYT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 284 SGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFerccenGMY-------YVGGCVGFYSG-DIK 355
Cdd:COG0318 109 SGTTGRPKGVMLTHRNLLANAAAIAAALG---LTPGDVVLVALPLFHVF------GLTvgllaplLAGATLVLLPRfDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 356 ELTNDLKMLKPTVMPAVPRLLNRVydkiqndisasglkrglfnmamrAKEKEIARGVLRRngcwdklvfkkvhqafggnL 435
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARL-----------------------LRHPEFARYDLSS-------------------L 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 436 RLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQ--GDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTG 513
Cdd:COG0318 218 RLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 514 EVCVRGSNVFHGYYKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN-IYTLSQyVNQ 592
Cdd:COG0318 297 EIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEvLAAHPG-VAE 373
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24666501 593 VYV-------YGESLKsciiAVVVP------DTDVLKQWATEN 622
Cdd:COG0318 374 AAVvgvpdekWGERVV----AFVVLrpgaelDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
122-700 |
7.55e-65 |
|
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: 225.70 E-value: 7.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 122 GWrETLTspyqWINYDEALLR-AKNFgagmLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFI 200
Cdd:cd05933 5 KW-HTLT----YKEYYEACRQaAKAF----LKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 201 IRQTDMQVVIVEDDGKAAMLLE---KAPRsLKIIVAIKpirqttlERARSRGIQIFSFIDVEKLGAkgnhpEVPPTAED- 276
Cdd:cd05933 76 AETSEANILVVENQKQLQKILQiqdKLPH-LKAIIQYK-------EPLKEKEPNLYSWDEFMELGR-----SIPDEQLDa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 277 ---------LCTVCYTSGTTGNPKGVMLTHGNVV----AGVCSVILQMGDHRiraGDVMVSFLPLAH----MFErcceng 339
Cdd:cd05933 143 iissqkpnqCCTLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDLRPATVG---QESVVSYLPLSHiaaqILD------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 340 MY---YVGGCVGFYSGD-IK-ELTNDLKMLKPTVMPAVPRllnrVYDKIQNDI-----SASGLKRGLFNMAMRA------ 403
Cdd:cd05933 214 IWlpiKVGGQVYFAQPDaLKgTLVKTLREVRPTAFMGVPR----VWEKIQEKMkavgaKSGTLKRKIASWAKGVgletnl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 404 KEKEIARGVLRRNGCWDKLVFKKVHQAFG-GNLRLMVVGSAPLAGNVLTFMrCALGCLVLEGYGQTECTGAITLTVQGDH 482
Cdd:cd05933 290 KLMGGESPSPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 483 VPNHVGPPVSCNAVKLVdvpemeyfaNQNT---GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRI 559
Cdd:cd05933 369 RLLSCGKALPGCKTKIH---------NPDAdgiGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 560 IDRRKHIFKLSQGEYIVPEKIEN-IYTLSQYVNQVYVYGESLK--SCIIAV---VVPDT----DVLKQWATENNVRG--- 626
Cdd:cd05933 440 TGRIKELIITAGGENVPPVPIEDaVKKELPIISNAMLIGDKRKflSMLLTLkceVNPETgeplDELTEEAIEFCRKLgsq 519
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666501 627 --TLSVLCNNKN--VKELImNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMY 700
Cdd:cd05933 520 atRVSEIAGGKDpkVYEAI-EEGIKRVNKKAISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
276-622 |
7.82e-55 |
|
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: 190.96 E-value: 7.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVIlqmGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIK 355
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALA---ASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 356 ELT-NDLKMLKPTVMPAVPRLLNRvydkiqndisasglkrglfnmamrakekeiargvLRRNGCWDKLVFKkvhqafggN 434
Cdd:cd04433 78 EAAlELIEREKVTILLGVPTLLAR----------------------------------LLKAPESAGYDLS--------S 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 435 LRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHV--PNHVGPPVSCNAVKLVDvPEMEYFANQNT 512
Cdd:cd04433 116 LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVD-PDGGELPPGEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 513 GEVCVRGSNVFHGYYKDPEKTAEAiDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENIytLSQY--V 590
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAV--LLGHpgV 270
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24666501 591 NQVYVYG---ESLKSCIIAVVVP------DTDVLKQWATEN 622
Cdd:cd04433 271 AEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
134-621 |
8.69e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 195.89 E-value: 8.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 D-GKAAMLLEKAPRSLKIIVAIKPirqttlERARSRGIQIFSFIDVEKLGAKGN-HPEVppTAEDLCTVCYTSGTTGNPK 291
Cdd:PRK07656 111 LfLGVDYSATTRLPALEHVVICET------EEDDPHTEKMKTFTDFLAAGDPAErAPEV--DPDDVADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 292 GVMLTHGNV---VAGVCSvILQmgdhrIRAGDVMVSFLPLAHMFercCengmYYVGGCVGFYSG---------DIKELTN 359
Cdd:PRK07656 183 GAMLTHRQLlsnAADWAE-YLG-----LTEGDRYLAANPFFHVF---G----YKAGVNAPLMRGatilplpvfDPDEVFR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 360 DLKMLKPTVMPAVPRLLNRvydkiqndisasglkrgLFNMAMRAKEKeiargvLRrngcwdklvfkkvhqafggNLRLMV 439
Cdd:PRK07656 250 LIETERITVLPGPPTMYNS-----------------LLQHPDRSAED------LS-------------------SLRLAV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 440 VGSAPLAGNVLTFMRCALGC-LVLEGYGQTECTGAITLTVQGD---HVPNHVGPPVSCNAVKLVDVPEMEYFANQnTGEV 515
Cdd:PRK07656 288 TGAASMPVALLERFESELGVdIVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVNELGEEVPVGE-VGEL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 516 CVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV 595
Cdd:PRK07656 367 LVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAV 445
|
490 500 510
....*....|....*....|....*....|....*
gi 24666501 596 YG---ESLKSCIIAVVVP------DTDVLKQWATE 621
Cdd:PRK07656 446 IGvpdERLGEVGKAYVVLkpgaelTEEELIAYCRE 480
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
132-610 |
8.57e-53 |
|
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: 189.31 E-value: 8.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 132 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIirqtdmqvviV 211
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHI----------L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 212 EDDGKAAMllekaprslkiivaikpirqttlerarsrgIQIFSFIDVEKLGAKGNhPEVPPTAEDLCTVCYTSGTTGNPK 291
Cdd:cd05936 93 NDSGAKAL------------------------------IVAVSFTDLLAAGAPLG-ERVALTPEDVAVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 292 GVMLTHGNVVAGVCSVILQMGDhRIRAGDVMVSFLPLAHMF-ERCCENGMYYVGGC-VGFYSGDIKELTNDLKMLKPTVM 369
Cdd:cd05936 142 GAMLTHRNLVANALQIKAWLED-LLEGDDVVLAALPLFHVFgLTVALLLPLALGATiVLIPRFRPIGVLKEIRKHRVTIF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 370 PAVPRllnrvydkiqndisasglkrgLFNMAMRAKEKEiargvlrrngcwdKLVFKkvhqafggNLRLMVVGSAPLAGNV 449
Cdd:cd05936 221 PGVPT---------------------MYIALLNAPEFK-------------KRDFS--------SLRLCISGGAPLPVEV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 450 LTFMRCALGCLVLEGYGQTECTGAITLT-VQGDHVPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVF 523
Cdd:cd05936 259 AERFEELTGVPIVEGYGLTETSPVVAVNpLDGPRKPGSIGIPLPGTEVKIVDddgeeLPPGE------VGELWVRGPQVM 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 524 HGYYKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV-------Y 596
Cdd:cd05936 333 KGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpyS 410
|
490
....*....|....
gi 24666501 597 GESLKsciiAVVVP 610
Cdd:cd05936 411 GEAVK----AFVVL 420
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
243-702 |
1.87e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 191.09 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 243 ERARSRGIQIFSFIDVeklgAKGNHPEVPPTAED---LCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVIlqmgDHRIRAG 319
Cdd:PTZ00342 273 EKAKKLGISIILFDDM----TKNKTTNYKIQNEDpdfITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLC----KHSIFKK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 320 ---DVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISA-SGLKRG 395
Cdd:PTZ00342 345 ynpKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNlPPLKRF 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 396 LFN--MAMRAKEKeiargvlrrNGCWDKL------VFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQ 467
Cdd:PTZ00342 425 LVKkiLSLRKSNN---------NGGFSKFlegithISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 468 TECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMeYFANQNT--GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHT 545
Cdd:PTZ00342 496 TETTGPIFVQHADDNNTESIGGPISPNTKYKVRTWET-YKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKT 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 546 GDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVR 625
Cdd:PTZ00342 575 GDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNML 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 626 GTLSVlcNNKNVKELIMND--------------MLNWGKQSGLKSFEQVKDIYLHPDPFSVQNgLLTPTFKAKRPQL--- 688
Cdd:PTZ00342 655 ESTGI--NEKNYLEKLTDEtinnniyvdyvkgkMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVfkd 731
|
490
....*....|....
gi 24666501 689 KSYFKPQLEDMYKH 702
Cdd:PTZ00342 732 YAFFIDQVKKIYKN 745
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
134-583 |
4.69e-49 |
|
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: 179.33 E-value: 4.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DGkaamlLEKAPRSLKIIVAIKPIRQTTLERARSRGIQIFSFidvEKLGAKGNHPEVPP--TAEDLCTVCYTSGTTGNPK 291
Cdd:cd05911 91 DG-----LEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLS---PTLGEEDEDLPPPLkdGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 292 GVMLTHGNVVAGVCSVILQMGDHrIRAGDVMVSFLPLAHMFerccenGM-----YYVGGCVG-----FYSGDIKELTNDL 361
Cdd:cd05911 163 GVCLSHRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIY------GLfttlaSLLNGATViimpkFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 362 KMlkpTVMPAVPRLLNRvydkiqndisasglkrgLFNMAMRAKEKeiargvlrrngcwdkLvfkkvhqafgGNLRLMVVG 441
Cdd:cd05911 236 KI---TFLYLVPPIAAA-----------------LAKSPLLDKYD---------------L----------SSLRVILSG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 442 SAPLAGNVLTFMRCALG-CLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGS 520
Cdd:cd05911 271 GAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGP 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666501 521 NVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKIENI 583
Cdd:cd05911 351 QVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV 412
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
103-598 |
7.04e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 179.61 E-value: 7.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 103 TLYQTFREGA-YASNngpclgwRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSF 181
Cdd:PRK06187 7 TIGRILRHGArKHPD-------KEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 182 SLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDD--GKAAMLLEKAPRSLKIIVAIKPIRQTTLERARSrgiqiFSfidvE 259
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGE-----YE----E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 260 KLGAKGNHPEVPPTAE-DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFERccen 338
Cdd:PRK06187 151 LLAAASDTFDFPDIDEnDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWL---KLSRDDVYLVIVPMFHVHAW---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 339 GMYYVGgcvgFYSG---------DIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrglfnMAMRAKekeIA 409
Cdd:PRK06187 224 GLPYLA----LMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQ---------------------MLLKAP---RA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 410 RGVlrrngcwdklvfkkvhqAFGGnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNH--- 486
Cdd:PRK06187 276 YFV-----------------DFSS-LRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtk 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 487 ---VGPPVSCNAVKLVDvPEMEYFANQN--TGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMWLPNGTLRIID 561
Cdd:PRK06187 338 rrsAGRPLPGVEARIVD-DDGDELPPDGgeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITD 415
|
490 500 510
....*....|....*....|....*....|....*....
gi 24666501 562 RRKHIFKlSQGEYIVPEKIENIytLSQY--VNQVYVYGE 598
Cdd:PRK06187 416 RIKDVII-SGGENIYPRELEDA--LYGHpaVAEVAVIGV 451
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
133-622 |
1.10e-45 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 170.19 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 133 WINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVE 212
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 213 DDGKAAmLLEKAPRSLKIIVAIkpirqtTLERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKG 292
Cdd:cd05926 94 KGELGP-ASRAASKLGLAILEL------ALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 293 VMLTHGNVVAGVCSVIlqmGDHRIRAGDVMVSFLPLAHMfercceNGM-------YYVGGCV----GFysgDIKELTNDL 361
Cdd:cd05926 167 VPLTHRNLAASATNIT---NTYKLTPDDRTLVVMPLFHV------HGLvasllstLAAGGSVvlppRF---SASTFWPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 362 KMLKPTVMPAVPRLLnrvydKIqndisasglkrgLFNMAMRAKEKEIARgvlrrngcwdklvfkkvhqafggnLRLMVVG 441
Cdd:cd05926 235 RDYNATWYTAVPTIH-----QI------------LLNRPEPNPESPPPK------------------------LRFIRSC 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 442 SAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLT--VQGDHVPNHVGPPVscnAVKLVDVPEM-EYFANQNTGEVCVR 518
Cdd:cd05926 274 SASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPV---GVEVRILDEDgEILPPGVVGEICLR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 519 GSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYV--- 595
Cdd:cd05926 351 GPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAVAfgv 429
|
490 500 510
....*....|....*....|....*....|....*..
gi 24666501 596 ----YGESlkscIIAVVVP------DTDVLKQWATEN 622
Cdd:cd05926 430 pdekYGEE----VAAAVVLregasvTEEELRAFCRKH 462
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
142-611 |
5.33e-40 |
|
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: 152.76 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 142 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIveddgkaamll 221
Cdd:cd17631 29 RVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 222 ekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaEDLCTVCYTSGTTGNPKGVMLTHGNVV 301
Cdd:cd17631 98 -----------------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 302 AGVCSVILQMGdhrIRAGDVMVSFLPLAHmferCCENGMY-----YVGGCV----GFysgDIKELTNDLKMLKPTVMPAV 372
Cdd:cd17631 125 WNAVNALAALD---LGPDDVLLVVAPLFH----IGGLGVFtlptlLRGGTVvilrKF---DPETVLDLIERHRVTSFFLV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 373 PRLLNRVYDkiqndisasglkrglfnmamrakekeiargvlrrngcwdklvfkkvHQAFGG----NLRLMVVGSAPLAGN 448
Cdd:cd17631 195 PTMIQALLQ----------------------------------------------HPRFATtdlsSLRAVIYGGAPMPER 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 449 VLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHV--PNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGY 526
Cdd:cd17631 229 LLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 527 YKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN-IYTLSQyVNQVYV-------YGE 598
Cdd:cd17631 307 WNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDvLYEHPA-VAEVAVigvpdekWGE 383
|
490
....*....|...
gi 24666501 599 SlkscIIAVVVPD 611
Cdd:cd17631 384 A----VVAVVVPR 392
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-597 |
1.93e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 142.05 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVed 213
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 dgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaeDLCTVCYTSGTTGNPKGV 293
Cdd:cd05934 82 --------------------------------------------------------------DPASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 294 MLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMfeRCCENGMY---YVGGCV---------GFYSgDIKE----L 357
Cdd:cd05934 100 VITHANLTFAGYYSARRFG---LGEDDVYLTVLPLFHI--NAQAVSVLaalSVGATLvllprfsasRFWS-DVRRygatV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 358 TNDLKMLKPTVMPAVPRllnrvydkiQNDisasglkrglfnmamrakekeiargvlRRNgcwdklvfkkvhqafggnlRL 437
Cdd:cd05934 174 TNYLGAMLSYLLAQPPS---------PDD---------------------------RAH-------------------RL 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 438 MVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCV 517
Cdd:cd05934 199 RAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELVI 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 518 R---GSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVY 594
Cdd:cd05934 278 RglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAA 355
|
...
gi 24666501 595 VYG 597
Cdd:cd05934 356 VVA 358
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
134-568 |
2.89e-36 |
|
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: 143.14 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVed 213
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 dgkAAMLLEKAPRSLKIIVaikpirqtTLERARSRGIQIFSFIDVEKLGAKgnhPEVPPTAEDLCTVCYTSGTTGNPKGV 293
Cdd:cd05904 111 ---TAELAEKLASLALPVV--------LLDSAEFDSLSFSDLLFEADEAEP---PVVVIKQDDVAALLYSSGTTGRSKGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 294 MLTHGNVVAGVCSVILQMGDHRIRaGDVMVSFLPLAHMFERC-CENGMYYVGGCV----GFysgDIKELTNDLKMLKPTV 368
Cdd:cd05904 177 MLTHRNLIAMVAQFVAGEGSNSDS-EDVFLCVLPMFHIYGLSsFALGLLRLGATVvvmpRF---DLEELLAAIERYKVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 369 MPAVPRLLnrvydkiqndisasglkrglfnMAMRAKEKEiargvlrrngcwDKLVFKKVHQafggnlrlMVVGSAPLAGN 448
Cdd:cd05904 253 LPVVPPIV----------------------LALVKSPIV------------DKYDLSSLRQ--------IMSGAAPLGKE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 449 VL-TFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGppvSC-----NA-VKLVDvPE--MEYFANQnTGEVCVRG 519
Cdd:cd05904 291 LIeAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYG---SVgrlvpNVeAKIVD-PEtgESLPPNQ-TGELWIRG 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 24666501 520 SNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFK 568
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
149-597 |
6.97e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 139.91 E-value: 6.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 149 GMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKA----AMLLEKA 224
Cdd:PRK12583 61 GLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTsdyhAMLQELL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 225 PR-SLKIIVAIKPIRQTTLERARSRGIQ----IFSFIDVEKLG-----AKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVM 294
Cdd:PRK12583 141 PGlAEGQPGALACERLPELRGVVSLAPApppgFLAWHELQARGetvsrEALAERQASLDRDDPINIQYTSGTTGFPKGAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 295 LTHGNVV--AGVCSVILQMGDHriragDVMVSFLPLAHMFerccengmyyvgGCVgfysgdikeLTNDLKMLKPTVMpav 372
Cdd:PRK12583 221 LSHHNILnnGYFVAESLGLTEH-----DRLCVPVPLYHCF------------GMV---------LANLGCMTVGACL--- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 373 prllnrVYDKIQNDISASglkrglfnmaMRAKEKEIARGVlrrNGCWDKLVFKKVHQAFG----GNLRLMVVGSAP---- 444
Cdd:PRK12583 272 ------VYPNEAFDPLAT----------LQAVEEERCTAL---YGVPTMFIAELDHPQRGnfdlSSLRTGIMAGAPcpie 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 445 LAGNVLTFMRCALgclVLEGYGQTECTGAITLTVQGDHVPNH---VGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSN 521
Cdd:PRK12583 333 VMRRVMDEMHMAE---VQIAYGMTETSPVSLQTTAADDLERRvetVGRTQPHLEVKVVD-PDGATVPRGEIGELCTRGYS 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666501 522 VFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:PRK12583 409 VMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
276-621 |
7.91e-35 |
|
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: 137.81 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMfercceNGMY-------YVGGCVG 348
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW---RWTEDDVLLHVLPLHHV------HGLVnallcplFAGASVE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 FYSGDIKELTNDLKMLKP-TVMPAVPRllnrVYDKIQNDISASglkrglfnmamrAKEKEIARGVLRRNgcwdklvfkkv 427
Cdd:cd05941 161 FLPKFDPKEVAISRLMPSiTVFMGVPT----IYTRLLQYYEAH------------FTDPQFARAAAAER----------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 428 hqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYF 507
Cdd:cd05941 214 -------LRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 508 ANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRK-HIFKlSQGEYIVPEKIENiyTL 586
Cdd:cd05941 287 PRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIER--VL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24666501 587 SQY--VNQVYVYGESLKS---CIIAVVVP-------DTDVLKQWATE 621
Cdd:cd05941 364 LAHpgVSECAVIGVPDPDwgeRVVAVVVLragaaalSLEELKEWAKQ 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-605 |
8.38e-34 |
|
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: 132.79 E-value: 8.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDhriRAGDVMvsflplahmferCCENGMYYVGGCVGfysGDI 354
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGL---TEQDRL------------CIPVPLFHCFGSVL---GVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 355 KELTNDLKMLKP------------------TVMPAVP----RLLNRVyDKIQNDISAsgLKRGLfnMAMRAKEKEiargv 412
Cdd:cd05917 64 ACLTHGATMVFPspsfdplavleaiekekcTALHGVPtmfiAELEHP-DFDKFDLSS--LRTGI--MAGAPCPPE----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 413 lrrngcwdklVFKKVHQAFggNLRLMVVGsaplagnvltfmrcalgclvlegYGQTECTGAITLTVQGDHVP---NHVGP 489
Cdd:cd05917 134 ----------LMKRVIEVM--NMKDVTIA-----------------------YGMTETSPVSTQTRTDDSIEkrvNTVGR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 490 PVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkL 569
Cdd:cd05917 179 IMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-I 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24666501 570 SQGEYIVPEKIEN-IYTLsQYVNQVYV-------YGESLKSCII 605
Cdd:cd05917 258 RGGENIYPREIEEfLHTH-PKVSDVQVvgvpderYGEEVCAWIR 300
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
148-622 |
2.56e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.43 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 148 AGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVV---PLYDT---LGP--DACAfiirqtdmQVVIVEDdgKAAM 219
Cdd:PRK05605 72 AGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAhelEHPfeDHGA--------RVAIVWD--KVAP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 220 LLEKAPR--------SLKIIVAIKPIRQTTLE----RARSRGIQIFS----FIDVEKL--------GAKGNHPEvpPTAE 275
Cdd:PRK05605 142 TVERLRRttpletivSVNMIAAMPLLQRLALRlpipALRKARAALTGpapgTVPWETLvdaaiggdGSDVSHPR--PTPD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVAGvcsviLQMGDH---RIRAGD-VMVSFLPLAHMF--ERCCENGMYYVGGCVGF 349
Cdd:PRK05605 220 DVALILYTSGTTGKPKGAQLTHRNLFAN-----AAQGKAwvpGLGDGPeRVLAALPMFHAYglTLCLTLAVSIGGELVLL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 350 YSGDIKELTNDLKMLKPTVMPAVPRLlnrvYDKI-----QNDISASGLkRGLFNMAMRAKEKEIARgvlrrngcWDKLVf 424
Cdd:PRK05605 295 PAPDIDLILDAMKKHPPTWLPGVPPL----YEKIaeaaeERGVDLSGV-RNAFSGAMALPVSTVEL--------WEKLT- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 425 kkvhqafGGNLrlmvvgsaplagnvltfmrcalgclvLEGYGQTECTGAITLTVQGDHV-PNHVGPPVSCNAVKLVDvPE 503
Cdd:PRK05605 361 -------GGLL--------------------------VEGYGLTETSPIIVGNPMSDDRrPGYVGVPFPDTEVRIVD-PE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 504 --MEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 581
Cdd:PRK05605 407 dpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVE 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24666501 582 NIYTLSQYVNQVYVYG-------ESLKSCIIAV--VVPDTDVLKQWATEN 622
Cdd:PRK05605 485 EVLREHPGVEDAAVVGlpredgsEEVVAAVVLEpgAALDPEGLRAYCREH 534
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
60-700 |
4.38e-32 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 133.83 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 60 ERPLVPLENQSplLEGPE--QIHVSKFYKESKNGKFVSYITENVRTLYQTFRegayasnngpCLGWRETLTSPyQWINYD 137
Cdd:PTZ00297 395 ERPFLTVEALK--EKGEEcfALNLPREYNPLAGVRSLGEMWERSVTRHSTFR----------CLGQTSESGES-EWLTYG 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 138 EALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTlgPDACAFIIRQTDMQVViVEDDGKA 217
Cdd:PTZ00297 462 TVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPLVGK--GSTMRTLIDEHKIKVV-FADRNSV 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 218 AMLLEKAPRSLKIIVAIKPIRQTTLER-ARSRGIQIFSFIDVEKlgaKGNHPEVPP----TAEDLCTVCY---TSGTTGN 289
Cdd:PTZ00297 539 AAILTCRSRKLETVVYTHSFYDEDDHAvARDLNITLIPYEFVEQ---KGRLCPVPLkehvTTDTVFTYVVdntTSASGDG 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGfySGDIKELTNDLKMLKPTVM 369
Cdd:PTZ00297 616 LAVVRVTHADVLRDISTLVMTGVLPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTIL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 370 PAVPRLLNrvydkiqndISASGLKRG----------LFNMAMRAKEKEIarGVLRRNGCWDKLVFKKVHQ-AFGGNLRLM 438
Cdd:PTZ00297 694 VAAPSLFS---------TSRLQLSRAnerysavyswLFERAFQLRSRLI--NIHRRDSSLLRFIFFRATQeLLGGCVEKI 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 439 VVGSA------PLAGNVLTfmrCALGCLVLEGYgqTECTGAITLtvqgDHVPnhvGPPVScnavklVDVPEMEYFANQNT 512
Cdd:PTZ00297 763 VLCVSeestsfSLLEHISV---CYVPCLREVFF--LPSEGVFCV----DGTP---APSLQ------VDLEPFDEPSDGAG 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 513 -GEVCV--RGsnvfhgyykDPEKTAEAidsegwhhtgdVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQY 589
Cdd:PTZ00297 825 iGQLVLakKG---------EPRRTLPI-----------AAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRY 884
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 590 VNQVYVYGESLKScIIAVVVPDTDVLK-QW--ATENNVRGTLSVLCNNKNVKE----LIMNDMLNWGKQSGLKSFEQVKD 662
Cdd:PTZ00297 885 VNDIFLYADPSRP-IIAIVSPNRDTVEfEWrqSHCMGEGGGPARQLGWTELVAyassLLTADFACIAKENGLHPSNVPEY 963
|
650 660 670
....*....|....*....|....*....|....*...
gi 24666501 663 IYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMY 700
Cdd:PTZ00297 964 VHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
259-605 |
2.29e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 129.33 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 259 EKLGAKGNHPEVPPTaeDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIraGDVM-VSFLPLAHMFER--- 334
Cdd:PLN02330 170 DRAGDTSDNEEILQT--DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMI--GQVVtLGLIPFFHIYGItgi 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 335 CCENgMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRL-LNRVYDKIQNDISASGLKrglfnmamrakekeiargvl 413
Cdd:PLN02330 246 CCAT-LRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIiLNLVKNPIVEEFDLSKLK-------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 414 rrngcwdklvfkkvhqafggnLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTgAITLTV------QGDHVPNH 486
Cdd:PLN02330 305 ---------------------LQAIMTAAAPLAPELLTaFEAKFPGVQVQEAYGLTEHS-CITLTHgdpekgHGIAKKNS 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 487 VGPPVSCNAVKLVDvPEMEYFANQNT-GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKH 565
Cdd:PLN02330 363 VGFILPNLEVKFID-PDTGRSLPKNTpGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKE 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24666501 566 IFKLsQGEYIVPEKIENIYTLSQYVNQVYVY-------GESLKSCII 605
Cdd:PLN02330 442 LIKY-KGFQVAPAELEAILLTHPSVEDAAVVplpdeeaGEIPAACVV 487
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
251-583 |
4.68e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 128.40 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 251 QIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHR------IRAG-DVMV 323
Cdd:PRK12492 183 QAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGpdgqplMKEGqEVMI 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 324 SFLPLAHMFErccengmyYVGGCVGFY-SGDIKEL-TNdlkmlkptvmpavPRLLNRVYDKIQN-DISAS-GLKRgLFNM 399
Cdd:PRK12492 263 APLPLYHIYA--------FTANCMCMMvSGNHNVLiTN-------------PRDIPGFIKELGKwRFSALlGLNT-LFVA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 400 AMRAKEkeiargvlrrngcwdklvFKKVHQAfggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQ 479
Cdd:PRK12492 321 LMDHPG------------------FKDLDFS---ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPY 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 480 GDHVP-NHVGPPVSCNAVKLVDVPEMEYFANQNtGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLR 558
Cdd:PRK12492 380 GELARlGTVGIPVPGTALKVIDDDGNELPLGER-GELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVR 458
|
330 340
....*....|....*....|....*
gi 24666501 559 IIDRRKHIFKLSqGEYIVPEKIENI 583
Cdd:PRK12492 459 IVDRKKDLIIVS-GFNVYPNEIEDV 482
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
136-612 |
1.99e-30 |
|
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: 124.80 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 136 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRqtdmqvvivedDG 215
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILR-----------RA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 216 KAAMLLekAPRSLKiivaikpirqttlerarsrgiqifsfidveklgaKGNHPEVPptaEDLCTVCYTSGTTGNPKGVML 295
Cdd:cd05903 73 KAKVFV--VPERFR----------------------------------QFDPAAMP---DAVALLLFTSGTTGEPKGVMH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 296 THGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMferccengmyyvggcVGFYSGdikeltndlkMLKPTVMPAvPRL 375
Cdd:cd05903 114 SHNTLSASIRQYAERLG---LGPGDVFLVASPMAHQ---------------TGFVYG----------FTLPLLLGA-PVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 376 LNRVYDkiqndisasglkrglfnmAMRAKEkeiargVLRRNGC---------WDKLVfkkVHQAFGG----NLRLMVVGS 442
Cdd:cd05903 165 LQDIWD------------------PDKALA------LMREHGVtfmmgatpfLTDLL---NAVEEAGeplsRLRTFVCGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 443 APLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDhvPNHV----GPPVSCNAVKLVDVPEMEYFANQnTGEVCVR 518
Cdd:cd05903 218 ATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAP--EDRRlytdGRPLPGVEIKVVDDTGATLAPGV-EGELLSR 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 519 GSNVFHGYYKDPEKTAEAiDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG- 597
Cdd:cd05903 295 GPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAl 372
|
490
....*....|....*..
gi 24666501 598 --ESLKSCIIAVVVPDT 612
Cdd:cd05903 373 pdERLGERACAVVVTKS 389
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
137-610 |
3.78e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 125.43 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 137 DEALLRAknfGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgk 216
Cdd:PRK08316 43 DAAVNRV---AAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 217 aamLLEKAPRSLkiivAIKPIRQTTLERARSRGIQIFSFIDVEKLGAKGN--HPEVPPTAEDLCTVCYTSGTTGNPKGVM 294
Cdd:PRK08316 118 ---LAPTAEAAL----ALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSvaEPDVELADDDLAQILYTSGTESLPKGAM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 295 LTHGNVVAGVCSVILqmgDHRIRAGDVMVSFLPLAHMFERCCENGMY-YVGGcvgfysgdikelTNdlkmlkpTVM--PA 371
Cdd:PRK08316 191 LTHRALIAEYVSCIV---AGDMSADDIPLHALPLYHCAQLDVFLGPYlYVGA------------TN-------VILdaPD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 372 VPRLLNRVydkiqndisasglkrglfnmamrakEKEIAR----------GVLRrngcwdklvfkkvHQAFG----GNLRL 437
Cdd:PRK08316 249 PELILRTI-------------------------EAERITsffapptvwiSLLR-------------HPDFDtrdlSSLRK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 438 MVVGSAPLAGNVLTFMRCAL-GCLVLEGYGQTECtgAITLTVQG--DHV--PNHVGPPVSCNAVKLVDvPEMEYFANQNT 512
Cdd:PRK08316 291 GYYGASIMPVEVLKELRERLpGLRFYNCYGQTEI--APLATVLGpeEHLrrPGSAGRPVLNVETRVVD-DDGNDVAPGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 513 GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN-IYTLSQyVN 591
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVASREVEEaLYTHPA-VA 444
|
490 500
....*....|....*....|....*.
gi 24666501 592 QVYVYG-------ESlkscIIAVVVP 610
Cdd:PRK08316 445 EVAVIGlpdpkwiEA----VTAVVVP 466
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
191-583 |
2.42e-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: 122.44 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 191 TLGPDACAFIIRQTDMQVVIVeddgkAAMLLEKApRSLKIIVAIKPIRQTTLERARSR-----GIQIFSFIDVEKLGAKG 265
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLT-----SKQFIEKL-KLHHLFDVEYDARIVYLEDLRAKiskadKCKAFLAGKFPPKWLLR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 266 NHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGV--CSVILqmgdhRIRAGDVMVSFLPLAHMFerccengmyyv 343
Cdd:cd05909 138 IFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeqITAIF-----DPNPEDVVFGALPFFHSF----------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 344 ggcvGFYSGDIKELTNDLKML---KPTVMPAVPRLlnrVYD-KIQNDISASGLKRGLFNmamRAKEKEIARgvlrrngcw 419
Cdd:cd05909 202 ----GLTGCLWLPLLSGIKVVfhpNPLDYKKIPEL---IYDkKATILLGTPTFLRGYAR---AAHPEDFSS--------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 420 dklvfkkvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITL-TVQGDHVPNHVGPPVSCNAVKL 498
Cdd:cd05909 263 ---------------LRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 499 VDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPE 578
Cdd:cd05909 328 VSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLE 405
|
....*
gi 24666501 579 KIENI 583
Cdd:cd05909 406 AIEDI 410
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
251-585 |
2.57e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 123.33 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 251 QIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAH 330
Cdd:PRK05677 183 QAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIAPLPLYH 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 331 MFerccengmyyvggCVGFYSGDIKELTN-DLKMLKPTVMPAVPRLLNRvydkiQNDISASGLKRgLFNmamrakekeia 409
Cdd:PRK05677 263 IY-------------AFTFHCMAMMLIGNhNILISNPRDLPAMVKELGK-----WKFSGFVGLNT-LFV----------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 410 rgVLRRNGCWDKLVFKKvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGP 489
Cdd:PRK05677 313 --ALCNNEAFRKLDFSA--------LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 490 PVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKL 569
Cdd:PRK05677 383 PVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILV 461
|
330
....*....|....*.
gi 24666501 570 SqGEYIVPEKIENIYT 585
Cdd:PRK05677 462 S-GFNVYPNELEDVLA 476
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
258-581 |
4.36e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 121.91 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 258 VEKLGAKG-------------NHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvcSVILQmgDH-RIRAGDVMV 323
Cdd:PRK07514 126 VETLDADGtgslleaaaaapdDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN--ALTLV--DYwRFTPDDVLI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 324 SFLPLAH---MFERCceNGMYYVGGCVGFYSG-DIKELTNdlKMLKPTVMPAVP----RLLnrvydkiQNDisasGLKRg 395
Cdd:PRK07514 202 HALPIFHthgLFVAT--NVALLAGASMIFLPKfDPDAVLA--LMPRATVMMGVPtfytRLL-------QEP----RLTR- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 396 lfnmamrakekEIARgvlrrngcwdklvfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAIT 475
Cdd:PRK07514 266 -----------EAAA-----------------------HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 476 LT-VQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPN 554
Cdd:PRK07514 311 SNpYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDER 390
|
330 340
....*....|....*....|....*..
gi 24666501 555 GTLRIIDRRKHIFkLSQGEYIVPEKIE 581
Cdd:PRK07514 391 GYVHIVGRGKDLI-ISGGYNVYPKEVE 416
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
268-606 |
1.47e-28 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 120.93 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVppTAEDLCTVCYTSGTTGNPKGVMLTHGNVVA------GVCSVILQMGDhriragDVMVSFLPLAHMFERCCeNGMY 341
Cdd:PRK08974 201 PEL--VPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqakAAYGPLLHPGK------ELVVTALPLYHIFALTV-NCLL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 342 YV--GGCVGFYSG--DIKELTNDLKMLKPTVMPAVprllnrvydkiqndisasglkRGLFNMAMRAKEkeiargvlrrng 417
Cdd:PRK08974 272 FIelGGQNLLITNprDIPGFVKELKKYPFTAITGV---------------------NTLFNALLNNEE------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 418 cwdklvFKKVHqaFGgNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLT-VQGDHVPNHVGPPVSCNAV 496
Cdd:PRK08974 319 ------FQELD--FS-SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNpYDLDYYSGSIGLPVPSTEI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 497 KLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIV 576
Cdd:PRK08974 390 KLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVY 466
|
330 340 350
....*....|....*....|....*....|....*..
gi 24666501 577 PEKIENIYTLSQYVNQVY-------VYGESLKSCIIA 606
Cdd:PRK08974 467 PNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
270-583 |
8.65e-28 |
|
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: 118.01 E-value: 8.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 270 VPPTA---EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMFerccenGMYYVGG- 345
Cdd:cd17642 176 KPPSFdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGF------GMFTTLGy 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 346 -CVGF-----YSGDIKELTNDLKMLKPTVMPAVPRLlnrvydkiqndisasglkrglfnMAMRAKEKEIARGVLrrngcw 419
Cdd:cd17642 250 lICGFrvvlmYKFEEELFLRSLQDYKVQSALLVPTL-----------------------FAFFAKSTLVDKYDL------ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 420 dklvfkkvhqafgGNLRLMVVGSAPLAGNV---------LTFMRcalgclvlEGYGQTECTGAITLTVQGDHVPNHVGPP 490
Cdd:cd17642 301 -------------SNLHEIASGGAPLSKEVgeavakrfkLPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKV 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 491 VSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLs 570
Cdd:cd17642 360 VPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY- 438
|
330
....*....|...
gi 24666501 571 QGEYIVPEKIENI 583
Cdd:cd17642 439 KGYQVPPAELESI 451
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
218-581 |
9.71e-28 |
|
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: 116.21 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 218 AMLLEKAprSLKIIVAIKPIRQTTLERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTH 297
Cdd:TIGR01733 65 AFILEDA--GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 298 GNVVAgvcsVILQMGDHRI-RAGDVMVSFLPLAH------MFerccenGMYYVGGCVGFYSGDikeltndlkMLKPTvmp 370
Cdd:TIGR01733 143 RSLVN----LLAWLARRYGlDPDDRVLQFASLSFdasveeIF------GALLAGATLVVPPED---------EERDD--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 371 avPRLLNRVYDkiQNDISASGLKRGLFNMAMRAKEKEIARgvlrrngcwdklvfkkvhqafggnLRLMVV-GSAPLAGNV 449
Cdd:TIGR01733 201 --AALLAALIA--EHPVTVLNLTPSLLALLAAALPPALAS------------------------LRLVILgGEALTPALV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 450 LTFMRCALGCLVLEGYGQTECTGAITLTVQGDH-----VPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFH 524
Cdd:TIGR01733 253 DRWRARGPGARLINLYGPTETTVWSTATLVDPDdapreSPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVAR 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666501 525 GYYKDPEKTAEAI--------DSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 581
Cdd:TIGR01733 332 GYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYRIELGEIE 395
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
152-614 |
1.53e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 117.39 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 152 ALGARPKQLIGIYSQNRPE-WILYEQGCYSfSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDD---GKAAMLLEKAPrS 227
Cdd:PRK06188 56 ALGLGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLDDHAYVLEDAGISTLIVDPApfvERALALLARVP-S 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 228 LKIIVAIKPirqttLERARSRGIQIFSFidveklgakGNHPEVPPTA-EDLCTVCYTSGTTGNPKGVMLTHGNVVAgvcS 306
Cdd:PRK06188 134 LKHVLTLGP-----VPDGVDLLAAAAKF---------GPAPLVAAALpPDIAGLAYTGGTTGKPKGVMGTHRSIAT---M 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 307 VILQMGDHRIRAGDVMVSFLPLAHMfercceNGMYYV-----GGCV----GFYSGD----IKELTNDLKMLKPTVMPAV- 372
Cdd:PRK06188 197 AQIQLAEWEWPADPRFLMCTPLSHA------GGAFFLptllrGGTVivlaKFDPAEvlraIEEQRITATFLVPTMIYALl 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 373 --PRLLNRvydkiqnDISAsglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnLRLMVVGSAPLAGNVL 450
Cdd:PRK06188 271 dhPDLRTR-------DLSS---------------------------------------------LETVYYGASPMSPVRL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 451 TFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHV------GPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFH 524
Cdd:PRK06188 299 AEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 525 GYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV-------YG 597
Cdd:PRK06188 378 GYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWG 455
|
490
....*....|....*..
gi 24666501 598 ESLKsciiAVVVPDTDV 614
Cdd:PRK06188 456 EAVT----AVVVLRPGA 468
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
276-597 |
1.74e-27 |
|
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: 113.75 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVaGVCSVILQMGDhrIRAGDVMVSFLPLAHMFerccengmyyvggcvGFYSGDIK 355
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL-RAAAAWADCAD--LTEDDRYLIINPFFHTF---------------GYKAGIVA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 356 ELTNDLKMLkPTVMPAVPRLLNRVY-DKIQNDISASGLKRGLFNMAMRAKEKEiargvlrrngcwdklvfkkvhqafgGN 434
Cdd:cd17638 63 CLLTGATVV-PVAVFDVDAILEAIErERITVLPGPPTLFQSLLDHPGRKKFDL-------------------------SS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 435 LRLMVVGSAPLAGNVLTFMRCALGC-LVLEGYGQTECtGAITLTVQGDH---VPNHVGPPVSCNAVKLVDvpemeyfanq 510
Cdd:cd17638 117 LRAAVTGAATVPVELVRRMRSELGFeTVLTAYGLTEA-GVATMCRPGDDaetVATTCGRACPGFEVRIAD---------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 511 nTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYV 590
Cdd:cd17638 186 -DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGV 263
|
....*..
gi 24666501 591 NQVYVYG 597
Cdd:cd17638 264 AQVAVIG 270
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-611 |
3.34e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 116.51 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 255 FIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGV--CSVILQMGDHRIRAGDVMVSFLPLAHMF 332
Cdd:PRK08751 188 FREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqAHQWLAGTGKLEEGCEVVITALPLYHIF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 333 ErCCENGMYY--VGGCVGFYSG--DIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrglfnmamrakekei 408
Cdd:PRK08751 268 A-LTANGLVFmkIGGCNHLISNprDMPGFVKELKKTRFTAFTGVNTLFN------------------------------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 409 arGVLRRNGcWDKLVFKKVHQAFGGNlrlMVVGSAplagnVLTFMRCALGCLVLEGYGQTE-----CTGAITLtvqgDHV 483
Cdd:PRK08751 316 --GLLNTPG-FDQIDFSSLKMTLGGG---MAVQRS-----VAERWKQVTGLTLVEAYGLTEtspaaCINPLTL----KEY 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 484 PNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRR 563
Cdd:PRK08751 381 NGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRK 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24666501 564 KHIFKLSqGEYIVPEKIENIYTLSQYVNQVyvygeslksciIAVVVPD 611
Cdd:PRK08751 460 KDMILVS-GFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD 495
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
271-562 |
1.53e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.18 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 271 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvcsvILQMGD-HRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGF 349
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDvFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 350 YSGDIKELTNDLKML---KPTVMPAVPRLLnRVYdkiqndisasglkrglfnmamrakekeiargvLRRngcwdklvfKK 426
Cdd:PRK08633 854 YHPDPTDALGIAKLVakhRATILLGTPTFL-RLY--------------------------------LRN---------KK 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 427 VHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITL----------TVQGDHVPNHVGPPVSCNAV 496
Cdd:PRK08633 892 LHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVnlpdvlaadfKRQTGSKEGSVGMPLPGVAV 971
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666501 497 KLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI---DSEGWHHTGDVGMWLPNGTLRIIDR 562
Cdd:PRK08633 972 RIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
124-605 |
1.60e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 114.52 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 124 RETLTSPYQWI--NYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVV---PLYDT--Lgpda 196
Cdd:PRK08315 32 REALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRLseL---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 197 cAFIIRQTDMQVVIVEDDGK----AAMLLEKAPRsLKIIV--AIKPIRQTTLER------ARSRGIqiFSFIDVEKLGAK 264
Cdd:PRK08315 108 -EYALNQSGCKALIAADGFKdsdyVAMLYELAPE-LATCEpgQLQSARLPELRRviflgdEKHPGM--LNFDELLALGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 265 GNHPEVPPTAEDL-----CTVCYTSGTTGNPKGVMLTHGNVVAGVCSVilqmGDH-RIRAGDVMVSFLPLAHMFerccen 338
Cdd:PRK08315 184 VDDAELAARQATLdpddpINIQYTSGTTGFPKGATLTHRNILNNGYFI----GEAmKLTEEDRLCIPVPLYHCF------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 339 gmyyvgGCVgfySGDIKELTNDLKMLKP-------TVMPAV---------------------PRLLNrvYDkiqndisAS 390
Cdd:PRK08315 254 ------GMV---LGNLACVTHGATMVYPgegfdplATLAAVeeerctalygvptmfiaeldhPDFAR--FD-------LS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 391 GLKRGLfnMAmrakekeiarG------VLRRngcwdklVFKKVHqafggnlrlmvvgsaplagnvltfMRcalgcLVLEG 464
Cdd:PRK08315 316 SLRTGI--MA----------GspcpieVMKR-------VIDKMH------------------------MS-----EVTIA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 465 YGQTECTGAITLTVQGDHVPNHVG------PPVScnaVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAID 538
Cdd:PRK08315 348 YGMTETSPVSTQTRTDDPLEKRVTtvgralPHLE---VKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAID 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666501 539 SEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIEN-IYTLSQyVNQVYV-------YGESLKSCII 605
Cdd:PRK08315 425 ADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEfLYTHPK-IQDVQVvgvpdekYGEEVCAWII 497
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
272-610 |
1.71e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 114.38 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 272 PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMferccengmyyvggcVGFYS 351
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG---LGADDVILMASPMAHQ---------------TGFMY 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 352 GdikeltndlkMLKPTVMPAvprllNRVYDKIQNDISASGLKR--GL-FNMAMRAKEKEIARGVlrrngcwdKLVFKKVH 428
Cdd:PRK13295 256 G----------LMMPVMLGA-----TAVLQDIWDPARAAELIRteGVtFTMASTPFLTDLTRAV--------KESGRPVS 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 429 QafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECtGAITLTVQGD---HVPNHVGPPVSCNAVKLVDVPEME 505
Cdd:PRK13295 313 S-----LRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEN-GAVTLTKLDDpdeRASTTDGCPLPGVEVRVVDADGAP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 506 YFANQnTGEVCVRGSNVFHGYYKDPEKTAEaiDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYT 585
Cdd:PRK13295 387 LPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLY 462
|
330 340
....*....|....*....|....*...
gi 24666501 586 LSQYVNQVYVYG---ESLKSCIIAVVVP 610
Cdd:PRK13295 463 RHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
122-562 |
3.33e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 113.67 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 122 GWRETLTspyqwinYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWI---LyeqGCYSFSLVVVPLYDTLGPDACA 198
Cdd:COG0365 35 GEERTLT-------YAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAViamL---ACARIGAVHSPVFPGFGAEALA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 199 FIIRQTDMQVVIVEDDG-----------KAAMLLEKAPRSLKIIVAikpirQTTLERARSRGiqifsFIDVEKL--GAKG 265
Cdd:COG0365 105 DRIEDAEAKVLITADGGlrggkvidlkeKVDEALEELPSLEHVIVV-----GRTGADVPMEG-----DLDWDELlaAASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 266 NHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdHRIRAGDVMVSFLPLA----HMfercceNGMY 341
Cdd:COG0365 175 EFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV--LDLKPGDVFWCTADIGwatgHS------YIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 342 ---YVGGCVGFYSGdiKELTND----LKML---KPTVMPAVPrllnrvydkiqndisasglkrGLFNMAMRAKEKEIARG 411
Cdd:COG0365 247 gplLNGATVVLYEG--RPDFPDpgrlWELIekyGVTVFFTAP---------------------TAIRALMKAGDEPLKKY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 412 VLRRngcwdklvfkkvhqafggnLRLMV-VGSaPLagNVLTFMRC--ALGCLVLEGYGQTECTGAITLTVQGDHV-PNHV 487
Cdd:COG0365 304 DLSS-------------------LRLLGsAGE-PL--NPEVWEWWyeAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSM 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 488 GPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSN--VFHGYYKDPEKTAEAI--DSEGWHHTGDVGMWLPNGTLR 558
Cdd:COG0365 362 GKPVPGYDVAVVDedgnpVPPGE------EGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFW 435
|
....
gi 24666501 559 IIDR 562
Cdd:COG0365 436 ILGR 439
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
256-614 |
4.70e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.01 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 256 IDVEkLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVcsvilqmgDHRIRA-----GDVMVSFLPLAH 330
Cdd:PRK07787 110 VPVR-LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADL--------DALAEAwqwtaDDVLVHGLPLFH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 331 mferccengmyyVGGCVgfysgdikeltndLKMLKPTvmpavpRLLNRVYD--KIQNDISASGLKRG---LF---NMAMR 402
Cdd:PRK07787 181 ------------VHGLV-------------LGVLGPL------RIGNRFVHtgRPTPEAYAQALSEGgtlYFgvpTVWSR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 403 -AKEKEIARgvlrrngcwdklvfkkvhqAFGGnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTgaITLTVQ-- 479
Cdd:PRK07787 230 iAADPEAAR-------------------ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETL--ITLSTRad 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 480 GDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNT-GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLR 558
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVDEDGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHR 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666501 559 IIDRRKH--I----FKLSQGEyivpekIENIYTLSQYVNQVYVYGE---SLKSCIIAVVVPDTDV 614
Cdd:PRK07787 368 IVGRESTdlIksggYRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGADDV 426
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
134-582 |
7.88e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 111.03 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVed 213
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 dgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnHPEVpptaEDLCTVCYTSGTTGNPKGV 293
Cdd:cd05935 80 -----------------------------------------------------GSEL----DDLALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 294 MLTHGNVVAGVC-SVILQMGDHriraGDVMVSFLPLAHMFERCCE-NGMYYVGGCVGFYSGDIKELTNDL-KMLKPTVMP 370
Cdd:cd05935 103 MHTHFSAAANALqSAVWTGLTP----SDVILACLPLFHVTGFVGSlNTAVYVGGTYVLMARWDRETALELiEKYKVTFWT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 371 AVPRLLNRVYDKIQNdisasglkrglfnmamrakekeiargvlrRNGCWDKLVfkkvhqAFGGnlrlmvvGSAPLAGNVL 450
Cdd:cd05935 179 NIPTMLVDLLATPEF-----------------------------KTRDLSSLK------VLTG-------GGAPMPPAVA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 451 TFMRCALGCLVLEGYGQTEctgaitlTVQGDHVPNHVGPPVSCNAV-------KLVDVPEMEYFANQNTGEVCVRGSNVF 523
Cdd:cd05935 217 EKLLKLTGLRFVEGYGLTE-------TMSQTHTNPPLRPKLQCLGIp*fgvdaRVIDIETGRELPPNEVGEIVVRGPQIF 289
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666501 524 HGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN 582
Cdd:cd05935 290 KGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEA 350
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
122-617 |
2.85e-25 |
|
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: 110.60 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 122 GWREtltspyqwINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSF---SLVVVPLYDTLGPD--A 196
Cdd:cd05921 22 GWRR--------VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMSQDlaK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 197 CAFIIRQTDMQVVIVEDdgkaamllekAPRSLKIIVAIKPIRQTTL-ERARSRGIQIFSFIDVEKLGAKGNHPEVPP--T 273
Cdd:cd05921 94 LKHLFELLKPGLVFAQD----------AAPFARALAAIFPLGTPLVvSRNAVAGRGAISFAELAATPPTAAVDAAFAavG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 274 AEDLCTVCYTSGTTGNPKGVMLTHGNVvagvCSVILQMGDHRIRAGD---VMVSFLPLAHMFERCCENGMYYVGGcvGFY 350
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVINTQRML----CANQAMLEQTYPFFGEeppVLVDWLPWNHTFGGNHNFNLVLYNG--GTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 351 --------SGDIKELTNDLKMLKPTVMPAVPRllnrvydkiqndisasglkrGlFNMAMRAKEKEIArgvLRRNgcwdkl 422
Cdd:cd05921 238 yiddgkpmPGGFEETLRNLREISPTVYFNVPA--------------------G-WEMLVAALEKDEA---LRRR------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 423 vfkkvhqaFGGNLRLMVVGSAPLAGNV------LTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAV 496
Cdd:cd05921 288 --------FFKRLKLMFYAGAGLSQDVwdrlqaLAVATVGERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 497 KLVdvpemeyfANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWL----PNGTLRIIDRRKHIFKLSQG 572
Cdd:cd05921 360 KLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLASG 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24666501 573 EYIV--PEKIENIYTLSQYVNQVYVYGESlKSCIIAVVVPDTDVLKQ 617
Cdd:cd05921 432 TWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACRR 477
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
275-584 |
3.50e-25 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 108.59 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAH------MFErccenGMYYvGGCVG 348
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLG---LTEDDNWLCALPLFHisglsiLMR-----SVIY-GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 FYSG-DIKELTNDLKMLKPTVMPAVPRLLNRVydkiqndisasglkrglfnmamrakekeiargvlrrngcwdklvFKKV 427
Cdd:cd05912 148 LVDKfDAEQVLHLINSGKVTIISVVPTMLQRL--------------------------------------------LEIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 428 HQAFGGNLRLMVVGSAPLAGNVLTfmRCA-LGCLVLEGYGQTE-CTGAITLTVQGDHV-PNHVGPPVSCNAVKLVDVPEM 504
Cdd:cd05912 184 GEGYPNNLRCILLGGGPAPKPLLE--QCKeKGIPVYQSYGMTEtCSQIVTLSPEDALNkIGSAGKPLFPVELKIEDDGQP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 505 EYfanqNTGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIY 584
Cdd:cd05912 262 PY----EVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
273-621 |
4.11e-25 |
|
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: 108.77 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 273 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAH------MFerccenGMYYVGGC 346
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP---LTPGDRVLQFTSFSFdvsvweIF------GALLAGAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 347 VGFYS----GDIKELTNDLKMLKPTVMPAVPRLLNRVydkiqndisASGLKRGLFNmamrakekeiargvlrrngcwdkl 422
Cdd:cd05930 162 LVVLPeevrKDPEALADLLAEEGITVLHLTPSLLRLL---------LQELELAALP------------------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 423 vfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLE-GYGQTECTGAITLTV------QGDHVPnhVGPPVSCNA 495
Cdd:cd05930 209 -----------SLRLVLVGGEALPPDLVRRWRELLPGARLVnLYGPTEATVDATYYRvppddeEDGRVP--IGRPIPNTR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 496 VKLVDvpemeyfANQN------TGEVCVRGSNVFHGYYKDPEKTAE---AIDSEGW---HHTGDVGMWLPNGTLRIIDRR 563
Cdd:cd05930 276 VYVLD-------ENLRpvppgvPGELYIGGAGLARGYLNRPELTAErfvPNPFGPGermYRTGDLVRWLPDGNLEFLGRI 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666501 564 KHIFKLSqGEYIVPEKIENIYTLSQYVNQVYV--YGESLKS-CIIAVVVP------DTDVLKQWATE 621
Cdd:cd05930 349 DDQVKIR-GYRIELGEIEAALLAHPGVREAAVvaREDGDGEkRLVAYVVPdeggelDEEELRAHLAE 414
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
271-612 |
1.00e-24 |
|
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: 107.78 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 271 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVagvcSVILQMGDH-RIRAGDVMVSFLPLAhmFERCCenGMYYVGGCVG- 348
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVL----NYVSQPPARlDVGPGSRVAQVLSIA--FDACI--GEIFSTLCNGg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 --FYSGDIKELTNDLKMLkpTVMPAVPRLLnrvydkiqndisasglkrglfnmamrakekeiarGVLRRNGcwdklvFKk 426
Cdd:cd17653 173 tlVLADPSDPFAHVARTV--DALMSTPSIL----------------------------------STLSPQD------FP- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 427 vhqafggNLRLMVVGSAPLAGNVLTfmRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEY 506
Cdd:cd17653 210 -------NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 507 FANQnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHH------TGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKI 580
Cdd:cd17653 281 PEGV-VGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350
....*....|....*....|....*....|....*
gi 24666501 581 EN-IYTLSQYVNQVY--VYGESLksciIAVVVPDT 612
Cdd:cd17653 359 EEvVLQSQPEVTQAAaiVVNGRL----VAFVTPET 389
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
153-597 |
1.02e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 108.41 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 153 LGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAMLLEKAPRSLKiiv 232
Cdd:PRK06839 48 LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 233 aiKPIRQTTLERARSRGIQIFsfidveklgakgnhpeVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMG 312
Cdd:PRK06839 125 --RVISITSLKEIEDRKIDNF----------------VEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAID 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 313 dhrIRAGDVMVSFLPLAHmferccengmyyVGGcVGFYSgdikeltndlkmlKPTVMPAVPRLLNRVYDKIQndisasgl 392
Cdd:PRK06839 187 ---LTMHDRSIVLLPLFH------------IGG-IGLFA-------------FPTLFAGGVIIVPRKFEPTK-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 393 krglfnmAMRAKEKE---IARGVlrrngcwdklvfKKVHQAFG----------GNLRLMVVGSAPLAgnvLTFMRCAL-- 457
Cdd:PRK06839 230 -------ALSMIEKHkvtVVMGV------------PTIHQALIncskfettnlQSVRWFYNGGAPCP---EELMREFIdr 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 458 GCLVLEGYGQTECTGAITLTVQGD--HVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE 535
Cdd:PRK06839 288 GFLFGQGFGMTETSPTVFMLSEEDarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666501 536 AIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:PRK06839 367 TI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
133-583 |
1.29e-24 |
|
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: 108.16 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 133 WINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEwiLYE--QGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 210
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPA--MYElhFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 211 VEddgkaamllekaprslkiivaikpirqttlerarsrgiQIFSFIDVEKLGaKGNHPEVPPTAE-DLCTVCYTSGTTGN 289
Cdd:cd12118 107 VD--------------------------------------REFEYEDLLAEG-DPDFEWIPPADEwDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTH-GNVVAGVCSVIL-QMGDHriragDVMVSFLPLAHMFERCCENGMYYVGGC-VGFYSGDIKELTNDLKMLKP 366
Cdd:cd12118 148 PKGVVYHHrGAYLNALANILEwEMKQH-----PVYLWTLPMFHCNGWCFPWTVAAVGGTnVCLRKVDAKAIYDLIEKHKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 367 TVMPAVPRLLNRVYDkiqndisasglkrglfnmAMRAKEKEIARGVlrrngcwdklvfkkvhqafggnlRLMVVGSAPLA 446
Cdd:cd12118 223 THFCGAPTVLNMLAN------------------APPSDARPLPHRV-----------------------HVMTAGAPPPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 447 gNVLTFMRcALGCLVLEGYGQTECTGAITLTV-------------------QGdhVPNHVGPPVSC-NAVKLVDVPemey 506
Cdd:cd12118 262 -AVLAKME-ELGFDVTHVYGLTETYGPATVCAwkpewdelpteerarlkarQG--VRYVGLEEVDVlDPETMKPVP---- 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666501 507 fANQNT-GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENI 583
Cdd:cd12118 334 -RDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGV 408
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
268-568 |
2.31e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 107.76 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgvcSVILQM-GDH---RIRAGDVMVSFLPLAHMFercCENGMYYV 343
Cdd:PLN02246 172 PEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT---SVAQQVdGENpnlYFHSDDVILCVLPMFHIY---SLNSVLLC 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 344 GGCVG--------FYSGDIKELTNDLKMlkpTVMPAVPRLLnrvydkiqndisasglkrglfnMAMrAKEKEIARGVLrr 415
Cdd:PLN02246 246 GLRVGaailimpkFEIGALLELIQRHKV---TIAPFVPPIV----------------------LAI-AKSPVVEKYDL-- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 416 ngcwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLTFMRCALGCLVL-EGYGQTECTGAITLTVQGDHVPNHVGPPvSC- 493
Cdd:PLN02246 298 -----------------SSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAGPVLAMCLAFAKEPFPVKSG-SCg 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 494 ----NA-VKLVDvPE--MEYFANQnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHI 566
Cdd:PLN02246 360 tvvrNAeLKIVD-PEtgASLPRNQ-PGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKEL 437
|
..
gi 24666501 567 FK 568
Cdd:PLN02246 438 IK 439
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
268-581 |
3.83e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 107.43 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV---AGVCSVILQMGDHriragDVMVSFLPlahmferccengMYYVG 344
Cdd:PRK06178 202 PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVAVVGGED-----SVFLSFLP------------EFWIA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 345 GcvgfysgdikeltNDLKMLKPTVMPAVPRLLNRvYDkiqndisASGlkrglfnmAMRAKEKeiaRGVLRRNGCWDKLVF 424
Cdd:PRK06178 265 G-------------ENFGLLFPLFSGATLVLLAR-WD-------AVA--------FMAAVER---YRVTRTVMLVDNAVE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 425 KKVHQAFGG-NLR-LMVVGsaplagnVLTFMR----------CAL-GCLVLEG-YGQTECTGAITLTV--QGDHV----- 483
Cdd:PRK06178 313 LMDHPRFAEyDLSsLRQVR-------VVSFVKklnpdyrqrwRALtGSVLAEAaWGMTETHTCDTFTAgfQDDDFdllsq 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 484 PNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRR 563
Cdd:PRK06178 386 PVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRR 464
|
330
....*....|....*...
gi 24666501 564 KHIFKLSqGEYIVPEKIE 581
Cdd:PRK06178 465 KEMLKVN-GMSVFPSEVE 481
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
148-582 |
2.75e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 103.67 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 148 AGMLALGARPKQLIGIYSQNRPEWI-LYEQ----GCySFSLVVVPLYDTLGPdacafiirqTDMQVVIVEDDGKAAMLLE 222
Cdd:cd05922 8 SALLEAGGVRGERVVLILPNRFTYIeLSFAvayaGG-RLGLVFVPLNPTLKE---------SVLRYLVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 223 KAPRSLKIIVAIKPIRQTtlerarsrgiqifsFIDVEKL-GAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV 301
Cdd:cd05922 78 GAADRLRDALPASPDPGT--------------VLDADGIrAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 302 AGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCV----GFYSGDikELTNDLKMLKPTVMPAVP---R 374
Cdd:cd05922 144 ANARSIAEYLG---ITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDD--AFWEDLREHGATGLAGVPstyA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 375 LLNRVydkIQNDISASGLkRGLFNMAMRAKEKEIARgvLRrngcwDKLVfkkvhqafGGNLRLMvvgsaplagnvltfmr 454
Cdd:cd05922 219 MLTRL---GFDPAKLPSL-RYLTQAGGRLPQETIAR--LR-----ELLP--------GAQVYVM---------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 455 calgclvlegYGQTECTGAITlTVQGDHV---PNHVGPPVSCNAVKLVDVPEMEYfANQNTGEVCVRGSNVFHGYYKDPE 531
Cdd:cd05922 264 ----------YGQTEATRRMT-YLPPERIlekPGSIGLAIPGGEFEILDDDGTPT-PPGEPGEIVHRGPNVMKGYWNDPP 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 24666501 532 KTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN 582
Cdd:cd05922 332 YRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
254-583 |
3.97e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 103.95 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 254 SFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDV----MVSFLPLA 329
Cdd:PRK07059 183 RFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlnFVCALPLY 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 330 HMFER--CCENGMYyVGGCVGFYSG--DIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrGLFNmamrake 405
Cdd:PRK07059 263 HIFALtvCGLLGMR-TGGRNILIPNprDIPGFIKELKKYQVHIFPAVNTLYN-----------------ALLN------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 406 keiargvlrrNGCWDKLVFKKVHQAFGGNlrlMVVgSAPLAGNVLTFMrcalGCLVLEGYGQTECTGAITLT-VQGDHVP 484
Cdd:PRK07059 318 ----------NPDFDKLDFSKLIVANGGG---MAV-QRPVAERWLEMT----GCPITEGYGLSETSPVATCNpVDATEFS 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 485 NHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRI 559
Cdd:PRK07059 380 GTIGLPLPSTEVSIRDddgndLPLGE------PGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKI 453
|
330 340
....*....|....*....|....
gi 24666501 560 IDRRKHIFKLSqGEYIVPEKIENI 583
Cdd:PRK07059 454 VDRKKDMILVS-GFNVYPNEIEEV 476
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
102-575 |
5.15e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 103.97 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 102 RTLYQTFREGAYASNNGPCLGWRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSF 181
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDRPWLAQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 182 SLVVVPL---YDTLGPD-----ACAFIIRQtdmQVVIVEDdgkaAMLLEKAPRSLK-----IIVAIKPIRqttlerarsr 248
Cdd:PRK12582 129 GVPAAPVspaYSLMSHDhaklkHLFDLVKP---RVVFAQS----GAPFARALAALDlldvtVVHVTGPGE---------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 249 GIQIFSFIDvekLGAKGNHPEVPPTAEDLC--TVC---YTSGTTGNPKGVMLTHGNvvagVCSVILQMGDHRIRAGD--- 320
Cdd:PRK12582 192 GIASIAFAD---LAATPPTAAVAAAIAAITpdTVAkylFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDppp 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 321 -VMVSFLPLAHMFE-RCCENGMYYVGGCvgFY-------SGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDisasg 391
Cdd:PRK12582 265 pVSLDWMPWNHTMGgNANFNGLLWGGGT--LYiddgkplPGMFEETIRNLREISPTVYGNVPAGYAMLAEAMEKD----- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 392 lkrglfnmamrakekeiarGVLRRNgcwdklVFKkvhqafggNLRLMVVGSAPLAGNVLTFMRcALGC-------LVLEG 464
Cdd:PRK12582 338 -------------------DALRRS------FFK--------NLRLMAYGGATLSDDLYERMQ-ALAVrttghriPFYTG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 465 YGQTEcTGAITLTVQGD-HVPNHVGPPVSCNAVKLVDVPEmeyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWH 543
Cdd:PRK12582 384 YGATE-TAPTTTGTHWDtERVGLIGLPLPGVELKLAPVGD--------KYEVRVKGPNVTPGYHKDPELTAAAFDEEGFY 454
|
490 500 510
....*....|....*....|....*....|....*.
gi 24666501 544 HTGDVGMWL----PNGTLRIIDRRKHIFKLSQGEYI 575
Cdd:PRK12582 455 RLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
122-619 |
6.67e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 103.81 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 122 GWREtltspyqwINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPL---YDTLGPD--A 196
Cdd:PRK08180 66 GWRR--------LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQDfgK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 197 CAFIIRQTDMQVVIVEDDGK-AAMLLEKAPRSLKIIVAikpirqttleRARSRGIQIFSFidvEKLGAKGNHPEVPP--- 272
Cdd:PRK08180 138 LRHVLELLTPGLVFADDGAAfARALAAVVPADVEVVAV----------RGAVPGRAATPF---AALLATPPTAAVDAaha 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 273 --TAEDLCTVCYTSGTTGNPKGVMLTHGNVvagvCSVILQMGDHRIRAGD---VMVSFLPLAHMFerccenG-------M 340
Cdd:PRK08180 205 avGPDTIAKFLFTSGSTGLPKAVINTHRML----CANQQMLAQTFPFLAEeppVLVDWLPWNHTF------GgnhnlgiV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 341 YYVGGCvgFY-------SGDIKELTNDLKMLKPTVMPAVPRLlnrvydkiqndisasglkrglFNMAMRAKEKEIArgvL 413
Cdd:PRK08180 275 LYNGGT--LYiddgkptPGGFDETLRNLREISPTVYFNVPKG---------------------WEMLVPALERDAA---L 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 414 RRNgcwdklvfkkvhqaFGGNLRLMVVGSAPLAGNVLT-FMRCA---LGCLV--LEGYGQTECTGAITLTvqgdHVPN-- 485
Cdd:PRK08180 329 RRR--------------FFSRLKLLFYAGAALSQDVWDrLDRVAeatCGERIrmMTGLGMTETAPSATFT----TGPLsr 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 486 --HVGPPVSCNAVKLVDvpemeyfaNQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWL----PNGTLRI 559
Cdd:PRK08180 391 agNIGLPAPGCEVKLVP--------VGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMF 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666501 560 IDRRKHIFKLSQGEYI-V-PEKIENIYTLSQYVNQVYVYGESLKsCIIAVVVPDTDVLKQWA 619
Cdd:PRK08180 463 DGRIAEDFKLSSGTWVsVgPLRARAVSAGAPLVQDVVITGHDRD-EIGLLVFPNLDACRRLA 523
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
136-614 |
1.28e-22 |
|
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: 101.89 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 136 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDACAFIIRqtdmqvv 209
Cdd:cd12117 25 YAELNERANRLARRLRAAGVGPGDVVGVLAERSPELvvallaVLKAGAAY------VPLDPELPAERLAFMLA------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 210 ivedDGKAAMLLEKAPrslkiivaikpirqttlERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGN 289
Cdd:cd12117 92 ----DAGAKVLLTDRS-----------------LAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTHGNVVAGVCSvilqmGDHR-IRAGDVMVSFLPL---AHMFErccengmYYV----GGCVgfysgdikELTNDL 361
Cdd:cd12117 151 PKGVAVTHRGVVRLVKN-----TNYVtLGPDDRVLQTSPLafdASTFE-------IWGallnGARL--------VLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 362 KMLKPTVMPAVPRllnrvydkiQNDISASGLKRGLFNMAMRAKEkeiargvlrrngcwdklvfkkvhQAFGGnLRLMVVG 441
Cdd:cd12117 211 TLLDPDALGALIA---------EEGVTVLWLTAALFNQLADEDP-----------------------ECFAG-LRELLTG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 442 ----SAPLAGNVLTfmRCALGCLVlEGYGQTECTGAIT------LTVQGDHVPnhVGPPVSCNAVKLVD-----VPEMEy 506
Cdd:cd12117 258 gevvSPPHVRRVLA--ACPGLRLV-NGYGPTENTTFTTshvvteLDEVAGSIP--IGRPIANTRVYVLDedgrpVPPGV- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 507 fanqnTGEVCVRGSNVFHGYYKDPEKTAE------AIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKI 580
Cdd:cd12117 332 -----PGELYVGGDGLALGYLNRPALTAErfvadpFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEI 405
|
490 500 510
....*....|....*....|....*....|....*....
gi 24666501 581 ENiyTLSQY--VNQVYVY---GESLKSCIIAVVVPDTDV 614
Cdd:cd12117 406 EA--ALRAHpgVREAVVVvreDAGGDKRLVAYVVAEGAL 442
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
134-622 |
1.35e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 102.35 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFgAGML--ALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIV 211
Cdd:PRK08314 36 ISYRELLEEAERL-AGYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 212 EDD--GKAAMLLEKAPRSLKII------------VAIKPIRQTTLERARSRGIQIFSFIDVekLGAKGNHPEVPPTAEDL 277
Cdd:PRK08314 115 GSElaPKVAPAVGNLRLRHVIVaqysdylpaepeIAVPAWLRAEPPLQALAPGGVVAWKEA--LAAGLAPPPHTAGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 278 CTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHrirAGDVMVSFLPLAH---MfeRCCENGMYYVGGCVgfysgdi 354
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST---PESVVLAVLPLFHvtgM--VHSMNAPIYAGATV------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 355 keltndlkmlkptVMpaVPRLlnrvydkiqndisasglkrglfnmamrakEKEIARGVLRRNGC--W--------DKLVF 424
Cdd:PRK08314 261 -------------VL--MPRW-----------------------------DREAAARLIERYRVthWtniptmvvDFLAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 425 KKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAitltvqgdhvPNHVGPP----VSCNAVKLVD 500
Cdd:PRK08314 297 PGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMA----------QTHSNPPdrpkLQCLGIPTFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 501 V------PEM-EYFANQNTGEVCVRGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLS 570
Cdd:PRK08314 366 VdarvidPETlEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINAS 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666501 571 qGEYIVPEKIENIYTLSQYVNQVYVY-------GESLKsciiAVVVPD--------TDVLKQWATEN 622
Cdd:PRK08314 446 -GFKVWPAEVENLLYKHPAIQEACVIatpdprrGETVK----AVVVLRpeargkttEEEIIAWAREH 507
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
128-597 |
1.93e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 101.68 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 128 TSPYQWINYDEALLRAKNFgagMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQ 207
Cdd:PRK08008 35 VRRYSYLELNEEINRTANL---FYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 208 VVIVEddgkaamllekaPRSLKIIVAIKPIRQTTLER---ARSRGIQIFSFIDVEKLgaKGNHP----EVPP-TAEDLCT 279
Cdd:PRK08008 112 LLVTS------------AQFYPMYRQIQQEDATPLRHiclTRVALPADDGVSSFTQL--KAQQPatlcYAPPlSTDDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 280 VCYTSGTTGNPKGVMLTHGNvvagvcsviLQMGDH------RIRAGDVMVSFLPLAHM-FErcCENGM--YYVGGC---V 347
Cdd:PRK08008 178 ILFTSGTTSRPKGVVITHYN---------LRFAGYysawqcALRDDDVYLTVMPAFHIdCQ--CTAAMaaFSAGATfvlL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 348 GFYS-----GDIKE----LTNDLKMLKPTVM--PAVPRLLNRVydkiqndisasgLKRGLFNMAMRAKEKE--IARgvlr 414
Cdd:PRK08008 247 EKYSarafwGQVCKyratITECIPMMIRTLMvqPPSANDRQHC------------LREVMFYLNLSDQEKDafEER---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 415 rngcwdklvfkkvhqaFGgnLRLMvvgsaplagnvltfmrcalgclvlEGYGQTECTGAITLTVQGD--HVPNhVGPPVS 492
Cdd:PRK08008 311 ----------------FG--VRLL------------------------TSYGMTETIVGIIGDRPGDkrRWPS-IGRPGF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 493 CNAVKLVDVPEMEYFANQnTGEVCVRG---SNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKL 569
Cdd:PRK08008 348 CYEAEIRDDHNRPLPAGE-IGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKR 426
|
490 500
....*....|....*....|....*...
gi 24666501 570 SqGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:PRK08008 427 G-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
192-597 |
7.84e-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: 99.63 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 192 LGPDACAFIIRQTDMQVVIVEDDgkaamllekaprSLKIIVAIKPiRQTTLER----------ARSRGIQIFSFidvEKL 261
Cdd:cd12119 84 LFPEQIAYIINHAEDRVVFVDRD------------FLPLLEAIAP-RLPTVEHvvvmtddaamPEPAGVGVLAY---EEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 262 GAKGNHPEVPPTAE--DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQ--MGdhrIRAGDVMVSFLPLAHMfercce 337
Cdd:cd12119 148 LAAESPEYDWPDFDenTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTdgLG---LSESDVVLPVVPMFHV------ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 338 N--GMYYVGGCVG---FYSG---DIKELTNDLKMLKPTVMPAVPR----LLNRVyDKIQNDISAsglkrglfnmamrake 405
Cdd:cd12119 219 NawGLPYAAAMVGaklVLPGpylDPASLAELIEREGVTFAAGVPTvwqgLLDHL-EANGRDLSS---------------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 406 keiargvlrrngcwdklvfkkvhqafggnLRLMVV-GSAPLAGNVLTFMRcaLGCLVLEGYGQTE-----CTGAITLTVQ 479
Cdd:cd12119 282 -----------------------------LRRVVIgGSAVPRSLIEAFEE--RGVRVIHAWGMTEtsplgTVARPPSEHS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 480 GDHVPNHV------GPPVSCNAVKLVDvPEMEYFAN--QNTGEVCVRGSNVFHGYYKDPEkTAEAIDSEGWHHTGDVGMW 551
Cdd:cd12119 331 NLSEDEQLalrakqGRPVPGVELRIVD-DDGRELPWdgKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATI 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24666501 552 LPNGTLRIIDRRKHIFKlSQGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:cd12119 409 DEDGYLTITDRSKDVIK-SGGEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
167-625 |
9.12e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 99.85 E-value: 9.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 167 NRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED--DGKAAMLLEKAPRSLKIIVAIKPIRQTTL-- 242
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAalAPVATAVRDIVPLLSTVVVAGGSSDDSVLgy 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 243 ERARSRGIQIFSFIDVeklgakgnhPEVPPTAedlctVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRirAGDVM 322
Cdd:PRK07786 156 EDLLAEAGPAHAPVDI---------PNDSPAL-----IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADI--NSDVG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 323 VSFLPLAHmferccengmyyvggcvgfysgdIKELTNDLKML---KPTVMPAVprllnrvydkiqndisasglkrGLFNM 399
Cdd:PRK07786 220 FVGVPLFH-----------------------IAGIGSMLPGLllgAPTVIYPL----------------------GAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 400 A--MRAKEKEIARGVLRRNGCWDKLVfkKVHQAFGGNLRLMVV--GSAPLAGNVLTFMRCAL-GCLVLEGYGQTECTgAI 474
Cdd:PRK07786 255 GqlLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDLALRVLswGAAPASDTLLRQMAATFpEAQILAAFGQTEMS-PV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 475 TLTVQGDHVPNH---VGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMW 551
Cdd:PRK07786 332 TCMLLGEDAIRKlgsVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 552 LPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVVVPDTDV-------LKQWATE 621
Cdd:PRK07786 410 DEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGradEKWGEVPVAVAAVRNDDaaltledLAEFLTD 488
|
....
gi 24666501 622 NNVR 625
Cdd:PRK07786 489 RLAR 492
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
134-610 |
1.27e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.19 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLyDTLGPDACAFI-IRQTDMQVVIVE 212
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPL-DPALPIAEQRVrSQAAGARVVLID 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 213 DDGKAAMLLEKApRSLKIIVAIKPirqttlERARSRGIQIFSFIDVEKLGAKGNHPEvpPTAEDLCTVCYTSGTTGNPKG 292
Cdd:PRK05852 123 ADGPHDRAEPTT-RWWPLTVNVGG------DSGPSGGTLSVHLDAATEPTPATSTPE--GLRPDDAMIMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 293 VMLTHGNVVAGVCSVIlqmGDHRIRAGDVMVSFLPLAHMferccengmyyvggcvgfySGDIKELTNDLKMLKPTVMPAV 372
Cdd:PRK05852 194 VPWTHANIASSVRAII---TGYRLSPRDATVAVMPLYHG-------------------HGLIAALLATLASGGAVLLPAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 373 PRLLNRVYdkiQNDISASGlkrGLFNMAMRAkekeIARGVLRRNgcwDKLVFKKVHQAfggnLRLMVVGSAPLAGNVLTF 452
Cdd:PRK05852 252 GRFSAHTF---WDDIKAVG---ATWYTAVPT----IHQILLERA---ATEPSGRKPAA----LRFIRSCSAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 453 MRCALGCLVLEGYGQTECTGAITLT-VQG---DHVPN-HVGPPVSCNAVKLVDV-PEMEYFANQNTGEVCVRGSNVFHGY 526
Cdd:PRK05852 315 LQTEFAAPVVCAFGMTEATHQVTTTqIEGigqTENPVvSTGLVGRSTGAQIRIVgSDGLPLPAGAVGEVWLRGTTVVRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 527 YKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYV-------YGES 599
Cdd:PRK05852 395 LGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVfgvpdqlYGEA 472
|
490
....*....|.
gi 24666501 600 lkscIIAVVVP 610
Cdd:PRK05852 473 ----VAAVIVP 479
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
276-629 |
1.51e-21 |
|
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: 96.25 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVA---GVCSVI-LQMGDHRIRAgdvmvsfLPLahmferccengmYYVGGCV---- 347
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLAsaaGLHSRLgFGGGDSWLLS-------LPL------------YHVGGLAilvr 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 348 GFYSGDIKELTN-------DLKMLKPTVMPAVPRLLNRVYDkiqNDISASGLKRglfnmamrakekeiargvlrrngcwd 420
Cdd:cd17630 62 SLLAGAELVLLErnqalaeDLAPPGVTHVSLVPTQLQRLLD---SGQGPAALKS-------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 421 klvfkkvhqafggnLRLMVVGSAPLAgNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVD 500
Cdd:cd17630 113 --------------LRAVLLGGAPIP-PELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 501 vpemeyfanqnTGEVCVRGSNVFHGYYKDPEKtaEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKI 580
Cdd:cd17630 178 -----------DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEI 243
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666501 581 ENIYTLSQYVNQVYVYG---ESLKSCIIAVVV----PDTDVLKQWatennVRGTLS 629
Cdd:cd17630 244 EAALAAHPAVRDAFVVGvpdEELGQRPVAVIVgrgpADPAELRAW-----LKDKLA 294
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
276-621 |
3.36e-21 |
|
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: 96.93 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVcSVILQMGDhrIRAGDVMVSFLPLAhmFERCcengMYYVGGCVGfySG--- 352
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHDNLVSFT-NWMLSDFP--LGPGDVFLNQAPFS--FDLS----VMDLYPALA--SGatl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 353 ---------DIKELTNDLKMLKPTVMPAVPRLLNRVydkiqndisasgLKRGLFNmamrakekeiargvlrrngcwdklv 423
Cdd:cd05945 167 vpvprdataDPKQLFRFLAEHGITVWVSTPSFAAMC------------LLSPTFT------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 424 fkkvhQAFGGNLRLMVvgsapLAGNVLT------FMRCALGCLVLEGYGQTECTGAITLTV-------QGDHVPnhVGPP 490
Cdd:cd05945 210 -----PESLPSLRHFL-----FCGEVLPhktaraLQQRFPDARIYNTYGPTEATVAVTYIEvtpevldGYDRLP--IGYA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 491 VSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDR 562
Cdd:cd05945 278 KPGAKLVILDedgrpVPPGE------KGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGR 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666501 563 RKHIFKLsQGEYIVPEKIENIYTLSQYVNQ---VYVYGESLKSCIIAVVVPDTDV----LKQWATE 621
Cdd:cd05945 352 LDFQVKL-NGYRIELEEIEAALRQVPGVKEavvVPKYKGEKVTELIAFVVPKPGAeaglTKAIKAE 416
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
269-597 |
3.50e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 98.18 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 269 EVPPTAE-DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCsvilqMGDHRI----RAGDVMVSFLPLAHMFERCCENGMYYV 343
Cdd:PRK06710 199 EVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTL-----MGVQWLynckEGEEVVLGVLPFFHVYGMTAVMNLSIM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 344 GG--CVGFYSGDIKELTNDLKMLKPTVMPAVPRLLnrvydkiqndisasglkRGLFNMAMrAKEKEIArgvlrrngcwdk 421
Cdd:PRK06710 274 QGykMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIY-----------------IALLNSPL-LKEYDIS------------ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 422 lvfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLT--VQGDHVPNHVGPPVSCNAVKLV 499
Cdd:PRK06710 324 ------------SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTE-SSPVTHSnfLWEKRVPGSIGVPWPDTEAMIM 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 500 DVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAeAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEK 579
Cdd:PRK06710 391 SLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPRE 468
|
330
....*....|....*...
gi 24666501 580 IENIYTLSQYVNQVYVYG 597
Cdd:PRK06710 469 VEEVLYEHEKVQEVVTIG 486
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
134-614 |
4.17e-21 |
|
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: 97.55 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DGKAamLLEKAPRSLKIIVAIKPIRQTTLERARSRGIQIFSFIDVEKLG-AKGNHPEVPPtaeDLCTVCYTSGTTGNPKG 292
Cdd:TIGR03098 106 ERLD--LLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGdADPPHPVIDS---DMAAILYTSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 293 VMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVgfysgdikeltndlkMLKPTVMPav 372
Cdd:TIGR03098 181 VVLSHRNLVAGAQSVATYL---ENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV---------------VLHDYLLP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 373 prllnrvydkiqNDIsasglkrglfnmaMRAKEKEIARGVLRRNGCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTF 452
Cdd:TIGR03098 241 ------------RDV-------------LKALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 453 MRCALG-CLVLEGYGQTECTGAITLTVQG-DHVPNHVGPPVScNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDP 530
Cdd:TIGR03098 296 LRSFLPnARLFLMYGLTEAFRSTYLPPEEvDRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 531 EKTAEAIDSEGWHH-----------TGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYVYG-- 597
Cdd:TIGR03098 375 EKTAERFRPLPPFPgelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVAEAVAFGvp 453
|
490
....*....|....*...
gi 24666501 598 -ESLKSCIIAVVVPDTDV 614
Cdd:TIGR03098 454 dPTLGQAIVLVVTPPGGE 471
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
269-583 |
6.37e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 97.13 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 269 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHmferccengmyyvggCVG 348
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN---LTWQDVFMMPAPLGH---------------ATG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 FYSGDIkeltndLKMLkptvmpavprllnrvydkiqndISASGLKRGLFNmamrakeKEIARGVLRRNGC---------- 418
Cdd:PRK06087 243 FLHGVT------APFL----------------------IGARSVLLDIFT-------PDACLALLEQQRCtcmlgatpfi 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 419 WDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLtfmRCAL--GCLVLEGYGQTECtgaitltvqgdhVPNHVGPPVSCNA- 495
Cdd:PRK06087 288 YDLLNLLEKQPADLSALRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTES------------SPHAVVNLDDPLSr 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 496 -------------VKLVDVPEMEyFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDR 562
Cdd:PRK06087 353 fmhtdgyaaagveIKVVDEARKT-LPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGR 431
|
330 340
....*....|....*....|.
gi 24666501 563 RKHIFkLSQGEYIVPEKIENI 583
Cdd:PRK06087 432 KKDII-VRGGENISSREVEDI 451
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
282-618 |
6.41e-21 |
|
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: 94.64 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 282 YTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGC-VGFYSGDIKELTND 360
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG---LTEADVYLNMLPLFHIAGLNLALATFHAGGAnVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 361 LKMLKPTVMPAVPRLLNRVYDKIQ-NDISASGLKrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnlrlMV 439
Cdd:cd17637 84 IEEEKVTLMGSFPPILSNLLDAAEkSGVDLSSLR--------------------------------------------HV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 440 VG-SAPlaGNVLTFMRCALGCLvLEGYGQTECTGAITLTVQGDHvPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTG 513
Cdd:cd17637 120 LGlDAP--ETIQRFEETTGATF-WSLYGQTETSGLVTLSPYRER-PGSAGRPGPLVRVRIVDdndrpVPAGE------TG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 514 EVCVRGSNVFHGYYKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRR--KHIFKlSQGEYIVPEKIENIYTLSQYVN 591
Cdd:cd17637 190 EIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPAIA 267
|
330 340
....*....|....*....|....*..
gi 24666501 592 QVYVYGeslksciiavvVPDTdvlkQW 618
Cdd:cd17637 268 EVCVIG-----------VPDP----KW 279
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-581 |
1.09e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 96.03 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 137 DEALLRAknfgAGML-ALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVvIVEDDG 215
Cdd:PRK09088 29 DALVGRL----AAVLrRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 216 KAAmllekaprslkiivaikpirqttlerARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLctVCYTSGTTGNPKGVML 295
Cdd:PRK09088 104 VAA--------------------------GRTDVEDLAAFIASADALEPADTPSIPPERVSL--ILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 296 THGNV--VAGVCSVILQMGDHRiragdvmvSFLplahmfercCENGMYYVGGCVgfysgdikelTNdlkmLKPTVM---- 369
Cdd:PRK09088 156 SERNLqqTAHNFGVLGRVDAHS--------SFL---------CDAPMFHIIGLI----------TS----VRPVLAvggs 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 370 --------PAvpRLLNRVYDKiqndisASGLKR--GLFNMAMRakekeiargvLRRNGCWDKlvfkkvhqAFGGNLRLMV 439
Cdd:PRK09088 205 ilvsngfePK--RTLGRLGDP------ALGITHyfCVPQMAQA----------FRAQPGFDA--------AALRHLTALF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 440 VGSAP-LAGNVLTFMrcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVG------PPVScnaVKLVDVPEMEYFANQnT 512
Cdd:PRK09088 259 TGGAPhAAEDILGWL--DDGIPMVDGFGMSEAGTVFGMSVDCDVIRAKAGaagiptPTVQ---TRVVDDQGNDCPAGV-P 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666501 513 GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 581
Cdd:PRK09088 333 GELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
132-597 |
2.40e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.95 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 132 QWINYDEALLRAKNfGAGML-ALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 210
Cdd:PRK06145 26 QEISYAEFHQRILQ-AAGMLhARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 211 VEDDgkaamllekaprsLKIIVAIKPIRQTTLERARSrgiqifsfiDVEKLGAKGNH-PEVPPTAE-DLCTVCYTSGTTG 288
Cdd:PRK06145 105 VDEE-------------FDAIVALETPKIVIDAAAQA---------DSRRLAQGGLEiPPQAAVAPtDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 289 NPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLahmferccengmYYVGGCvgfysgdikeltnDLkmlkptv 368
Cdd:PRK06145 163 RPKGVMHSYGNLHWKSIDHVIALG---LTASERLLVVGPL------------YHVGAF-------------DL------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 369 mPAVPRLLNRVYDKIQNDISASGlkrglfnmAMRAKEKEiargvlRRNGCW---------------DKLVFKKVHQAFGG 433
Cdd:PRK06145 208 -PGIAVLWVGGTLRIHREFDPEA--------VLAAIERH------RLTCAWmapvmlsrvltvpdrDRFDLDSLAWCIGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 434 nlrlmvvGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPN--HVGPPVSCNAVKLVDVPEMEYFANQN 511
Cdd:PRK06145 273 -------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKigSTGRALAHVEIRIADGAGRWLPPNMK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 512 tGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIEN-IYTLSQyV 590
Cdd:PRK06145 346 -GEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPE-V 421
|
....*..
gi 24666501 591 NQVYVYG 597
Cdd:PRK06145 422 AEAAVIG 428
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
132-563 |
3.09e-20 |
|
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: 96.08 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 132 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLyDTLGPDA-CAFIIRQT 204
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMvvallaVLKAGAAY------VPL-DPAYPAErLAYMLEDA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 205 DMQVVIVEDDgkaamllekaprslkiivaikpirqtTLERARSRGIQIFSfIDVEKLGAKGNH-PEVPPTAEDLCTVCYT 283
Cdd:COG1020 573 GARLVLTQSA--------------------------LAARLPELGVPVLA-LDALALAAEPATnPPVPVTPDDLAYVIYT 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 284 SGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVM---------VS----FLPLAHmferccengmyyvGGCVGFY 350
Cdd:COG1020 626 SGSTGRPKGVMVEHRALVNLLAWMQRRYG---LGPGDRVlqfaslsfdASvweiFGALLS-------------GATLVLA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 351 S----GDIKELTNDLKMLKPTVMPAVPrllnrvydkiqndisasglkrGLFNMAMRAkekeiARGVLRRngcwdklvfkk 426
Cdd:COG1020 690 PpearRDPAALAELLARHRVTVLNLTP---------------------SLLRALLDA-----APEALPS----------- 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 427 vhqafggnLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTGAITLTV------QGDHVPnhVGPPVSCNAVKLV 499
Cdd:COG1020 733 --------LRLVLVGGEALPPELVRrWRARLPGARLVNLYGPTETTVDSTYYEvtppdaDGGSVP--IGRPIANTRVYVL 802
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666501 500 DvpemeyfANQN------TGEVCVRGSNVFHGYYKDPEKTAEA-------IDSEGWHHTGDVGMWLPNGTLRIIDRR 563
Cdd:COG1020 803 D-------AHLQpvpvgvPGELYIGGAGLARGYLNRPELTAERfvadpfgFPGARLYRTGDLARWLPDGNLEFLGRA 872
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
142-622 |
3.24e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 94.26 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 142 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAmll 221
Cdd:PRK03640 36 AVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAK--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 222 ekaprslkiIVAIKPIRQTTLERARSRGIQIFSFIDVEklgakgnhpevpptaeDLCTVCYTSGTTGNPKGVMLTHGNVV 301
Cdd:PRK03640 113 ---------LIPGISVKFAELMNGPKEEAEIQEEFDLD----------------EVATIMYTSGTTGKPKGVIQTYGNHW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 302 AGVCSVILQMGdhrIRAGDVMVSFLPLAH------MFErcceNGMYyvGGCVGFYSG-DIKELTNDLKMLKPTVMPAVPR 374
Cdd:PRK03640 168 WSAVGSALNLG---LTEDDCWLAAVPIFHisglsiLMR----SVIY--GMRVVLVEKfDAEKINKLLQTGGVTIISVVST 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 375 LLNRVYDKIQNDisasglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqAFGGNLRLMVVGSAPLAGNVLTfmR 454
Cdd:PRK03640 239 MLQRLLERLGEG-------------------------------------------TYPSSFRCMLLGGGPAPKPLLE--Q 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 455 CAL-GCLVLEGYGQTE-CTGAITLTVQgDHVPNH--VGPPVSCNAVKLVDvpEMEYFANQNTGEVCVRGSNVFHGYYKDP 530
Cdd:PRK03640 274 CKEkGIPVYQSYGMTEtASQIVTLSPE-DALTKLgsAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNRE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 531 EKTAEAIDSeGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLK---SCIIAV 607
Cdd:PRK03640 351 DATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDkwgQVPVAF 428
|
490
....*....|....*....
gi 24666501 608 VVPDTDV----LKQWATEN 622
Cdd:PRK03640 429 VVKSGEVteeeLRHFCEEK 447
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
125-614 |
2.65e-19 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 91.92 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 125 ETLTspYQWINydealLRAKNFGAGMLALGARPKQLIGIYSQNrPEWILYEQGCYSFSLVVVPLYDTLGPdacafiiRQT 204
Cdd:cd05931 23 ETLT--YAELD-----RRARAIAARLQAVGKPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPG-------RHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 205 DMQVVIVEDDGKAAMLLEKAPRSLkiivaikpIRQTTLERARSRGIQIFsFIDVEKLGAKGNHPEVPPTAEDLCTVCYTS 284
Cdd:cd05931 88 ERLAAILADAGPRVVLTTAAALAA--------VRAFAASRPAAGTPRLL-VVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 285 GTTGNPKGVMLTHGNVVAGVCSVILQMGDhriRAGDVMVSFLPLAH-MferccenGMY-------YVGGCVGFYSgdike 356
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGL---DPGDVVVSWLPLYHdM-------GLIgglltplYSGGPSVLMS----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 357 lTND--------LKML---KPTVMPAvPrllNRVYDKIQNDISASGLK-------RGLFNMAMRakekeIARGVLRRngc 418
Cdd:cd05931 224 -PAAflrrplrwLRLIsryRATISAA-P---NFAYDLCVRRVRDEDLEgldlsswRVALNGAEP-----VRPATLRR--- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 419 wdklvFkkvHQAFGG-NLR--------------LMVVGSAPLAG-NVLTFMRCALGCLVLEGYGQTEctGAITLTVqgdh 482
Cdd:cd05931 291 -----F---AEAFAPfGFRpeafrpsyglaeatLFVSGGPPGTGpVVLRVDRDALAGRAVAVAADDP--AARELVS---- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 483 vpnhVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE------AIDSEGWHHTGDVGMwLPNGT 556
Cdd:cd05931 357 ----CGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGF-LHDGE 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666501 557 LRIIDRRKHIFKLSqGEYIVPEKIEniYTLSQyvnqvyVYGESLKSCIIAVVVPDTDV 614
Cdd:cd05931 432 LYITGRLKDLIIVR-GRNHYPQDIE--ATAEE------AHPALRPGCVAAFSVPDDGE 480
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
134-618 |
3.20e-19 |
|
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: 91.66 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 D--GKAAMLLEKAPRSLKIIVAIKPIRQTTLERARSRGIQIFSfidvEKLGAKGNHPEvpptaeDLCTVCYTSGTTGNPK 291
Cdd:cd05959 110 ElaPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEA----EQLKPAATHAD------DPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 292 GVMLTHGNVVAgVCSV----ILqmgdhRIRAGDVMVSFLPLahMFERCCENGMYY---VGGCVGFYSGDIKELT--NDLK 362
Cdd:cd05959 180 GVVHLHADIYW-TAELyarnVL-----GIREDDVCFSAAKL--FFAYGLGNSLTFplsVGATTVLMPERPTPAAvfKRIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 363 MLKPTVMPAVPRLLNrvydkiqndisasglkrglfnmAMRAKEKEIARGVLRrngcwdklvfkkvhqafggnLRLMVVGS 442
Cdd:cd05959 252 RYRPTVFFGVPTLYA----------------------AMLAAPNLPSRDLSS--------------------LRLCVSAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 443 APLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLT-VQGDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSN 521
Cdd:cd05959 290 EALPAEVGERWKARFGLDILDGIGSTE-MLHIFLSnRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 522 VFHGYYKDPEKTAEAIDSEgWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENiyTLSQY--VNQVYVYGES 599
Cdd:cd05959 368 SATMYWNNRDKTRDTFQGE-WTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVES--ALVQHpaVLEAAVVGVE 443
|
490 500 510
....*....|....*....|....*....|.
gi 24666501 600 LKSCII---AVVVP---------DTDVLKQW 618
Cdd:cd05959 444 DEDGLTkpkAFVVLrpgyedseaLEEELKEF 474
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
268-583 |
4.47e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.44 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGV-CSVILQMGDHRIRAGD-VMVSFLPLAHMFerccenGM-YYVG 344
Cdd:PLN02574 191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVeLFVRFEASQYEYPGSDnVYLAALPMFHIY------GLsLFVV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 345 GCVGFYSG-------DIKELTNDLKMLKPTVMPAVPRLLnrvydkiqndisasglkrglfnMAMRAKEKEIARGVLrrng 417
Cdd:PLN02574 265 GLLSLGSTivvmrrfDASDMVKVIDRFKVTHFPVVPPIL----------------------MALTKKAKGVCGEVL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 418 cwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNH--VGPPVSCN 494
Cdd:PLN02574 319 ---------------KSLKQVSCGAAPLSGKFIQdFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNM 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 495 AVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEY 574
Cdd:PLN02574 384 QAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQ 462
|
....*....
gi 24666501 575 IVPEKIENI 583
Cdd:PLN02574 463 IAPADLEAV 471
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
135-617 |
9.12e-19 |
|
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: 89.32 E-value: 9.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 135 NYDEaLLRAKNFGAGMLA-LGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPdacafiirqtdmqvvived 213
Cdd:cd05972 2 SFRE-LKRESAKAANVLAkLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGP------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 dgkaamllekaprslkiivaiKPIRQTtLERARSRGIQIfsfidveklgakgnhpevppTAEDLCTVCYTSGTTGNPKGV 293
Cdd:cd05972 62 ---------------------KDIEYR-LEAAGAKAIVT--------------------DAEDPALIYFTSGTTGLPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 294 MLTHGNVVAgvcsVILQMGD-HRIRAGDVMVS--------------FLPLAHmferccengmyyvGGCVGFYSG---DIK 355
Cdd:cd05972 100 LHTHSYPLG----HIPTAAYwLGLRPDDIHWNiadpgwakgawssfFGPWLL-------------GATVFVYEGprfDAE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 356 ELTNDLKMLKPTVM---PAVPRLLnrvydkIQNDISAsglkrglfnmamrakekeiargvlrrngcwdklvFKKVHqafg 432
Cdd:cd05972 163 RILELLERYGVTSFcgpPTAYRML------IKQDLSS----------------------------------YKFSH---- 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 433 gnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVD-----VPEMEyf 507
Cdd:cd05972 199 --LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDddgreLPPGE-- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 508 anqnTGEVCVRGSNV--FHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENiyT 585
Cdd:cd05972 275 ----EGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVES--A 346
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24666501 586 LSQY--VNQVYV-------YGESLKsciiAVVV-----PDTDVLKQ 617
Cdd:cd05972 347 LLEHpaVAEAAVvgspdpvRGEVVK----AFVVltsgyEPSEELAE 388
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
134-606 |
9.94e-19 |
|
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: 89.88 E-value: 9.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DGKAAmllekaprslkiivaikpirqttlERARSRGIQIFSFIDVEKLGAKGNH----PEVPPTAEDLCTVCYTSGTTGN 289
Cdd:cd05923 109 DAQVM------------------------DAIFQSGVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYTSGTTGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTHGNVVAGVCSVILQMGdHRIRAGDVMVSFLPLAH-------MFERCCENGMYYVggCVGFYSGDIKELTNDLK 362
Cdd:cd05923 165 PKGAVIPQRAAESRVLFMSTQAG-LRHGRHNVVLGLMPLYHvigffavLVAALALDGTYVV--VEEFDPADALKLIEQER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 363 MlkpTVMPAVPRLlnrvYDKIQNDISASGLKrglfnmaMRAKEKEIARGVLRRNGcwdklVFKKVHQAFGGnlrlmvvgs 442
Cdd:cd05923 242 V---TSLFATPTH----LDALAAAAEFAGLK-------LSSLRHVTFAGATMPDA-----VLERVNQHLPG--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 443 aplagnvltfmrcalgcLVLEGYGQTEctgAITLTVQGDHVPNHVGPPVSCNAVKLVDVPE--MEYFANQNTGEVCVR-- 518
Cdd:cd05923 294 -----------------EKVNIYGTTE---AMNSLYMRDARTGTEMRPGFFSEVRIVRIGGspDEALANGEEGELIVAaa 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 519 GSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV--- 595
Cdd:cd05923 354 ADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVigv 431
|
490
....*....|....*
gi 24666501 596 ----YGESLKSCIIA 606
Cdd:cd05923 432 aderWGQSVTACVVP 446
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
119-614 |
1.26e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 89.74 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 119 PCLGWRETLTSpyqWinyDEALLRAKNFGAGMLAL--GARPKQlIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDA 196
Cdd:PRK07867 20 RGLYFEDSFTS---W---REHIRGSAARAAALRARldPTRPPH-VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 197 CAFIIRQTDMQVVIVEDdgKAAMLLEKAPRSLKIIVAIKPirQTTLERARSRGIQIfsfidveklgakgnhPEVPPTAED 276
Cdd:PRK07867 93 LARDIAHADCQLVLTES--AHAELLDGLDPGVRVINVDSP--AWADELAAHRDAEP---------------PFRVADPDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 277 LCTVCYTSGTTGNPKGVMLTHGNVV-AGVcsvilQMGDHR-IRAGDVMVSFLPLAHmferccENGMYyVGGCVGFYSGdi 354
Cdd:PRK07867 154 LFMLIFTSGTSGDPKAVRCTHRKVAsAGV-----MLAQRFgLGPDDVCYVSMPLFH------SNAVM-AGWAVALAAG-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 355 keltndlkmlkptvmpavprllnrvydkiqndisASglkrglfnMAMRAKEKeiARGVL---RRNGC-WDKLVFKKVHQA 430
Cdd:PRK07867 220 ----------------------------------AS--------IALRRKFS--ASGFLpdvRRYGAtYANYVGKPLSYV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 431 FG---------GNLRlMVVGSAPLAGNVLTFMRcALGCLVLEGYGQTEctGAITLTVQGDHVPNHVGPPVScnAVKLVDV 501
Cdd:PRK07867 256 LAtperpddadNPLR-IVYGNEGAPGDIARFAR-RFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPP--GVAIVDP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 502 ------PEMEY------FANQNTGE-VCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTL----RIIDRRK 564
Cdd:PRK07867 330 dtgtecPPAEDadgrllNADEAIGElVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAyfagRLGDWMR 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24666501 565 hifklSQGEYIVPEKIENIytLSQY--VNQVYVYGeslksciiavvVPDTDV 614
Cdd:PRK07867 409 -----VDGENLGTAPIERI--LLRYpdATEVAVYA-----------VPDPVV 442
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
276-610 |
4.53e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 88.15 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVIL--QMGdhrirAGDVMVSFLPLAHMFERCCENGMYYVGG---CVGFY 350
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIgwEMG-----TCPVYLWTLPMFHCNGWTFTWGTAARGGtsvCMRHV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 351 SGdiKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISasglkrglfnmamrakekeiargvlrrngcwdklvfkkvHQA 430
Cdd:PLN03102 262 TA--PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS---------------------------------------PRS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 431 fgGNLRLMVVGSAPLAGNVLTFMRcaLGCLVLEGYGQTECTGAITLTVQGDH---VPNH------VGPPVSCNAVKLVDV 501
Cdd:PLN03102 301 --GPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFCEWQDEwnrLPENqqmelkARQGVSILGLADVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 502 PEMEYFAN-----QNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIV 576
Cdd:PLN03102 377 KNKETQESvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENIS 454
|
330 340 350
....*....|....*....|....*....|....
gi 24666501 577 PEKIENIytlsqyvnqVYVYGESLKSCIIAVVVP 610
Cdd:PLN03102 455 SVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
273-563 |
1.39e-17 |
|
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: 86.06 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 273 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMG-DHRIR-------AGDVMV--SFLPLAHmferccengmyy 342
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGlTSESRvlqfasyTFDVSIleIFTTLAA------------ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 343 vGGCVGFYS-----GDIKELTNDLK----MLKPTVMpavpRLLNRvydkiqndisasglkrglfnmamrakekeiargvl 413
Cdd:cd05918 172 -GGCLCIPSeedrlNDLAGFINRLRvtwaFLTPSVA----RLLDP----------------------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 414 rrngcwdKLVFkkvhqafggNLRLMVVGSAPLAGNVLTfmRCALGCLVLEGYGQTECTGAITLTVQGDHV-PNHVGPPVS 492
Cdd:cd05918 212 -------EDVP---------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVPSTdPRNIGRPLG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 493 CNAVkLVDvPEmeyfaNQN-------TGEVCVRGSNVFHGYYKDPEKTAEA-IDSEGWHH------------TGDVGMWL 552
Cdd:cd05918 274 ATCW-VVD-PD-----NHDrlvpigaVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYN 346
|
330
....*....|.
gi 24666501 553 PNGTLRIIDRR 563
Cdd:cd05918 347 PDGSLEYVGRK 357
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
192-624 |
2.59e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 85.67 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 192 LGPDACAFIIRQTDMQVVIVED------DGKAAMLLEKAPRSLK----IIVAIKPIRQTTLERARSRGIqifsfIDVEKL 261
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQefftlaEEALKILAEKKKSSFKppllIVIGDPTCDPKSLQYALGKGA-----IEYEKF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 262 GAKGNhPEV---PPTAE-DLCTVCYTSGTTGNPKGVMLTH--GNVVAGVCSVILQMGDhriraGDVMVSFLPLAHmferc 335
Cdd:PLN02479 179 LETGD-PEFawkPPADEwQSIALGYTSGTTASPKGVVLHHrgAYLMALSNALIWGMNE-----GAVYLWTLPMFH----- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 336 CeNGMYYVGGCVGFYSGDI-------KELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrglfnMAMRAKEKEI 408
Cdd:PLN02479 248 C-NGWCFTWTLAALCGTNIclrqvtaKAIYSAIANYGVTHFCAAPVVLN---------------------TIVNAPKSET 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 409 ARGVLRrngcwdklvfkKVHqafggnlrLMVVGSAPLAgNVLTFMRcALGCLVLEGYGQTECTGAITLTV---QGDHVPN 485
Cdd:PLN02479 306 ILPLPR-----------VVH--------VMTAGAAPPP-SVLFAMS-EKGFRVTHTYGLSETYGPSTVCAwkpEWDSLPP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 486 HVGPPVSC---------NAVKLVDVPEMEYFANQNT--GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPN 554
Cdd:PLN02479 365 EEQARLNArqgvryiglEGLDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPD 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666501 555 GTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV-------YGESlkSCIIAVVVPDTDVLKQWATENNV 624
Cdd:PLN02479 444 GYIEIKDRSKDII-ISGGENISSLEVENVVYTHPAVLEASVvarpderWGES--PCAFVTLKPGVDKSDEAALAEDI 517
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
102-564 |
2.69e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 85.78 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 102 RTLYQTFREGAYASNNGPCL-------GWRETLTspyqwINYDEaLLRAKNFGAGML-ALGARPKQLIGIYSQNRPEWIl 173
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALsflldadPLDRPET-----WTYAE-LLADVTRTANLLhSLGVGPGDVVAFLLPNLPETH- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 174 yeqgcysFSL-------VVVPLYDTLGPDACAFIIRQTDMQVVIV--EDDG-----KAAMLLEKAPrSLKIIVAIKPIRQ 239
Cdd:PRK07529 98 -------FALwggeaagIANPINPLLEPEQIAELLRAAGAKVLVTlgPFPGtdiwqKVAEVLAALP-ELRTVVEVDLARY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 240 TTLER-------ARSRGIQIFSFiDVEKLGAKGNHPEV--PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQ 310
Cdd:PRK07529 170 LPGPKrlavpliRRKAHARILDF-DAELARQPGDRLFSgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 311 MGdhrIRAGDVMVSFLPLAHMFErCCENGMYYV--GGCVGF-----YSGD--IKELTNDLKMLKPTVMPAVPR----LLN 377
Cdd:PRK07529 249 LG---LGPGDTVFCGLPLFHVNA-LLVTGLAPLarGAHVVLatpqgYRGPgvIANFWKIVERYRINFLSGVPTvyaaLLQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 378 RVYDKiqNDISAsglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnLRLMVVGSAPLAGNVL-TFMRcA 456
Cdd:PRK07529 325 VPVDG--HDISS---------------------------------------------LRYALCGAAPLPVEVFrRFEA-A 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 457 LGCLVLEGYGQTECTGAITLT-VQGDHVPNHVGPPVSCNAVKLVDV-PEMEYF---ANQNTGEVCVRGSNVFHGYYkDPE 531
Cdd:PRK07529 357 TGVRIVEGYGLTEATCVSSVNpPDGERRIGSVGLRLPYQRVRVVILdDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAA 435
|
490 500 510
....*....|....*....|....*....|...
gi 24666501 532 KTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRK 564
Cdd:PRK07529 436 HNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
132-614 |
2.80e-17 |
|
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: 85.04 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 132 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIV 211
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 212 EDDgkaamLLEKAPRSLKIIVaikpirqttlerarsrgiqifsfIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPK 291
Cdd:cd12116 91 DDA-----LPDRLPAGLPVLL-----------------------LALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 292 GVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVS-------------FLPLAHmferccengmyyvGGCVGFYSGDIKELT 358
Cdd:cd12116 143 GVVVSHRNLVNFLHSMRERLG---LGPGDRLLAvttyafdisllelLLPLLA-------------GARVVIAPRETQRDP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 359 NDLKML----KPTVMPAVPRLLnrvydkiqndisasglkRGLFNMAMRAKEkeiargvlrrngcwdklvfkkvhqafggN 434
Cdd:cd12116 207 EALARLieahSITVMQATPATW-----------------RMLLDAGWQGRA----------------------------G 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 435 LRLMVVGSA---PLAGNVltfmrCALGCLVLEGYGQTECT--GAITLtVQGDHVPNHVGPPVSCNAVKLVD-----VPEM 504
Cdd:cd12116 242 LTALCGGEAlppDLAARL-----LSRVGSLWNLYGPTETTiwSTAAR-VTAAAGPIPIGRPLANTQVYVLDaalrpVPPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 505 EyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAI-------DSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVP 577
Cdd:cd12116 316 V------PGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIEL 388
|
490 500 510
....*....|....*....|....*....|....*....
gi 24666501 578 EKIENIYTLSQYVNQ--VYVYGESLKSCIIAVVVPDTDV 614
Cdd:cd12116 389 GEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGA 427
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
259-564 |
2.94e-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: 85.41 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 259 EKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILqmgDHRIRAGDVMVSFLPLAHmferccen 338
Cdd:cd05906 151 ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ---HNGLTPQDVFLNWVPLDH-------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 339 gmyyVGGCVGFYSGDIkeltnDLKMLK---PTV-MPAVPRLLNRVYDKIQNDISASGlkrglfNMA---MRAKEKEIARG 411
Cdd:cd05906 220 ----VGGLVELHLRAV-----YLGCQQvhvPTEeILADPLRWLDLIDRYRVTITWAP------NFAfalLNDLLEEIEDG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 412 vlrrngCWDKlvfkkvhqafgGNLRLMVVGSAPL---AGNVLTFM--RCALGCLVLE-GYGQTE-CTGAI------TLTV 478
Cdd:cd05906 285 ------TWDL-----------SSLRYLVNAGEAVvakTIRRLLRLlePYGLPPDAIRpAFGMTEtCSGVIysrsfpTYDH 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 479 QGDHVPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGmWLP 553
Cdd:cd05906 348 SQALEFVSLGRPIPGVSMRIVDdegqlLPEGE------VGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLD 420
|
330
....*....|.
gi 24666501 554 NGTLRIIDRRK 564
Cdd:cd05906 421 NGNLTITGRTK 431
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
269-621 |
3.02e-17 |
|
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: 85.07 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 269 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV--------AGVCSVILQMGDHRIRAGDVMVS--FLPLAhmfercCEN 338
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVnlvewankVIYQGEHLRVALFASISFDASVTeiFASLL------SGN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 339 GMYYVGgcvgfysgdikeltndlkmlKPTVMPAVPrlLNRVYDkiQNDISASGLKRGLFNMAMRAKEKEiargvlrrngc 418
Cdd:cd17655 205 TLYIVR--------------------KETVLDGQA--LTQYIR--QNRITIIDLTPAHLKLLDAADDSE----------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 419 wdklvfkkvhqafGGNLRLMVVG----SAPLAGNVLTFMRcaLGCLVLEGYGQTECTGAITL------TVQGDHVPnhVG 488
Cdd:cd17655 250 -------------GLSLKHLIVGgealSTELAKKIIELFG--TNPTITNAYGPTETTVDASIyqyepeTDQQVSVP--IG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 489 PPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEA------IDSEGWHHTGDVGMWLPNGTL 557
Cdd:cd17655 313 KPLGNTRIYILDqygrpQPVGV------AGELYIGGEGVARGYLNRPELTAEKfvddpfVPGERMYRTGDLARWLPDGNI 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666501 558 RIIDRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVY---GESLKSCIIAVVVPDTDV----LKQWATE 621
Cdd:cd17655 387 EFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEAVVIarkDEQGQNYLCAYIVSEKELpvaqLREFLAR 456
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
192-575 |
3.70e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 85.38 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 192 LGPDACAFIIRQTDMQVVIVE----DDGKAAMLLEKAPRSLKIIVAIKPirqttlerarSRGIQIFSFIDVEKLGAKGNh 267
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDtefaEVAREALALLPGPKPLVIDVDDPE----------YPGGRFIGALDYEAFLASGD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PE---VPPTAE-DLCTVCYTSGTTGNPKGVMLTH--------GNVVAGvcsvilQMGDHriragDVMVSFLPLAHmferc 335
Cdd:PRK08162 171 PDfawTLPADEwDAIALNYTSGTTGNPKGVVYHHrgaylnalSNILAW------GMPKH-----PVYLWTLPMFH----- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 336 CeNG------MYYVGG---CV-GFYSGDIKELTNDLKMlkpTVMPAVPRLLNrvydkiqndisasglkrGLFNMAMRAKE 405
Cdd:PRK08162 235 C-NGwcfpwtVAARAGtnvCLrKVDPKLIFDLIREHGV---THYCGAPIVLS-----------------ALINAPAEWRA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 406 KeIARGVlrrngcwdklvfkkvhqafggnlRLMVVGSAPLAGnVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDH--- 482
Cdd:PRK08162 294 G-IDHPV-----------------------HAMVAGAAPPAA-VIAKME-EIGFDLTHVYGLTETYGPATVCAWQPEwda 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 483 --------------VPNHVgppvsCNAVKLVDVPEMEYFAN--QNTGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTG 546
Cdd:PRK08162 348 lplderaqlkarqgVRYPL-----QEGVTVLDPDTMQPVPAdgETIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTG 421
|
410 420
....*....|....*....|....*....
gi 24666501 547 DVGMWLPNGTLRIIDRRKHIFkLSQGEYI 575
Cdd:PRK08162 422 DLAVLHPDGYIKIKDRSKDII-ISGGENI 449
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
247-689 |
5.32e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.85 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 247 SRGIQIFSFIDVE---KLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMV 323
Cdd:PLN02860 141 SVFIFLNSFLTTEmlkQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVG---YGEDDVYL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 324 SFLPLAHMFERCCENGMYYVGGC-VGFYSGDIKELTNDLKMLKPTVMPAVPRLLNrvydkiqnDISASGlkrglfNMAMR 402
Cdd:PLN02860 218 HTAPLCHIGGLSSALAMLMVGAChVLLPKFDAKAALQAIKQHNVTSMITVPAMMA--------DLISLT------RKSMT 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 403 AKEKEIARGVLRRNGCWDKLVFKKVHQAFGgNLRLMVVGSAPLAGNVLTFMRCalgclvlegYGQTECTGAITLTVQGDH 482
Cdd:PLN02860 284 WKVFPSVRKILNGGGSLSSRLLPDAKKLFP-NAKLFSAYGMTEACSSLTFMTL---------HDPTLESPKQTLQTVNQT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 483 VPNHVGPPVSCNAVKlvDVPEMEYFANQN----TGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLR 558
Cdd:PLN02860 354 KSSSVHQPQGVCVGK--PAPHVELKIGLDessrVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 559 IIDRRKHIFKlSQGEYIVPEKIENIytLSQY--VNQVYVYG---ESLKSCIIAVVvpdtdVLKQ-WATENNvrgtlsVLC 632
Cdd:PLN02860 432 LIGRSNDRIK-TGGENVYPEEVEAV--LSQHpgVASVVVVGvpdSRLTEMVVACV-----RLRDgWIWSDN------EKE 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 24666501 633 NNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSvqnglLTPTFKAKRPQLK 689
Cdd:PLN02860 498 NAKKNLTLSSETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
464-610 |
8.07e-17 |
|
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: 82.35 E-value: 8.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 464 GYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAID 538
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDedgreVPDGE------VGEIVARGPTVMAGYWNRPEVNARRTR 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 539 SeGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENiyTLSQY--VNQVYV-------YGESLKsciiAVVV 609
Cdd:cd17636 216 G-GWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVER--CLRQHpaVADAAVigvpdprWAQSVK----AIVV 287
|
.
gi 24666501 610 P 610
Cdd:cd17636 288 L 288
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
132-596 |
1.32e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 83.65 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 132 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPL-YDTLGPDaCAFIIRQTDMQVVI 210
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPInTALRGPQ-LEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 211 VEDDGKAAM-LLEKAPRSLKIIVAIKPIRQTTLERArsrgiqiFSFIDVEKLGAKGnhPEVPPTAEDLCTVCYTSGTTGN 289
Cdd:PRK06155 124 VEAALLAALeAADPGDLPLPAVWLLDAPASVSVPAG-------WSTAPLPPLDAPA--PAAAVQPGDTAAILYTSGTTGP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTHGNV-VAGVCSViLQMGdhrIRAGDVMVSFLPLAH-----MFERCCENGMYYV-----------------GGC 346
Cdd:PRK06155 195 SKGVCCPHAQFyWWGRNSA-EDLE---IGADDVLYTTLPLFHtnalnAFFQALLAGATYVleprfsasgfwpavrrhGAT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 347 VGFYSGDIkeltndlkmlkptvmpaVPRLLNRvyDKIQNDiSASGLKRGLfnmamrakekeiARGVLRRngcwdklvfkk 426
Cdd:PRK06155 271 VTYLLGAM-----------------VSILLSQ--PARESD-RAHRVRVAL------------GPGVPAA----------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 427 VHQAFggnlrlmvvgsaplagnvltFMRCalGCLVLEGYGQTEcTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEY 506
Cdd:PRK06155 308 LHAAF--------------------RERF--GVDLLDGYGSTE-TNFVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 507 FANQnTGEVCVRGSNVF---HGYYKDPEKTAEAIDSEgWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENI 583
Cdd:PRK06155 365 PDGE-PGELLLRADEPFafaTGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV 441
|
490
....*....|...
gi 24666501 584 YTLSQYVNQVYVY 596
Cdd:PRK06155 442 LLSHPAVAAAAVF 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
134-581 |
1.73e-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: 82.51 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaeDLCTVCYTSGTTGNPKGV 293
Cdd:cd05919 91 D-------------------------------------------------------------DIAYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 294 MLTHGNVVAGV---CSVILqmgdhRIRAGDVMVSflpLAHM-FERCCENGMY---YVGGCVGFYSG--DIKELTNDLKML 364
Cdd:cd05919 110 MHAHRDPLLFAdamAREAL-----GLTPGDRVFS---SAKMfFGYGLGNSLWfplAVGASAVLNPGwpTAERVLATLARF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 365 KPTVMPAVPRLLNRVYDkiQNDISASglkrglfnmAMRAkekeiargvlrrngcwdklvfkkvhqafggnLRLMVVGSAP 444
Cdd:cd05919 182 RPTVLYGVPTFYANLLD--SCAGSPD---------ALRS-------------------------------LRLCVSAGEA 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 445 LAGNVLTFMRCALGCLVLEGYGQTEcTGAITLTVQ-GDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVF 523
Cdd:cd05919 220 LPRGLGERWMEHFGGPILDGIGATE-VGHIFLSNRpGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAA 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666501 524 HGYYKDPEKTaEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 581
Cdd:cd05919 298 VGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVE 353
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
134-581 |
2.59e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.48 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DGK----AAMLLEKAP---RSLKIIVAIKPIRQTTLERARSRGIQIFSFIDVEKLGAKGnhpeVPPTAEDLCTVCYT-SG 285
Cdd:PRK06164 116 GFKgidfAAILAAVPPdalPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAG----ERAADPDAGALLFTtSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 286 TTGNPKGVM------LTHGNVVAGVCSVilqmgdhriRAGDVMVSFLPLAHMFerccenGMyyvGGCVGFYSGDIkeltn 359
Cdd:PRK06164 192 TTSGPKLVLhrqatlLRHARAIARAYGY---------DPGAVLLAALPFCGVF------GF---STLLGALAGGA----- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 360 dlkmlkPTVMPAV---PRLLNRVYD-KIQNDISASGLKRGLFNMAMRAKekeiARGVLRRNGcwdklvFKKVHQAFGGNL 435
Cdd:PRK06164 249 ------PLVCEPVfdaARTARALRRhRVTHTFGNDEMLRRILDTAGERA----DFPSARLFG------FASFAPALGELA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 436 RLMVVGSAPLAGNvltfmrcalgclvlegYGQTE-----CTGAITLTVQGDHVPNhvGPPVSCNA-VKLVDVPEMEYFAN 509
Cdd:PRK06164 313 ALARARGVPLTGL----------------YGSSEvqalvALQPATDPVSVRIEGG--GRPASPEArVRARDPQDGALLPD 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666501 510 QNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 581
Cdd:PRK06164 375 GESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIE 445
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-582 |
1.10e-15 |
|
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: 80.17 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 136 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVedDG 215
Cdd:cd05971 9 FKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--DG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 216 kaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptAEDLCTVCYTSGTTGNPKGVMl 295
Cdd:cd05971 87 ----------------------------------------------------------SDDPALIIYTSGTTGPPKGAL- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 296 tHGnvvagvcsvilqmgdHRIRAGDVMVSFLPLaHMFERCcENGMY------YVGGCVGfysgdikeltndlkMLKPTVM 369
Cdd:cd05971 108 -HA---------------HRVLLGHLPGVQFPF-NLFPRD-GDLYWtpadwaWIGGLLD--------------VLLPSLY 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 370 PAVPRLLNRV--YDK-------IQNDISASGLKRGLFNMaMRAKEKEIARgvlrrngcwdklvfkkvhqaFGGNLRLMVV 440
Cdd:cd05971 156 FGVPVLAHRMtkFDPkaaldlmSRYGVTTAFLPPTALKM-MRQQGEQLKH--------------------AQVKLRAIAT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 441 GSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAIT-LTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQnTGEVCVR- 518
Cdd:cd05971 215 GGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGnCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGE-VGEIAVEl 293
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666501 519 -GSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN 582
Cdd:cd05971 294 pDPVAFLGYWNNPSATEKKMAG-DWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEE 356
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
148-611 |
1.26e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 80.47 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 148 AGMLALGARPKQLIGIYSQNRPEwiLYEQGCYSFSL--VVVPLYDTLGPDACAFIIRQTDMQVVIVEDD--GKAAMLLEK 223
Cdd:PRK07470 47 AALAARGVRKGDRILVHSRNCNQ--MFESMFAAFRLgaVWVPTNFRQTPDEVAYLAEASGARAMICHADfpEHAAAVRAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 224 APrSLKIIVAIKPIRQTTlerarsrgiqifsfiDVEKLGAKGNHPEVPPTA---EDLCTVCYTSGTTGNPKGVMLTHGN- 299
Cdd:PRK07470 125 SP-DLTHVVAIGGARAGL---------------DYEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGQm 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 300 --VVAG-VCSVILQMGDHriragDVMVSFLPLAHmferccengmyyvggcvgfySGDIKELTNDLKMLKpTVMPAVPRL- 375
Cdd:PRK07470 189 afVITNhLADLMPGTTEQ-----DASLVVAPLSH--------------------GAGIHQLCQVARGAA-TVLLPSERFd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 376 LNRVYDKIQndisasglKRGLFNM-------AMRAKEKEIARgvlrrngcWDklvfkkvHqafgGNLRLMVVGSAPLAGN 448
Cdd:PRK07470 243 PAEVWALVE--------RHRVTNLftvptilKMLVEHPAVDR--------YD-------H----SSLRYVIYAGAPMYRA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 449 VLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHvGPPV---SCN------AVKLVDVPEMEYFANQnTGEVCVRG 519
Cdd:PRK07470 296 DQKRALAKLGKVLVQYFGLGEVTGNITVLPPALHDAED-GPDArigTCGfertgmEVQIQDDEGRELPPGE-TGEICVIG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 520 SNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYGes 599
Cdd:PRK07470 374 PAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-- 449
|
490
....*....|..
gi 24666501 600 lksciiavvVPD 611
Cdd:PRK07470 450 ---------VPD 452
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
275-626 |
2.93e-15 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 77.69 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVVAgvCSVILQMGDHRIRAGDVMVSFLPLAHMFE----RCCengMYYVGGCVGFy 350
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFA--VPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiLTC---LIHGGLCVTG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 351 sGDIKELTNDLKML---KPTVMPAVPRLLNRVYDKIQNDISASglkrglfnmamrakekeiargvlrrngcwdklvfkkv 427
Cdd:cd17635 75 -GENTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATV------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 428 hqafgGNLRLMVVGSA-PLAGNVLTFMRCALgCLVLEGYGQTECTGAITLTVQGDHVP-NHVGPPVSCNAVKLVDVPEME 505
Cdd:cd17635 117 -----PSLRLIGYGGSrAIAADVRFIEATGL-TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 506 YFANQNtGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYT 585
Cdd:cd17635 191 GPSASF-GTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAE 267
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24666501 586 LSQYVNQVYVYgeSLKSCIIAVVVPDTDVLKQWATENNVRG 626
Cdd:cd17635 268 GVSGVQECACY--EISDEEFGELVGLAVVASAELDENAIRA 306
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
217-582 |
1.09e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 77.25 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 217 AAMLLEKAPRSLKIIVAIKP---IRQTTLERARSRGiqifsfidveklgAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGV 293
Cdd:PRK09274 126 ARRLFGWGKPSVRRLVTVGGrllWGGTTLATLLRDG-------------AAAPFPMADLAPDDMAAILFTSGSTGTPKGV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 294 MLTHGNVVAgvcsVILQMGDHR-IRAGDVMVSFLPLAHMFERCCenGMYYVggcvgfysgdIKELtnDLKmlKP-TVMPA 371
Cdd:PRK09274 193 VYTHGMFEA----QIEALREDYgIEPGEIDLPTFPLFALFGPAL--GMTSV----------IPDM--DPT--RPaTVDPA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 372 vprllnRVYDKIQndisasglKRGLFNMA-----MRakekeiargVLRRNGCWDKLVFkkvhqafgGNLRLMVVGSAPLA 446
Cdd:PRK09274 253 ------KLFAAIE--------RYGVTNLFgspalLE---------RLGRYGEANGIKL--------PSLRRVISAGAPVP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 447 GNVLTFMRCAL--GCLVLEGYGQTEC------TGAITLTVQGDHVPNH----VGPPVSCNAVKLVDV---P-----EMEY 506
Cdd:PRK09274 302 IAVIERFRAMLppDAEILTPYGATEAlpissiESREILFATRAATDNGagicVGRPVDGVEVRIIAIsdaPipewdDALR 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 507 FANQNTGEVCVRGSNVFHGYYKDPEKTAEA--IDSEG--WHHTGDVGmWL-PNGTLRIIDRRKHIFKLSQGEY--IVPEK 579
Cdd:PRK09274 382 LATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCER 460
|
...
gi 24666501 580 IEN 582
Cdd:PRK09274 461 IFN 463
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
268-595 |
1.99e-14 |
|
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: 76.16 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQM-GDHRIRAGDVM---------VS----FLPLAhmfe 333
Cdd:cd17646 131 PLVPPRPDNLAYVIYTSGSTGRPKGVMVTH----AGIVNRLLWMqDEYPLGPGDRVlqktplsfdVSvwelFWPLV---- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 334 rccengmyyVGGCVGFYS----GDIKELTNDLKMLKPTVMPAVPRLLnrvydkiqndisasglkrglfnmamrakekEIA 409
Cdd:cd17646 203 ---------AGARLVVARpgghRDPAYLAALIREHGVTTCHFVPSML------------------------------RVF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 410 RGVLRRNGCwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITL-TVQGDHVPNHV- 487
Cdd:cd17646 244 LAEPAAGSC--------------ASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVp 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 488 -GPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLRII 560
Cdd:cd17646 310 iGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpfgPGSRMYRTGDLARWRPDGALEFL 388
|
330 340 350
....*....|....*....|....*....|....*
gi 24666501 561 DRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYV 595
Cdd:cd17646 389 GRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVV 422
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-581 |
3.02e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVPPtaEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvcSVILQMGdHRIRAG--DVMVSFLPLAHmferccenGMYYVGG 345
Cdd:PRK05691 161 PALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVAN--EQLIRHG-FGIDLNpdDVIVSWLPLYH--------DMGLIGG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 346 CV-GFYSGdikeltndlkmlKPTVMPAVPRLLNRVYDKIQNDISASGLKRGLFNMAMRAKEKEIARGVLRRngcwdkLVF 424
Cdd:PRK05691 228 LLqPIFSG------------VPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALER------LDL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 425 KKVHQAFGG-------NLRLMVVGSAPLAGNVLTFMRCalgclvlegYGQTECTGAITLTVQGDHVP-----------NH 486
Cdd:PRK05691 290 SRWRVAYSGsepirqdSLERFAEKFAACGFDPDSFFAS---------YGLAEATLFVSGGRRGQGIPaleldaealarNR 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 487 V----GPPV-SC------NAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI---DSEGWHHTGDVGmWL 552
Cdd:PRK05691 361 AepgtGSVLmSCgrsqpgHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLG-FL 439
|
330 340
....*....|....*....|....*....
gi 24666501 553 PNGTLRIIDRRKHIFkLSQGEYIVPEKIE 581
Cdd:PRK05691 440 RDGELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
246-581 |
3.38e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.80 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 246 RSRGIQIfsfIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVilqmgdhRIRAG-----D 320
Cdd:PRK07768 126 EEKGIRV---LTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAM-------FVAAEfdvetD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 321 VMVSFLPLAH-MferccenGMyyVGG-CVGFYSGdikeltNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASglkrGLFN 398
Cdd:PRK07768 196 VMVSWLPLFHdM-------GM--VGFlTVPMYFG------AELVKVTPMDFLRDPLLWAELISKYRGTMTAA----PNFA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 399 MAMRAKekeiargVLRRngcwdklvfkkvhQAFGGN-----LRLMVVGSAPL----------AGNVLTFMRCALGClvle 463
Cdd:PRK07768 257 YALLAR-------RLRR-------------QAKPGAfdlssLRFALNGAEPIdpadvedlldAGARFGLRPEAILP---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 464 GYGQTECTGAIT-----------------LTVQGDHVPNH---------VGPPVSCNAVKLVD-----VPEMEyfanqnT 512
Cdd:PRK07768 313 AYGMAEATLAVSfspcgaglvvdevdadlLAALRRAVPATkgntrrlatLGPPLPGLEVRVVDedgqvLPPRG------V 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666501 513 GEVCVRGSNVFHGyYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 581
Cdd:PRK07768 387 GVIELRGESVTPG-YLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
125-617 |
6.40e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 74.66 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 125 ETLTspYQWINYDEALLRAKNFGAGMlalgaRPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQT 204
Cdd:PRK13390 23 EQVS--YRQLDDDSAALARVLYDAGL-----RTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 205 DMQVVIVED--DGKAAMLleKAPRSLKIivaikpirqttlerarSRGIQIFSFIDVEK-LGAKGnhpevPPTAEDLC--T 279
Cdd:PRK13390 96 GARVLVASAalDGLAAKV--GADLPLRL----------------SFGGEIDGFGSFEAaLAGAG-----PRLTEQPCgaV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 280 VCYTSGTTGNPKGVM--LTHGNVVA-GVCSVILQMGDHRIRAGDVMVSFLPLAHMFE-RCCenGMYY-VGGCVGFYSG-D 353
Cdd:PRK13390 153 MLYSSGTTGFPKGIQpdLPGRDVDApGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWC--SMVHaLGGTVVLAKRfD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 354 IKELTNDLKMLKPTVMPAVPRLLNRVYdKIQNDIsasglkRGLFNMAmrakekeiargvlrrngcwdklvfkkvhqafgg 433
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLL-KLDADV------RTRYDVS--------------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 434 NLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGaITLTVQGDHV--PNHVGPPVsCNAVKLVDVPEMEYFANQn 511
Cdd:PRK13390 271 SLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHG-MTFIDSPDWLahPGSVGRSV-LGDLHICDDDGNELPAGR- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 512 TGEVCVRGSNVFHGYYKDPEKTAEAIDSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQY 589
Cdd:PRK13390 348 IGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPA 426
|
490 500
....*....|....*....|....*...
gi 24666501 590 VNQVYVYGeslksciiavvVPDTDVLKQ 617
Cdd:PRK13390 427 VHDVAVIG-----------VPDPEMGEQ 443
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
283-621 |
7.08e-14 |
|
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: 74.67 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 283 TSGTTGNPKGVMLTHGNVV------AGVCsvilqmgdhRIRAGDVMVSFLPLAHMFERCCEN--GMYYVGGCVGFYSGDI 354
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAynvrasAEVC---------GLDQDTVYLAVLPAAHNFPLACPGvlGTLLAGGRVVLAPDPS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 355 KELTNDL-KMLKPTVMPAVPRLLNRVYDkiqndiSASGLKRGLfnmamrakekeiargvlrrngcwdklvfkkvhqafgG 433
Cdd:cd05920 218 PDAAFPLiEREGVTVTALVPALVSLWLD------AAASRRADL------------------------------------S 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 434 NLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEctGAITLTVQGDhvPNHV-----GPPVSC-NAVKLVD-----VP 502
Cdd:cd05920 256 SLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTRLDD--PDEViihtqGRPMSPdDEIRVVDeegnpVP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 503 EMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN 582
Cdd:cd05920 332 PGE------EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24666501 583 IYTLSQYVNQVYV-------YGEslKSCiiAVVV-----PDTDVLKQWATE 621
Cdd:cd05920 405 LLLRHPAVHDAAVvampdelLGE--RSC--AFVVlrdppPSAAQLRRFLRE 451
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
127-581 |
1.07e-13 |
|
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: 73.92 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 127 LTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLyDTLGPDA-CAFIIRQTD 205
Cdd:cd17651 14 LVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL-DPAYPAErLAFMLADAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 206 MQVVIVEDDgkaamLLEKAPRSLKIIVAIKPIRQTTLERARsrgiqifsfidveklgakgnhPEVPPTAEDLCTVCYTSG 285
Cdd:cd17651 93 PVLVLTHPA-----LAGELAVELVAVTLLDQPGAAAGADAE---------------------PDPALDADDLAYVIYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 286 TTGNPKGVMLTHGNVV-----------AGVCSVILQMgdhrirAG---DVMVS--FLPLAHmferccengmyyvGGCVGF 349
Cdd:cd17651 147 STGRPKGVVMPHRSLAnlvawqarassLGPGARTLQF------AGlgfDVSVQeiFSTLCA-------------GATLVL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 350 YSGDIKeltNDLkmlkptvmPAVPRLLNRvydkiqNDISASGLKrglfNMAMRAKEKEIARgvlrrngcwdklvfkkvHQ 429
Cdd:cd17651 208 PPEEVR---TDP--------PALAAWLDE------QRISRVFLP----TVALRALAEHGRP-----------------LG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 430 AFGGNLRLMVVGSAPLAGNVLT--FMRCALGCLVLEGYGQTECTGAITLTVQGDHV----PNHVGPPVSCNAVKLVD--- 500
Cdd:cd17651 250 VRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAawpaPPPIGRPIDNTRVYVLDaal 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 501 --VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGW------HHTGDVGMWLPNGTLRIIDRRKHIFKLSqG 572
Cdd:cd17651 330 rpVPPGV------PGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIR-G 402
|
....*....
gi 24666501 573 EYIVPEKIE 581
Cdd:cd17651 403 FRIELGEIE 411
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
184-581 |
1.07e-13 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 74.07 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 184 VVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAMLLEKAPRSLKiivaikpirqTTLERARSRGIQIFSFIDVEKLGA 263
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECP----------SKPKLVWVGDPVPEGWIDFRKLIK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 264 KGNHPEVPPTA------EDLCTVCYTSGTTGNPKgvMLTH------GNVVAGvcsvilqMGDHRIRAGDVMVSFLPLAhm 331
Cdd:cd05970 168 NASPDFERPTAnsypcgEDILLVYFSSGTTGMPK--MVEHdftyplGHIVTA-------KYWQNVREGGLHLTVADTG-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 332 FERCCENGMY--YVGGCVGFysgdikelTNDLKMLKPTVM---------------PAVPRLLnrvydkIQNDISASGLKr 394
Cdd:cd05970 237 WGKAVWGKIYgqWIAGAAVF--------VYDYDKFDPKALleklskygvttfcapPTIYRFL------IREDLSRYDLS- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 395 glfnmamrakekeiargvlrrngcwdklvfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAI 474
Cdd:cd05970 302 ---------------------------------------SLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 475 TLTVQGDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSN-----VFHGYYKDPEKTAEAIdSEGWHHTGDVG 549
Cdd:cd05970 343 ATFPWMEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAA 420
|
410 420 430
....*....|....*....|....*....|..
gi 24666501 550 MWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIE 581
Cdd:cd05970 421 WMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVE 451
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
269-583 |
1.13e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 74.36 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 269 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVcSVILQMGDHRIRagDVMVSFLPLAHMFerccengmyyvGGCVG 348
Cdd:PRK08043 359 QVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANV-EQIKTIADFTPN--DRFMSALPLFHSF-----------GLTVG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 FYSgdiKELTNDLKMLKPTVM--PAVPRLlnrVYDkiQNDISASGLKRGLFNMAMRAKEKEIARgvlrrngcwdklvfkk 426
Cdd:PRK08043 425 LFT---PLLTGAEVFLYPSPLhyRIVPEL---VYD--RNCTVLFGTSTFLGNYARFANPYDFAR---------------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 427 vhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEy 506
Cdd:PRK08043 481 --------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 507 fanqNTGEVCVRGSNVFHGYYK--DP-------EKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVP 577
Cdd:PRK08043 552 ----QGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSL 626
|
....*.
gi 24666501 578 EKIENI 583
Cdd:PRK08043 627 EMVEQL 632
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
275-621 |
1.15e-13 |
|
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: 73.66 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCS------------VILQMGDhriragdvmVSFLPLAHMFERCCENG--M 340
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwrreyeldsfpvRLLQMAS---------FSFDVFAGDFARSLLNGgtL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 341 YYVGGCVGFysgDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQndisasglkrglfnmamrakekeiargvlrrngcWD 420
Cdd:cd17650 164 VICPDEVKL---DPAALYDLILKSRITLMESTPALIRPVMAYVY----------------------------------RN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 421 KLVFKkvhqafggNLRLMVVGS--------APLAGNVLTFMRcalgclVLEGYGQTECT-------GAITLTVQGDHVPn 485
Cdd:cd17650 207 GLDLS--------AMRLLIVGSdgckaqdfKTLAARFGQGMR------IINSYGVTEATidstyyeEGRDPLGDSANVP- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 486 hVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLRI 559
Cdd:cd17650 272 -IGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFvenpfaPGERMYRTGDLARWRADGNVEL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666501 560 IDRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVY------GE-SLKSCIIAVVVPDTDVLKQWATE 621
Cdd:cd17650 350 LGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVAvredkgGEaRLCAYVVAAATLNTAELRAFLAK 417
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
271-581 |
1.18e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.27 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 271 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvCSVILQMGDHrIRAGDVMVSFLPLAH-MferccengmyyvgGCVGF 349
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMAN-LRAISHDGLK-VRPGDRCVSWLPFYHdM-------------GLVGF 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 350 YsgdIKELTNDLKM-LKPTVMPAV-PRLLNRVYDKIQNDISAS---GLKRglfnMAMRAKEKEIARGVL---RRNGCWDK 421
Cdd:PRK09192 237 L---LTPVATQLSVdYLPTRDFARrPLQWLDLISRNRGTISYSppfGYEL----CARRVNSKDLAELDLscwRVAGIGAD 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 422 LVFKKVHQAFGGNLrlmvvgsAPLAGNVLTFMRCalgclvlegYGQTECT----------GAITLTV-------QGDHVP 484
Cdd:PRK09192 310 MIRPDVLHQFAEAF-------APAGFDDKAFMPS---------YGLAEATlavsfsplgsGIVVEEVdrdrleyQGKAVA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 485 NHV-----------GPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEkTAEAIDSEGWHHTGDV 548
Cdd:PRK09192 374 PGAetrrvrtfvncGKALPGHEIEIRNeagmpLPERV------VGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDL 446
|
330 340 350
....*....|....*....|....*....|...
gi 24666501 549 GmWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 581
Cdd:PRK09192 447 G-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
142-581 |
1.24e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.15 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 142 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED--DGKAAM 219
Cdd:PRK07798 37 RANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYERefAPRVAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 220 LLEKAPRsLKIIVAIkpirqttlerARSRGIQIFSF-IDVEKLGAKG--NHPEVPPTAEDLcTVCYTSGTTGNPKGVMLT 296
Cdd:PRK07798 117 VLPRLPK-LRTLVVV----------EDGSGNDLLPGaVDYEDALAAGspERDFGERSPDDL-YLLYTGGTTGMPKGVMWR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 297 HGNVVAgvcsVILQMGDH--------------RIRAGDVMVSFL--PLAHMFERCCENGMYYVGGCVGFYsgDIKELTND 360
Cdd:PRK07798 185 QEDIFR----VLLGGRDFatgepiedeeelakRAAAGPGMRRFPapPLMHGAGQWAAFAALFSGQTVVLL--PDVRFDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 361 lkmlkpTVMPAVPRllNRVydkiqNDISASGlkrglfnMAMrakekeiARGV---LRRNGCWDklvfkkvhqafGGNLRL 437
Cdd:PRK07798 259 ------EVWRTIER--EKV-----NVITIVG-------DAM-------ARPLldaLEARGPYD-----------LSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 438 MVVGSAPLAGNV-LTFMRCALGCLVLEGYGQTEcTGAITLTVQGDHVPNHVGPPVSCNA-VKLVDvpEMEYFANQNTGEV 515
Cdd:PRK07798 301 IASGGALFSPSVkEALLELLPNVVLTDSIGSSE-TGFGGSGTVAKGAVHTGGPRFTIGPrTVVLD--EDGNPVEPGSGEI 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666501 516 CV--RGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRkhifklSQ-----GEYIVPEKIE 581
Cdd:PRK07798 378 GWiaRRGHIPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRG------SVcintgGEKVFPEEVE 447
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
102-616 |
1.59e-13 |
|
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: 73.64 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 102 RTLYQTFREGAYASNNgpclgwRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCysF 181
Cdd:COG1021 25 ETLGDLLRRRAERHPD------RIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFAL--F 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 182 SLVVVPLYdtlgpdacA----------FIIRQTDMQVVIVED-------DGKAAMLLEKAPrSLKIIVAikpirqttLER 244
Cdd:COG1021 97 RAGAIPVF--------AlpahrraeisHFAEQSEAVAYIIPDrhrgfdyRALARELQAEVP-SLRHVLV--------VGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 245 ARSrgiqifsFIDVEKLGAKGNHPEVP-PTAEDLCTVCYTSGTTGNPKGVMLTHG----NVV--AGVCsvilqmgdhRIR 317
Cdd:COG1021 160 AGE-------FTSLDALLAAPADLSEPrPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVRasAEIC---------GLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 318 AGDVMVSFLPLAHMFERCCEN--GMYYVGGCVgfysgdikeltndlkmlkptVMPAVPRLlNRVYDKI-QNDISASGLKR 394
Cdd:COG1021 224 ADTVYLAALPAAHNFPLSSPGvlGVLYAGGTV--------------------VLAPDPSP-DTAFPLIeRERVTVTALVP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 395 GLFNMAMRAKEKEIARGvlrrngcwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEctGAI 474
Cdd:COG1021 283 PLALLWLDAAERSRYDL---------------------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 475 TLTVQGD---HVPNHVGPPVSC-NAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHT 545
Cdd:COG1021 340 NYTRLDDpeeVILTTQGRPISPdDEVRIVDedgnpVPPGE------VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRT 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 546 GDVGMWLPNGTLRIIDRRK-HIFKlsQGEYIVPEKIENIytLSQY--VNQVYV-------YGEslKSCiiAVVVPDTDVL 615
Cdd:COG1021 414 GDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENL--LLAHpaVHDAAVvampdeyLGE--RSC--AFVVPRGEPL 485
|
.
gi 24666501 616 K 616
Cdd:COG1021 486 T 486
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
275-581 |
1.97e-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: 73.17 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVVAgVCSVIlqMGDHRIRAGDVMVSFLPLAhmFERCCENGM--YYVGGCVgfysg 352
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAA-HCQAT--AERYGLTPGDRELQFASFN--FDGAHEQLLppLICGACV----- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 353 dikeltndlkmlkptVMPAVPRLL--NRVYDKIQND-ISASGLKRGLFNMAMRAKEKEIARGVLRrngcwdklvfkkvhq 429
Cdd:cd17649 164 ---------------VLRPDELWAsaDELAEMVRELgVTVLDLPPAYLQQLAEEADRTGDGRPPS--------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 430 afggnLRLMVVGSAPLAGNVLTfMRCALGCLVLEGYGQTECTgaITLTV---------QGDHVPnhVGPPVSCNAVKLVD 500
Cdd:cd17649 214 -----LRLYIFGGEALSPELLR-RWLKAPVRLFNAYGPTEAT--VTPLVwkceagaarAGASMP--IGRPLGGRSAYILD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 501 vPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI-----DSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGE 573
Cdd:cd17649 284 -ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGF 361
|
....*...
gi 24666501 574 YIVPEKIE 581
Cdd:cd17649 362 RIELGEIE 369
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
124-628 |
2.39e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.04 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 124 RETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDAC 197
Cdd:PRK12467 528 RPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMvvgllaVLKAGGAY------VPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 198 AFIIRQTDMQVVIVEDDGKAAMLLEKAPRSLKIIVAIKPIRqttlerarsrgiqifsfidveklGAKGNHPEVPPTAEDL 277
Cdd:PRK12467 602 AYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPADLLC-----------------------GYSGHNPEVALDPDNL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 278 CTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAhmFERCCEngMYYVGGCVGfysgdikel 357
Cdd:PRK12467 659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERL---QLAADDSMLMVSTFA--FDLGVT--ELFGALASG--------- 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 358 tNDLKMLKPTVMPAVPRLLNRVYDKiqnDISASGLKRGLFNMAMRAKEKEIARGvlrrngcwdklvfkkvhqafggnLRL 437
Cdd:PRK12467 723 -ATLHLLPPDCARDAEAFAALMADQ---GVTVLKIVPSHLQALLQASRVALPRP-----------------------QRA 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 438 MVVGSAPLAGNVLTFMR-CALGCLVLEGYGQTECT-GAITLTVQGDHVPNH---VGPPVSCNAVKLVDvPEMEYFANQNT 512
Cdd:PRK12467 776 LVCGGEALQVDLLARVRaLGPGARLINHYGPTETTvGVSTYELSDEERDFGnvpIGQPLANLGLYILD-HYLNPVPVGVV 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 513 GEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKIENIYT 585
Cdd:PRK12467 855 GELYIGGAGLARGYHRRPALTAErfvpdpfGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLL 933
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24666501 586 LSQYVNQ--VYVYGESLKSCIIAVVVPDT--DVLKQWATENNVRGTL 628
Cdd:PRK12467 934 AQPGVREavVLAQPGDAGLQLVAYLVPAAvaDGAEHQATRDELKAQL 980
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-583 |
4.26e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 71.36 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVA-GVCSVILQMGDhrirAGDVMVSFLPLAHMFERCCENG-MYYVGGCVGFYS-- 351
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYnAWMLALNSLFD----PDDVLLCGLPLFHVNGSVVTLLtPLASGAHVVLAGpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 352 -----GDIKELTNDLKMLKPTVMPAVPRLLNRVYDK-IQNDISAsglkrglfnmamrakekeiargvlrrngcwdklvfk 425
Cdd:cd05944 79 gyrnpGLFDNFWKLVERYRITSLSTVPTVYAALLQVpVNADISS------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 426 kvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTV-QGDHVPNHVGPPVSCNAVKLVDV-PE 503
Cdd:cd05944 123 ---------LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPpDGPKRPGSVGLRLPYARVRIKVLdGV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 504 MEYF---ANQNTGEVCVRGSNVFHGYYKDpEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKI 580
Cdd:cd05944 194 GRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALI 271
|
...
gi 24666501 581 ENI 583
Cdd:cd05944 272 EEA 274
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
274-583 |
5.87e-13 |
|
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: 71.75 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 274 AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFerccengmyyvgGCVGFYsgd 353
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST---EWKTKDRILSWMPLTHDM------------GLIAFH--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 354 ikeLTNDLKMLKPTVMPAV-----PRL-LNRVYDKIQNDISASGLKRGLFnmAMRAKEKEIARgvlrrngcWDKlvfkkv 427
Cdd:cd05908 167 ---LAPLIAGMNQYLMPTRlfirrPILwLKKASEHKATIVSSPNFGYKYF--LKTLKPEKAND--------WDL------ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 428 hqafgGNLRLMVVGSAPLAGNVL-TFM-RCALGCL----VLEGYGQTECTGAITLTVQGDH--VPNH------------- 486
Cdd:cd05908 228 -----SSIRMILNGAEPIDYELChEFLdHMSKYGLkrnaILPVYGLAEASVGASLPKAQSPfkTITLgrrhvthgepepe 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 487 -------------VGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMwLP 553
Cdd:cd05908 303 vdkkdsecltfveVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGF-IR 380
|
330 340 350
....*....|....*....|....*....|
gi 24666501 554 NGTLRIIDRRKHIFkLSQGEYIVPEKIENI 583
Cdd:cd05908 381 NGRLVITGREKDII-FVNGQNVYPHDIERI 409
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
275-583 |
1.72e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 70.23 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVVAG--VCsviLQMGDHRirAGDVMVSFLPLAHMFE-RCCENGMYYVGGCVGF-- 349
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANqrAC---LKFFSPK--EDDVMMSFLPPFHAYGfNSCTLFPLLSGVPVVFay 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 350 ---YSGDIKELTNDLKMlkpTVMPAVPRLLNRVydkiqndisasgLKRglfnmamrAKEKEIARGvlrrngcwdklvfkk 426
Cdd:PRK06334 258 nplYPKKIVEMIDEAKV---TFLGSTPVFFDYI------------LKT--------AKKQESCLP--------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 427 vhqafggNLRLMVVGSAPL-----AGNVLTFMRCALgclvLEGYGQTECTGAITLTVQGDhvPNH---VGPPVSCNAVKL 498
Cdd:PRK06334 300 -------SLRFVVIGGDAFkdslyQEALKTFPHIQL----RQGYGTTECSPVITINTVNS--PKHescVGMPIRGMDVLI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 499 VDVPEMEYFANQNTGEVCVRGSNVFHGYY-KDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVP 577
Cdd:PRK06334 367 VSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSL 445
|
....*.
gi 24666501 578 EKIENI 583
Cdd:PRK06334 446 EALESI 451
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
253-595 |
1.79e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 69.90 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 253 FSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVA---GVCSVIlqmgdhRIRAGDVMVSFLPLA 329
Cdd:PRK09029 113 FSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLAsaeGVLSLM------PFTAQDSWLLSLPLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 330 HMfercceNGM------YYVGGCVGFysGDIKELTNDLKM-----LKPTvmpAVPRLLnrvydkiQNDISASGLKRGLFN 398
Cdd:PRK09029 187 HV------SGQgivwrwLYAGATLVV--RDKQPLEQALAGcthasLVPT---QLWRLL-------DNRSEPLSLKAVLLG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 399 MAM-------RAKEKEIArgvlrrngCWdklvfkkvhqafggnlrlmvvgsaplagnvltfmrcalgClvleGYGQTECt 471
Cdd:PRK09029 249 GAAipvelteQAEQQGIR--------CW---------------------------------------C----GYGLTEM- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 472 gAITLT-VQGDHVPNhVGPPVSCNAVKLVDvpemeyfanqntGEVCVRGSNVFHGYYKDPEKTAeAIDSEGWHHTGDVGM 550
Cdd:PRK09029 277 -ASTVCaKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGE 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24666501 551 WLpNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV 595
Cdd:PRK09029 342 WQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
111-611 |
3.74e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 66.20 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 111 GAYASNNGPCLGWRETltsPYQWINY-DEALLRAKNFGAgmLALGARPKQlIGIYSQNRPEWILYEQGCYSFSLVVVPLY 189
Cdd:PRK13388 10 RDRAGDDTIAVRYGDR---TWTWREVlAEAAARAAALIA--LADPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 190 DTLGPDACAFIIRQTDMQVVIVEDDGKAamLLEkaprslkiivaikpirqtTLERARSRgiqifsFIDV------EKLGA 263
Cdd:PRK13388 84 TTRRGAALAADIRRADCQLLVTDAEHRP--LLD------------------GLDLPGVR------VLDVdtpayaELVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 264 KGN-HPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRiraGDVMVSFLPLAHmferccENGMYY 342
Cdd:PRK13388 138 AGAlTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTR---DDVCYVSMPLFH------SNAVMA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 343 -------VGGCV---------GFYSgdikeltnDLKMLKPTVMPAVPRLLNRVY------DKIQNDisasgLKRGLFNma 400
Cdd:PRK13388 209 gwapavaSGAAValpakfsasGFLD--------DVRRYGATYFNYVGKPLAYILatperpDDADNP-----LRVAFGN-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 401 mRAKEKEIARgVLRRngcwdklvfkkvhqafggnlrlmvvgsaplagnvltfmrcaLGCLVLEGYGQTEctGAITLTVQG 480
Cdd:PRK13388 274 -EASPRDIAE-FSRR-----------------------------------------FGCQVEDGYGSSE--GAVIVVREP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 481 DHVPNHVGPP----VSCNAVKLVDVPEMEYFAN-------QNTGE-VCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDV 548
Cdd:PRK13388 309 GTPPGSIGRGapgvAIYNPETLTECAVARFDAHgallnadEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDL 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666501 549 GMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYVYGeslksciiavvVPD 611
Cdd:PRK13388 388 AYRDADGWIYFAGRTADWMRVD-GENLSAAPIERILLRHPAINRVAVYA-----------VPD 438
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
153-597 |
6.89e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 65.19 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 153 LGARPKQLIGIYSQNRPEW--ILYEQGCysFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVE--DDGKAAMLLEKAPrSL 228
Cdd:PRK05620 59 LGITGDQRVGSMMYNCAEHleVLFAVAC--MGAVFNPLNKQLMNDQIVHIINHAEDEVIVADprLAEQLGEILKECP-CV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 229 KIIVAIKPIRQTTLERARSRGIQIFSFidvEKL----GAKGNHPEVPPTaeDLCTVCYTSGTTGNPKGVMLTHGnvvagv 304
Cdd:PRK05620 136 RAVVFIGPSDADSAAAHMPEGIKVYSY---EALldgrSTVYDWPELDET--TAAAICYSTGTTGAPKGVVYSHR------ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 305 cSVILQ-MGdhrIRAGDVM-----VSFLplahmferCCENGMYYVGGCV---GFYSGdikeltndlkmlKPTVMPAvprl 375
Cdd:PRK05620 205 -SLYLQsLS---LRTTDSLavthgESFL--------CCVPIYHVLSWGVplaAFMSG------------TPLVFPG---- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 376 lnrvydkiqNDISASGLKRgLFNMAMrakeKEIARGVlrrNGCWDKLVfkkVHQAFGG----NLRLMVVGSAPLAGNVLT 451
Cdd:PRK05620 257 ---------PDLSAPTLAK-IIATAM----PRVAHGV---PTLWIQLM---VHYLKNPpermSLQEIYVGGSAVPPILIK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 452 FMRCALGCLVLEGYGQTEcTGAITlTVQgdHVPNHVGP-------------PVSCNaVKLVDVPEMEYFANQNTGEVCVR 518
Cdd:PRK05620 317 AWEERYGVDVVHVWGMTE-TSPVG-TVA--RPPSGVSGearwayrvsqgrfPASLE-YRIVNDGQVMESTDRNEGEIQVR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 519 GSNVFHGYYKDP----------------EKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN 582
Cdd:PRK05620 392 GNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLEN 470
|
490
....*....|....*
gi 24666501 583 IYTLSQYVNQVYVYG 597
Cdd:PRK05620 471 YIMAAPEVVECAVIG 485
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
435-582 |
1.02e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 64.63 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 435 LRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEctGAITLTVQGD---HVPNHVGPPVSCN-AVKLVD-----VPEME 505
Cdd:PRK10946 302 LKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE--GLVNYTRLDDsdeRIFTTQGRPMSPDdEVWVADadgnpLPQGE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 506 yfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKhifklSQ----GEYIVPEKIE 581
Cdd:PRK10946 380 ------VGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREK-----DQinrgGEKIAAEEIE 448
|
.
gi 24666501 582 N 582
Cdd:PRK10946 449 N 449
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
278-583 |
1.07e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 64.77 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 278 CTVCYTSGTTGNPKGVMLTH-GNVVAgvcSVILQMGDHR-IRAGDVMVSFLPLAHmferccEN--GMYYVGGCVGfysgd 353
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVLH---ALMANNGDALgTSAADTMLPVVPLFH------ANswGIAFSAPSMG----- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 354 ikeltndLKMlkptVMPAVPRLLNRVYDKIQND-ISASGLKRGLFNMAMRAKEKEIArgvlrrngcwdKLVFKKvhqafg 432
Cdd:PRK06018 246 -------TKL----VMPGAKLDGASVYELLDTEkVTFTAGVPTVWLMLLQYMEKEGL-----------KLPHLK------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 433 gnlrlMVV--GSAPLAGNVLTFMRcaLGCLVLEGYGQTECTGAITLTVQGDHVPNHVG------------PPVSCNaVKL 498
Cdd:PRK06018 298 -----MVVcgGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAALKPPFSKLPGdarldvlqkqgyPPFGVE-MKI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 499 VD-----VPemeyFANQNTGEVCVRGSNVFHGYYKdpeKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGE 573
Cdd:PRK06018 370 TDdagkeLP----WDGKTFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGE 441
|
330
....*....|
gi 24666501 574 YIVPEKIENI 583
Cdd:PRK06018 442 WISSIDLENL 451
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
263-621 |
3.09e-10 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 63.17 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 263 AKGNHPEVPPTAEDLCT-VCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMF-ERCCENGM 340
Cdd:cd05929 112 AEGGSPETPIEDEAAGWkMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAApFRWSMTAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 341 YYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNR---VYDKIQNDISASGLKRgLFNMA--MRAKEKEIargvlrr 415
Cdd:cd05929 192 FMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRllkLPEAVRNAYDLSSLKR-VIHAAapCPPWVKEQ------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 416 ngcWDKLVFKKVHQAFGGNlrlmvvgsaplagnvltfmrcalgclvlEGYGQTECTGAITLTvqgdHvPNHVGPPVScNA 495
Cdd:cd05929 264 ---WIDWGGPIIWEYYGGT----------------------------EGQGLTIINGEEWLT----H-PGSVGRAVL-GK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 496 VKLVDvPEMEYFANQNTGEVCVRGSNVFHgYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYI 575
Cdd:cd05929 307 VHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNI 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24666501 576 VPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVV--VPDTDVLKQWATE 621
Cdd:cd05929 384 YPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVqpAPGADAGTALAEE 434
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
136-352 |
3.98e-10 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 62.89 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 136 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED-- 213
Cdd:cd05968 94 YGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 --DGKAAMLLEKA-------PRSLKIIVaikpIRQTTLERARSRGIQIFSFIDVEKLGAKGNHPEvpptAEDLCTVCYTS 284
Cdd:cd05968 174 trRGREVNLKEEAdkacaqcPTVEKVVV----VRHLGNDFTPAKGRDLSYDEEKETAGDGAERTE----SEDPLMIIYTS 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666501 285 GTTGNPKGVMLTH-GNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSG 352
Cdd:cd05968 246 GTTGKPKGTVHVHaGFPLKAAQDMYFQFD---LKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDG 311
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
87-611 |
6.07e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 87 ESKNGKFVSYITEnvRTLYQTFREGAYASNNGPCLGWREtltspyQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQ 166
Cdd:PRK12316 3044 EAWNATAAEYPLE--RGVHRLFEEQVERTPDAVALAFGE------QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVE 3115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 167 NRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIrqtdmqvvivEDDGKAAMLlekaprslkiivaikpiRQTTLERAR 246
Cdd:PRK12316 3116 RSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML----------EDSGAQLLL-----------------SQSHLRLPL 3168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 247 SRGIQIFsFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFL 326
Cdd:PRK12316 3169 AQGVQVL-DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG---LGVGDRVLQFT 3244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 327 PLAhmferccengmyyvggcvgfYSGDIKELTNDLkMLKPTVMPAVPRLLNRVyDKIQNDISASGLKRGLFNMAMRAKek 406
Cdd:PRK12316 3245 TFS--------------------FDVFVEELFWPL-MSGARVVLAGPEDWRDP-ALLVELINSEGVDVLHAYPSMLQA-- 3300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 407 eiargvlrrngcwdklVFKKVHQAFGGNLRLMVVGSAPLAGNVLTfmRCALGCLVLEGYGQTECTGAITLTVQGDHVPNH 486
Cdd:PRK12316 3301 ----------------FLEEEDAHRCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDA 3362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 487 --VGPPVSCNAVKLVDVpEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLR 558
Cdd:PRK12316 3363 vpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLARYRADGVIE 3441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24666501 559 IIDRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVYGESLKScIIAVVVPD 611
Cdd:PRK12316 3442 YIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPE 3492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
58-618 |
6.12e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 58 VPERPLVPLENQSPLLEGPEQihvskfykeskngkfVSYITENVRTLYQTFREGAYASNNGPCLGWREtltspyQWINYD 137
Cdd:PRK12316 482 VDELPMLDAEERGQLVEGWNA---------------TAAEYPLQRGVHRLFEEQVERTPEAPALAFGE------ETLDYA 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 138 EALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDACAFIIRQTDMQVVIV 211
Cdd:PRK12316 541 ELNRRANRLAHALIERGVGPDVLVGVAMERSIEMvvallaILKAGGAY------VPLDPEYPAERLAYMLEDSGVQLLLS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 212 EddgkaAMLLEKAPRSlkiivaikpirqttlerarsRGIQIFSF--IDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGN 289
Cdd:PRK12316 615 Q-----SHLGRKLPLA--------------------AGVQVLDLdrPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGK 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVMLTHGNVVAGVCSV--ILQMGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSgDIKELTNDLKMLKPT 367
Cdd:PRK12316 670 PKGAGNRHRALSNRLCWMqqAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHR-DPAKLVELINREGVD 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 368 VMPAVPRLLNrvydkiqndisasglkrglfnmAMRAKEKEIARGVLRRNGCwdklvfkkVHQAFGGNLRLMVVGSAPLAG 447
Cdd:PRK12316 749 TLHFVPSMLQ----------------------AFLQDEDVASCTSLRRIVC--------SGEALPADAQEQVFAKLPQAG 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 448 nvltfmrcalgclVLEGYGQTECTGAIT----LTVQGDHVPnhVGPPVSCNAVKLVDVpEMEYFANQNTGEVCVRGSNVF 523
Cdd:PRK12316 799 -------------LYNLYGPTEAAIDVThwtcVEEGGDSVP--IGRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLA 862
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 524 HGYYKDPEKTAEA------IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:PRK12316 863 RGYHGRPGLTAERfvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLA 941
|
570 580
....*....|....*....|....*..
gi 24666501 598 ESLKScIIAVVVPDT------DVLKQW 618
Cdd:PRK12316 942 VDGKQ-LVGYVVLESeggdwrEALKAH 967
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
268-614 |
6.34e-10 |
|
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: 61.90 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQMGDH-RIRAGDVMVSFLPLAH------MFerccenGM 340
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISH----RAALNTILDINRRfAVGPDDRVLALSSLSFdlsvydIF------GA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 341 YYVGGCVGFYSGDIKELTNDLKML----KPTVMPAVPRLLNRVYDKIQndiSASGLKRGLfnmamrakekeiaRGVLRrN 416
Cdd:cd12114 189 LSAGATLVLPDEARRRDPAHWAELierhGVTLWNSVPALLEMLLDVLE---AAQALLPSL-------------RLVLL-S 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 417 GCWDKLVFKKVHQAFGGNLRLMvvgsaplagnvltfmrcALGclvlegyGQTEctGAITLTVQG-DHVPNHV-----GPP 490
Cdd:cd12114 252 GDWIPLDLPARLRALAPDARLI-----------------SLG-------GATE--ASIWSIYHPiDEVPPDWrsipyGRP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 491 VSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEA----IDSEGWHHTGDVGMWLPNGTLRIID 561
Cdd:cd12114 306 LANQRYRVLDprgrdCPDWV------PGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLG 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24666501 562 RRKHIFKLsQGEYIVPEKIENIYTLSQYVNQ--VYVYGESLKSCIIAVVVPDTDV 614
Cdd:cd12114 380 RRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDG 433
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
134-610 |
7.21e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 61.84 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPE-----WILYEQGCYSfslvvVPLYDTLGPDACAFIIRQTDMQV 208
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEffevyWAARRSGLYY-----TPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 209 VIVEDDGKAAM--LLEKAPRSLKIIVAIkpirqttlerarsrGIQIFSFIDVEKLGAKgnHPEVPPTAEDL-CTVCYTSG 285
Cdd:PRK08276 87 LIVSAALADTAaeLAAELPAGVPLLLVV--------------AGPVPGFRSYEEALAA--QPDTPIADETAgADMLYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 286 TTGNPKGVM--LTHGNV--VAGVCSVILQMGDHrIRAGDVMVSFLPLAHmferccengmyyvgGCVGFYSGDIKELTNDL 361
Cdd:PRK08276 151 TTGRPKGIKrpLPGLDPdeAPGMMLALLGFGMY-GGPDSVYLSPAPLYH--------------TAPLRFGMSALALGGTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 362 ---------KML------KPTVMPAVP----RLLnRVYDKIQN--DISAsglkrglfnmamrakekeiargvlrrngcwd 420
Cdd:PRK08276 216 vvmekfdaeEALalieryRVTHSQLVPtmfvRML-KLPEEVRAryDVSS------------------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 421 klvfkkvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQG--DHvPNHVGPPVSCnAVKL 498
Cdd:PRK08276 264 --------------LRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDwlAH-PGSVGKAVLG-EVRI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 499 VD-----VPEME----YFAnqntgevcvRGSNVFHgYYKDPEKTAEAIDSEGWHHTGDVGmWL-PNGTLRIIDRRKHIFk 568
Cdd:PRK08276 328 LDedgneLPPGEigtvYFE---------MDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI- 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 24666501 569 LSQGEYIVPEKIENIYTLSQYVNQVYV-------YGESLKsciiAVVVP 610
Cdd:PRK08276 396 ISGGVNIYPQEIENLLVTHPKVADVAVfgvpdeeMGERVK----AVVQP 440
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
134-610 |
7.61e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 62.02 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 D--GKAAMLLEKAPRSLKIIVAIKPirqTTLERarsrgiqifsFIDVEKlgAKGNHPEVPPTAEDLCT-VCYTSGTTGNP 290
Cdd:PRK13391 105 AklDVARALLKQCPGVRHRLVLDGD---GELEG----------FVGYAE--AVAGLPATPIADESLGTdMLYSSGTTGRP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 291 KGVM--LTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCV----GFYSGDIKELTNDLK-- 362
Cdd:PRK13391 170 KGIKrpLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVivmeHFDAEQYLALIEEYGvt 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 363 --MLKPTVMPAVPRLLNRVYDKIqnDISAsglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnLRLMVV 440
Cdd:PRK13391 250 htQLVPTMFSRMLKLPEEVRDKY--DLSS---------------------------------------------LEVAIH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 441 GSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQG--DHvPNHVGPPVsCNAVKLVDvPEMEYFANQNTGEVCVR 518
Cdd:PRK13391 283 AAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEwlAH-PGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 519 GSNVFHgYYKDPEKTAEAIDSEG-WHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:PRK13391 360 GGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
490
....*....|....*.
gi 24666501 598 ---ESLKSCIIAVVVP 610
Cdd:PRK13391 438 vpnEDLGEEVKAVVQP 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
274-599 |
7.70e-10 |
|
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: 61.72 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 274 AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhRIRAGDVM----VSFLPLAH-MFERCCENGMYYVggcvg 348
Cdd:cd17656 127 SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTN--INFSDKVLqfatCSFDVCYQeIFSTLLSGGTLYI----- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 fysgdikeLTNDLKMlkptvmpAVPRLLNRVYdkiQNDISASGLKRGLFNMAmrAKEKEIARGVlrrngcwdklvFKKVH 428
Cdd:cd17656 200 --------IREETKR-------DVEQLFDLVK---RHNIEVVFLPVAFLKFI--FSEREFINRF-----------PTCVK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 429 QAFGGNLRLMVVgsaplagNVLTFMRCALGCLVLEGYGQTECTGAITLTVQ-GDHVPNH--VGPPVSCNAVKLVDvpemE 505
Cdd:cd17656 249 HIITAGEQLVIT-------NEFKEMLHEHNVHLHNHYGPSETHVVTTYTINpEAEIPELppIGKPISNTWIYILD----Q 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 506 YFANQ---NTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGW------HHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIV 576
Cdd:cd17656 318 EQQLQpqgIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIE 396
|
330 340
....*....|....*....|....*..
gi 24666501 577 PEKIE----NIYTLSQYVnqVYVYGES 599
Cdd:cd17656 397 LGEIEaqllNHPGVSEAV--VLDKADD 421
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
272-574 |
1.19e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 60.94 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 272 PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCenGMYYVGGCVGFY- 350
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG---IRPGEVDLATFPLFALFGPAL--GLTSVIPDMDPTr 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 351 --SGDIKELTNDLKMLKPTVMPAVPRLLNRVYDK-IQNDISASGLKRGLfnmamrakekeiargvlrrngcwdklvfkkv 427
Cdd:cd05910 157 paRADPQKLVGAIRQYGVSIVFGSPALLERVARYcAQHGITLPSLRRVL------------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 428 hqAFGgnlrlmvvgsAPLAGNVLTFMRCAL--GCLVLEGYGQTEC--TGAIT----LTVQGDHVPNH----VGPPVSCNA 495
Cdd:cd05910 206 --SAG----------APVPIALAARLRKMLsdEAEILTPYGATEAlpVSSIGsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 496 VKLVDVPEMEYFANQNT--------GEVCVRGSNVFHGYYKDPEKTAEA-IDSEG---WHHTGDVGMWLPNGTLRIIDRR 563
Cdd:cd05910 274 VRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330
....*....|.
gi 24666501 564 KHIFKLSQGEY 574
Cdd:cd05910 354 AHRVITTGGTL 364
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
268-583 |
1.54e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 61.52 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 268 PEVPPT---AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRiraGDVMVSFLPLAHMFerccengmyyvg 344
Cdd:PRK06814 783 PLVYFCnrdPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSP---EDKVFNALPVFHSF------------ 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 345 gcvGFYSGDIKELTNDLKM-LKPTvmP----AVPRLlnrVYDK-----IQNDISASGLKRGLFNMAMRAkekeiargvlr 414
Cdd:PRK06814 848 ---GLTGGLVLPLLSGVKVfLYPS--PlhyrIIPEL---IYDTnatilFGTDTFLNGYARYAHPYDFRS----------- 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 415 rngcwdklvfkkvhqafggnLRLMVVGSAPL-AGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSC 493
Cdd:PRK06814 909 --------------------LRYVFAGAEKVkEETRQTWME-KFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPG 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 494 NAVKLVDVPEMEyfanqNTGEVCVRGSNVFHGYYKdPEK--TAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSq 571
Cdd:PRK06814 968 IEYRLEPVPGID-----EGGRLFVRGPNVMLGYLR-AENpgVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA- 1039
|
330
....*....|..
gi 24666501 572 GEYIVPEKIENI 583
Cdd:PRK06814 1040 GEMISLAAVEEL 1051
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
273-585 |
1.80e-09 |
|
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: 60.34 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 273 TAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQMGDH-RIRAGDVMVSFLPL---AHMFERC---CENGMYYVGG 345
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTH----RGLANLAAAQIAAfDVGPGSRVLQFASPsfdASVWELLmalLAGATLVLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 346 CVGFYSGDikELTNDLKMLKPTVMPAVPRLLNRVydkiqndiSASGLKrglfnmamrakekeiargvlrrngcwdklvfk 425
Cdd:cd17652 167 AEELLPGE--PLADLLREHRITHVTLPPAALAAL--------PPDDLP-------------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 426 kvhqafgGNLRLMVVGSAPLAGNVltfMRCALGCLVLEGYGQTECTGAITL---TVQGDHVPnhVGPPVSCNAVKLVDvP 502
Cdd:cd17652 205 -------DLRTLVVAGEACPAELV---DRWAPGRRMINAYGPTETTVCATMagpLPGGGVPP--IGRPVPGTRVYVLD-A 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 503 EMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYI 575
Cdd:cd17652 272 RLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErfvadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKI-RGFRI 350
|
330
....*....|
gi 24666501 576 VPEKIENIYT 585
Cdd:cd17652 351 ELGEVEAALT 360
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
273-581 |
5.56e-09 |
|
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: 58.86 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 273 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgvcsvILQMGDH--RIRAGDVMVSF-------------LPLAHmfercce 337
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLA-----LFAATQRwfGFNEDDVWTLFhsyafdfsvweiwGALLH------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 338 ngmyyvGGCVGFYSGDIKELTNDLKML----KPTVMPAVPrllnrvydkiqndiSAsglkrglFNMAMRAkekeiargvL 413
Cdd:cd17643 159 ------GGRLVVVPYEVARSPEDFARLlrdeGVTVLNQTP--------------SA-------FYQLVEA---------A 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 414 RRNGCWDKlvfkkvhqafggNLRLMVVGSAPLAGNVLT--FMRCALGC-LVLEGYGQTECTGAITLT-VQGDHVPNH--- 486
Cdd:cd17643 203 DRDGRDPL------------ALRYVIFGGEALEAAMLRpwAGRFGLDRpQLVNMYGITETTVHVTFRpLDAADLPAAaas 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 487 -VGPPVSCNAVKLVDvpemeyfANQN------TGEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGWHHTGDVGMWL 552
Cdd:cd17643 271 pIGRPLPGLRVYVLD-------ADGRpvppgvVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRL 343
|
330 340
....*....|....*....|....*....
gi 24666501 553 PNGTLRIIDRRKHIFKLSqGEYIVPEKIE 581
Cdd:cd17643 344 PDGELEYLGRADEQVKIR-GFRIELGEIE 371
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
273-581 |
5.72e-09 |
|
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: 59.03 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 273 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgVCSV----ILqmgdhRIRAGDVMVSFLPLAHMFERcceNGM----YYVG 344
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLA-SADRyavnVL-----RLREDDRFVGSPPLAFTFGL---GGVllfpFGVG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 345 G-CVGFYSGDIKELTNDLKMLKPTVMPAVPrllnrvydkiqndisasglkrglfnMAMRAkekeiargvlrrngcwdKLV 423
Cdd:cd05958 166 AsGVLLEEATPDLLLSAIARYKPTVLFTAP-------------------------TAYRA-----------------MLA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 424 FKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTgAITLTVQGDHV-PNHVGPPVSCNAVKLVD-- 500
Cdd:cd05958 204 HPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMF-HIFISARPGDArPGATGKPVPGYEAKVVDde 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 501 ---VPEMEyfanqnTGEVCVRGSNvfhGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVP 577
Cdd:cd05958 283 gnpVPDGT------IGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAP 352
|
....
gi 24666501 578 EKIE 581
Cdd:cd05958 353 PEVE 356
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
274-583 |
6.68e-09 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 58.73 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 274 AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVM--VSFLPLA-HMFErcCENGMYYVGGCVGFY 350
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIG---LKPGDVHwnISSPGWAkHAWS--CFFAPWNAGATVFLF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 351 SG---DIKELTNDLKMLKPTVM---PAVPRLLnrvydkIQNDISASGLKrglfnmamrakekeiargvlrrngcwdklvf 424
Cdd:cd05974 159 NYarfDAKRVLAALVRYGVTTLcapPTVWRML------IQQDLASFDVK------------------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 425 kkvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEM 504
Cdd:cd05974 202 ----------LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 505 EyfanQNTGEVCV-----RGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqgEY-IVPE 578
Cdd:cd05974 272 P----ATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS--DYrISPF 344
|
....*
gi 24666501 579 KIENI 583
Cdd:cd05974 345 ELESV 349
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
135-583 |
8.04e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 58.56 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 135 NYDEALLRAKNFGAGMLALGARPKQLIGIYSQN--RPEWILYeqGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVe 212
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNgyRHLEAYY--GVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLF- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 213 dDGKAAMLLEK-APR--SLKIIVAIkpirqTTLERARSRGIQIFSFIDVekLGAKGNHPEVPPTAEDL-CTVCYTSGTTG 288
Cdd:PRK07008 118 -DLTFLPLVDAlAPQcpNVKGWVAM-----TDAAHLPAGSTPLLCYETL--VGAQDGDYDWPRFDENQaSSLCYTSGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 289 NPKGVMLTHGNVVAGVCSVIL--QMGdhrIRAGDVMVSFLPLAHMfercceN--GMYYVGGCVG---FYSG---DIKELT 358
Cdd:PRK07008 190 NPKGALYSHRSTVLHAYGAALpdAMG---LSARDAVLPVVPMFHV------NawGLPYSAPLTGaklVLPGpdlDGKSLY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 359 NDLKMLKPTVMPAVPRllnrVYDKIQNDISASGLKRGLFNmamrakekeiargvlrrngcwdklvfkkvhqafggnlRLM 438
Cdd:PRK07008 261 ELIEAERVTFSAGVPT----VWLGLLNHMREAGLRFSTLR-------------------------------------RTV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 439 VVGSA-PLAgnVLTFMRCALGCLVLEGYGQTECT--GAI-TLTVQGDHVP----NHV----GPPVSCNAVKLVDVPEMEY 506
Cdd:PRK07008 300 IGGSAcPPA--MIRTFEDEYGVEVIHAWGMTEMSplGTLcKLKWKHSQLPldeqRKLlekqGRVIYGVDMKIVGDDGREL 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666501 507 -FANQNTGEVCVRGSNVFHGYYKDpeKTAEAIDseGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENI 583
Cdd:PRK07008 378 pWDGKAFGDLQVRGPWVIDRYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIENV 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
132-612 |
8.21e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 132 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLyDTLGP-DACAFIIRQT 204
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELvvallaVLKAGGAY------VPL-DPNYPaERLAYMLEDS 2099
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 205 DMQVVIVEDDGKAAMLLEKAPRSLkiivaikpirqtTLERarsrgiqifsfiDVEKLGAKGNHPEVPPTAEDLCTVCYTS 284
Cdd:PRK12316 2100 GAALLLTQRHLLERLPLPAGVARL------------PLDR------------DAEWADYPDTAPAVQLAGENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 285 GTTGNPKGVMLTHGNVVAGvCSVILQMgdHRIRAGDVMVSFLPLAhmFErccengmyyvggcvGFYSGDIKELTNDLKML 364
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVAH-CQAAGER--YELSPADCELQFMSFS--FD--------------GAHEQWFHPLLNGARVL 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 365 kptVMPAVPRLLNRVYDKIQNdisaSGLKRGLFNMAMRAKEKEIArgvlRRNGCwdklvfkkvhqafGGNLRLMVVGSAP 444
Cdd:PRK12316 2217 ---IRDDELWDPEQLYDEMER----HGVTILDFPPVYLQQLAEHA----ERDGR-------------PPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 445 LAGNVLTFMRCALGCLVL-EGYGQTECTGAITLTVQGDHVPNH-----VGPPVSCNAVKLVDVpEMEYFANQNTGEVCVR 518
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYLfNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDA-DLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 519 GSNVFHGYYKDPEKTAE-----AIDSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKIENIYTLSQYVN 591
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAErfvpdPFSASGerLYRTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVR 2430
|
490 500
....*....|....*....|...
gi 24666501 592 QVYVYGESLKSC--IIAVVVPDT 612
Cdd:PRK12316 2431 EAVVVAQDGASGkqLVAYVVPDD 2453
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
127-581 |
8.26e-09 |
|
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: 58.48 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 127 LTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDACAFI 200
Cdd:cd12115 18 LVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLvvallaVLKAGAAY------VPLDPAYPPERLRFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 201 IRQTDMQVVIVeddgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevppTAEDLCTV 280
Cdd:cd12115 92 LEDAQARLVLT-------------------------------------------------------------DPDDLAYV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 281 CYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAgdVMVS------------FLPLAHmferccengmyyvGGCVg 348
Cdd:cd12115 111 IYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAG--VLAStsicfdlsvfelFGPLAT-------------GGKV- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 fysgdikELTNDLKMLkptvmPAVPR-----LLNRVYDKIQNDISASGLKRGL--FNMAMRAKEKEIARGVlrrngcWDK 421
Cdd:cd12115 175 -------VLADNVLAL-----PDLPAaaevtLINTVPSAAAELLRHDALPASVrvVNLAGEPLPRDLVQRL------YAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 422 LVFKKVHqafggNLrlmvvgsaplagnvltfmrcalgclvlegYGQTECTGAITLTV--QGDHVPNHVGPPVSCNAVKLV 499
Cdd:cd12115 237 LQVERVV-----NL-----------------------------YGPSEDTTYSTVAPvpPGASGEVSIGRPLANTQAYVL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 500 DvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWH------HTGDVGMWLPNGTLRIIDRRKHIFKLsQGE 573
Cdd:cd12115 283 D-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGF 360
|
....*...
gi 24666501 574 YIVPEKIE 581
Cdd:cd12115 361 RIELGEIE 368
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
136-581 |
8.64e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.56 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 136 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDg 215
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 216 kaamLLEKA----PRSLKIIVAIKP--IRQTTLERARSRGIQIFSfIDVEKLGAKGNHPEVPPTAEDlCTVCYTSGTTGN 289
Cdd:PRK12406 93 ----LLHGLasalPAGVTVLSVPTPpeIAAAYRISPALLTPPAGA-IDWEGWLAQQEPYDGPPVPQP-QSMIYTSGTTGH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 290 PKGVML---THGNVVAGVCSVILQMGDHR-IRAgdVMVSflPLAHmferCCENGMYYVGGCVG--------FysgDIKEL 357
Cdd:PRK12406 167 PKGVRRaapTPEQAAAAEQMRALIYGLKPgIRA--LLTG--PLYH----SAPNAYGLRAGRLGgvlvlqprF---DPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 358 TNDLKMLKPTVMPAVPRLLNRVydkiqndisasglkrglfnmaMRAKEKEIARGVLrrngcwdklvfkkvhqafgGNLRL 437
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRL---------------------LKLPEEVRAKYDV-------------------SSLRH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 438 MVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLTVQGDHV--PNHVGPPVSCNAVKLVD-----VPEMEyfanq 510
Cdd:PRK12406 276 VIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALshPGTVGKAAPGAELRFVDedgrpLPQGE----- 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666501 511 nTGEVCVR--GSNVFhGYYKDPEKTAEaIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 581
Cdd:PRK12406 350 -IGEIYSRiaGNPDF-TYHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIE 418
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
59-569 |
2.72e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 59 PERPLVPLenqsPLLEGPEQIHVSKFYKESKNGkfvsYITEnvRTLYQTFREGAYASNNGPCLGWREtltspyQWINYDE 138
Cdd:PRK12316 4518 PQRRLGEL----QLLEKAEQQRIVALWNRTDAG----YPAT--RCVHQLVAERARMTPDAVAVVFDE------EKLTYAE 4581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 139 ALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDACAFIIrqtdmqvvivE 212
Cdd:PRK12316 4582 LNRRANRLAHALIARGVGPEVLVGIAMERSAEMmvgllaVLKAGGAY------VPLDPEYPRERLAYMM----------E 4645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 213 DDGkAAMLLEKApRSLKIIVAIKPIRQTTLERARsrgiqifsfidvEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKG 292
Cdd:PRK12316 4646 DSG-AALLLTQS-HLLQRLPIPDGLASLALDRDE------------DWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKG 4711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 293 VMLTHGNVVAGVCSvilqMGD-HRIRAGDVMVSFLPLAhmferccengmyYVGGCVGFYSGdikeLTNDLKMLKPTVMPA 371
Cdd:PRK12316 4712 VAVSHGSLVNHLHA----TGErYELTPDDRVLQFMSFS------------FDGSHEGLYHP----LINGASVVIRDDSLW 4771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 372 VPRLLNRVYDKiqNDISASGLKRGLFNMAMRAKEKEIARGVLRrngcwdklvfkkvHQAFGGNlrLMVVGSAPLAgnvlt 451
Cdd:PRK12316 4772 DPERLYAEIHE--HRVTVLVFPPVYLQQLAEHAERDGEPPSLR-------------VYCFGGE--AVAQASYDLA----- 4829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 452 fMRCALGCLVLEGYGQTECTGAITLTVQGDHVPN-----HVGPPVSCNAVKLVDVpEMEYFANQNTGEVCVRGSNVFHGY 526
Cdd:PRK12316 4830 -WRALKPVYLFNGYGPTETTVTVLLWKARDGDACgaaymPIGTPLGNRSGYVLDG-QLNPLPVGVAGELYLGGEGVARGY 4907
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24666501 527 YKDPEKTAE-----AIDSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKL 569
Cdd:PRK12316 4908 LERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI 4957
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
274-582 |
3.58e-08 |
|
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: 56.41 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 274 AEDLCTVCYTSGTTGNPKGVMLTHGNVVaGVCSVilqmgdHRiragdvmvsflplaHMFERCCE-NGMYYVGgcVGFYSG 352
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEW------HR--------------PYFGVTPAdKSLVYAS--FSFDAS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 353 DIKELTNDLKMLKPTVMPAVPRL----LNRVYDkiQNDISASGLKRGLFNMAMRAKEKeiargvlrrngcwdklvfkkvh 428
Cdd:cd17645 160 AWEIFPHLTAGAALHVVPSERRLdldaLNDYFN--QEGITISFLPTGAAEQFMQLDNQ---------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 429 qafggNLRLMVVGsaplaGNVLTFMRcALGCLVLEGYGQTECTGAIT-LTVQGDHVPNHVGPPVSCNAVKLVDvpemEYF 507
Cdd:cd17645 216 -----SLRVLLTG-----GDKLKKIE-RKGYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD----EAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 508 ANQN---TGEVCVRGSNVFHGYYKDPEKTAEA------IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPE 578
Cdd:cd17645 281 QLQPigvAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPG 359
|
....
gi 24666501 579 KIEN 582
Cdd:cd17645 360 EIEP 363
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
435-582 |
4.13e-08 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 56.32 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 435 LRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLTVQGDHV-PNHVGPPVSCNAVKLVDV------PEMEyf 507
Cdd:cd05928 293 LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGMKIkPGSMGKASPPYDVQIIDDngnvlpPGTE-- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 508 anqntGEVCVRGSNV-----FHGYYKDPEKTAEAIDSEGWhHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIEN 582
Cdd:cd05928 370 -----GDIGIRVKPIrpfglFSGYVDNPEKTAATIRGDFY-LTGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVES 442
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
123-298 |
5.98e-08 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 56.05 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 123 WRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIR 202
Cdd:cd17634 74 YEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 203 QTDMQVVIVEDDG-KAAMLLEKAPRSLKIIVAIKPIRQTTLERARSR---GIQIFSFIDVEKLGAKGN--HPEVPPTAED 276
Cdd:cd17634 154 DSSSRLLITADGGvRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGsdiDWQEGRDLWWRDLIAKASpeHQPEAMNAED 233
|
170 180
....*....|....*....|..
gi 24666501 277 LCTVCYTSGTTGNPKGVMLTHG 298
Cdd:cd17634 234 PLFILYTSGTTGKPKGVLHTTG 255
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-569 |
1.24e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 55.55 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 71 PLLEGPEQihvsKFYKESKNGKFVSYITEnvRTLYQTFREGAYASNNGPCLGWREtltspyQWINYDEALLRAKNFGAGM 150
Cdd:PRK12467 3070 PTLAAHER----RQVLHAWNATAAAYPSE--RLVHQLIEAQVARTPEAPALVFGD------QQLSYAELNRRANRLAHRL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 151 LALGARPKQLIGIYSQNRPEWI------LYEQGCYsfslvvVPLYDTLGPDACAFIIRQTDMQVVIVEddgkaAMLLEKA 224
Cdd:PRK12467 3138 IAIGVGPDVLVGVAVERSVEMIvallavLKAGGAY------VPLDPEYPRERLAYMIEDSGVKLLLTQ-----AHLLEQL 3206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 225 PRSlkiivaikpirqttlerarsRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGnVVAGV 304
Cdd:PRK12467 3207 PAP--------------------AGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHG-ALANH 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 305 CSVILQMgdHRIRAGDVMVSFLPLAhmFERCCEN--GMYYVGGCVGFYSGDIkeltndlkmlkptvmpavprllnRVYDK 382
Cdd:PRK12467 3266 LCWIAEA--YELDANDRVLLFMSFS--FDGAQERflWTLICGGCLVVRDNDL-----------------------WDPEE 3318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 383 IQNDISASGLKRGLFNMAMRAKEKEIARGvlrrngcwdklvfkkvhqAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVL 462
Cdd:PRK12467 3319 LWQAIHAHRISIACFPPAYLQQFAEDAGG------------------ADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGL 3380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 463 -EGYGQTECTGAITL-TVQGDHVPNH----VGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE- 535
Cdd:PRK12467 3381 tNGYGPTEAVVTVTLwKCGGDAVCEApyapIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAEr 3459
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24666501 536 ----AIDSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKL 569
Cdd:PRK12467 3460 fvadPFSGSGgrLYRTGDLARYRADGVIEYLGRIDHQVKI 3499
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
226-610 |
2.43e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 53.75 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 226 RSLKIIVAIKP-----IRQTTLERArsrGIQIFSFIDVEKLGAKGNHPEV--PPTAEDLCTVCYTSGTTGNPKGVMLTHG 298
Cdd:PRK04813 90 RIEMIIEVAKPsliiaTEELPLEIL---GIPVITLDELKDIFATGNPYDFdhAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 299 NVVAGVCSVIlqmGDHRIRAGDVMVSFLPlahmferccengmyyvggcvgfYSGDI-------------------KELTN 359
Cdd:PRK04813 167 NLVSFTNWML---EDFALPEGPQFLNQAP----------------------YSFDLsvmdlyptlasggtlvalpKDMTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 360 DLKMLKPTvMPAVPR-------------LLNRVYDKIQNdisaSGLKRGLFnmamrakekeiargvlrrngCWDKL---V 423
Cdd:PRK04813 222 NFKQLFET-LPQLPInvwvstpsfadmcLLDPSFNEEHL----PNLTHFLF--------------------CGEELphkT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 424 FKKVHQAFggnlrlmvvgsaPLAgnvltfmrcalgcLVLEGYGQTECTGAIT-------LTVQGDHVPnhVGPPVSCNAV 496
Cdd:PRK04813 277 AKKLLERF------------PSA-------------TIYNTYGPTEATVAVTsieitdeMLDQYKRLP--IGYAKPDSPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 497 KLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMwLPNGTLRIIDRRKHIFKLSqGE 573
Cdd:PRK04813 330 LIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GY 406
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 24666501 574 YIVPEKIENIYTLSQYVNQ---VYVYGESLKSCIIAVVVP 610
Cdd:PRK04813 407 RIELEEIEQNLRQSSYVESavvVPYNKDHKVQYLIAYVVP 446
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
142-583 |
2.71e-07 |
|
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: 53.59 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 142 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgkaamLL 221
Cdd:cd05915 33 RARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN-----LL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 222 EKAPRSLKIIVAI--KPIRQTTLERarsrgiqifsFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGN 299
Cdd:cd05915 108 PLVEAIRGELKTVqhFVVMDEKAPE----------GYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 300 VVAGVCSVILqMGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFysgdIKELTNDlkmlkptvmpavprllNRV 379
Cdd:cd05915 178 LVLHSLAASL-VDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVL----PGPRLDP----------------ASL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 380 YDKI-QNDISASGLKRGLFNMAMRAKEKeiargvlrrngcwdklvfkkVHQAFGGNLRLMVVGSAPlaGNVLTFMRCALG 458
Cdd:cd05915 237 VELFdGEGVTFTAGVPTVWLALADYLES--------------------TGHRLKTLRRLVVGGSAA--PRSLIARFERMG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 459 CLVLEGYGQTECTGAIT----------------LTVQGDHVPNHVGppvscNAVKLVDVPEMEYFANQNTGEV-CVRGSN 521
Cdd:cd05915 295 VEVRQGYGLTETSPVVVqnfvkshleslseeekLTLKAKTGLPIPL-----VRLRVADEEGRPVPKDGKALGEvQLKGPW 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666501 522 VFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENI 583
Cdd:cd05915 370 ITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENA 430
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
254-589 |
3.40e-07 |
|
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: 53.17 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 254 SFIdVEKLGAKGnhpeVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhRIRAGDVMVSFLPlAHMFE 333
Cdd:cd17648 78 QFI-LEDTGARV----VITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF--GRDNGDEAVLFFS-NYVFD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 334 RCCENgMyyvggCVGFYSGdikeltNDLKMLKPTVMPAVPRLlnrvYDKIQND----ISASGLKRGLFNMAMRAKEKeia 409
Cdd:cd17648 150 FFVEQ-M-----TLALLNG------QKLVVPPDEMRFDPDRF----YAYINREkvtyLSGTPSVLQQYDLARLPHLK--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 410 rgvlrrngcwdklvfkkvhqafggnlRLMVVGSApLAGNVLTFMRCALGCLVLEGYGQTECTgaITLTVQ----GDHVPN 485
Cdd:cd17648 211 --------------------------RVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETT--VTNHKRffpgDQRFDK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 486 HVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGW-------HHTGDVGMW 551
Cdd:cd17648 262 SLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfQTEQERArgrnarlYKTGDLVRW 340
|
330 340 350
....*....|....*....|....*....|....*...
gi 24666501 552 LPNGTLRIIDRRKHIFKLsQGEYIVPEKIENiyTLSQY 589
Cdd:cd17648 341 LPSGELEYLGRNDFQVKI-RGQRIEPGEVEA--ALASY 375
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
134-330 |
3.53e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 53.34 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 213
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DGKAAmlLEKAPRSLKIivaikPIRQTTLERARsrGIQIFSFIDVEKLGAkgNHPEVPP------TAEDLCTVCYTSGTT 287
Cdd:PRK08279 143 ELVEA--FEEARADLAR-----PPRLWVAGGDT--LDDPEGYEDLAAAAA--GAPTTNPasrsgvTAKDTAFYIYTSGTT 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24666501 288 GNPKGVMLTH------GNVVAGVCsvilqmgdhRIRAGDVMVSFLPLAH 330
Cdd:PRK08279 212 GLPKAAVMSHmrwlkaMGGFGGLL---------RLTPDDVLYCCLPLYH 251
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-597 |
7.57e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 52.14 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 136 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDG 215
Cdd:cd05973 3 FGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 216 KAamllekaprslkiivaikpirqttlerarsrgiqifsfidveKLgakgnhpevpptAEDLCTVCYTSGTTGNPKGVML 295
Cdd:cd05973 83 RH------------------------------------------KL------------DSDPFVMMFTSGTTGLPKGVPV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 296 THGNVVAGVCSVILQMGdhrIRAGDVmvsflplahmFERCCENGMYYvggcvGFYSGdikeLTNDLKMLKPTVMPAVPRL 375
Cdd:cd05973 109 PLRALAAFGAYLRDAVD---LRPEDS----------FWNAADPGWAY-----GLYYA----ITGPLALGHPTILLEGGFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 376 LNRVYDKIQndisasglKRGLFNMAMrakekeiARGVLRrngcwdKLVFKKVHQAFGGNLRLMVVGSA--PLAGNVLTFM 453
Cdd:cd05973 167 VESTWRVIE--------RLGVTNLAG-------SPTAYR------LLMAAGAEVPARPKGRLRRVSSAgePLTPEVIRWF 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 454 RCALGCLVLEGYGQTEcTGAITLTVQGDHVPNHVGP---PVSCNAVKLVDVPEMEYFANQnTGEVCVRGSNV----FHGY 526
Cdd:cd05973 226 DAALGVPIHDHYGQTE-LGMVLANHHALEHPVHAGSagrAMPGWRVAVLDDDGDELGPGE-PGRLAIDIANSplmwFRGY 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666501 527 YKDPEKTAEAidseGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYVYG 597
Cdd:cd05973 304 QLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
102-305 |
1.12e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.47 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 102 RTLYQTFREGAYASNNGPCLGWREtltspyQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYE 175
Cdd:PRK12467 1574 RLVHQLIEDQAAATPEAVALVFGE------QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMvvgllaILKA 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 176 QGCYsfslvvVPLYDTLGPDACAFIIRQTDMQVVIVEddgkaAMLLEKAPrslkiivAIKPIRQTTLErarsrgiQIFSF 255
Cdd:PRK12467 1648 GGAY------VPLDPEYPRERLAYMIEDSGIELLLTQ-----SHLQARLP-------LPDGLRSLVLD-------QEDDW 1702
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24666501 256 IDveklGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVC 305
Cdd:PRK12467 1703 LE----GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLC 1748
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
267-614 |
3.57e-06 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 50.39 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 267 HPEVPPTAEDLCTVCYTSGTTGNPKGVML-THGNVVAGVCSVI----LQMGDHRIRAGDV-------MVSFLPLAHmfer 334
Cdd:cd05967 222 VDCVPVAATDPLYILYTSGTTGKPKGVVRdNGGHAVALNWSMRniygIKPGDVWWAASDVgwvvghsYIVYGPLLH---- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 335 ccenGMYYVggcvgFYSGdikeltndlkmlKPTVMPAvPRLLNRVYDKIQndisasglKRGLFN--MAMRAKEKEIARGv 412
Cdd:cd05967 298 ----GATTV-----LYEG------------KPVGTPD-PGAFWRVIEKYQ--------VNALFTapTAIRAIRKEDPDG- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 413 lrrngcwdklvfKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTE--------CTGAITLTVQgdhvP 484
Cdd:cd05967 347 ------------KYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTEtgwpitanPVGLEPLPIK----A 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 485 NHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRG---SNVFHGYYKDPE--KTAEAIDSEGWHHTGDVGMWLPNGTLRI 559
Cdd:cd05967 411 GSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLplpPGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFI 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666501 560 IDRRKHIF-----KLSQGEyivpekIENIYTLSQYVNQVYVYG--ESLKSCI-IAVVVPDTDV 614
Cdd:cd05967 490 MGRTDDVInvaghRLSTGE------MEESVLSHPAVAECAVVGvrDELKGQVpLGLVVLKEGV 546
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
275-595 |
5.34e-06 |
|
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: 49.36 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 275 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAhmFERCCENgMYyvggcVGFYSGdi 354
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYG---ITSSDRVLQFASIA--FDVAAEE-IY-----VTLLSG-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 355 keltNDLKMLKPTVMPAVPRLLnrvyDKI-QNDISASGLKRGLFNMAMRAKEKEIARGVlrrngcwdklvfkkvhqafgG 433
Cdd:cd17644 173 ----ATLVLRPEEMRSSLEDFV----QYIqQWQLTVLSLPPAYWHLLVLELLLSTIDLP--------------------S 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 434 NLRLMVVGSAPLAGNVLTFMRCALGCLV--LEGYGQTECTGAITL-------TVQGDHVPnhVGPPVSCNAVKLVD---- 500
Cdd:cd17644 225 SLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEATIAATVcrltqltERNITSVP--IGRPIANTQVYILDenlq 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 501 -VPEmeyfanQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHH--------TGDVGMWLPNGTLRIIDRRKHIFKLsQ 571
Cdd:cd17644 303 pVPV------GVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-R 375
|
330 340
....*....|....*....|....
gi 24666501 572 GEYIVPEKIENIYTLSQYVNQVYV 595
Cdd:cd17644 376 GFRIELGEIEAVLSQHNDVKTAVV 399
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
214-328 |
5.47e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.04 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 214 DGKAAMLLEKAPRSLKIIVAIkpirqttlERARSRGIQIFSFIDVEK-LGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKG 292
Cdd:PRK10252 544 DDRLKMMLEDARPSLLITTAD--------QLPRFADVPDLTSLCYNApLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKG 615
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24666501 293 VMLTHGNVVagvcSVILQMGDH-RIRAGDVM---------VS----FLPL 328
Cdd:PRK10252 616 VMVGQTAIV----NRLLWMQNHyPLTADDVVlqktpcsfdVSvwefFWPF 661
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
272-608 |
5.54e-06 |
|
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: 49.30 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 272 PTAEDLcTVCYTSGTTGNPKGVMLTHG----------NVVAGVCSVILQMGDHRIRAGD-VMVSFLPLAHmferccenGM 340
Cdd:cd05924 1 RSADDL-YILYTGGTTGMPKGVMWRQEdifrmlmggaDFGTGEFTPSEDAHKAAAAAAGtVMFPAPPLMH--------GT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 341 YYVGGCVGFYSGDiKELTNDLKMLKPTVMPAVPRllNRVydkiqNDISASGLKrglfnMAMRAKEKeiargvLRRNGCWD 420
Cdd:cd05924 72 GSWTAFGGLLGGQ-TVVLPDDRFDPEEVWRTIEK--HKV-----TSMTIVGDA-----MARPLIDA------LRDAGPYD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 421 KlvfkkvhqafgGNLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTGAITLTVQGDhvPNHVGPPVSCNA-VKL 498
Cdd:cd05924 133 L-----------SSLFAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSGHSAGS--GPETGPFTRANPdTVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 499 VD-----VPEmeyfANQNTGEVCVRGsNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlS 570
Cdd:cd05924 200 LDddgrvVPP----GSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-T 273
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24666501 571 QGEYIVPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVV 608
Cdd:cd05924 274 GGEKVFPEEVEEALKSHPAVYDVLVVGrpdERWGQEVVAVV 314
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
257-569 |
1.27e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.01 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 257 DVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVI--LQMGDHRIRAG------DVMV-SFLP 327
Cdd:PRK05691 3851 EVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVpyLALSEADVIAQtasqsfDISVwQFLA 3930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 328 lAHMFerccengmyyvGGCVGFYSGDI----KELTNDLKMLKPTVMPAVPRLLNRvydkiqndisasglkrglfnmaMRA 403
Cdd:PRK05691 3931 -APLF-----------GARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQG----------------------MLA 3976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 404 KEkeiargvlrrngcwdklvfkkvHQAFGGnLRLMV-VGSA---PLAGNVLtfMRCALGCLVlEGYGQTECTGAITL--- 476
Cdd:PRK05691 3977 ED----------------------RQALDG-LRWMLpTGEAmppELARQWL--QRYPQIGLV-NAYGPAECSDDVAFfrv 4030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 477 ---TVQGDHVPnhVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI-------DSEGWHHTG 546
Cdd:PRK05691 4031 dlaSTRGSYLP--IGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTG 4107
|
330 340
....*....|....*....|...
gi 24666501 547 DVGMWLPNGTLRIIDRRKHIFKL 569
Cdd:PRK05691 4108 DLARRRSDGVLEYVGRIDHQVKI 4130
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
244-583 |
2.00e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.84 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 244 RARSRGIQIFsfiDVEKLGAKGNHPEVPPTA-EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRirAGDVM 322
Cdd:PRK05851 123 RAVDSSVTVH---DLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDA--ATDVG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 323 VSFLPLAHmferccENGMYYVggCVGFYSGdiKELtndlkMLKPT-VMPAVP-RLLNRvydkiqndISASGlkrglfnmA 400
Cdd:PRK05851 198 CSWLPLYH------DMGLAFL--LTAALAG--APL-----WLAPTtAFSASPfRWLSW--------LSDSR--------A 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 401 MRAKEKEIARGVLRRNGcwdklvfKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCL------VLEGYGQTECTGAI 474
Cdd:PRK05851 247 TLTAAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFgfdagaAAPSYGLAESTCAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 475 TLTVQG-----DHVPNHVGPPVSCNAVKLVDVPEMEY----------FANQNTGEVCVRGSNVFHGYYKDPektaeAIDS 539
Cdd:PRK05851 320 TVPVPGiglrvDEVTTDDGSGARRHAVLGNPIPGMEVrispgdgaagVAGREIGEIEIRGASMMSGYLGQA-----PIDP 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24666501 540 EGWHHTGDVGmWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENI 583
Cdd:PRK05851 395 DDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
276-599 |
2.04e-05 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 47.01 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVAgvcSVILQMGDHRIRAGDVMVSFLPLAH-MFERCCENGMYYVGGCVGFYSGDI 354
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIE---SFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 355 KELTNDLKMLKPTVMPAVPRLLNRVYdKIQNDISAsglkrglfnmamrakekeiARGVLRRNGCWDKLVFKKVHQAFggn 434
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALA-RTLEPESK-------------------IKSIFSSGQKLFESTKKKLKNIF--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 435 lrlmvvgsaPLAgNVLTFmrcalgclvlegYGQTECTGAITLTVQGDHVPNHVGPPvsCNAVKLvdvpEMEYFANQNTGE 514
Cdd:cd17633 135 ---------PKA-NLIEF------------YGTSELSFITYNFNQESRPPNSVGRP--FPNVEI----EIRNADGGEIGK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 515 VCVRGSNVFHGYYKdpektAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVY 594
Cdd:cd17633 187 IFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAI 260
|
....*
gi 24666501 595 VYGES 599
Cdd:cd17633 261 VVGIP 265
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
465-618 |
2.09e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 47.68 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 465 YGQTECTGAI-TLT----VQGDhvpNHVGPPVSCNAVKLVdvpemeyfaNQNTGEVCVRGSNVFHGYYkdPEKtaeaIDS 539
Cdd:PRK07445 261 YGMTETASQIaTLKpddfLAGN---NSSGQVLPHAQITIP---------ANQTGNITIQAQSLALGYY--PQI----LDS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 540 EGWHHTGDVGMWLPNGTLRIIDR--RKHIfklSQGEYIVPEKIENIYTLSQYVNQVYVYGesLKSC-----IIAVVVPDT 612
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAILATGLVQDVCVLG--LPDPhwgevVTAIYVPKD 397
|
170
....*....|.
gi 24666501 613 DV-----LKQW 618
Cdd:PRK07445 398 PSisleeLKTA 408
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
276-613 |
2.94e-05 |
|
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: 46.96 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 276 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVilqMGDHRIRAGDVMVSFLPLAHMFER-CCENGMYYVGGCV------- 347
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF---AGSGGALPSDVLYTCLPLYHSTALiVGWSACLASGATLvirkkfs 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 348 --GFYSGDIKEltndlkmlKPTVMPAVPRLLnrvydkiqndisasglkRGLFNmamrAKEKEIARGvlrrngcwdklvfK 425
Cdd:cd05940 159 asNFWDDIRKY--------QATIFQYIGELC-----------------RYLLN----QPPKPTERK-------------H 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 426 KVHQAFGGNLRLMVVGSAPLAGNVLTfmrcalgclVLEGYGQTECT-GAITLtvqgDHVPNHVG------PPVSCNAVKL 498
Cdd:cd05940 197 KVRMIFGNGLRPDIWEEFKERFGVPR---------IAEFYAATEGNsGFINF----FGKPGAIGrnpsllRKVAPLALVK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 499 VDVPEMEYFANQN----------TGEVCVRGSNV--FHGYYkDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLRII 560
Cdd:cd05940 264 YDLESGEPIRDAEgrcikvprgePGLLISRINPLepFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFV 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24666501 561 DRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVYGeslksciiaVVVPDTD 613
Cdd:cd05940 343 DRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG---------VQVPGTD 385
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
124-622 |
3.59e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 47.06 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 124 RETLTspyqWINYDEallRAKNFGAGMLALGARPKQLIGIYSQNRPEWILyeqgcysfSLVV-------VPLYDT--LGP 194
Cdd:PRK13382 66 LGTLT----WRELDE---RSDALAAALQALPIGEPRVVGIMCRNHRGFVE--------ALLAanrigadILLLNTsfAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 195 DACAFIIRQtdmQVVIVEDDGKAAMLLEKA----PRSLKIIVAIKPIRQTTlerarsrgiqifsfidVEKLGAKGNHPEV 270
Cdd:PRK13382 131 ALAEVVTRE---GVDTVIYDEEFSATVDRAladcPQATRIVAWTDEDHDLT----------------VEVLIAAHAGQRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 271 PPTAEDLCTVCYTSGTTGNPKGVMLThGNVVAGVCSVILQmgdhRI--RAGDVMVSFLPLAHMFerccengmyyvggcvG 348
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRS-GPGGIGTLKAILD----RTpwRAEEPTVIVAPMFHAW---------------G 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 349 F----YSGDIK-----------ELTNDL-KMLKPTVMPAVPRLLNRVYDkIQNDISASGLKRGLfnmamrakekeiargv 412
Cdd:PRK13382 252 FsqlvLAASLActivtrrrfdpEATLDLiDRHRATGLAVVPVMFDRIMD-LPAEVRNRYSGRSL---------------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 413 lrrngcwdklvfkKVHQAFGGNLRLMVVgsaplagnvLTFMRcALGCLVLEGYGQTEcTGAITLTVQGD--HVPNHVGPP 490
Cdd:PRK13382 315 -------------RFAAASGSRMRPDVV---------IAFMD-QFGDVIYNNYNATE-AGMIATATPADlrAAPDTAGRP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 491 VSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYykDPEKTAEAIDseGWHHTGDVGMWLPNGTLRIIDRRKHIFkLS 570
Cdd:PRK13382 371 AEGTEIRILD-QDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMI-VS 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666501 571 QGEYIVPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVVVPDTDV------LKQWATEN 622
Cdd:PRK13382 445 GGENVYPIEVEKTLATHPDVAEAAVIGvddEQYGQRLAAFVVLKPGAsatpetLKQHVRDN 505
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
269-330 |
7.55e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.88 E-value: 7.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666501 269 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAH 330
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE---GQEGDRGVSWLPFFH 232
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
282-330 |
1.20e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.32 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 24666501 282 YTSGTTGNPKGVMLTHGNVVAGVCSVILQ-MGDH--RIRAGDVMVSFLPLAH 330
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFEQLMSDyFGDTggVPPPDTTVVSWLPFYH 218
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
270-348 |
1.69e-04 |
|
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: 44.97 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 270 VPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgvCSVILQM-GdhrIRAGDVMVSFLPLAHMferccENGMYYVGGCVG 348
Cdd:cd05938 139 AHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ--CSGFLSLcG---VTADDVIYITLPLYHS-----SGFLLGIGGCIE 208
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
134-298 |
2.46e-04 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 44.16 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 134 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLV--VVplYDTLGPDACAFIIRQTDMQVVIV 211
Cdd:TIGR02188 89 ITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIhsVV--FGGFSAEALADRINDAGAKLVIT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 212 EDD----GKAAML-------LEKAPRSLK-IIVaikpIRQTtlerarsrGIQIFSFI---DV--EKLGAKGNhPEVPPT- 273
Cdd:TIGR02188 167 ADEglrgGKVIPLkaivdeaLEKCPVSVEhVLV----VRRT--------GNPVVPWVegrDVwwHDLMAKAS-AYCEPEp 233
|
170 180
....*....|....*....|....*..
gi 24666501 274 --AEDLCTVCYTSGTTGNPKGVMLTHG 298
Cdd:TIGR02188 234 mdSEDPLFILYTSGSTGKPKGVLHTTG 260
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
184-302 |
4.10e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 43.73 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 184 VVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgkaamLLEKAPR----SLKIIVAIKpirqttlerarSRGIQIFSFIDVE 259
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVLITTPA-----LLERKPAddlpSLKHVLLVG-----------EDVEEGPGTLDFN 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24666501 260 KLGAKGN-HPEVPPT-AEDLCTVCYTSGTTGNPKGVMLTHGNVVA 302
Cdd:PRK04319 188 ALMEQASdEFDIEWTdREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
270-565 |
5.10e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.19 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 270 VPPTAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQMgdhrIRAGDVM------VSFLPLAH-------MFERCC 336
Cdd:PRK12476 188 VELDTDDVSHLQYTSGSTRPPVGVEITH----RAVGTNLVQM----ILSIDLLdrnthgVSWLPLYHdmglsmiGFPAVY 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 337 engmyyvGGCVGFYSGD---------IKELTNDLKMLKptVMPAVPrllNRVYD-KIQNDISASGLKRGLFNMAMRAKEK 406
Cdd:PRK12476 260 -------GGHSTLMSPTafvrrpqrwIKALSEGSRTGR--VVTAAP---NFAYEwAAQRGLPAEGDDIDLSNVVLIIGSE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 407 EIARGVLRrngcwdklVFKKVHQAFG------------GNLRLMVVGSAPLA-GNVLTFMRCALGclvlEGYGqtectga 473
Cdd:PRK12476 328 PVSIDAVT--------TFNKAFAPYGlprtafkpsygiAEATLFVATIAPDAePSVVYLDREQLG----AGRA------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666501 474 itLTVQGDHvPNHVgPPVSCNAVK------LVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKT-------------- 533
Cdd:PRK12476 389 --VRVAADA-PNAV-AHVSCGQVArsqwavIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlae 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24666501 534 ----AEAIDSEGWHHTGDVGMWLpNGTL----RI-----IDRRKH 565
Cdd:PRK12476 465 gshaDGAADDGTWLRTGDLGVYL-DGELyitgRIadlivIDGRNH 508
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
264-298 |
1.14e-03 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 42.16 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|....*...
gi 24666501 264 KGNHPEVPPT---AEDLCTVCYTSGTTGNPKGVMLTHG 298
Cdd:cd05966 217 AKQSPECEPEwmdSEDPLFILYTSGSTGKPKGVVHTTG 254
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
272-303 |
1.17e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 41.95 E-value: 1.17e-03
10 20 30
....*....|....*....|....*....|..
gi 24666501 272 PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAG 303
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTAS 63
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
262-298 |
1.90e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.66 E-value: 1.90e-03
10 20 30
....*....|....*....|....*....|....*..
gi 24666501 262 GAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHG 298
Cdd:PRK00174 232 GASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTG 268
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
268-330 |
4.30e-03 |
|
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: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24666501 268 PEVPPTAED------LCTVcYTSGTTGNPKGVMLTHGN---VVAGVCSVIlqmgdhRIRAGDVMVSFLPLAH 330
Cdd:cd05939 92 STEPPSQDDvnfrdkLFYI-YTSGTTGLPKAAVIVHSRyyrIAAGAYYAF------GMRPEDVVYDCLPLYH 156
|
|
| |
