|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
7-600 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 822.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 7 HFVNRIREQAKLLLNETALRYHTPSGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAV 86
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 87 VVPIYATSAAKQVEYILNNADVKILFVGDQEEYNCTLEIIDACPQIQKIVTMkDNVDLKNHPKACDWQTFLLEGSPLQ-Q 165
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVL-DPRGLRDDPRLLSLDELLALGREVAdP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 166 TALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLSHIFERAWVAYVLH 245
Cdd:COG1022 171 AELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL---PLGPGDRTLSFLPLAHVFERTVSYYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 246 RGAVNCYLEDTNRVREALSEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAIAVGQKRFQFISQKKPIPFVLR 325
Cdd:COG1022 248 AGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKSPSLLLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 326 QQYALADKLVLSKLRQLLGGRIRMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGA 405
Cdd:COG1022 328 LKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 406 EVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVG 485
Cdd:COG1022 408 EVKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 486 KDKFIEQIAVIADAKKYVSALIVPCFNSLEEYAKQLNIKYHDRLELIKHSDILQMFEQRINDLQKELPSFEQIKKFTLLP 565
Cdd:COG1022 488 ASPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYTSYAELAQDPEVRALIQEEVDRANAGLSRAEQIKRFRLLP 567
|
570 580 590
....*....|....*....|....*....|....*
gi 1178481066 566 QAFTTKMEEITPTLKLRRKVILERYKAQIEAMYKE 600
Cdd:COG1022 568 KEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
32-586 |
0e+00 |
|
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: 581.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 32 GWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKIL 111
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 112 FVGDqeeynctleiidacpqiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqkqLTDLFTLIYTSGTTG 191
Cdd:cd05907 82 FVED-------------------------------------------------------------PDDLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 192 EPKGVMLDYANLAHQLKAHDEAFTTLNVsqyDSSLSFLPLSHIFE-RAWVAYVLHRGAVNCYLEDTNRVREALSEIRPTL 270
Cdd:cd05907 101 RPKGVMLSHRNILSNALALAERLPATEG---DRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 271 MCAVPRFYEKIYTAVwdKVQKAPLFRRMIFNWAIavgqkrfqfisqkkpipfvlrqqyaladklvlsklrqllGGRIRMM 350
Cdd:cd05907 178 FLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAV---------------------------------------GGRLRFA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 351 PCGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKIGENNEILVRGGMVMRGYYKKP 430
Cdd:cd05907 217 ASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDGEILVRGPNVMLGYYKNP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 431 QETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVSALIVPC 510
Cdd:cd05907 297 EATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPD 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 511 FNSLEEYAKQLNIKYHDRLELIKHSDILQMFEQRINDLQKELPSFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVI 586
Cdd:cd05907 377 PEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
61-599 |
5.72e-131 |
|
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: 394.66 E-value: 5.72e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 61 DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDqeeyncTLEIIDacpqiqkivtmkd 140
Cdd:cd05927 33 SFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA------GVKVYS------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 141 nvdlknhpkacdWQTFLLEGSPLQQTALQARLEqkqltDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTTLN-V 219
Cdd:cd05927 94 ------------LEEFEKLGKKNKVPPPPPKPE-----DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 220 SQYDSSLSFLPLSHIFERAWVAYVLHRGA-VNCYLEDTNRVREALSEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRM 298
Cdd:cd05927 157 NPTDVYISYLPLAHIFERVVEALFLYHGAkIGFYSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 299 IFNWAIAVGQKRFQ-FISQKKPIpfvlrqqyalADKLVLSKLRQLLGGRIRMMPCGGAKLEPNIGLFFHSI-GINVKLGY 376
Cdd:cd05927 237 LFNFALNYKLAELRsGVVRASPF----------WDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVAlGCPVLEGY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 377 GMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI-----------GENN--EILVRGGMVMRGYYKKPQETADSFTEDGFL 443
Cdd:cd05927 307 GQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdvpemnydakDPNPrgEVCIRGPNVFSGYYKDPEKTAEALDEDGWL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 444 KTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKK-YVSALIVPCFNSLEEYAKQLN 522
Cdd:cd05927 387 HTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKsFLVAIVVPDPDVLKEWAASKG 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 523 IKYHDRLELIKHSDILQMFEQRINDLQKE--LPSFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVILERYKAQIEAMYK 599
Cdd:cd05927 467 GGTGSFEELCKNPEVKKAILEDLVRLGKEngLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
33-590 |
1.50e-118 |
|
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: 363.67 E-value: 1.50e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 33 WENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILF 112
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 113 VGDQEEYNCTLEIIDACPQIQKIVTMkDNVDLKNH--PKACDWQTFLLEGSPLQQT---ALQARLEQKQLTDLFTLIYTS 187
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYC-DPRGMRKYddPRLISFEDVVALGRALDRRdpgLYEREVAAGKGEDVAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 188 GTTGEPKGVMLDYANLAHQLKAHDEAFTTLNVSQYdssLSFLPLSHIFERAWV--AYVLHRGAVNCyLEDTNRVREALSE 265
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEY---VSVLPLPWIGEQMYSvgQALVCGFIVNF-PEEPETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 266 IRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAIAVGQKRFQFISQKKPIPFVLRQQYALADKLVLSKLRQLLG- 344
Cdd:cd17641 244 IGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPLRDRLGf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 345 GRIRMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKIGENNEILVRGGMVMR 424
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILVRSPGVFV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 425 GYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVS 504
Cdd:cd17641 404 GYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLT 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 505 ALIVPCFNSLEEYAKQLNIKYHDRLELIKHSDILQMFEQRINDLQKELPSFEQIKKFTLLPQAFTTKMEEITPTLKLRRK 584
Cdd:cd17641 484 AFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELTRTRKVRRG 563
|
....*.
gi 1178481066 585 VILERY 590
Cdd:cd17641 564 VIAEKY 569
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
36-586 |
1.29e-104 |
|
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: 324.31 E-value: 1.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgd 115
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 116 qeeynctleiidacpqiqkivtmkdnvdlKNHPKacdwqtfllegsplqqtalqarleqkqltDLFTLIYTSGTTGEPKG 195
Cdd:cd17640 84 -----------------------------ENDSD-----------------------------DLATIIYTSGTTGNPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 196 VMLDYANLAHQLKahdeafttlNVSQY------DSSLSFLPLSHIFERAWVAYVLHRGAVNCY------LEDtnrvreaL 263
Cdd:cd17640 106 VMLTHANLLHQIR---------SLSDIvppqpgDRFLSILPIWHSYERSAEYFIFACGCSQAYtsirtlKDD-------L 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 264 SEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAiavgqkrfqfisqkkpipfvlrqqyaladklvlsklrqLL 343
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF--------------------------------------LS 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 344 GGRIRMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI-----------GEN 412
Cdd:cd17640 212 GGIFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIvdpegnvvlppGEK 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 413 NEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQ 492
Cdd:cd17640 292 GIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQ 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 493 IAVIADAKKYVSALIVPCFNSLEEYAKQLNIKY-HDRLELIKHSDILQMFEQRINDLQKELP---SFEQIKKFTLLPQAF 568
Cdd:cd17640 372 IMVVGQDQKRLGALIVPNFEELEKWAKESGVKLaNDRSQLLASKKVLKLYKNEIKDEISNRPgfkSFEQIAPFALLEEPF 451
|
570
....*....|....*...
gi 1178481066 569 tTKMEEITPTLKLRRKVI 586
Cdd:cd17640 452 -IENGEMTQTMKIKRNVV 468
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
32-598 |
1.55e-99 |
|
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: 315.07 E-value: 1.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 32 GWENISWHQFQQDLDTFSYALLanHIGVQD--KIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVK 109
Cdd:cd05933 5 KWHTLTYKEYYEACRQAAKAFL--KLGLERfhGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 110 ILFVGDQEEYNCTLEIIDACPQIQKIVTMKDnvDLKNH-PKACDWQTFLLEGSPLQQTALQARLEQKQLTDLFTLIYTSG 188
Cdd:cd05933 83 ILVVENQKQLQKILQIQDKLPHLKAIIQYKE--PLKEKePNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 189 TTGEPKGVMLDYANLAHQLKAHDEAFTTLNVSQYDSSL-SFLPLSHIFER---AWVAyVLHRGAVncYLEDTNRVR---- 260
Cdd:cd05933 161 TTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVvSYLPLSHIAAQildIWLP-IKVGGQV--YFAQPDALKgtlv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 261 EALSEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAIAVGQKRFQFISQKKPIPFVlrqQYALADKLVLSKLR 340
Cdd:cd05933 238 KTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPL---FYRLAKKLVFKKVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 341 QLLG-GRIRMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETTA--TVScwEEGHFEPNSIGTLMPGAEVKIGENN---- 413
Cdd:cd05933 315 KALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGphTIS--NPQAYRLLSCGKALPGCKTKIHNPDadgi 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 414 -EILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKD-KFIE 491
Cdd:cd05933 393 gEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIIS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 492 QIAVIADAKKYVSALI-VPCFNSLE-------------EYAKQLNIKYHDRLELIKHSD--ILQMFEQRINDLQKELPSF 555
Cdd:cd05933 473 NAMLIGDKRKFLSMLLtLKCEVNPEtgepldelteeaiEFCRKLGSQATRVSEIAGGKDpkVYEAIEEGIKRVNKKAISN 552
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1178481066 556 EQ-IKKFTLLPQAFTTKMEEITPTLKLRRKVILERYKAQIEAMY 598
Cdd:cd05933 553 AQkIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
34-590 |
1.38e-92 |
|
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: 294.38 E-value: 1.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFV 113
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 114 GDQEEYNCTLEIIdacPQIQKIVTMKDNVDLKNHPKacdWQTFLLEGSPLQQTALQARLEqkqltdLFTLIYTSGTTGEP 193
Cdd:cd05932 85 GKLDDWKAMAPGV---PEGLISISLPPPSAANCQYQ---WDDLIAQHPPLEERPTRFPEQ------LATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 194 KGVMLDYANLAHqlkAHDEAFTTLNVSQYDSSLSFLPLSHIFERAWVAY-VLHRGAVNCYLEDTNRVREALSEIRPTLMC 272
Cdd:cd05932 153 KGVMLTFGSFAW---AAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGgSLYGGVLVAFAESLDTFVEDVQRARPTLFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 273 AVPRFYEKIYTAVWDKVQKAPLFRRMifnwaiavgqkrfqfisqkkPIPFVlrqqyalaDKLVLSKLRQLLG-GRIRMMP 351
Cdd:cd05932 230 SVPRLWTKFQQGVQDKIPQQKLNLLL--------------------KIPVV--------NSLVKRKVLKGLGlDQCRLAG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 352 CGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKIGENNEILVRGGMVMRGYYKKPQ 431
Cdd:cd05932 282 CGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 432 ETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVSALIVPcf 511
Cdd:cd05932 362 ATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVL-- 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 512 nSLEEYAKQLNikyHDRLELikhsdiLQMFEQRINDLQKELPSFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVILERY 590
Cdd:cd05932 440 -SEEARLRADA---FARAEL------EASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
51-600 |
1.63e-92 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 298.17 E-value: 1.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEeYNCTLEIIDACP 130
Cdd:PLN02736 94 GLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQT-LNTLLSCLSEIP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 131 QIQKIVTMK-DNVDLKNHPkacdwQTFLLEGSPLQQTALQARLEQKQL-----TDLFTLIYTSGTTGEPKGVMLDYANLA 204
Cdd:PLN02736 173 SVRLIVVVGgADEPLPSLP-----SGTGVEIVTYSKLLAQGRSSPQPFrppkpEDVATICYTSGTTGTPKGVVLTHGNLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 205 HQLkahdeAFTTLNVSQY--DSSLSFLPLSHIFERAWVAYVLHRG-AVNCYLEDTNRVREALSEIRPTLMCAVPRFYEKI 281
Cdd:PLN02736 248 ANV-----AGSSLSTKFYpsDVHISYLPLAHIYERVNQIVMLHYGvAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 282 YTAVWDKVQKAPLFRRMIFNwaIAVGQKRFQFISQKKPIPfvlrqqyaLADKLVLSKLRQLLGGRIRMMPCGGAKLEPNI 361
Cdd:PLN02736 323 YDGITNAVKESGGLKERLFN--AAYNAKKQALENGKNPSP--------MWDRLVFNKIKAKLGGRVRFMSSGASPLSPDV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 362 GLFFH-SIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVK---IGENN-----------EILVRGGMVMRGY 426
Cdd:PLN02736 393 MEFLRiCFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKlvdVPEMNytsedqpyprgEICVRGPIIFKGY 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 427 YKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADA-KKYVSA 505
Cdd:PLN02736 473 YKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSlNSSLVA 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 506 LIVPCFNSLEEYAKQLNIKYHDRLELIKHSDILQMFEQRINDLQKE--LPSFEQIKKFTLLPQAFTTKMEEITPTLKLRR 583
Cdd:PLN02736 553 VVVVDPEVLKAWAASEGIKYEDLKQLCNDPRVRAAVLADMDAVGREaqLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKR 632
|
570
....*....|....*..
gi 1178481066 584 KVILERYKAQIEAMYKE 600
Cdd:PLN02736 633 PQAKAYFAKAISDMYAE 649
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
31-586 |
4.41e-90 |
|
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: 287.57 E-value: 4.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 31 SGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKI 110
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 111 LFvgdqeeynctleiidacpqiqkivtmkdnvdlknhpkaCDwqtflleGSPlqqtalqarleqkqlTDLFTLIYTSGTT 190
Cdd:cd17639 81 IF--------------------------------------TD-------GKP---------------DDLACIMYTSGST 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 191 GEPKGVMLDYANLAHQLKAHDEafttlNVSQY----DSSLSFLPLSHIFERAWVAYVLHRGAVNCY-----LEDTNRVRE 261
Cdd:cd17639 101 GNPKGVMLTHGNLVAGIAGLGD-----RVPELlgpdDRYLAYLPLAHIFELAAENVCLYRGGTIGYgsprtLTDKSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 262 A--LSEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAIAVGQKRfqfisqkkpipfvLRQQY--ALADKLVLS 337
Cdd:cd17639 176 KgdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKA-------------LKEGPgtPLLDELVFK 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 338 KLRQLLGGRIRMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI------GE 411
Cdd:cd17639 243 KVRAALGGRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLvdweegGY 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 412 NN-------EILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKV 484
Cdd:cd17639 323 STdkppprgEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIY 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 485 GKDKFIEQIAVIAD-AKKYVSALIVPCFNSLEEYAKQLNIKYHDRLELIKHSDILQMFEQRINDLQKE--LPSFEQIKKF 561
Cdd:cd17639 403 RSNPLVNNICVYADpDKSYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETARAagLEKFEIPQGV 482
|
570 580
....*....|....*....|....*
gi 1178481066 562 TLLPQAFTTKMEEITPTLKLRRKVI 586
Cdd:cd17639 483 VLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
12-470 |
4.65e-90 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 284.59 E-value: 4.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 12 IREQAKLLLNETALryhTPSGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIY 91
Cdd:pfam00501 1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 92 ATSAAKQVEYILNNADVKILFVGDqeeyNCTLEIIDACPQIQKIVTMKDNVDLKNHPKacdwqTFLLEGSPLQQTALQAR 171
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDD----ALKLEELLEALGKLEVVKLVLVLDRDPVLK-----EEPLPEEAKPADVPPPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 172 LEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTT-LNVSQYDSSLSFLPLSHIFERAWVAY-VLHRGAV 249
Cdd:pfam00501 149 PPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgFGLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 250 NCYLE-----DTNRVREALSEIRPTLMCAVPRFYEKIYtavwdkvqKAPLFRRMIFnwaiavgqkrfqfisqkkpipfvl 324
Cdd:pfam00501 229 VVLPPgfpalDPAALLELIERYKVTVLYGVPTLLNMLL--------EAGAPKRALL------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 325 rqqyaladklvlsklrqllgGRIRMMPCGGAKLEPNIGLFFHSIGIN-VKLGYGMTETTATVSC---WEEGHFEPNSIGT 400
Cdd:pfam00501 277 --------------------SSLRLVLSGGAPLPPELARRFRELFGGaLVNGYGLTETTGVVTTplpLDEDLRSLGSVGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 401 LMPGAEVKI-----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKT 469
Cdd:pfam00501 337 PLPGTEVKIvddetgepvppGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
.
gi 1178481066 470 S 470
Cdd:pfam00501 417 G 417
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
49-583 |
2.27e-84 |
|
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: 271.24 E-value: 2.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 49 SYALLANHIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEeynctleii 126
Cdd:cd05914 19 KFALLLKINGVGtgDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDED--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 127 dacpqiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqkqltDLFTLIYTSGTTGEPKGVMLDYANLAHQ 206
Cdd:cd05914 90 ----------------------------------------------------DVALINYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 207 LKAHDEaftTLNVSQYDSSLSFLPLSHIFERAW-VAYVLHRGAVNCYLEDTNRVR---EALSEIRPTLMCAVPRFYEKIY 282
Cdd:cd05914 118 VDGVKE---VVLLGKGDKILSILPLHHIYPLTFtLLLPLLNGAHVVFLDKIPSAKiiaLAFAQVTPTLGVPVPLVIEKIF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 283 tavwdKVQKAPLFRRMIFNWAIAVgqkrfqfisqkkpIPFVLRQQyaladKLVLSKLRQLLGGRIRMMPCGGAKLEPNIG 362
Cdd:cd05914 195 -----KMDIIPKLTLKKFKFKLAK-------------KINNRKIR-----KLAFKKVHEAFGGNIKEFVIGGAKINPDVE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 363 LFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI------GENNEILVRGGMVMRGYYKKPQETADS 436
Cdd:cd05914 252 EFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIdspdpaTGEGEIIVRGPNVMKGYYKNPEATAEA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 437 FTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVsALIVPCFNSLEE 516
Cdd:cd05914 332 FDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLV-ALAYIDPDFLDV 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178481066 517 YAKQLNikyhDRLELIKhsdilqmfEQRINDLQKELPSFEQIKKFTLLPQAFttkmeEITPTLKLRR 583
Cdd:cd05914 411 KALKQR----NIIDAIK--------WEVRDKVNQKVPNYKKISKVKIVKEEF-----EKTPKGKIKR 460
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
62-605 |
8.20e-77 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 257.05 E-value: 8.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 62 KIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQE-----EYNCtleiidACPQIQKIV 136
Cdd:PLN02430 103 RVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKikellEPDC------KSAKRLKAI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 137 TMKDNVDLKNHPKACD-------WQTFLLEG--SPLQQTALQArleqkqlTDLFTLIYTSGTTGEPKGVMLDYANLAHQL 207
Cdd:PLN02430 177 VSFTSVTEEESDKASQigvktysWIDFLHMGkeNPSETNPPKP-------LDICTIMYTSGTSGDPKGVVLTHEAVATFV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 208 KAHD---EAFTTlNVSQYDSSLSFLPLSHIFERAWVAYVLHRGA-VNCYLEDTNRVREALSEIRPTLMCAVPRFYEKIYT 283
Cdd:PLN02430 250 RGVDlfmEQFED-KMTHDDVYLSFLPLAHILDRMIEEYFFRKGAsVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 284 AVWDKVQKAPLFRRMIFNwaiAVGQKRFQFI----SQKKPIPfvlrqqyaLADKLVLSKLRQLLGGRIRMMPCGGAKLEP 359
Cdd:PLN02430 329 GIQKALQELNPRRRLIFN---ALYKYKLAWMnrgySHKKASP--------MADFLAFRKVKAKLGGRLRLLISGGAPLST 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 360 NIGLFFHSIGIN-VKLGYGMTETTATVS-CWEEghfEPNSIGTLMPGA--------EVK------IGEN--NEILVRGGM 421
Cdd:PLN02430 398 EIEEFLRVTSCAfVVQGYGLTETLGPTTlGFPD---EMCMLGTVGAPAvynelrleEVPemgydpLGEPprGEICVRGKC 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 422 VMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADA-K 500
Cdd:PLN02430 475 LFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSfK 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 501 KYVSALIVPCFNSLEEYAKQLNIKyhDRLELIKHSDILQmfEQRINDLQ-----KELPSFEQIKKFTLLPQAFTTKMEEI 575
Cdd:PLN02430 554 SMLVAVVVPNEENTNKWAKDNGFT--GSFEELCSLPELK--EHILSELKstaekNKLRGFEYIKGVILETKPFDVERDLV 629
|
570 580 590
....*....|....*....|....*....|
gi 1178481066 576 TPTLKLRRKVILERYKAQIEAMYKEYTHKK 605
Cdd:PLN02430 630 TATLKKRRNNLLKYYQVEIDEMYRKLAEKR 659
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
61-600 |
3.59e-76 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 255.15 E-value: 3.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 61 DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgDQEEYNCTLEIIDAC-PQIQKIVTMK 139
Cdd:PLN02861 103 DRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFV-QESKISSILSCLPKCsSNLKTIVSFG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 140 D-----NVDLKNHPKAC-DWQTFLLEGSplqqtaLQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEA 213
Cdd:PLN02861 182 DvsseqKEEAEELGVSCfSWEEFSLMGS------LDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 214 F--TTLNVSQYDSSLSFLPLSHIFERAWVAYVLHRGA-VNCYLEDTNRVREALSEIRPTLMCAVPRFYEKIYTAVWDKVQ 290
Cdd:PLN02861 256 LkvTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGAsIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKIS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 291 KAPLFRRMIFNWAI--AVGQKRFQFiSQKKPIPFVlrqqyalaDKLVLSKLRQLLGGRIRMMPCGGAKLEPNIGLFFHSI 368
Cdd:PLN02861 336 SGGMLRKKLFDFAYnyKLGNLRKGL-KQEEASPRL--------DRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVT 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 369 GI-NVKLGYGMTETTAtvSCWEEGHFEPNSIGTL---MPGAEVKIGE-------------NNEILVRGGMVMRGYYKKPQ 431
Cdd:PLN02861 407 SCsVLSQGYGLTESCG--GCFTSIANVFSMVGTVgvpMTTIEARLESvpemgydalsdvpRGEICLRGNTLFSGYHKRQD 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 432 ETADSFTeDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADA-KKYVSALIVPC 510
Cdd:PLN02861 485 LTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSfESFLVAVVVPD 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 511 FNSLEEYAKQLNiKYHDRLELIKHSDILQMFEQRINDLQKE--LPSFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVILE 588
Cdd:PLN02861 564 RQALEDWAANNN-KTGDFKSLCKNLKARKYILDELNSTGKKlqLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLK 642
|
570
....*....|..
gi 1178481066 589 RYKAQIEAMYKE 600
Cdd:PLN02861 643 YYKDCIDQLYSE 654
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
57-599 |
1.39e-70 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 240.31 E-value: 1.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 57 IGVQD--KIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEeyncTLEIIDACP---Q 131
Cdd:PLN02614 99 VGVKDeaKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKK----ISELFKTCPnstE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 132 IQKIVTMKDNVDLKNHPKA-------CDWQTFLLEGSplqqtALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLD----- 199
Cdd:PLN02614 175 YMKTVVSFGGVSREQKEEAetfglviYAWDEFLKLGE-----GKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISnesiv 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 200 --YANLAHQLKAHDEAFTtlnvsQYDSSLSFLPLSHIFERAWV-AYVLHRGAVNCYLEDTNRVREALSEIRPTLMCAVPR 276
Cdd:PLN02614 250 tlIAGVIRLLKSANAALT-----VKDVYLSYLPLAHIFDRVIEeCFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 277 FYEKIYTAVWDKVQKAPLFRRMIFNWAIAvgqkrFQFISQKKPIPFVlrQQYALADKLVLSKLRQLLGGRIRMMPCGGAK 356
Cdd:PLN02614 325 VLDRVYSGLQKKLSDGGFLKKFVFDSAFS-----YKFGNMKKGQSHV--EASPLCDKLVFNKVKQGLGGNVRIILSGAAP 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 357 LEPNIGLFFHSIGI-NVKLGYGMTETTA-TVSCWEEGHFEPNSIGTLMPGAEVKIGE-------------NNEILVRGGM 421
Cdd:PLN02614 398 LASHVESFLRVVACcHVLQGYGLTESCAgTFVSLPDELDMLGTVGPPVPNVDIRLESvpemeydalastpRGEICIRGKT 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 422 VMRGYYKKPQETADSFTeDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADA-K 500
Cdd:PLN02614 478 LFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSfE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 501 KYVSALIVPCFNSLEEYAKQ--LNIKYHDRLELIKHSDILqMFEQRINDLQKELPSFEQIKKFTLLPQAFTTKMEEITPT 578
Cdd:PLN02614 557 SFLVAIANPNQQILERWAAEngVSGDYNALCQNEKAKEFI-LGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPT 635
|
570 580
....*....|....*....|.
gi 1178481066 579 LKLRRKVILERYKAQIEAMYK 599
Cdd:PLN02614 636 FKKKRPQLLKYYQSVIDEMYK 656
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
12-593 |
2.23e-65 |
|
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: 220.84 E-value: 2.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 12 IREQAKLLLNETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIY 91
Cdd:COG0318 5 LRRAAARHPDRPALVF----GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 92 ATSAAKQVEYILNNADVKILFVgdqeeynctleiidacpqiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqar 171
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 172 leqkqltdlFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLSHIFerAWVAYV---LHRGA 248
Cdd:COG0318 103 ---------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAL---GLTPGDVVLVALPLFHVF--GLTVGLlapLLAGA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 249 VNCYLE--DTNRVREALSEIRPTLMCAVPrfyekiytavwdkvqkaPLFRRMIfnwaiavgqkrfqfisqkkpipfvlrq 326
Cdd:COG0318 169 TLVLLPrfDPERVLELIERERVTVLFGVP-----------------TMLARLL--------------------------- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 327 QYALADKLVLSKLRQLLggrirmmpCGGAKLEPN-IGLFFHSIGINVKLGYGMTETTATVSCWEEGHFE--PNSIGTLMP 403
Cdd:COG0318 205 RHPEFARYDLSSLRLVV--------SGGAPLPPElLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGErrPGSVGRPLP 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 GAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKtSNGK 473
Cdd:COG0318 277 GVEVRIvdedgrelppGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMII-SGGE 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 474 YIAPQYIETKVGKDKFIEQIAVIA--DAKKY--VSALIVPcfnslEEYAKqlnikyHDRLELIKHsdilqmfeqrindLQ 549
Cdd:COG0318 355 NVYPAEVEEVLAAHPGVAEAAVVGvpDEKWGerVVAFVVL-----RPGAE------LDAEELRAF-------------LR 410
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1178481066 550 KELPSFEQIKKFTLLpqafttkmEEI--TPTLKLRRKVILERYKAQ 593
Cdd:COG0318 411 ERLARYKVPRRVEFV--------DELprTASGKIDRRALRERYAAG 448
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
7-600 |
1.17e-64 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 224.86 E-value: 1.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 7 HFVNRIREQAKLLLNETALRYHT-----------PSG----WE--------NISWHQFQQDLDTFSYALLAnhIGVQ--D 61
Cdd:PTZ00216 70 NFLQRLERICKERGDRRALAYRPvervekevvkdADGkertMEvthfnetrYITYAELWERIVNFGRGLAE--LGLTkgS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 62 KIAIFAHNMPRWTIADIGTMQVRAVVVPIYAT-------SAAKQVE---YILNNADVKIL--FVGDQEEYNCTLEIIDAC 129
Cdd:PTZ00216 148 NVAIYEETRWEWLASIYGIWSQSMVAATVYANlgedalaYALRETEckaIVCNGKNVPNLlrLMKSGGMPNTTIIYLDSL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 130 PqiqkivtmkDNVDLKNHpKACDWQTFLLEGSPLQQTALQARLEQKqltDLFTLI-YTSGTTGEPKGVMLDYANLAHQLK 208
Cdd:PTZ00216 228 P---------ASVDTEGC-RLVAWTDVVAKGHSAGSHHPLNIPENN---DDLALImYTSGTTGDPKGVMHTHGSLTAGIL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 209 AHDEAFTTL--NVSQYDSSLSFLPLSHIFERAWVAYVLHRGAVNCY------LEDTNRVREALSEIRPTLMCAVPRFYEK 280
Cdd:PTZ00216 295 ALEDRLNDLigPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGFgsprtlTDTFARPHGDLTEFRPVFLIGVPRIFDT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 281 IYTAVWDKVQKAPLFRRMIFNWAIavgQKRFQFISQKKPIPFVlrqqyalaDKLVLSKLRQLLGGRIRMMPCGGAKLEPN 360
Cdd:PTZ00216 375 IKKAVEAKLPPVGSLKRRVFDHAY---QSRLRALKEGKDTPYW--------NEKVFSAPRAVLGGRVRAMLSGGGPLSAA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 361 IGLFfhsigINVKL-----GYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKIGENN------------EILVRGGMVM 423
Cdd:PTZ00216 444 TQEF-----VNVVFgmviqGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEeykhtdtpeprgEILLRGPFLF 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 424 RGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFI--EQIAVIAD-AK 500
Cdd:PTZ00216 519 KGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVvpNGVCVLVHpAR 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 501 KYVSALIVPCFNSLEEYAKQLNIK--YHDrleLIKHSDILQMFEQRINDLQKEL--PSFEQIKKFTLLPQAFTTKMEEIT 576
Cdd:PTZ00216 599 SYICALVLTDEAKAMAFAKEHGIEgeYPA---ILKDPEFQKKATESLQETARAAgrKSFEIVRHVRVLSDEWTPENGVLT 675
|
650 660
....*....|....*....|....
gi 1178481066 577 PTLKLRRKVILERYKAQIEAMYKE 600
Cdd:PTZ00216 676 AAMKLKRRVIDERYADLIKELFAD 699
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
38-598 |
1.82e-63 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 221.91 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 38 WHQFQQDLD---TFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILfVG 114
Cdd:PLN02387 106 WITYGQVFErvcNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV-IC 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 115 DQEEYNCTLEIIDACPQIQKIVTMKDN--VDLKNHPKACDWQTFLLE--GSPLQQTALQARLEQKqlTDLFTLIYTSGTT 190
Cdd:PLN02387 185 DSKQLKKLIDISSQLETVKRVIYMDDEgvDSDSSLSGSSNWTVSSFSevEKLGKENPVDPDLPSP--NDIAVIMYTSGST 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 191 GEPKGVMLDYANLAHQLKAHDEAFTTLNVSqyDSSLSFLPLSHIFERAWVAYVLHRGAVNCY-----LEDT-NRVREA-- 262
Cdd:PLN02387 263 GLPKGVMMTHGNIVATVAGVMTVVPKLGKN--DVYLAYLPLAHILELAAESVMAAVGAAIGYgspltLTDTsNKIKKGtk 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 263 --LSEIRPTLMCAVPRFYEKIYTAVWDKVQKA-----PLF-----RRMIF---NWAIAVGQKRFqfisqkkpipfvlrqq 327
Cdd:PLN02387 341 gdASALKPTLMTAVPAILDRVRDGVRKKVDAKgglakKLFdiaykRRLAAiegSWFGAWGLEKL---------------- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 328 yaLADKLVLSKLRQLLGGRIRMMPCGGAKLEPNIGLFFH-SIGINVKLGYGMTETTA-----------------TVSC-- 387
Cdd:PLN02387 405 --LWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINiCLGAPIGQGYGLTETCAgatfsewddtsvgrvgpPLPCcy 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 388 -----WEEGHF----EPnsigtlMPGAEVKIGENNeilvrggmVMRGYYKKPQETADSFTEDG----FLKTGDAGEFDPQ 454
Cdd:PLN02387 483 vklvsWEEGGYlisdKP------MPRGEIVIGGPS--------VTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPD 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 455 GNLYITDRIKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADA-KKYVSALIVPCFNSLEEYAKQLNIKYHDRLELIK 533
Cdd:PLN02387 549 GCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPfHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCE 628
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178481066 534 HSDILQMFEQRINDLQKE--LPSFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVILERYKAQIEAMY 598
Cdd:PLN02387 629 KEEAVKEVQQSLSKAAKAarLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
34-509 |
1.11e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 193.86 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLAnhIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKIL 111
Cdd:PRK06187 30 RRTTYAELDERVNRLANALRA--LGVKkgDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 112 FVGdqEEYNCTLE-IIDACPQIQKIVTMKDnvdLKNHPKACDWQTF--LLEGSPlqqtalqARLEQKQLT--DLFTLIYT 186
Cdd:PRK06187 108 LVD--SEFVPLLAaILPQLPTVRTVIVEGD---GPAAPLAPEVGEYeeLLAAAS-------DTFDFPDIDenDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 187 SGTTGEPKGVMLDYANL-AHQLKAHdeafTTLNVSQYDSSLSFLPLSHIFerAW-VAYV-LHRGAVNCYLE--DTNRVRE 261
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLfLHSLAVC----AWLKLSRDDVYLVIVPMFHVH--AWgLPYLaLMAGAKQVIPRrfDPENLLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 262 ALSEIRPTLMCAVPrfyekiytAVWDKVQKAPLFRRMIFNwaiavgqkrfqfisqkkpipfvlrqqyaladklvlsklrq 341
Cdd:PRK06187 250 LIETERVTFFFAVP--------TIWQMLLKAPRAYFVDFS---------------------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 342 llggRIRMMPCGGAKLEPNIGLFFHS-IGINVKLGYGMTETTATVSC-WEEGHFEPN-----SIGTLMPGAEVKI----- 409
Cdd:PRK06187 282 ----SLRLVIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPVVSVlPPEDQLPGQwtkrrSAGRPLPGVEARIvdddg 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -------GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKtSNGKYIAPQYIET 482
Cdd:PRK06187 358 delppdgGEVGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELED 435
|
490 500 510
....*....|....*....|....*....|.
gi 1178481066 483 KVGKDKFIEQIAVIA--DAK--KYVSALIVP 509
Cdd:PRK06187 436 ALYGHPAVAEVAVIGvpDEKwgERPVAVVVL 466
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
35-496 |
7.22e-53 |
|
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: 188.19 E-value: 7.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 35 NISWHQFQQDLDTFSYALLAnhIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILF 112
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRK--LGLKkgDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 113 VgDQEEYNCTLEIIDACPQIQKIVTMKDNVDLKNHPkacdwQTFLlegSPLQQTALQARLEQKQL--TDLFTLIYTSGTT 190
Cdd:cd05911 88 T-DPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSI-----EDLL---SPTLGEEDEDLPPPLKDgkDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 191 GEPKGVMLDYANLAHQLKaHDEAFTTLNVSQYDSSLSFLPLSHIFERAWVAYVLHRGAvncyledtnrvrealseirPTL 270
Cdd:cd05911 159 GLPKGVCLSHRNLIANLS-QVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGA-------------------TVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 271 MCavPRFYEKiytavwdkvqkapLFRRMIfnwaiavgQK-RFQFISQKKPIpFVLRQQYALADKLVLSKLRqllggrirM 349
Cdd:cd05911 219 IM--PKFDSE-------------LFLDLI--------EKyKITFLYLVPPI-AAALAKSPLLDKYDLSSLR--------V 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 350 MPCGGAKLEPNIGLFFHSIGINVKL--GYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI-----------GENNEIL 416
Cdd:cd05911 267 ILSGGAPLSKELQELLAKRFPNATIkqGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIvdddgkdslgpNEPGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 417 VRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVI 425
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
179-510 |
4.12e-51 |
|
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: 179.40 E-value: 4.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPLSHIFERAWVAYVLHRGAVNCYLEDTN- 257
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA---LAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 258 -RVREALSEIRPTLMCAVPRFYEKIytavwdkvQKAPLFRRmifnwaiavgqkrfqfisqkkpipfvlrqqyaladkLVL 336
Cdd:cd04433 78 eAALELIEREKVTILLGVPTLLARL--------LKAPESAG------------------------------------YDL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 337 SKLRQLLggrirmmpCGGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSCW--EEGHFEPNSIGTLMPGAEVKI---- 409
Cdd:cd04433 114 SSLRALV--------SGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGppDDDARKPGSVGRPVPGVEVRIvdpd 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 ------GENNEILVRGGMVMRGYYKKPqETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKtSNGKYIAPQYIETK 483
Cdd:cd04433 186 ggelppGEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAV 263
|
330 340 350
....*....|....*....|....*....|.
gi 1178481066 484 VGKDKFIEQIAVIA--DAKK--YVSALIVPC 510
Cdd:cd04433 264 LLGHPGVAEAAVVGvpDPEWgeRVVAVVVLR 294
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
34-466 |
4.49e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 183.95 E-value: 4.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFV 113
Cdd:PRK07656 29 QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 114 GDQ---EEYnctlEIIDACPQIQKIVTMKDNVDLKNHPKACDWQTFLLEGSPLQQTALQARleqkqlTDLFTLIYTSGTT 190
Cdd:PRK07656 109 LGLflgVDY----SATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDP------DDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 191 GEPKGVMLDYANLahqLKAHDEAFTTLNVSQYDSSLSFLPLSHIF--ERAWVAyVLHRGAVnCYLE---DTNRVREALSE 265
Cdd:PRK07656 179 GRPKGAMLTHRQL---LSNAADWAEYLGLTEGDRYLAANPFFHVFgyKAGVNA-PLMRGAT-ILPLpvfDPDEVFRLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 266 IRPTLMCAVPRFYEKIYtavwDKVQKAplfrrmifnwAIAVGQKRFqFISQKKPIPFVLrqqyaladklvLSKLRQLLGG 345
Cdd:PRK07656 254 ERITVLPGPPTMYNSLL----QHPDRS----------AEDLSSLRL-AVTGAASMPVAL-----------LERFESELGV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 346 RIrmmpcggaklepniglffhsiginVKLGYGMTETTATVS-CWEEGHFE--PNSIGTLMPGAEVKI----------GEN 412
Cdd:PRK07656 308 DI------------------------VLTGYGLSEASGVTTfNRLDDDRKtvAGTIGTAIAGVENKIvnelgeevpvGEV 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 413 NEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKEL 466
Cdd:PRK07656 364 GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDM 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
34-496 |
1.48e-48 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 175.83 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFV 113
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 114 GDqeeynctleiidacpqiqkivtmkdnvdlknhpkacDWQTFLLEGSPLQQTAlqarleQKQLTDLFTLIYTSGTTGEP 193
Cdd:cd05936 103 AV------------------------------------SFTDLLAAGAPLGERV------ALTPEDVAVLQYTSGTTGVP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 194 KGVMLDYANLAHQLKAHDEAFTTLNVSQyDSSLSFLPLSHIFerAW-VAYVL--HRGAVNcYLEDTNRVREALSEI---R 267
Cdd:cd05936 141 KGAMLTHRNLVANALQIKAWLEDLLEGD-DVVLAALPLFHVF--GLtVALLLplALGATI-VLIPRFRPIGVLKEIrkhR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 268 PTLMCAVPRFYEKIYtavwdkvqKAPLFRRMIFNwaiavgqkrfqfisqkkpipfvlrqqyaladklvlsklrqllggRI 347
Cdd:cd05936 217 VTIFPGVPTMYIALL--------NAPEFKKRDFS--------------------------------------------SL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 348 RMMPCGGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSCWE-EGHFEPNSIGTLMPGAEVKI----------GENNEI 415
Cdd:cd05936 245 RLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPlDGPRKPGSIGIPLPGTEVKIvdddgeelppGEVGEL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 416 LVRGGMVMRGYYKKPQETADSFTeDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIAV 495
Cdd:cd05936 325 WVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKD-MIIVGGFNVYPREVEEVLYEHPAVAEAAV 402
|
.
gi 1178481066 496 I 496
Cdd:cd05936 403 V 403
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
36-509 |
3.35e-43 |
|
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: 160.47 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFvgd 115
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 116 qeeynctleiidacpqiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqkqlTDLFTLIYTSGTTGEPKG 195
Cdd:cd17631 98 --------------------------------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 196 VMLDYANLAHQLKAHdeaFTTLNVSQYDSSLSFLPLSHIFE-RAWVAYVLHRGAVNCYLE--DTNRVREALSEIRPTLMC 272
Cdd:cd17631 116 AMLTHRNLLWNAVNA---LAALDLGPDDVLLVVAPLFHIGGlGVFTLPTLLRGGTVVILRkfDPETVLDLIERHRVTSFF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 273 AVPrfyekiytAVWDKVQKAPLFRRmifnwaiavgqkrfqfisqkkpipfvlrqqyalADklvLSKLRQLLggrirmmpC 352
Cdd:cd17631 193 LVP--------TMIQALLQHPRFAT---------------------------------TD---LSSLRAVI--------Y 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 353 GGAKLEPNIGLFFHSIGINVKLGYGMTETTATVsCW--EEGHFE-PNSIGTLMPGAEVKI----------GENNEILVRG 419
Cdd:cd17631 221 GGAPMPERLLRALQARGVKFVQGYGMTETSPGV-TFlsPEDHRRkLGSAGRPVFFVEVRIvdpdgrevppGEVGEIVVRG 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 420 GMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIAVIA-- 497
Cdd:cd17631 300 PHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKD-MIISGGENVYPAEVEDVLYEHPAVAEVAVIGvp 377
|
490
....*....|....
gi 1178481066 498 DAK--KYVSALIVP 509
Cdd:cd17631 378 DEKwgEAVVAVVVP 391
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
53-477 |
1.62e-42 |
|
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: 160.09 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 53 LANHIGVQ-DKIAIFAHNMPRWTIADIGTMQVRAVVV---PIYaTSA--AKQVEyilnNADVKILFVgdqeeyncTLEII 126
Cdd:cd05904 49 LAKRGGRKgDVVLLLSPNSIEFPVAFLAVLSLGAVVTtanPLS-TPAeiAKQVK----DSGAKLAFT--------TAELA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 127 DACPQI-QKIVTMKDNVDlknHPKACDWQTFLLEGSPLQQTALQArleqkqlTDLFTLIYTSGTTGEPKGVMLDYANLAH 205
Cdd:cd05904 116 EKLASLaLPVVLLDSAEF---DSLSFSDLLFEADEAEPPVVVIKQ-------DDVAALLYSSGTTGRSKGVMLTHRNLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 206 QLkAHDEAFTTLNVSQYDSSLSFLPLSHIFERAWVAY-VLHRGAVNCYLE--DTNRVREALSEIRPTLMCAVPrfyekiy 282
Cdd:cd05904 186 MV-AQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALgLLRLGATVVVMPrfDLEELLAAIERYKVTHLPVVP------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 283 tavwdkvqkaPLFRRMIfnwaiavgqkrfqfisqKKPIpfvlrqqyalADKLVLSKLRQLLggrirmmpCGGAKLEPNIG 362
Cdd:cd05904 258 ----------PIVLALV-----------------KSPI----------VDKYDLSSLRQIM--------SGAAPLGKELI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 363 LFFHSIGINVKL--GYGMTETTA-TVSCW--EEGHFEPNSIGTLMPGAEVKI-----------GENNEILVRGGMVMRGY 426
Cdd:cd05904 293 EAFRAKFPNVDLgqGYGMTESTGvVAMCFapEKDRAKYGSVGRLVPNVEAKIvdpetgeslppNQTGELWIRGPSIMKGY 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1178481066 427 YKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAP 477
Cdd:cd05904 373 LNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAP 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
29-588 |
1.96e-40 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 154.01 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 29 TPSGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADV 108
Cdd:cd05926 8 VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 109 KILFVGDQEEYNC-------TLEIIDACPQIQKIVTMKDNVDLKNHPKACDWQTFLLEGSPlqqtalqarleqkqlTDLF 181
Cdd:cd05926 88 KLVLTPKGELGPAsraasklGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLP---------------DDLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 182 TLIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPLSHIfeRAWVAYVL----HRGAVNCyledtn 257
Cdd:cd05926 153 LILHTSGTTGRPKGVPLTHRNLAASATN---ITNTYKLTPDDRTLVVMPLFHV--HGLVASLLstlaAGGSVVL------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 258 rvrealseirPtlmcavPRFYEkiyTAVWDKVQKAPLfrrmifNWAIAVGQkrfqfISQkkpipfVLRQQYALADKLVLS 337
Cdd:cd05926 222 ----------P------PRFSA---STFWPDVRDYNA------TWYTAVPT-----IHQ------ILLNRPEPNPESPPP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 338 KLRqllggRIRmmpCGGAKLEPNIglfFHSI----GINVKLGYGMTETTATVSC--WEEGHFEPNSIG-------TLMP- 403
Cdd:cd05926 266 KLR-----FIR---SCSASLPPAV---LEALeatfGAPVLEAYGMTEAAHQMTSnpLPPGPRKPGSVGkpvgvevRILDe 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 -GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIET 482
Cdd:cd05926 335 dGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDG 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 483 KVGKDKFIEQIAVIA--DAkKY---VSALIVPCFNSleeyakqlnikYHDRLELIKHsdilqmfeqrindLQKELPSFEQ 557
Cdd:cd05926 414 VLLSHPAVLEAVAFGvpDE-KYgeeVAAAVVLREGA-----------SVTEEELRAF-------------CRKHLAAFKV 468
|
570 580 590
....*....|....*....|....*....|....
gi 1178481066 558 IKKFTL---LPQafttkmeeiTPTLKLRRKVILE 588
Cdd:cd05926 469 PKKVYFvdeLPK---------TATGKIQRRKVAE 493
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
34-542 |
6.46e-36 |
|
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: 142.59 E-value: 6.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLANH-IGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILF 112
Cdd:cd17632 66 ETITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 113 VgDQEEYNCTLEIIDACPQIQKIVTMKDNVDLKNHPKACDWQTFLLEGSPLQQTALQA------------RLEQKQLTD- 179
Cdd:cd17632 146 V-SAEHLDLAVEAVLEGGTPPRLVVFDHRPEVDAHRAALESARERLAAVGIPVTTLTLiavrgrdlppapLFRPEPDDDp 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 180 LFTLIYTSGTTGEPKGVMLDYANLAHqlkAHDEAFTTLNVSQYDSS-LSFLPLSHIFERAWVAYVLHRGAVNCYL--EDT 256
Cdd:cd17632 225 LALLIYTSGSTGTPKGAMYTERLVAT---FWLKVSSIQDIRPPASItLNFMPMSHIAGRISLYGTLARGGTAYFAaaSDM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 257 NRVREALSEIRPTLMCAVPRfyekiytaVWDkvqkaplfrrMIFnwaiavgqKRFQfisqkkpiPFVLRQQYALADKLVL 336
Cdd:cd17632 302 STLFDDLALVRPTELFLVPR--------VCD----------MLF--------QRYQ--------AELDRRSVAGADAETL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 337 SK-----LRQ-LLGGRIRMMPCGGAKLEPNIGLFFHS-IGINVKLGYGMTETTAT----------------VSCWEEGHF 393
Cdd:cd17632 348 AErvkaeLRErVLGGRLLAAVCGSAPLSAEMKAFMESlLDLDLHDGYGSTEAGAVildgvivrppvldyklVDVPELGYF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 394 ---EPNSIGtlmpgaevkigennEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDA-GEFDPQGNLYItDRIKELMKT 469
Cdd:cd17632 428 rtdRPHPRG--------------ELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVmAELGPDRLVYV-DRRNNVLKL 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178481066 470 SNGKYIAPQYIETKVGKDKFIEQIAVIAD-AKKYVSALIVPCFNSLEEY-AKQLNIKYHDRLELIKHSDILQMFE 542
Cdd:cd17632 493 SQGEFVTVARLEAVFAASPLVRQIFVYGNsERAYLLAVVVPTQDALAGEdTARLRAALAESLQRIAREAGLQSYE 567
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
53-508 |
2.00e-35 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 138.38 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 53 LANHI---GVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGdqeeynctleiid 127
Cdd:cd05935 14 LASFLsnkGVRkgDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 128 acpqiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQL 207
Cdd:cd05935 81 -----------------------------------------------SELDDLALIPYTSGTTGLPKGCMHTHFSAAANA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 208 KAHDEAFttlNVSQYDSSLSFLPLSHIferawvayvlhrgavncyledtnrvrealSEIRPTLMCAVPRFYEKIYTAVWD 287
Cdd:cd05935 114 LQSAVWT---GLTPSDVILACLPLFHV-----------------------------TGFVGSLNTAVYVGGTYVLMARWD 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 288 KVQKAPLFR--RMIFNWAIAvgqkrfqfisqkkPIPFVLRQQYALADKlVLSKLRQLLGGRIRMMPCGGAKLEPNIGLFF 365
Cdd:cd05935 162 RETALELIEkyKVTFWTNIP-------------TMLVDLLATPEFKTR-DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRF 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 366 HSiginvklGYGMTETTATV----------SCWEEGHFEPNS-IGTLMPGAEVKIGENNEILVRGGMVMRGYYKKPQETA 434
Cdd:cd05935 228 VE-------GYGLTETMSQThtnpplrpklQCLGIP*FGVDArVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 435 DSFTEDG---FLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVIADAKKY----VSALI 507
Cdd:cd05935 301 ESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVISVPDERvgeeVKAFI 379
|
.
gi 1178481066 508 V 508
Cdd:cd05935 380 V 380
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
21-509 |
4.56e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 139.32 E-value: 4.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 21 NETALRYHTPSgwenISWHQFQQDLDTFSyALLANHIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQ 98
Cdd:PRK08314 25 DKTAIVFYGRA----ISYRELLEEAERLA-GYLQQECGVRkgDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 99 VEYILNNADVKILFVGdQEEYNCTLEIIDACPQIQKIVT-MKDNVDLKNHPKACDWqtfLLEGSPLQ----------QTA 167
Cdd:PRK08314 100 LAHYVTDSGARVAIVG-SELAPKVAPAVGNLRLRHVIVAqYSDYLPAEPEIAVPAW---LRAEPPLQalapggvvawKEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 168 LQARLEQKQLT----DLFTLIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPLSHIferawvayv 243
Cdd:PRK08314 176 LAAGLAPPPHTagpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVG---SVLWSNSTPESVVLAVLPLFHV--------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 244 lhRGAVNC-----YLEDTnrvrealseirptlMCAVPRfyekiytavWDKVQKAPLFRRM-IFNWAiavgqkrfqfisqk 317
Cdd:PRK08314 244 --TGMVHSmnapiYAGAT--------------VVLMPR---------WDREAAARLIERYrVTHWT-------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 318 kPIP-----FVLRQQYALADklvLSKLRQLLGGRIRMMPCGGAKLEPNIGLFFHSiginvklGYGMTETTATVscweegH 392
Cdd:PRK08314 285 -NIPtmvvdFLASPGLAERD---LSSLRYIGGGGAAMPEAVAERLKELTGLDYVE-------GYGLTETMAQT------H 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 393 FEP------NSIGtlMP-------------GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTE-DG--FLKTGDAGE 450
Cdd:PRK08314 348 SNPpdrpklQCLG--IPtfgvdarvidpetLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGR 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178481066 451 FDPQGNLYITDRIKELMKTSNGKyIAPQYIETKVGKDKFIEQIAVIA--DAKK--YVSALIVP 509
Cdd:PRK08314 426 MDEEGYFFITDRLKRMINASGFK-VWPAEVENLLYKHPAIQEACVIAtpDPRRgeTVKAVVVL 487
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
34-509 |
6.82e-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: 137.04 E-value: 6.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLAN-HIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKIlf 112
Cdd:cd05941 10 DSITYADLVARAARLANRLLALgKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 113 vgdqeeynctleIIDACpqiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqkqltdlfTLIYTSGTTGE 192
Cdd:cd05941 88 ------------VLDPA----------------------------------------------------LILYTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 193 PKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLSHIferawvayvlHrGAVN---CYLEDTNRV---------R 260
Cdd:cd05941 104 PKGVVLTHANLAANVRALVDAW---RWTEDDVLLHVLPLHHV----------H-GLVNallCPLFAGASVeflpkfdpkE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 261 EALSEIRP--TLMCAVPRFYEKiytavwdkvqkaplfrrmifnwaiavgqkrfqfisqkkpipfvLRQQYALADKLVLSK 338
Cdd:cd05941 170 VAISRLMPsiTVFMGVPTIYTR-------------------------------------------LLQYYEAHFTDPQFA 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 339 LRQLLGgRIRMMPCGGAKLEPNIGLFFHSIGINVKLG-YGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI-------- 409
Cdd:cd05941 207 RAAAAE-RLRLMVSGSAALPVPTLEEWEAITGHTLLErYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIvdeetgep 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 ---GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKYIAPQYIETKVGK 486
Cdd:cd05941 286 lprGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLA 365
|
490 500
....*....|....*....|....*..
gi 1178481066 487 DKFIEQIAVI----ADAKKYVSALIVP 509
Cdd:cd05941 366 HPGVSECAVIgvpdPDWGERVVAVVVL 392
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
34-496 |
6.98e-34 |
|
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: 135.73 E-value: 6.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFV 113
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 114 gDQEEYNCTLEIIDACPQIQKIVTMKDNVDLKNhpKACDwQTFLLEGSPLQQTALQARLEQKQLTDLFTLI-YTSGTTGE 192
Cdd:cd17642 123 -SKKGLQKVLNVQKKLKIIKTIIILDSKEDYKG--YQCL-YTFITQNLPPGFNEYDFKPPSFDRDEQVALImNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 193 PKGVMLDYANLAHQLKAHDEAFTTLNVSQYDSSLSFLPLSHIFERAWVAYVLHRGAvncyledtnrvrealseiRPTLMc 272
Cdd:cd17642 199 PKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGF------------------RVVLM- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 273 avPRFYEKIY-TAVWD-KVQKAPLFrrmifnwaiavgqkrfqfisqkkPIPFVLRQQYALADKLVLSKLRQLLggrirmm 350
Cdd:cd17642 260 --YKFEEELFlRSLQDyKVQSALLV-----------------------PTLFAFFAKSTLVDKYDLSNLHEIA------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 351 pCGGAKLEPNIG-LFFHSIGIN-VKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI-----------GENNEILV 417
Cdd:cd17642 308 -SGGAPLSKEVGeAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVvdldtgktlgpNERGELCV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 418 RGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:cd17642 387 KGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVA 464
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
182-604 |
7.83e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 137.54 E-value: 7.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 182 TLIYTSGTTGEPKGVMLDYANLAHQ---LKAHDeAFTTLNVSQYdssLSFLPLSHIFER--AWVAYVLhRGAVNCYLEDT 256
Cdd:PTZ00342 308 SIVYTSGTSGKPKGVMLSNKNLYNTvvpLCKHS-IFKKYNPKTH---LSYLPISHIYERviAYLSFML-GGTINIWSKDI 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 257 NRVREALSEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAIAVGqKRFQFISQKKPIpfvlrqqyalaDKL-- 334
Cdd:PTZ00342 383 NYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLR-KSNNNGGFSKFL-----------EGIth 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 335 VLSKLRQLLGGRIRMMPCGGAKLEPNIGLFFhSIGINVKL--GYGMTETTATVSCWEEGHFEPNSIG-TLMPGAEVKIGE 411
Cdd:PTZ00342 451 ISSKIKDKVNPNLEVILNGGGKLSPKIAEEL-SVLLNVNYyqGYGLTETTGPIFVQHADDNNTESIGgPISPNTKYKVRT 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 412 -----------NNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGkyiapQYI 480
Cdd:PTZ00342 530 wetykatdtlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQG-----EYI 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 481 ETKV-----------------GKDKFIEQIAVIAdAKKYVSALIVPCFNSLEEYAkqLNIK-YHDRL--ELIKHSDILQM 540
Cdd:PTZ00342 605 ETDMlnnlysqisfinfcvvyGDDSMDGPLAIIS-VDKYLLFKCLKDDNMLESTG--INEKnYLEKLtdETINNNIYVDY 681
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 541 FEQRINDLQKE--LPSFEQIKKFTLLPQAFTTKmEEITPTLKLRRKVILERYKAQIEAMYKEYTHK 604
Cdd:PTZ00342 682 VKGKMLEVYKKtnLNRYNIINDIYLTSKVWDTN-NYLTPTFKVKRFYVFKDYAFFIDQVKKIYKNK 746
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-497 |
3.31e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 128.95 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILfvgdqeeynctleiidacp 130
Cdd:cd05934 19 ALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 131 qiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqkqLTDLFTLIYTSGTTGEPKGVMLDYANLAH--QLK 208
Cdd:cd05934 80 ----------------------------------------------VVDPASILYTSGTTGPPKGVVITHANLTFagYYS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 209 AHDEAFTtlnvsQYDSSLSFLPLSHIFERAWVAYV-LHRGAvncyledtnrvREALseirptlmcaVPRFYEkiyTAVWD 287
Cdd:cd05934 114 ARRFGLG-----EDDVYLTVLPLFHINAQAVSVLAaLSVGA-----------TLVL----------LPRFSA---SRFWS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 288 KVQKAplfRRMIFNwaiAVGqkrfqfisqkKPIPFVLRQQYALADKlvlsklrqllGGRIRMMpCGGAKLEPNIGLFFHS 367
Cdd:cd05934 165 DVRRY---GATVTN---YLG----------AMLSYLLAQPPSPDDR----------AHRLRAA-YGAPNPPELHEEFEER 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 368 IGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI----------GENNEILVRG----GMvMRGYYKKPQET 433
Cdd:cd05934 218 FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIvdddgqelpaGEPGELVIRGlrgwGF-FKGYYNMPEAT 296
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 434 ADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:cd05934 297 AEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAAVVA 358
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
9-521 |
8.50e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 129.89 E-value: 8.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 9 VNRIREQAKLLLNETALRYhtpsgweniSWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVV 88
Cdd:PRK12583 28 VARFPDREALVVRHQALRY---------TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 89 PIYATSAAKQVEYILNNADVKILFVGDQEEYNCTLEIID--------------AC---PQIQKIVTMkdnvDLKNHPKAC 151
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQellpglaegqpgalACerlPELRGVVSL----APAPPPGFL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 152 DWQTFLLEGSPLQQTALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAfttLNVSQYDSSLSFLPL 231
Cdd:PRK12583 175 AWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAES---LGLTEHDRLCVPVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 232 SHIFER--AWVAYVLHRGAVNCYLE--DTNRVREALSEIRPTLMCAVPRFyekiytavwdkvqkaplfrrmifnwaiavg 307
Cdd:PRK12583 252 YHCFGMvlANLGCMTVGACLVYPNEafDPLATLQAVEEERCTALYGVPTM------------------------------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 308 qkrfqFISQkkpipfVLRQQYALADklvLSKLRQ-LLGGrirmMPCGGAKLEPNIGLFFHSigiNVKLGYGMTET----- 381
Cdd:PRK12583 302 -----FIAE------LDHPQRGNFD---LSSLRTgIMAG----APCPIEVMRRVMDEMHMA---EVQIAYGMTETspvsl 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 382 -TATVSCWEEghfEPNSIGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGE 450
Cdd:PRK12583 361 qTTAADDLER---RVETVGRTQPHLEVKVvdpdgatvprGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLAT 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178481066 451 FDPQGNLYITDRIKElMKTSNGKYIAPQYIEtkvgkDKFIEQIAVIAdakkyVSALIVPCfnslEEYAKQL 521
Cdd:PRK12583 438 MDEQGYVRIVGRSKD-MIIRGGENIYPREIE-----EFLFTHPAVAD-----VQVFGVPD----EKYGEEI 493
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
23-508 |
1.21e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 128.85 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 23 TALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYI 102
Cdd:PRK06145 19 AALVY----RDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 103 LNNADVKILFVGDQEEYNCTLE----IIDACPQiqkivtmKDNVDLKNHPKACdwqtfllegsplqqTALQARLEqkqlT 178
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAIVALEtpkiVIDAAAQ-------ADSRRLAQGGLEI--------------PPQAAVAP----T 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAfttLNVSQYDSSLSFLPLSHI--FERAWVAYVLHRGAVNCYLE-D 255
Cdd:PRK06145 150 DLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIA---LGLTASERLLVVGPLYHVgaFDLPGIAVLWVGGTLRIHREfD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 256 TNRVREALSEIRPTLMCAVPRFYEKIYTavwdkVQKAPLFRRMIFNWAIAVGQKRFQFisqkkpipfvlrqqyaladklv 335
Cdd:PRK06145 227 PEAVLAAIERHRLTCAWMAPVMLSRVLT-----VPDRDRFDLDSLAWCIGGGEKTPES---------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 336 lsklrqllggRIRMmpcggaklepniglfFHSIGINVKL--GYGMTETTATVSCWEEGHfEPNSIGTL---MPGAEVKI- 409
Cdd:PRK06145 280 ----------RIRD---------------FTRVFTRARYidAYGLTETCSGDTLMEAGR-EIEKIGSTgraLAHVEIRIa 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 ---------GENNEILVRGGMVMRGYYKKPQETADSFTeDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYI 480
Cdd:PRK06145 334 dgagrwlppNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKD-MIISGGENIASSEV 411
|
490 500 510
....*....|....*....|....*....|..
gi 1178481066 481 ETKVGKDKFIEQIAVIA--DAK--KYVSALIV 508
Cdd:PRK06145 412 ERVIYELPEVAEAAVIGvhDDRwgERITAVVV 443
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
51-475 |
6.50e-31 |
|
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: 126.59 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEEYncTLEII-DAC 129
Cdd:cd12119 41 ALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFLP--LLEAIaPRL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 130 PQIQKIVTMKDNVDLKNH--PKACDWQTFLLEGSPLqqtalqARLEQKQLTDLFTLIYTSGTTGEPKGVMLDY-ANLAHQ 206
Cdd:cd12119 119 PTVEHVVVMTDDAAMPEPagVGVLAYEELLAAESPE------YDWPDFDENTAAAICYTSGTTGNPKGVVYSHrSLVLHA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 207 LKAhdEAFTTLNVSQYDSSLSFLPLSHIfeRAW-VAYV-LHRGA--VncyLEDTNRVREALSEI----RPTLMCAVPrfy 278
Cdd:cd12119 193 MAA--LLTDGLGLSESDVVLPVVPMFHV--NAWgLPYAaAMVGAklV---LPGPYLDPASLAELiereGVTFAAGVP--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 279 ekiytAVWdkvqkaplfrRMIFnwaiavgqkrfqfisqkkpipfvlrqQYALADKLVLSKLRQLLggrirmmpCGGAKLE 358
Cdd:cd12119 263 -----TVW----------QGLL--------------------------DHLEANGRDLSSLRRVV--------IGGSAVP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 359 PNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPN-----------SIGTLMPGAEVKI-----------GEN-NEI 415
Cdd:cd12119 294 RSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNlsedeqlalraKQGRPVPGVELRIvdddgrelpwdGKAvGEL 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 416 LVRGGMVMRGYYKKPqETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKtSNGKYI 475
Cdd:cd12119 374 QVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWI 431
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-498 |
1.62e-29 |
|
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: 121.78 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 49 SYALLANHIGVQDKIAIFA--HNMPRWTIADI--GTMQVRAVVVPIYATSAAKQVEYILNNADVKILfvgdqeeynctle 124
Cdd:cd05922 7 ASALLEAGGVRGERVVLILpnRFTYIELSFAVayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIV------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 125 IIDAcpqiqkivTMKDNVDlKNHPKACDWQTFL-LEGSPLQQTALQARLEQKQltDLFTLIYTSGTTGEPKGVMLDYANL 203
Cdd:cd05922 74 LADA--------GAADRLR-DALPASPDPGTVLdADGIRAARASAPAHEVSHE--DLALLLYTSGSTGSPKLVRLSHQNL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 204 -------AHQLKAH--DEAFTTLNVSqYDSSLSFLpLSHIFERAwvAYVLHRGAVncyLEDTnrVREALSEIRPTLMCAV 274
Cdd:cd05922 143 lanarsiAEYLGITadDRALTVLPLS-YDYGLSVL-NTHLLRGA--TLVLTNDGV---LDDA--FWEDLREHGATGLAGV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 275 PRFYEKIYTAVWDKVQKAPLfrRMIFNWAIAVGQKRfqfisqkkpipfvlrqqyaladklvLSKLRQLL-GGRIRMMpcg 353
Cdd:cd05922 214 PSTYAMLTRLGFDPAKLPSL--RYLTQAGGRLPQET-------------------------IARLRELLpGAQVYVM--- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 354 gaklepniglffhsiginvklgYGMTETTATVSCW--EEGHFEPNSIGTLMPGAEVKI----------GENNEILVRGGM 421
Cdd:cd05922 264 ----------------------YGQTEATRRMTYLppERILEKPGSIGLAIPGGEFEIldddgtptppGEPGEIVHRGPN 321
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178481066 422 VMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVIAD 498
Cdd:cd05922 322 VMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAARSIGLIIEAAAVGL 397
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
30-600 |
2.14e-29 |
|
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: 122.54 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 30 PSGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVR---AVVVPIYATSAAK--QVEYILN 104
Cdd:cd05921 20 NGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaAPVSPAYSLMSQDlaKLKHLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 105 NADVKILFVGDQEEYNCTLEIIDAcpqiqkivTMKDNVDLKNHPKACDWQTF--LLEGSPLqqTALQARLEQKQLTDLFT 182
Cdd:cd05921 100 LLKPGLVFAQDAAPFARALAAIFP--------LGTPLVVSRNAVAGRGAISFaeLAATPPT--AAVDAAFAAVGPDTVAK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLA--HQLKAHDEAFTTLNVSQydsSLSFLPLSHIF-ERAWVAYVLHRGAvNCYLED---- 255
Cdd:cd05921 170 FLFTSGSTGLPKAVINTQRMLCanQAMLEQTYPFFGEEPPV---LVDWLPWNHTFgGNHNFNLVLYNGG-TLYIDDgkpm 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 256 ----TNRVREaLSEIRPTLMCAVPRFYEKIYTAVW-DKVQKAPLFRRMifnwaiavgqkRFQFISQKKPIPFVLRQQYAL 330
Cdd:cd05921 246 pggfEETLRN-LREISPTVYFNVPAGWEMLVAALEkDEALRRRFFKRL-----------KLMFYAGAGLSQDVWDRLQAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 331 ADKLVlsklrqllGGRIRMMPcggaklepniglffhsiginvklGYGMTET--TATVSCWeeghfePNS----IGTLMPG 404
Cdd:cd05921 314 AVATV--------GERIPMMA-----------------------GLGATETapTATFTHW------PTErsglIGLPAPG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 405 AEVKIGENN---EILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEF----DPQGNLYITDRIKELMKTSNGKYIAp 477
Cdd:cd05921 357 TELKLVPSGgkyEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVS- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 478 qyietkVG--KDKFIEQIA-VIADA------KKYVSALIVPCFNSLEEYAKQLNIkyhDRLELIKHSDILQMFEQRINDL 548
Cdd:cd05921 436 ------VGplRARAVAACApLVHDAvvagedRAEVGALVFPDLLACRRLVGLQEA---SDAEVLRHAKVRAAFRDRLAAL 506
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1178481066 549 QKEL-PSFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVILERYKAQIEAMYKE 600
Cdd:cd05921 507 NGEAtGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
21-481 |
2.77e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 122.53 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 21 NETALRYHTPSGWE-NISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQV 99
Cdd:COG0365 24 DKVALIWEGEDGEErTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 100 EYILNNADVKILFVGDQEEYNCTL--------EIIDACPQIQKIVTMKDNVDLKNHPKACDWQTFLLEGSP-LQQTALQA 170
Cdd:COG0365 104 ADRIEDAEAKVLITADGGLRGGKVidlkekvdEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAeFEPEPTDA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 171 rleqkqlTDLFTLIYTSGTTGEPKGVMLD----------YANLAHQLKAHDEAFTTlnvsqydSSLSFlplshIFERAWV 240
Cdd:COG0365 184 -------DDPLFILYTSGTTGKPKGVVHThggylvhaatTAKYVLDLKPGDVFWCT-------ADIGW-----ATGHSYI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 241 AY---------VLHRGAVNcyLEDTNRVREALSEIRPTLMCAVPRFYekiytavwdkvqkaplfrRMIFNWAIAVGQKRf 311
Cdd:COG0365 245 VYgpllngatvVLYEGRPD--FPDPGRLWELIEKYGVTVFFTAPTAI------------------RALMKAGDEPLKKY- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 312 qfisqkkpipfvlrqqyalaDklvLSKLRQLLggrirmmpCGGAKLEPNIGLFFHS-IGINVKLGYGMTETTAT-VSCWE 389
Cdd:COG0365 304 --------------------D---LSSLRLLG--------SAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIfISNLP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 390 EGHFEPNSIGTLMPGAEVKI----------GENNEILVRG---GMvMRGYYKKPQETADSF--TEDGFLKTGDAGEFDPQ 454
Cdd:COG0365 353 GLPVKPGSMGKPVPGYDVAVvdedgnpvppGEEGELVIKGpwpGM-FRGYWNDPERYRETYfgRFPGWYRTGDGARRDED 431
|
490 500
....*....|....*....|....*..
gi 1178481066 455 GNLYITDRIKELMKTSnGKYIAPQYIE 481
Cdd:COG0365 432 GYFWILGRSDDVINVS-GHRIGTAEIE 457
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
179-502 |
3.50e-28 |
|
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: 115.82 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLD----YANLAHQLKAhdeaftTLNVSQYDSSLSFLPLSHIFERAWVAYVL-HRGA--VNC 251
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLAnktfFAVPDILQKE------GLNWVVGDVTYLPLPATHIGGLWWILTCLiHGGLcvTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 252 YLEDTNRVREALSEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAIAVGQKRfqfisqkkpipfvlrqQYALA 331
Cdd:cd17635 76 ENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADV----------------RFIEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 332 DKLVlsklrqllggrirmmpcggaklepniglffhsigiNVKLGYGMTETTaTVSC--WEEGHFEPNSIGTLMPGAEVKI 409
Cdd:cd17635 140 TGLT-----------------------------------NTAQVYGLSETG-TALClpTDDDSIEINAVGRPYPGVDVYL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 ----------GENNEILVRGGMVMRGYYKKPQETADSFTeDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQY 479
Cdd:cd17635 184 aatdgiagpsASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDE 261
|
330 340
....*....|....*....|...
gi 1178481066 480 IEtkvgkdKFIEQIAVIADAKKY 502
Cdd:cd17635 262 VE------RIAEGVSGVQECACY 278
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
32-598 |
1.22e-27 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 117.67 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 32 GWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNmprwtiaDI-------GTMQVRAVVVPI---YATSAA--KQV 99
Cdd:PRK08180 66 GWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGN-------SIehallalAAMYAGVPYAPVspaYSLVSQdfGKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 100 EYILNNADVKILFVGDQEEYNCTLE-IIDACPQIqkivtmkdnVDLKNHPKACDWQTF--LLEGSPLqqTALQARLEQKQ 176
Cdd:PRK08180 139 RHVLELLTPGLVFADDGAAFARALAaVVPADVEV---------VAVRGAVPGRAATPFaaLLATPPT--AAVDAAHAAVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 177 LTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTTLnVSQYDSSLSFLPLSHIF-ERAWVAYVLHRGAvNCYLED 255
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFL-AEEPPVLVDWLPWNHTFgGNHNLGIVLYNGG-TLYIDD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 256 ----------TNRvreALSEIRPTLMCAVPRFYEKIYTAV-WDKVQKAPLFRR--MIFNWAIAVGQkrfqfisqkkpipF 322
Cdd:PRK08180 286 gkptpggfdeTLR---NLREISPTVYFNVPKGWEMLVPALeRDAALRRRFFSRlkLLFYAGAALSQ-------------D 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 323 VLRQQYALAdklvlsklRQLLGGRIRMMPcggaklepniglffhsiginvklGYGMTET--TATVSCWEEGHfePNSIGT 400
Cdd:PRK08180 350 VWDRLDRVA--------EATCGERIRMMT-----------------------GLGMTETapSATFTTGPLSR--AGNIGL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 401 LMPGAEVKIGENN---EILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEF----DPQGNLYITDRIKELMKTSNGK 473
Cdd:PRK08180 397 PAPGCEVKLVPVGgklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvdpaDPERGLMFDGRIAEDFKLSSGT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 474 YIApqyietkVG--KDKFIEQIA-VIADA------KKYVSALIVPCFNSLEEYAKQLniKYHDRLELIKHSDILQMFEQR 544
Cdd:PRK08180 477 WVS-------VGplRARAVSAGApLVQDVvitghdRDEIGLLVFPNLDACRRLAGLL--ADASLAEVLAHPAVRAAFRER 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1178481066 545 INDLQKELP-SFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVILERYKAQIEAMY 598
Cdd:PRK08180 548 LARLNAQATgSSTRVARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVEALY 602
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
75-510 |
1.60e-27 |
|
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: 116.28 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 75 IADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEEYNCTLEIIDACPQIQKIVTMKDnvdLKNH---PKAC 151
Cdd:cd05909 46 LANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKLHHLFDVEYDARIVYLED---LRAKiskADKC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 152 dwQTFLLEGSPLQQTALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPL 231
Cdd:cd05909 123 --KAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQ---ITAIFDPNPEDVVFGALPF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 232 SHIF--ERAWVAYVLHRGAVNCYLE--DTNRVREALSEIRPTLMCAVPRFYeKIYTAVWDKvqkaplfrrmifnwaiavg 307
Cdd:cd05909 198 FHSFglTGCLWLPLLSGIKVVFHPNplDYKKIPELIYDKKATILLGTPTFL-RGYARAAHP------------------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 308 qkrFQFISqkkpipfvLRQQYALADKLVlSKLRQLlggrirmmpcggaklepniglFFHSIGINVKLGYGMTETTATVSC 387
Cdd:cd05909 258 ---EDFSS--------LRLVVAGAEKLK-DTLRQE---------------------FQEKFGIRILEGYGTTECSPVISV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 388 -WEEGHFEPNSIGTLMPGAEVKI-----------GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQG 455
Cdd:cd05909 305 nTPQSPNKEGTVGRPLPGMEVKIvsvetheevpiGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 456 NLYITDRIKELMKtsngkyIAPQYIETKVgkdkfIEQIA-VIADAKKYVSALIVPC 510
Cdd:cd05909 384 FLTITGRLSRFAK------IAGEMVSLEA-----IEDILsEILPEDNEVAVVSVPD 428
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
167-584 |
3.52e-27 |
|
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: 113.98 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 167 ALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANlaHQLKAHDEAFTtLNVSQYDSSLSFLPLSHIFERAwvayVLHR 246
Cdd:cd05912 66 AFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGN--HWWSAIGSALN-LGLTEDDNWLCALPLFHISGLS----ILMR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 247 GAVN---CYLE---DTNRVREALSEIRPTLMCAVPRFYEKIytavwdkvqkaplfrrmifnwaiavgqkrfqfisqkkpi 320
Cdd:cd05912 139 SVIYgmtVYLVdkfDAEQVLHLINSGKVTIISVVPTMLQRL--------------------------------------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 321 pfvlrqqyaladklvLSKLRQLLGGRIRMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETT---ATVScWEEGHFEPNS 397
Cdd:cd05912 180 ---------------LEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCsqiVTLS-PEDALNKIGS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 398 IGTLMPGAEVKIGENN-------EILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMkTS 470
Cdd:cd05912 244 AGKPLFPVELKIEDDGqppyevgEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-IS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 471 NGKYIAPQYIETKVGKDKFIEQIAVIA-DAKKYVSaliVPCfnsleeyakqlnikyhdrLELIKHSDILQmfEQRINDLQ 549
Cdd:cd05912 322 GGENIYPAEIEEVLLSHPAIKEAGVVGiPDDKWGQ---VPV------------------AFVVSERPISE--EELIAYCS 378
|
410 420 430
....*....|....*....|....*....|....*...
gi 1178481066 550 KELPSFEQIKKFTL---LPQafttkmeeiTPTLKLRRK 584
Cdd:cd05912 379 EKLAKYKVPKKIYFvdeLPR---------TASGKLLRH 407
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
32-600 |
7.29e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 115.53 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 32 GWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPI---YATSA---AKqVEYILNN 105
Cdd:PRK12582 77 QWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMShdhAK-LKHLFDL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 106 ADVKILFVGDQEEYNCTLEIIDAcpqiqkivtmkDNVDLKNHPKACDWQTflleGSPLQQ---TALQARLEQK--QLTD- 179
Cdd:PRK12582 156 VKPRVVFAQSGAPFARALAALDL-----------LDVTVVHVTGPGEGIA----SIAFADlaaTPPTAAVAAAiaAITPd 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 180 -LFTLIYTSGTTGEPKGV-----MLdYANLAHQLKAHDEAfTTLNVSQydsSLSFLPLSHIFE-RAWVAYVLHRGAVnCY 252
Cdd:PRK12582 221 tVAKYLFTSGSTGMPKAVintqrMM-CANIAMQEQLRPRE-PDPPPPV---SLDWMPWNHTMGgNANFNGLLWGGGT-LY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LEDTNRVRE-------ALSEIRPTLMCAVPrfyeKIYTAVWDKVQKAPLFRRMIFNwaiavgqkrfqfisqkkpipfvlr 325
Cdd:PRK12582 295 IDDGKPLPGmfeetirNLREISPTVYGNVP----AGYAMLAEAMEKDDALRRSFFK------------------------ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 326 qqyaladklvlsklrqllggRIRMMPCGGAKLEPNI-----GLFFHSIG--INVKLGYGMTETTATVScweEGHFEPNSI 398
Cdd:PRK12582 347 --------------------NLRLMAYGGATLSDDLyermqALAVRTTGhrIPFYTGYGATETAPTTT---GTHWDTERV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 399 GTL---MPGAEVK---IGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEF----DPQGNLYITDRIKELMK 468
Cdd:PRK12582 404 GLIglpLPGVELKlapVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFvdpdDPEKGLIFDGRVAEDFK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 469 TSNGKYIApqyietkVGKDKfIEQIA----VIADA------KKYVSALIVPCFNSLEEYAKQLNIKYHDrleLIKHSDIL 538
Cdd:PRK12582 484 LSTGTWVS-------VGTLR-PDAVAacspVIHDAvvagqdRAFIGLLAWPNPAACRQLAGDPDAAPED---VVKHPAVL 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178481066 539 QMFEQRINDLQKELP-SFEQIKKFTLLPQAFTTKMEEITPTLKLRRKVILERYKAQIEAMYKE 600
Cdd:PRK12582 553 AILREGLSAHNAEAGgSSSRIARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
23-509 |
9.89e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 114.26 E-value: 9.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 23 TALRYhtpsgwENISW--HQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVE 100
Cdd:PRK08316 28 TALVF------GDRSWtyAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 101 YILNNADVKILFVGDQeeyncTLEIIDACPQIQKIVTMK--DNVDLKNHPKAC-DWQTFLLEGSplqQTALQARLEQkql 177
Cdd:PRK08316 102 YILDHSGARAFLVDPA-----LAPTAEAALALLPVDTLIlsLVLGGREAPGGWlDFADWAEAGS---VAEPDVELAD--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 178 TDLFTLIYTSGTTGEPKGVMLDYANLAHQlkaHDEAFTTLNVSQYDSSLSFLPLSH-----IFERAWVaYVlhrGAVNCY 252
Cdd:PRK08316 171 DDLAQILYTSGTESLPKGAMLTHRALIAE---YVSCIVAGDMSADDIPLHALPLYHcaqldVFLGPYL-YV---GATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LE--DTNRVREALSEIRPTLMCAVPrfyekiytAVWdkvqkAPLFRRMIFNwaiavgqkRFQFISQKK--------PIPf 322
Cdd:PRK08316 244 LDapDPELILRTIEAERITSFFAPP--------TVW-----ISLLRHPDFD--------TRDLSSLRKgyygasimPVE- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 323 vlrqqyaladklVLSKLRQLLggrirmmpcggaklePNIGLFfhsigiNVklgYGMTET--TATVSCWEEGHFEPNSIGt 400
Cdd:PRK08316 302 ------------VLKELRERL---------------PGLRFY------NC---YGQTEIapLATVLGPEEHLRRPGSAG- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 401 lMP------------GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMK 468
Cdd:PRK08316 345 -RPvlnvetrvvdddGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIK 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1178481066 469 TSnGKYIAPQYIETKVGKDKFIEQIAVIA--DAK--KYVSALIVP 509
Cdd:PRK08316 423 TG-GENVASREVEEALYTHPAVAEVAVIGlpDPKwiEAVTAVVVP 466
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
37-509 |
3.84e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 112.60 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 37 SWHQFQQDLDTFSYALLAnhIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVV---PIYATSaakQVEYILNNADVKIL 111
Cdd:PRK08315 45 TYREFNEEVDALAKGLLA--LGIEkgDRVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRLS---ELEYALNQSGCKAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 112 FVGDQEEYNCTLEII-DACPQIQKIVTMKDNV----DLKN--------HPKACDWQTFLLEGSPLQQTALQARLEQKQLT 178
Cdd:PRK08315 120 IAADGFKDSDYVAMLyELAPELATCEPGQLQSarlpELRRviflgdekHPGMLNFDELLALGRAVDDAELAARQATLDPD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHqlkahDEAFT--TLNVSQYDSSLSFLPLSHIFerAWV----AYVLHRGAVNCY 252
Cdd:PRK08315 200 DPINIQYTSGTTGFPKGATLTHRNILN-----NGYFIgeAMKLTEEDRLCIPVPLYHCF--GMVlgnlACVTHGATMVYP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LE--DTNRVREALSEIRPTLMCAVPrfyeKIYTAVWDKvqkaPLFrrmifnwaiavgqKRFQFISQKK--------PIPf 322
Cdd:PRK08315 273 GEgfDPLATLAAVEEERCTALYGVP----TMFIAELDH----PDF-------------ARFDLSSLRTgimagspcPIE- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 323 VLRQqyaladklVLSKlrqllggrirM-MPcggaklepniglffhsigiNVKLGYGMTETtATVSCWEEGH--FEP--NS 397
Cdd:PRK08315 331 VMKR--------VIDK----------MhMS-------------------EVTIAYGMTET-SPVSTQTRTDdpLEKrvTT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 398 IGTLMPGAEVKI-----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKEl 466
Cdd:PRK08315 373 VGRALPHLEVKIvdpetgetvprGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKD- 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1178481066 467 MKTSNGKYIAPQYIEtkvgkdKFIEQIAVIADA-------KKY---VSALIVP 509
Cdd:PRK08315 452 MIIRGGENIYPREIE------EFLYTHPKIQDVqvvgvpdEKYgeeVCAWIIL 498
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
44-501 |
1.87e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 110.90 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 44 DLDTFS---YALLANH-IGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQ--- 116
Cdd:PRK06178 63 ELDELSdrfAALLRQRgVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQlap 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 117 ------EEynCTLEII------DACPQIQKIVtMKDNVDLKNhPKACDWQTFLlegSPLQQTALQARLEQKQLTDLFTLI 184
Cdd:PRK06178 143 vveqvrAE--TSLRHVivtslaDVLPAEPTLP-LPDSLRAPR-LAAAGAIDLL---PALRACTAPVPLPPPALDALAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 185 YTSGTTGEPKGVMLDYANLAHQLKAHDEAftTLNVSQYDSSLSFLPlshIFeraWVA-------YVLHRGAVNCYLedtN 257
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMVYTAAAAYAV--AVVGGEDSVFLSFLP---EF---WIAgenfgllFPLFSGATLVLL---A 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 258 RvREALseirpTLMCAVPRFYEKIYTAVWD---KVQKAPlfrrmifnwaiAVGQKRFQFISQKKPIPFV------LRQQY 328
Cdd:PRK06178 285 R-WDAV-----AFMAAVERYRVTRTVMLVDnavELMDHP-----------RFAEYDLSSLRQVRVVSFVkklnpdYRQRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 329 aladklvlsklRQLLGGRIRmmpcggaklepniglffhsiginvKLGYGMTETTaTVSCWEEG--------HFEPNSIGT 400
Cdd:PRK06178 348 -----------RALTGSVLA------------------------EAAWGMTETH-TCDTFTAGfqdddfdlLSQPVFVGL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 401 LMPGAEVKI-----------GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKT 469
Cdd:PRK06178 392 PVPGTEFKIcdfetgellplGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510
....*....|....*....|....*....|....
gi 1178481066 470 sNGKYIAPQYIETKVGKDKFIEQIAVI--ADAKK 501
Cdd:PRK06178 471 -NGMSVFPSEVEALLGQHPAVLGSAVVgrPDPDK 503
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
47-508 |
2.38e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 110.47 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 47 TFSYALLANHI----------GVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVV---PIYAtsaAKQVEYILNNADVKIL 111
Cdd:PRK05605 57 TTTYAELGKQVrraaaglralGVRpgDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYT---AHELEHPFEDHGARVA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 112 FVGD-------------QEEYNCTLEIIDACPQIQ---------KIVTMKDNVDLKNhPKACDWQTFLleGSPLQQTALQ 169
Cdd:PRK05605 134 IVWDkvaptverlrrttPLETIVSVNMIAAMPLLQrlalrlpipALRKARAALTGPA-PGTVPWETLV--DAAIGGDGSD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 170 ARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLkAHDEAFTTLNVSQYDSSLSFLPLSHIFERAWV-AYVLHRGA 248
Cdd:PRK05605 211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWVPGLGDGPERVLAALPMFHAYGLTLClTLAVSIGG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 249 VNCYLE--DTNRVREALSEIRPTLMCAVPRFYEKIYTAvwdkvqkaplfrrmifnwaiavgqkrfqfiSQKKPIPfvlrq 326
Cdd:PRK05605 290 ELVLLPapDIDLILDAMKKHPPTWLPGVPPLYEKIAEA------------------------------AEERGVD----- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 327 qyaladklvlsklrqlLGGrIRMMPCGGAKLEPNIGLFFHSI--GINVKlGYGMTETTATVSCWEEG-HFEPNSIGTLMP 403
Cdd:PRK05605 335 ----------------LSG-VRNAFSGAMALPVSTVELWEKLtgGLLVE-GYGLTETSPIIVGNPMSdDRRPGYVGVPFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 GAEVKI------------GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSn 471
Cdd:PRK05605 397 DTEVRIvdpedpdetmpdGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITG- 474
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1178481066 472 GKYIAPQYIETKVGKDKFIEQIAVI----ADAKKYVSALIV 508
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEDAAVVglprEDGSEEVVAAVV 515
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
150-496 |
5.36e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 109.30 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 150 ACDWQTFLLEGSPLQQTALQARLEQkqlTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTTLNVSQYdSSLSFL 229
Cdd:PLN02330 159 AVNWKELLEAADRAGDTSDNEEILQ---TDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQV-VTLGLI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 230 PLSHIFerawvayvlhrGAVN-CYLEDTNRVRealseirptlMCAVPRFYEKIY--TAVWDKVQKAPLFRRMIFNWAiav 306
Cdd:PLN02330 235 PFFHIY-----------GITGiCCATLRNKGK----------VVVMSRFELRTFlnALITQEVSFAPIVPPIILNLV--- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 307 gqkrfqfisqKKPIpfvlrqqyalADKLVLSKLRqllggrIRMMPCGGAKLEPNIGLFFHSI--GINVKLGYGMTETtat 384
Cdd:PLN02330 291 ----------KNPI----------VEEFDLSKLK------LQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEH--- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 385 vSCWEEGHFEP---------NSIGTLMPGAEVK---------IGENN--EILVRGGMVMRGYYKKPQETADSFTEDGFLK 444
Cdd:PLN02330 342 -SCITLTHGDPekghgiakkNSVGFILPNLEVKfidpdtgrsLPKNTpgELCVRSQCVMQGYYNNKEETDRTIDEDGWLH 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1178481066 445 TGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:PLN02330 421 TGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAVV 471
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
51-496 |
7.98e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 108.41 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgdQEEYNCTLEIIDA 128
Cdd:PRK06839 42 AYLIYELNVKkgERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFV--EKTFQNMALSMQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 129 CPQIQKIVTMKDNVDLKNHPKAcdwqtfllegsplqqtalqaRLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAhqLK 208
Cdd:PRK06839 120 VSYVQRVISITSLKEIEDRKID--------------------NFVEKNESASFIICYTSGTTGKPKGAVLTQENMF--WN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 209 AHDEAFTtLNVSQYDSSLSFLPLSHIFERAWVAY-VLHRGAVNCYLE--DTNRVREALSEIRPTLMCAVPRFYEKIytav 285
Cdd:PRK06839 178 ALNNTFA-IDLTMHDRSIVLLPLFHIGGIGLFAFpTLFAGGVIIVPRkfEPTKALSMIEKHKVTVVMGVPTIHQAL---- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 286 wdkvQKAPLFRRMIFNwaiavgqkrfqfisqkkpipfvlrqqyaladklvlsklrqllggRIRMMPCGGAKLEPNIGLFF 365
Cdd:PRK06839 253 ----INCSKFETTNLQ--------------------------------------------SVRWFYNGGAPCPEELMREF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 366 HSIGINVKLGYGMTETTATVSCWEEGHF--EPNSIGTLMP----------GAEVKIGENNEILVRGGMVMRGYYKKPQET 433
Cdd:PRK06839 285 IDRGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLfcdyelidenKNKVEVGEVGELLIRGPNVMKEYWNRPDAT 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178481066 434 ADSFtEDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:PRK06839 365 EETI-QDGWLCTGDLARVDEDGFVYIVGRKKE-MIISGGENIYPLEVEQVINKLSDVYEVAVV 425
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
179-497 |
1.77e-24 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 104.72 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPLSHIferAWVAyVLHRGA---VNCYLED 255
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGDSWLLSLPLYHV---GGLA-ILVRSLlagAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 256 TNR-VREALSEIRPTLMCAVPRFYEKIYTAvwdkvqkaplfrrmifnwaiavgqkrfqfiSQKKPIPFVLRQqyaladkl 334
Cdd:cd17630 74 RNQaLAEDLAPPGVTHVSLVPTQLQRLLDS------------------------------GQGPAALKSLRA-------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 335 VLSklrqllggrirmmpcGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKIGENNE 414
Cdd:cd17630 116 VLL---------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 415 ILVRGGMVMRGYYKKPQEtaDSFTEDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIA 494
Cdd:cd17630 181 IWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADN-MIISGGENIQPEEIEAALAAHPAVRDAF 257
|
...
gi 1178481066 495 VIA 497
Cdd:cd17630 258 VVG 260
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
53-495 |
1.18e-23 |
|
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: 103.50 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 53 LANHI------GVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFvgdqeeynCTLEII 126
Cdd:TIGR01733 12 LARHLraaggvGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL--------TDSALA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 127 DACPQIQKIVTMKDNVDLKNHPKAcdwqtfllegsplqqTALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQ 206
Cdd:TIGR01733 84 SRLAGLVLPVILLDPLELAALDDA---------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 207 LKAHDEAFttlNVSQYDSSLSFLPLSHiferawvayvlhrgavncyleDTnrvreALSEIRPTLM-----CAVPRFYEKI 281
Cdd:TIGR01733 149 LAWLARRY---GLDPDDRVLQFASLSF---------------------DA-----SVEEIFGALLagatlVVPPEDEERD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 282 YTAVWdkvqkAPLFRRMIFNWAIAVgqkrfqfisqkkPIPFvlrQQYALADKLVLSKLRQLLggrirmmpCGGAKLEPNI 361
Cdd:TIGR01733 200 DAALL-----AALIAEHPVTVLNLT------------PSLL---ALLAAALPPALASLRLVI--------LGGEALTPAL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 362 GLFFHSIGINVKL--GYGMTETTATVSCWE-----EGHFEPNSIGTLMPGAE----------VKIGENNEILVRGGMVMR 424
Cdd:TIGR01733 252 VDRWRARGPGARLinLYGPTETTVWSTATLvdpddAPRESPVPIGRPLANTRlyvldddlrpVPVGVVGELYIGGPGVAR 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 425 GYYKKPQETADSFTEDGFL--------KTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAV 495
Cdd:TIGR01733 332 GYLNRPELTAERFVPDPFAggdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
176-584 |
1.50e-23 |
|
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: 103.76 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 176 QLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAF---TTLNVSQYdSSLSFLPlsHIFE--RAWVA----YVLHR 246
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYpltPGDRVLQF-TSFSFDV--SVWEifGALLAgatlVVLPE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 247 GAVncylEDTNRVREALSEIRPTLMCAVPRFYEkiytavwdkvqkaplfrrmifnwaiavgqkrfqfisqkkpipfVLRQ 326
Cdd:cd05930 168 EVR----KDPEALADLLAEEGITVLHLTPSLLR-------------------------------------------LLLQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 327 QYALADklvLSKLRQLLggrirmmpCGGAKLEPNIGLFFHSIGINVKL--GYGMTETTATVSCW----EEGHFEPNSIGT 400
Cdd:cd05930 201 ELELAA---LPSLRLVL--------VGGEALPPDLVRRWRELLPGARLvnLYGPTEATVDATYYrvppDDEEDGRVPIGR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 401 LMPGAE----------VKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFL------KTGDAGEFDPQGNLYITDRIK 464
Cdd:cd05930 270 PIPNTRvyvldenlrpVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRID 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 465 ELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIA----DAKKYVSALIVPcfnsleeyakqlnikyhDRLELIKHSDILQM 540
Cdd:cd05930 350 DQVKI-RGYRIELGEIEAALLAHPGVREAAVVAredgDGEKRLVAYVVP-----------------DEGGELDEEELRAH 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1178481066 541 feqrindLQKELPSFeqikkftLLPQAFTTkMEEI--TPTLKLRRK 584
Cdd:cd05930 412 -------LAERLPDY-------MVPSAFVV-LDALplTPNGKVDRK 442
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
179-496 |
2.06e-23 |
|
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: 101.42 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLdyanlAHQ--LKAHDEAFTTLNVSQYDSSLSFLPLSHIF--ERAWVAYVLhRGA--VNCY 252
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMC-----AHRqtLRAAAAWADCADLTEDDRYLIINPFFHTFgyKAGIVACLL-TGAtvVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LEDTNRVREALSEIRPTLMCAVPRFYEKIYT-AVWDKVQKAPLfrRMIFNWAIAVgqkrfqfisqkkPIPFVLRQQYALA 331
Cdd:cd17638 75 VFDVDAILEAIERERITVLPGPPTLFQSLLDhPGRKKFDLSSL--RAAVTGAATV------------PVELVRRMRSELG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 332 DKLVLSklrqllggrirmmpcggaklepniglffhsiginvklGYGMTETTATVSCWEEGHFE--PNSIGTLMPGAEVKI 409
Cdd:cd17638 141 FETVLT-------------------------------------AYGLTEAGVATMCRPGDDAEtvATTCGRACPGFEVRI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKF 489
Cdd:cd17638 184 ADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKD-MYIVGGFNVYPAEVEGALAEHPG 262
|
....*..
gi 1178481066 490 IEQIAVI 496
Cdd:cd17638 263 VAQVAVI 269
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
51-496 |
2.44e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 104.07 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVV---PIYAtsaAKQVEYILNNADVKILFV----GDQEE--- 118
Cdd:PRK05677 64 AWLQQHTDLKpgDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLYT---AREMEHQFNDSGAKALVClanmAHLAEkvl 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 119 ------YNCTLEIIDACPQIQKIVT------MKDNVDLKNHPKACDWQTFLLEGS--PLQQTALQArleqkqlTDLFTLI 184
Cdd:PRK05677 141 pktgvkHVIVTEVADMLPPLKRLLInavvkhVKKMVPAYHLPQAVKFNDALAKGAgqPVTEANPQA-------DDVAVLQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 185 YTSGTTGEPKGVMLDYANLAH---QLKAH-----DEAFTTLnvsqydssLSFLPLSHIFerawvAYVLHRGAVncyLEDT 256
Cdd:PRK05677 214 YTGGTTGVAKGAMLTHRNLVAnmlQCRALmgsnlNEGCEIL--------IAPLPLYHIY-----AFTFHCMAM---MLIG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 257 NRvrealseirpTLMCAVPRfyekiytavwdkvqKAPLFRRMIFNWAIA--VGQKRFqfisqkkpipFVlrqqyALADKl 334
Cdd:PRK05677 278 NH----------NILISNPR--------------DLPAMVKELGKWKFSgfVGLNTL----------FV-----ALCNN- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 335 vlSKLRQLLGGRIRMMPCGGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMP---------- 403
Cdd:PRK05677 318 --EAFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPstlckviddd 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIETK 483
Cdd:PRK05677 396 GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDV 474
|
490
....*....|...
gi 1178481066 484 VGKDKFIEQIAVI 496
Cdd:PRK05677 475 LAALPGVLQCAAI 487
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
16-497 |
4.21e-23 |
|
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: 102.76 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 16 AKLLLNETALRYHTPSgwenISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSA 95
Cdd:cd12118 14 AAVYPDRTSIVYGDRR----YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 96 AKQVEYILNNADVKILFVGDQEEYNCTLEIIDACPQIQkivtmkdnvdlknhPKACDWqtfllegsplqqtalqarleqk 175
Cdd:cd12118 90 AEEIAFILRHSEAKVLFVDREFEYEDLLAEGDPDFEWI--------------PPADEW---------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 176 qltDLFTLIYTSGTTGEPKGVMLdyanlahqlkahdeafttlnvsqydsslsflplsHiferawvayvlHRGAvncYLEd 255
Cdd:cd12118 134 ---DPIALNYTSGTTGRPKGVVY----------------------------------H-----------HRGA---YLN- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 256 tnrvreALSEI-------RPTLMCAVPRFYEKIYTavwdkvqkaplfrrmiFNWAI-AVG-----------QKRFQFISQ 316
Cdd:cd12118 162 ------ALANIlewemkqHPVYLWTLPMFHCNGWC----------------FPWTVaAVGgtnvclrkvdaKAIYDLIEK 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 317 KK-------PIPFVLRQQYALADKLVLSklrqllgGRIRMMpCGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVS-C- 387
Cdd:cd12118 220 HKvthfcgaPTVLNMLANAPPSDARPLP-------HRVHVM-TAGAPPPAAVLAKMEELGFDVTHVYGLTETYGPATvCa 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 388 ----WEEGHFEPNSI-----GTLMPGAE-----------------VKIGEnneILVRGGMVMRGYYKKPQETADSFtEDG 441
Cdd:cd12118 292 wkpeWDELPTEERARlkarqGVRYVGLEevdvldpetmkpvprdgKTIGE---IVFRGNIVMKGYLKNPEATAEAF-RGG 367
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 442 FLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
34-508 |
2.27e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 101.26 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFV 113
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 114 GD-------------QEEYNCTLEIIDACPQIQKIV---TMKDNVDLKnhPKACDWQTFLLEGSPLQQTALQARLEQKQL 177
Cdd:PRK06710 128 LDlvfprvtnvqsatKIEHVIVTRIADFLPFPKNLLypfVQKKQSNLV--VKVSESETIHLWNSVEKEVNTGVEVPCDPE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 178 TDLFTLIYTSGTTGEPKGVMLDYANL-AHQLKAHDEAFTTlnVSQYDSSLSFLPLSHIFErawVAYVLHRGAVNCYLE-- 254
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNC--KEGEEVVLGVLPFFHVYG---MTAVMNLSIMQGYKMvl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 255 ----DTNRVREALSEIRPTLMCAVPrfyeKIYTAVWDkvqkAPLFRRMIFNWAIAVgqkrfqfISQKKPIPFVLRQqyal 330
Cdd:PRK06710 281 ipkfDMKMVFEAIKKHKVTLFPGAP----TIYIALLN----SPLLKEYDISSIRAC-------ISGSAPLPVEVQE---- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 331 adklvlsKLRQLLGGRIrmmpcggakLEpniglffhsiginvklGYGMTETTATVSC---WEEGhfEPNSIGTLMPGAEV 407
Cdd:PRK06710 342 -------KFETVTGGKL---------VE----------------GYGLTESSPVTHSnflWEKR--VPGSIGVPWPDTEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 408 KI-----------GENNEILVRGGMVMRGYYKKPQETAdSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIA 476
Cdd:PRK06710 388 MImsletgealppGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVAS-GFNVY 465
|
490 500 510
....*....|....*....|....*....|....*.
gi 1178481066 477 PQYIETKVGKDKFIEQIAVIADAKKY----VSALIV 508
Cdd:PRK06710 466 PREVEEVLYEHEKVQEVVTIGVPDPYrgetVKAFVV 501
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
161-500 |
2.39e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 100.42 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 161 SPLQQTALQARLEQK--QLTDLFTLIYTSGTTGEPKGVMLDYANlaHQLKAHDEAFTtLNVSQYDSSLSFLPLSHI--FE 236
Cdd:PRK03640 122 AELMNGPKEEAEIQEefDLDEVATIMYTSGTTGKPKGVIQTYGN--HWWSAVGSALN-LGLTEDDCWLAAVPIFHIsgLS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 237 rawvayVLHRGAV---NCYLE---DTNRVREALSEIRPTLMCAVPRFYEKIyTAVWDKVQKAPLFRRMIFNWAiavgqkr 310
Cdd:PRK03640 199 ------ILMRSVIygmRVVLVekfDAEKINKLLQTGGVTIISVVSTMLQRL-LERLGEGTYPSSFRCMLLGGG------- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 311 fqfisqkkPIPFVLRQQyaladklvlSKLRqllggrirmmpcggaklepniglffhsiGINVKLGYGMTETT---ATVSC 387
Cdd:PRK03640 265 --------PAPKPLLEQ---------CKEK----------------------------GIPVYQSYGMTETAsqiVTLSP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 388 wEEGHFEPNSIGTLMPGAEVKI---------GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLY 458
Cdd:PRK03640 300 -EDALTKLGSAGKPLFPCELKIekdgvvvppFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLY 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1178481066 459 ITDRIKELMkTSNGKYIAPQYIETKVGKDKFIEQIAVI--ADAK 500
Cdd:PRK03640 378 VLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVgvPDDK 420
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
179-481 |
2.88e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.83 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANL----AHQLkahDEAFTTLNVSQYDSSLSFLPLSHIFerawvayvlhrgAVNCYLE 254
Cdd:PLN02246 180 DVVALPYSSGTTGLPKGVMLTHKGLvtsvAQQV---DGENPNLYFHSDDVILCVLPMFHIY------------SLNSVLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 255 DTNRVREALSEIR----PTLMCAVPRFyekiytavwdKVQKAPLFRRMIFnwAIAvgqkrfqfisqKKPIpfvlrqqyal 330
Cdd:PLN02246 245 CGLRVGAAILIMPkfeiGALLELIQRH----------KVTIAPFVPPIVL--AIA-----------KSPV---------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 331 ADKLVLSKLRQLLGGRIRMmpcgGAKLEPNIGLFFHsigiNVKL--GYGMTETTATVS-CW----EEGHFEPNSIGTLMP 403
Cdd:PLN02246 292 VEKYDLSSIRMVLSGAAPL----GKELEDAFRAKLP----NAVLgqGYGMTEAGPVLAmCLafakEPFPVKSGSCGTVVR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 GAEVKI---------GEN--NEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTsNG 472
Cdd:PLN02246 364 NAELKIvdpetgaslPRNqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KG 442
|
....*....
gi 1178481066 473 KYIAPQYIE 481
Cdd:PLN02246 443 FQVAPAELE 451
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
43-496 |
3.10e-22 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 100.87 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 43 QDLDTFSYALLA--NHIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVV---PIYAtsaAKQVEYILNNADVKILFVgd 115
Cdd:PRK07059 52 GELDELSRALAAwlQSRGLAkgARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYT---PRELEHQLKDSGAEAIVV-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 116 QEEYNCTLEIIDACPQIQKIV--TMKDNVDLKNH------------------PKACDWQTFLLEGSPLqqtalqaRLEQK 175
Cdd:PRK07059 127 LENFATTVQQVLAKTAVKHVVvaSMGDLLGFKGHivnfvvrrvkkmvpawslPGHVRFNDALAEGARQ-------TFKPV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 176 QLT--DLFTLIYTSGTTGEPKGVMLDYANL-------------AHQLKAHDEAFTTLNVsqydsslsfLPLSHIFERAwV 240
Cdd:PRK07059 200 KLGpdDVAFLQYTGGTTGVSKGATLLHRNIvanvlqmeawlqpAFEKKPRPDQLNFVCA---------LPLYHIFALT-V 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 241 AYVL--HRGAVNcyledtnrvrealseirptLMCAVPRfyekiytavwdkvqKAPLFRRMIfnwaiavgqKRFQFISqkk 318
Cdd:PRK07059 270 CGLLgmRTGGRN-------------------ILIPNPR--------------DIPGFIKEL---------KKYQVHI--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 319 pIPFVLRQQYALA-----DKLVLSKLRQLLGGrirmmpcGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSC--WEEG 391
Cdd:PRK07059 305 -FPAVNTLYNALLnnpdfDKLDFSKLIVANGG-------GMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCnpVDAT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 392 HFEpNSIGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITD 461
Cdd:PRK07059 377 EFS-GTIGLPLPSTEVSIrdddgndlplGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVD 455
|
490 500 510
....*....|....*....|....*....|....*
gi 1178481066 462 RIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:PRK07059 456 RKKDMILVS-GFNVYPNEIEEVVASHPGVLEVAAV 489
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
51-495 |
5.24e-22 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 100.13 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVV---PIYAtsaAKQVEYILNNADVK-ILFVGDqeeYNCTLE 124
Cdd:PRK08974 63 AYLQNGLGLKkgDRVALMMPNLLQYPIALFGILRAGMIVVnvnPLYT---PRELEHQLNDSGAKaIVIVSN---FAHTLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 125 -IIDACPQIQKIVT-MKDN--------VDL----------KNH-PKACDWQTFLLEGSPLQQtaLQARLEQkqlTDLFTL 183
Cdd:PRK08974 137 kVVFKTPVKHVILTrMGDQlstakgtlVNFvvkyikrlvpKYHlPDAISFRSALHKGRRMQY--VKPELVP---EDLAFL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 184 IYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTTLNVSQYDSSLSFLPLSHIFERAwvayvlhrgaVNCYLedtnrvreal 263
Cdd:PRK08974 212 QYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELVVTALPLYHIFALT----------VNCLL---------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 264 seirptlmcavprFYEKIYTAVwdkvqkaplfrrMIFNWAIAVGqkrfqFISQKKPIPFV-LRQQYALADKLVLSK-LRQ 341
Cdd:PRK08974 272 -------------FIELGGQNL------------LITNPRDIPG-----FVKELKKYPFTaITGVNTLFNALLNNEeFQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 342 LLGGRIRMMPCGGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSCWE---EGHfePNSIGTLMPGAEVKI-------- 409
Cdd:PRK08974 322 LDFSSLKLSVGGGMAVQQAVAERWVKLtGQYLLEGYGLTECSPLVSVNPydlDYY--SGSIGLPVPSTEIKLvdddgnev 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 --GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIETKVG-K 486
Cdd:PRK08974 400 ppGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMlH 477
|
....*....
gi 1178481066 487 DKFIEQIAV 495
Cdd:PRK08974 478 PKVLEVAAV 486
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
57-510 |
1.15e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 98.90 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 57 IGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEEYNCTLEIIDACPQIQKIV 136
Cdd:PRK06188 59 LGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 137 TMKDNvdlknhPKACDwqtFLLEGSPLQQTALQARleqKQLTDLFTLIYTSGTTGEPKGVMLdyanlahqlkaHDEAFTT 216
Cdd:PRK06188 139 TLGPV------PDGVD---LLAAAAKFGPAPLVAA---ALPPDIAGLAYTGGTTGKPKGVMG-----------THRSIAT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 217 LNVSQYDS-----SLSFL---PLSHIfERAWVAYVLHRGAVNCYLE--DTNRVREALSEIRPTLMCAVPRfyekiytavw 286
Cdd:PRK06188 196 MAQIQLAEwewpaDPRFLmctPLSHA-GGAFFLPTLLRGGTVIVLAkfDPAEVLRAIEEQRITATFLVPT---------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 287 dkvqkaplfrrMIfnwaiavgqkrfqfisqkkpipfvlrqqYALAD-----KLVLSKLRQLLGGRIRMMPC----GGAKL 357
Cdd:PRK06188 265 -----------MI----------------------------YALLDhpdlrTRDLSSLETVYYGASPMSPVrlaeAIERF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 358 EPnigLFFHSiginvklgYGMTETTATVSCWEEGHFEPNSIGTL------MPGAEVKI----------GENNEILVRGGM 421
Cdd:PRK06188 306 GP---IFAQY--------YGQTEAPMVITYLRKRDHDPDDPKRLtscgrpTPGLRVALldedgrevaqGEVGEICVRGPL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 422 VMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIAVIA--DA 499
Cdd:PRK06188 375 VMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKD-MIVTGGFNVFPREVEDVLAEHPAVAQVAVIGvpDE 452
|
490
....*....|...
gi 1178481066 500 K--KYVSALIVPC 510
Cdd:PRK06188 453 KwgEAVTAVVVLR 465
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-496 |
1.23e-21 |
|
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: 96.58 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 185 YTSGTTGEPKGVMLDYANLAhqlkahDEAFTT---LNVSQYDSSLSFLPLSHIFER--AWVAYVLHrGAVNCYLEDTNRV 259
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIV------NNGYFIgerLGLTEQDRLCIPVPLFHCFGSvlGVLACLTH-GATMVFPSPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 260 REALSEI---RPTLMCAVPRFYEKIYTAvwdkvqkaPLFrrmifnwaiavgqKRFQFISQKKPIpfvlrqqyaLADKLVL 336
Cdd:cd05917 82 LAVLEAIekeKCTALHGVPTMFIAELEH--------PDF-------------DKFDLSSLRTGI---------MAGAPCP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 337 SKLRQLLGGRIRMMpcggaklepniglffhsigiNVKLGYGMTETTATVSCWEEGHFEP---NSIGTLMPGAEVKI---- 409
Cdd:cd05917 132 PELMKRVIEVMNMK--------------------DVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIvdpe 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIET 482
Cdd:cd05917 192 ggivppvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKD-MIIRGGENIYPREIEE 270
|
330
....*....|....
gi 1178481066 483 KVGKDKFIEQIAVI 496
Cdd:cd05917 271 FLHTHPKVSDVQVV 284
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
175-463 |
1.54e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 99.61 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 175 KQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLSHIFE-RAWVAYVLHRGAVNCYL 253
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVF---NLRNDDVILSSLPFFHSFGlTVTLWLPLLEGIKVVYH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 254 E---DTNRVREALSEIRPTLMCAVPRFYeKIYTavwdKVQKAplfrrmifnwaiavgqkrfqfisqkkpipfvlrqqyal 330
Cdd:PRK08633 856 PdptDALGIAKLVAKHRATILLGTPTFL-RLYL----RNKKL-------------------------------------- 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 331 aDKLVLSKLRqllggrirMMPCGGAKLEPNIGLFFH-SIGINVKLGYGMTETTATVSC----------WEEGHFEPNSIG 399
Cdd:PRK08633 893 -HPLMFASLR--------LVVAGAEKLKPEVADAFEeKFGIRILEGYGATETSPVASVnlpdvlaadfKRQTGSKEGSVG 963
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 400 TLMPGAEVKI-----------GENNEILVRGGMVMRGYYKKPQETADSFTE---DGFLKTGDAGEFDPQGNLYITDRI 463
Cdd:PRK08633 964 MPLPGVAVRIvdpetfeelppGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLDEDGFLTITDRY 1041
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
36-553 |
1.55e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 98.41 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLAN-HIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVG 114
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 115 DQeeYNCTLEIIDACPQIQKIVTMKDNvDLKNHPKAC--------------DWQtflLEGSPLQQTAL----QARLEQKQ 176
Cdd:PRK08751 131 DN--FGTTVQQVIADTPVKQVITTGLG-DMLGFPKAAlvnfvvkyvkklvpEYR---INGAIRFREALalgrKHSMPTLQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 177 LT--DLFTLIYTSGTTGEPKGVMLDYANL-AHQLKAHDEAFTTLNVSQ-YDSSLSFLPLSHIFERAWVAYVLHR-GAVNC 251
Cdd:PRK08751 205 IEpdDIAFLQYTGGTTGVAKGAMLTHRNLvANMQQAHQWLAGTGKLEEgCEVVITALPLYHIFALTANGLVFMKiGGCNH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 252 YLEDTNRVREALSEIRPTlmcavpRFyeKIYTAV---WDKVQKAPLFrrmifnwaiavgqkrfqfisqkkpipfvlrqqy 328
Cdd:PRK08751 285 LISNPRDMPGFVKELKKT------RF--TAFTGVntlFNGLLNTPGF--------------------------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 329 alaDKLVLSKLRQLLGGrirmmpcgGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSCWEEGHFEPN-SIGTLMPGAE 406
Cdd:PRK08751 324 ---DQIDFSSLKMTLGG--------GMAVQRSVAERWKQVtGLTLVEAYGLTETSPAACINPLTLKEYNgSIGLPIPSTD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 407 V----------KIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIA 476
Cdd:PRK08751 393 AcikddagtvlAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-GFNVY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 477 PQYIETKVGKDKFIEQIAVIA--DAK--KYVSALIV---PCFNSLEeyakqlnIKYHDRLELIKHSdilqmfEQRINDLQ 549
Cdd:PRK08751 472 PNEIEDVIAMMPGVLEVAAVGvpDEKsgEIVKVVIVkkdPALTAED-------VKAHARANLTGYK------QPRIIEFR 538
|
....
gi 1178481066 550 KELP 553
Cdd:PRK08751 539 KELP 542
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
36-481 |
2.00e-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: 97.93 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILfVGD 115
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-VTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 116 QEEYNCTLEIIDACPQIQKIVTMKDNV-DLKNHP--KACDWQTfllegspLQQTALQARLEQKQLTDLFTLIYTSGTTGE 192
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIVGDPAhASEGHPgeEPASWPK-------LLALGDADPPHPVIDSDMAAILYTSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 193 PKGVMLDYANLAhqLKAHDEAfTTLNVSQYDSSLSFLPLS--HIFERAWVAY------VLHRgavncYLEDTNRVReALS 264
Cdd:TIGR03098 178 PKGVVLSHRNLV--AGAQSVA-TYLENRPDDRLLAVLPLSfdYGFNQLTTAFyvgatvVLHD-----YLLPRDVLK-ALE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 265 EIRPTLMCAVPrfyekiytAVWdkvqkAPLFRrmiFNWAIAVGQKRFQFISQKKPIPfvlrqqyaladKLVLSKLRQLLg 344
Cdd:TIGR03098 249 KHGITGLAAVP--------PLW-----AQLAQ---LDWPESAAPSLRYLTNSGGAMP-----------RATLSRLRSFL- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 345 grirmmpcggaklePNIGLFfhsiginvkLGYGMTET-TATVSCWEEGHFEPNSIGTLMPGAEVKI----------GENN 413
Cdd:TIGR03098 301 --------------PNARLF---------LMYGLTEAfRSTYLPPEEVDRRPDSIGKAIPNAEVLVlredgsecapGEEG 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 414 EILVRGGMVMRGYYKKPQETADSFT----EDGFLK-------TGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIE 481
Cdd:TIGR03098 358 ELVHRGALVAMGYWNDPEKTAERFRplppFPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVE 435
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
37-532 |
2.57e-21 |
|
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: 97.07 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 37 SWHQFQQDLDTFSYALLANHIGVQDKIAIfahNMPRW---TIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFV 113
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAF---QLPNWwefAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 114 GDQeeynctleiidacpqiqkivtmkdnvdlknhpkacdWQTFllegSPLQQTAlqarleqkqltDLFTLIYTSGTTGEP 193
Cdd:cd05903 80 PER------------------------------------FRQF----DPAAMPD-----------AVALLLFTSGTTGEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 194 KGVMLDYANL---AHQLKAHdeafttLNVSQYDSSLSFLPLSHI---FERAWVAYVLHRGAVNCYLEDTNRVREALSEIR 267
Cdd:cd05903 109 KGVMHSHNTLsasIRQYAER------LGLGPGDVFLVASPMAHQtgfVYGFTLPLLLGAPVVLQDIWDPDKALALMREHG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 268 PTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAiavgqkrfqfisqkkPIPFVLRQQYAladklvlsklrqllggri 347
Cdd:cd05903 183 VTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGA---------------TVPRSLARRAA------------------ 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 348 rmmPCGGAKLEPniglffhsiginvklGYGMTET-TATVSCW--EEGHFEpNSIGTLMPGAEVKI----------GENNE 414
Cdd:cd05903 230 ---ELLGAKVCS---------------AYGSTECpGAVTSITpaPEDRRL-YTDGRPLPGVEIKVvddtgatlapGVEGE 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 415 ILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQYIETKVGKDKFIEQIA 494
Cdd:cd05903 291 LLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAA 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 495 VIA--DAK--KYVSALIV------PCFNSLEEY------AKQlniKYHDRLELI 532
Cdd:cd05903 369 VVAlpDERlgERACAVVVtksgalLTFDELVAYldrqgvAKQ---YWPERLVHV 419
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
23-484 |
1.76e-20 |
|
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: 95.38 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 23 TALRY--HTPSGWENISWHQFQQDLDTFSYALLAnHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYA---TSAAK 97
Cdd:cd05931 10 PAYTFldDEGGREETLTYAELDRRARAIAARLQA-VGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPptpGRHAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 98 QVEYILNNADVKILFvgdqeeynCTLEIIDACPQIQkivtmkDNVDLKNHPKACDWQTFLLEGSPLQQTAlqarleQKQL 177
Cdd:cd05931 89 RLAAILADAGPRVVL--------TTAAALAAVRAFA------ASRPAAGTPRLLVVDLLPDTSAADWPPP------SPDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 178 TDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPLSH-------IFERAWVAYVLHRGAVN 250
Cdd:cd05931 149 DDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQ---IRRAYGLDPGDVVVSWLPLYHdmgliggLLTPLYSGGPSVLMSPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 251 CYLEDTNRVREALSEIRPTLMcAVPRFyekiytavwdkvqkAplfrrmiFNWAIavgqKRfqfisqkkpipfVLRQQyal 330
Cdd:cd05931 226 AFLRRPLRWLRLISRYRATIS-AAPNF--------------A-------YDLCV----RR------------VRDED--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 331 ADKLVLSKLRQLLGG--RIRM----------MPCGgakLEPNiglffhsigiNVKLGYGMTETTATVSC----------- 387
Cdd:cd05931 265 LEGLDLSSWRVALNGaePVRPatlrrfaeafAPFG---FRPE----------AFRPSYGLAEATLFVSGgppgtgpvvlr 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 388 ----WEEGHFEPN-----------SIGTLMPGAEVKI-----------GENNEILVRGGMVMRGYYKKPQETADSF---- 437
Cdd:cd05931 332 vdrdALAGRAVAVaaddpaarelvSCGRPLPDQEVRIvdpetgrelpdGEVGEIWVRGPSVASGYWGRPEATAETFgala 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1178481066 438 --TEDGFLKTGDAGeFDPQGNLYITDRIKELMkTSNGKYIAPQYIETKV 484
Cdd:cd05931 412 atDEGGWLRTGDLG-FLHDGELYITGRLKDLI-IVRGRNHYPQDIEATA 458
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
179-509 |
2.15e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 94.56 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHQLKA-HDE-AFTtlnvsQYDSSLSFLPLSH---IFerawVAY--VLHRGAVNC 251
Cdd:PRK07514 157 DLAAILYTSGTTGRSKGAMLSHGNLLSNALTlVDYwRFT-----PDDVLIHALPIFHthgLF----VATnvALLAGASMI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 252 YLE--DTNRVREALSeiRPTLMCAVPRFYEKIytavwdkVQKAPLFRRmifnwaiAVGQKRFqFISQKKPIpfvlrqqya 329
Cdd:PRK07514 228 FLPkfDPDAVLALMP--RATVMMGVPTFYTRL-------LQEPRLTRE-------AAAHMRL-FISGSAPL--------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 330 LADKLVlsKLRQLLGGRIrmmpcggakLEPniglffhsiginvklgYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKI 409
Cdd:PRK07514 282 LAETHR--EFQERTGHAI---------LER----------------YGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQ 478
Cdd:PRK07514 335 tdpetgaelppGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLI-ISGGYNVYPK 413
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1178481066 479 YIETkvgkdkFIEQI------AVI----ADAKKYVSALIVP 509
Cdd:PRK07514 414 EVEG------EIDELpgvvesAVIgvphPDFGEGVTAVVVP 448
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
23-481 |
2.42e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 95.02 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 23 TALRY-HTPSGWEN---ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTmQVRAVVVPIYATSAAKQ 98
Cdd:PRK07529 42 PALSFlLDADPLDRpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EAAGIANPINPLLEPEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 99 VEYILNNADVKILF-VG---DQEEYNCTLEIIDACPQIQKIVTmkdnVDLKNH-PKACDWQTFLLEGSP----LQQTALQ 169
Cdd:PRK07529 121 IAELLRAAGAKVLVtLGpfpGTDIWQKVAEVLAALPELRTVVE----VDLARYlPGPKRLAVPLIRRKAhariLDFDAEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 170 ARL--------EQKQLTDLFTLIYTSGTTGEPKGVMLDYAN------LAHQLKAHDEAfttlnvsqyDSSLSFLPLSHIF 235
Cdd:PRK07529 197 ARQpgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanawLGALLLGLGPG---------DTVFCGLPLFHVN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 236 erawVAYV-----LHRGAvncyledtnrvrealseirpTLMCAVPRFYekiytavwdkvqKAP-LFRRMifnWAIaVGQK 309
Cdd:PRK07529 268 ----ALLVtglapLARGA--------------------HVVLATPQGY------------RGPgVIANF---WKI-VERY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 310 RFQFISQkkpIPFVLRqqyALADKLV----LSKLRQLLggrirmmpCGGAKLEPNIG-LFFHSIGINVKLGYGMTETTAT 384
Cdd:PRK07529 308 RINFLSG---VPTVYA---ALLQVPVdghdISSLRYAL--------CGAAPLPVEVFrRFEAATGVRIVEGYGLTEATCV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 385 VSC-WEEGHFEPNSIGTLMPGAEVKI---------------GENNEILVRGGMVMRGYYKKPQEtADSFTEDGFLKTGDA 448
Cdd:PRK07529 374 SSVnPPDGERRIGSVGLRLPYQRVRVvilddagrylrdcavDEVGVLCIAGPNVFSGYLEAAHN-KGLWLEDGWLNTGDL 452
|
490 500 510
....*....|....*....|....*....|...
gi 1178481066 449 GEFDPQGNLYITDRIKELMkTSNGKYIAPQYIE 481
Cdd:PRK07529 453 GRIDADGYFWLTGRAKDLI-IRGGHNIDPAAIE 484
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
49-496 |
3.13e-20 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 94.43 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 49 SYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgDQEEYNCTLEIIDA 128
Cdd:PRK06018 53 SQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DLTFVPILEKIADK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 129 CPQIQKIVTMKD-----NVDLKN----------HPKACDWQTFLlegsplQQTALqarleqkqltdlfTLIYTSGTTGEP 193
Cdd:PRK06018 132 LPSVERYVVLTDaahmpQTTLKNavayeewiaeADGDFAWKTFD------ENTAA-------------GMCYTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 194 KGVMLDY-ANLAHQLKAHDEafTTLNVSQYDSSLSFLPLSHifERAW-VAYVLHRGAVNCYLE----DTNRVREALSEIR 267
Cdd:PRK06018 193 KGVLYSHrSNVLHALMANNG--DALGTSAADTMLPVVPLFH--ANSWgIAFSAPSMGTKLVMPgaklDGASVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 268 PTLMCAVPrfyekiytAVWdkvqkaplfrRMIFnwaiavgqkrfqfisqkkpipfvlrqQYALADKLVLSKLRqllggri 347
Cdd:PRK06018 269 VTFTAGVP--------TVW----------LMLL--------------------------QYMEKEGLKLPHLK------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 348 rMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETT--ATVSCWEeGHFEPNSIGTLMP----------GAEVKI--GENN 413
Cdd:PRK06018 298 -MVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplGTLAALK-PPFSKLPGDARLDvlqkqgyppfGVEMKItdDAGK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 414 EI----------LVRGGMVMRGYYKKPQETADsftEDGFLKTGDAGEFDPQGNLYITDRIKELMKtSNGKYIAPQYIET- 482
Cdd:PRK06018 376 ELpwdgktfgrlKVRGPAVAAAYYRVDGEILD---DDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDLENl 451
|
490
....*....|....
gi 1178481066 483 KVGKDKFIEQiAVI 496
Cdd:PRK06018 452 AVGHPKVAEA-AVI 464
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
53-482 |
5.19e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 93.13 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 53 LANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEEYnctleiiDACPQI 132
Cdd:PRK07787 38 VAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDP-------AGLPHV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 133 QkivtmkdnVDLKnhpkACDWQTflLEGSPLQQTALqarleqkqltdlftLIYTSGTTGEPKGVMLDYANLAHQLKAHDE 212
Cdd:PRK07787 111 P--------VRLH----ARSWHR--YPEPDPDAPAL--------------IVYTSGTTGPPKGVVLSRRAIAADLDALAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 213 AFttlNVSQYDSSLSFLPLSHIfeRAWVAYVLhrGAvncyLEDTNRVR-----------EALSEiRPTLMCAVPrfyeki 281
Cdd:PRK07787 163 AW---QWTADDVLVHGLPLFHV--HGLVLGVL--GP----LRIGNRFVhtgrptpeayaQALSE-GGTLYFGVP------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 282 ytAVWDKVQKAPlfrrmifNWAIAVGQKRFqFISQKKPIPFVlrqqyaladklVLSKLRQLLGGRI--Rmmpcggaklep 359
Cdd:PRK07787 225 --TVWSRIAADP-------EAARALRGARL-LVSGSAALPVP-----------VFDRLAALTGHRPveR----------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 360 niglffhsiginvklgYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVKIGENN------------EILVRGGMVMRGYY 427
Cdd:PRK07787 273 ----------------YGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDggpvphdgetvgELQVRGPTLFDGYL 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 428 KKPQETADSFTEDGFLKTGDAGEFDPQGNLYI-----TDRIKelmktSNGKYIAPQYIET 482
Cdd:PRK07787 337 NRPDATAAAFTADGWFRTGDVAVVDPDGMHRIvgresTDLIK-----SGGYRIGAGEIET 391
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
23-509 |
5.22e-20 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 93.58 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 23 TALRYHTPSGwENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYI 102
Cdd:PRK13295 44 TAVRLGTGAP-RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 103 LNNADVKILFVG------DQEEYNCTLEiiDACPQIQKIVTMkdnvdlkNHPKACDWQTFLLEGSPLQQTALQARLEQKQ 176
Cdd:PRK13295 123 LKHAESKVLVVPktfrgfDHAAMARRLR--PELPALRHVVVV-------GGDGADSFEALLITPAWEQEPDAPAILARLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 177 L--TDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAfttLNVSQYDSSLSFLPLSH---IFERAWVAYVLHRGAVnc 251
Cdd:PRK13295 194 PgpDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER---LGLGADDVILMASPMAHqtgFMYGLMMPVMLGATAV-- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 252 yLEDTNRVREALSEIRPT----LMCAVPrFYEKIYTAVWDKVQKAPLFRRmifnwaiavgqkrfqFISQKKPIPFVLRQQ 327
Cdd:PRK13295 269 -LQDIWDPARAAELIRTEgvtfTMASTP-FLTDLTRAVKESGRPVSSLRT---------------FLCAGAPIPGALVER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 328 yaladklvlskLRQLLGGRIrmmpCGGaklepniglffhsiginvklgYGMTETTAtVSCWEEGHFEPNSIGT---LMPG 404
Cdd:PRK13295 332 -----------ARAALGAKI----VSA---------------------WGMTENGA-VTLTKLDDPDERASTTdgcPLPG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 405 AEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFteDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKY 474
Cdd:PRK13295 375 VEVRVvdadgaplpaGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIRISGRSKDVI-IRGGEN 451
|
490 500 510
....*....|....*....|....*....|....*....
gi 1178481066 475 IAPQYIETKVGKDKFIEQIAVIA--DAK--KYVSALIVP 509
Cdd:PRK13295 452 IPVVEIEALLYRHPAIAQVAIVAypDERlgERACAFVVP 490
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
157-466 |
2.36e-19 |
|
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: 91.57 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 157 LLEGSPLQQTALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPLSHife 236
Cdd:cd05906 146 VLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG---KIQHNGLTPQDVFLNWVPLDH--- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 237 rawVAYVLHrgavncyledtnrvrealSEIRPT-LMCavprfyEKIYTAVWDKVQKAPLFRRMIfnwaiavgQKRfqfis 315
Cdd:cd05906 220 ---VGGLVE------------------LHLRAVyLGC------QQVHVPTEEILADPLRWLDLI--------DRY----- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 316 qkkpipfvlRQQYALADKLVLSKLRQLLG---------GRIRMMPCGGaklEPNI---GLFFHSI----GIN---VKLGY 376
Cdd:cd05906 260 ---------RVTITWAPNFAFALLNDLLEeiedgtwdlSSLRYLVNAG---EAVVaktIRRLLRLlepyGLPpdaIRPAF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 377 GMTETTA----TVSCWEEGHFEPN---SIGTLMPGAEVKI-GENNEIL---------VRGGMVMRGYYKKPQETADSFTE 439
Cdd:cd05906 328 GMTETCSgviySRSFPTYDHSQALefvSLGRPIPGVSMRIvDDEGQLLpegevgrlqVRGPVVTKGYYNNPEANAEAFTE 407
|
330 340
....*....|....*....|....*..
gi 1178481066 440 DGFLKTGDAGeFDPQGNLYITDRIKEL 466
Cdd:cd05906 408 DGWFRTGDLG-FLDNGNLTITGRTKDT 433
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
179-500 |
2.79e-19 |
|
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: 89.25 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLahqLKAHDEAFTTLNVSQYDSSLSFLPLSHIFERAWVAYVLHRGAVNCYLE--DT 256
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNL---IAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEkfDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 257 NRVREALSEIRPTLMCAVPrfyeKIYTAVWDKVQKAPLfrrmifnwaiavgqkrfqfisqkkpipfvlrqqyaladklVL 336
Cdd:cd17637 78 AEALELIEEEKVTLMGSFP----PILSNLLDAAEKSGV----------------------------------------DL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 337 SKLRQLLGGRirmMPCGGAKLEPNIGLFFHSiginvklGYGMTETT--ATVSCWEEghfEPNSIGTLMPGAEVKI----- 409
Cdd:cd17637 114 SSLRHVLGLD---APETIQRFEETTGATFWS-------LYGQTETSglVTLSPYRE---RPGSAGRPGPLVRVRIvddnd 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -----GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRI--KELMKTSnGKYIAPQYIET 482
Cdd:cd17637 181 rpvpaGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPG-GENVYPAEVEK 258
|
330 340
....*....|....*....|
gi 1178481066 483 KVGKDKFIEQIAVI--ADAK 500
Cdd:cd17637 259 VILEHPAIAEVCVIgvPDPK 278
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
179-497 |
5.78e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 90.67 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAhqlkAHDEAFTTLNVSQYDSS------LSFLPLSHIFERA-WVAYVLHRGAVNC 251
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLI----AMVELFVRFEASQYEYPgsdnvyLAALPMFHIYGLSlFVVGLLSLGSTIV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 252 YLE--DTNRVREALSEIRPTLMCAVPrfyekiytavwdkvqkaplfrrmifnwaiavgqkrfqfisqkkPIPFVLRQQYA 329
Cdd:PLN02574 275 VMRrfDASDMVKVIDRFKVTHFPVVP-------------------------------------------PILMALTKKAK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 330 LADKLVLSKLRQLLGGrirMMPCGGAKLEPNIGLFFHsigINVKLGYGMTETTA--TVSCWEEGHFEPNSIGTLMPGAEV 407
Cdd:PLN02574 312 GVCGEVLKSLKQVSCG---AAPLSGKFIQDFVQTLPH---VDFIQGYGMTESTAvgTRGFNTEKLSKYSSVGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 408 KI-----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIA 476
Cdd:PLN02574 386 KVvdwstgcllppGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
330 340
....*....|....*....|.
gi 1178481066 477 PQYIETKVGKDKFIEQIAVIA 497
Cdd:PLN02574 465 PADLEAVLISHPEIIDAAVTA 485
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
179-498 |
4.25e-18 |
|
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: 87.40 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAF---TTLNVSQYdSSLSFlplshiferawvayvlhrgavncyleD 255
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASslgPGARTLQF-AGLGF--------------------------D 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 256 TnrvreALSEIRPTLMCA----VPRfyEKIYT---AVWDKVQKAPLFRrmIFnwaiavgqkrfqfisqkkpIPFVLRQQY 328
Cdd:cd17651 190 V-----SVQEIFSTLCAGatlvLPP--EEVRTdppALAAWLDEQRISR--VF-------------------LPTVALRAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 329 ALADKL---VLSKLRQLL-GG-------RIRMMPCGgaklEPNIGLFFHsiginvklgYGMTETTaTVSCWE-----EGH 392
Cdd:cd17651 242 AEHGRPlgvRLAALRYLLtGGeqlvlteDLREFCAG----LPGLRLHNH---------YGPTETH-VVTALSlpgdpAAW 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 393 FEPNSIGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFL------KTGDAGEFDPQGN 456
Cdd:cd17651 308 PAPPPIGRPIDNTRVYVldaalrpvppGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGE 387
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1178481066 457 LYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIAD 498
Cdd:cd17651 388 LEFLGRADDQVKI-RGFRIELGEIEAALARHPGVREAVVLAR 428
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
51-584 |
8.34e-18 |
|
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: 86.58 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEE--YNCTLEIIDA 128
Cdd:cd12116 28 RLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDALPdrLPAGLPVLLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 129 CPQIqkivtmkdnvdlknhpkacdwqtflLEGSPLQQTALQArleqkqLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLK 208
Cdd:cd12116 108 ALAA-------------------------AAAAPAAPRTPVS------PDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 209 AHDEAFTT------LNVSQY--DSSL--SFLPLSHiferAWVAYVLHRGAVncylEDTNRVREALSEIRPTLMCAVPrfy 278
Cdd:cd12116 157 SMRERLGLgpgdrlLAVTTYafDISLleLLLPLLA----GARVVIAPRETQ----RDPEALARLIEAHSITVMQATP--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 279 ekiytAVWdkvqkaplfrRMIFnwaiAVGQKRfqfisqkkpipfvlrqqyaladklvLSKLRQLlggrirmmpCGGAKLE 358
Cdd:cd12116 226 -----ATW----------RMLL----DAGWQG-------------------------RAGLTAL---------CGGEALP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 359 PNIGLFFHSIG---INVklgYGMTETT--ATVS--CWEEGHFepnSIGTLMPGAE----------VKIGENNEILVRGGM 421
Cdd:cd12116 253 PDLAARLLSRVgslWNL---YGPTETTiwSTAArvTAAAGPI---PIGRPLANTQvyvldaalrpVPPGVPGELYIGGDG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 422 VMRGYYKKPQETADSFTEDGFL-------KTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIA 494
Cdd:cd12116 327 VAQGYLGRPALTAERFVPDPFAgpgsrlyRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQAA 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 495 VIA---DAKKYVSALIVPCFNSLEeyakqlnikyhDRLELIKHsdilqmfeqrindLQKELPSFeqikkftLLPQAFTTk 571
Cdd:cd12116 406 VVVredGGDRRLVAYVVLKAGAAP-----------DAAALRAH-------------LRATLPAY-------MVPSAFVR- 453
|
570
....*....|....*
gi 1178481066 572 MEEI--TPTLKLRRK 584
Cdd:cd12116 454 LDALplTANGKLDRK 468
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
29-586 |
1.21e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.39 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 29 TPSGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPR---WTIAdigTMQVRAVVVPI-Y------ATSAAKQ 98
Cdd:PLN02860 26 TISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLyleWLLA---VACAGGIVAPLnYrwsfeeAKSAMLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 99 VEyilnnadvKILFVGDQE-EYNCTLEIIDACPQIQKIVTMKDNVDLKNHpkacDWQTFLLEGSPLQQTALQARLEQKQL 177
Cdd:PLN02860 103 VR--------PVMLVTDETcSSWYEELQNDRLPSLMWQVFLESPSSSVFI----FLNSFLTTEMLKQRALGTTELDYAWA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 178 TDLFTLI-YTSGTTGEPKGVMLDYANLAHQlkahdeAFTTLNVSQYDSSLSFL---PLSHIFERAWVAYVLHRGAVNCYL 253
Cdd:PLN02860 171 PDDAVLIcFTSGTTGRPKGVTISHSALIVQ------SLAKIAIVGYGEDDVYLhtaPLCHIGGLSSALAMLMVGACHVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 254 E--DTNRVREALSEIRPTLMCAVPrfyekiyTAVWDKVQKAplfrRMIFNWAiavgqkrfqfisqkkpipfvlrqqyala 331
Cdd:PLN02860 245 PkfDAKAALQAIKQHNVTSMITVP-------AMMADLISLT----RKSMTWK---------------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 332 dklVLSKLRQLL--GGRI--RMMPcGGAKLEPNIGLFFhsiginvklGYGMTE-------------TTATVSCWEEGHFE 394
Cdd:PLN02860 286 ---VFPSVRKILngGGSLssRLLP-DAKKLFPNAKLFS---------AYGMTEacssltfmtlhdpTLESPKQTLQTVNQ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 395 PNS----------IGTLMPGAEVKIGENN-----EILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYI 459
Cdd:PLN02860 353 TKSssvhqpqgvcVGKPAPHVELKIGLDEssrvgRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 460 TDRIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVSALIVPCFNSLEEYakqlnIKYHDRLELIKHSDILQ 539
Cdd:PLN02860 433 IGRSNDRIKTG-GENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGW-----IWSDNEKENAKKNLTLS 506
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1178481066 540 MFEQRINDLQKELPSFEQIKKFTLLPQAFTTkmeeiTPTLKLRRKVI 586
Cdd:PLN02860 507 SETLRHHCREKNLSRFKIPKLFVQWRKPFPL-----TTTGKIRRDEV 548
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
57-482 |
1.32e-17 |
|
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: 86.01 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 57 IGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDqeEYNCTLEIIDA---CPQIQ 133
Cdd:cd05970 69 IGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA--EDNIPEEIEKAapeCPSKP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 134 KIVTMKDNVdlknhPKA-CDWQTFLLEGSPLQqTALQARLEQKQlTDLFTLIYTSGTTGEPKGVMLDYA-NLAHQLKA-- 209
Cdd:cd05970 147 KLVWVGDPV-----PEGwIDFRKLIKNASPDF-ERPTANSYPCG-EDILLVYFSSGTTGMPKMVEHDFTyPLGHIVTAky 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 210 -HDEAFTTLNVSQYDSSLSFLPLSHIFERaWVAyvlhrGAvNCYLEDTNR-----VREALSEIRPTLMCAVPRFYEkiyt 283
Cdd:cd05970 220 wQNVREGGLHLTVADTGWGKAVWGKIYGQ-WIA-----GA-AVFVYDYDKfdpkaLLEKLSKYGVTTFCAPPTIYR---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 284 avwdkvqkaplfrrmifnwaiavgqkrfqfisqkkpipFVLRQQYALADklvLSKLRQLLggrirmmpCGGAKLEPNI-G 362
Cdd:cd05970 289 --------------------------------------FLIREDLSRYD---LSSLRYCT--------TAGEALNPEVfN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 363 LFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMP----------GAEVKIGENNEILVRG------GMvMRGY 426
Cdd:cd05970 320 TFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPgyeidlidreGRSCEAGEEGEIVIRTskgkpvGL-FGGY 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 427 YKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIET 482
Cdd:cd05970 399 YKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVES 452
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
174-481 |
1.89e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 85.62 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 174 QKQLTDLFTLI-YTSGTTGEPKGVMLDYANLAHQLKAHDEAfttLNVSQYDSSLSFLPLSHIFERAWVAYVLHRGAVNCY 252
Cdd:cd05908 101 LCELADELAFIqFSSGSTGDPKGVMLTHENLVHNMFAILNS---TEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LEDTNR--VREAL-----SEIRPTLMCAvPRFYEKIY--------TAVWDKVQKaplfrRMIFNWAiavgqkrfqfisqk 317
Cdd:cd05908 178 LMPTRLfiRRPILwlkkaSEHKATIVSS-PNFGYKYFlktlkpekANDWDLSSI-----RMILNGA-------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 318 KPIPFVLRQQyaLADKLVLSKLRqllggRIRMMPCGG------AKLEPNIGLFFHSIGIN---VKLGYGMTETTATvscw 388
Cdd:cd05908 238 EPIDYELCHE--FLDHMSKYGLK-----RNAILPVYGlaeasvGASLPKAQSPFKTITLGrrhVTHGEPEPEVDKK---- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 389 eeghfEPN-----SIGTLMPGAEVKI-GENNEIL---------VRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGeFDP 453
Cdd:cd05908 307 -----DSEcltfvEVGKPIDETDIRIcDEDNKILpdgyighiqIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIR 380
|
330 340
....*....|....*....|....*...
gi 1178481066 454 QGNLYITDRIKELMKTsNGKYIAPQYIE 481
Cdd:cd05908 381 NGRLVITGREKDIIFV-NGQNVYPHDIE 407
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
21-496 |
2.44e-17 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 85.12 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 21 NETALRYHTPSGweniswhqfqqDLDTFSYALLANHI----------GVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVV 88
Cdd:PRK08008 22 HKTALIFESSGG-----------VVRRYSYLELNEEInrtanlfyslGIRkgDKVALHLDNCPEFIFCWFGLAKIGAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 89 PIYATSAAKQVEYILNNADVKILFVGD----------QEEYNCTLEIIDACPQIQKIVTMKDNVDLKNHPKACdwqtfLL 158
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAqfypmyrqiqQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPAT-----LC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 159 EGSPLQQTalqarleqkqltDLFTLIYTSGTTGEPKGVMLDYANLahQLKAHDEAFTTlNVSQYDSSLSFLPLSHI-FER 237
Cdd:PRK08008 166 YAPPLSTD------------DTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWQC-ALRDDDVYLTVMPAFHIdCQC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 238 AWVAYVLHRGAVNCYLEDtnrvrealseirptlmcavprfyekiYTA--VWDKVQKaplFRRMIfnwaiavgqkrfqfis 315
Cdd:PRK08008 231 TAAMAAFSAGATFVLLEK--------------------------YSAraFWGQVCK---YRATI---------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 316 qKKPIPFVLRQ---QYALADKlvlsklRQllgGRIRMMpcggaklepnigLFFHSIG----------INVKL--GYGMTE 380
Cdd:PRK08008 266 -TECIPMMIRTlmvQPPSAND------RQ---HCLREV------------MFYLNLSdqekdafeerFGVRLltSYGMTE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 381 TTATV---SCWEEGHFEpnSIGTLMPGAEVKI----------GENNEILVRG---GMVMRGYYKKPQETADSFTEDGFLK 444
Cdd:PRK08008 324 TIVGIigdRPGDKRRWP--SIGRPGFCYEAEIrddhnrplpaGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLH 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1178481066 445 TGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:PRK08008 402 TGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVV 452
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
36-508 |
2.76e-17 |
|
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: 84.61 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFV-G 114
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIAdG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 115 DqeeynctleiidacpqiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqkqltDLFTLIYTSGTTGEPK 194
Cdd:cd05945 97 D---------------------------------------------------------------DNAYIIFTSGSTGRPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 195 GVMLDYANLAhqlkahdeAFTTLNVSQYD----------SSLSF-LPLSHIFErAWVA----YVLHRGAVNcyleDTNRV 259
Cdd:cd05945 114 GVQISHDNLV--------SFTNWMLSDFPlgpgdvflnqAPFSFdLSVMDLYP-ALASgatlVPVPRDATA----DPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 260 REALSEIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFnwaiaVGQkrfqfisqkkpiPFVLRQqyaladklvLSKL 339
Cdd:cd05945 181 FRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLF-----CGE------------VLPHKT---------ARAL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 340 RQLL-GGRIrmmpcggaklepniglffhsigINvklGYGMTETTATVSCWE------EGHfEPNSIGTLMPGAEVKI--- 409
Cdd:cd05945 235 QQRFpDARI----------------------YN---TYGPTEATVAVTYIEvtpevlDGY-DRLPIGYAKPGAKLVIlde 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -------GENNEILVRGGMVMRGYYKKPQETADSFTED---GFLKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQY 479
Cdd:cd05945 289 dgrpvppGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEE 367
|
490 500 510
....*....|....*....|....*....|
gi 1178481066 480 IETKVGKDKFIEQIAVIADAKK-YVSALIV 508
Cdd:cd05945 368 IEAALRQVPGVKEAVVVPKYKGeKVTELIA 397
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
44-484 |
4.93e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 84.49 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 44 DLDTFSYAL---LANHIGVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVV---PIYAtsaAKQVEYILNNADVKILF--- 112
Cdd:PRK12492 54 ELERHSAAFaayLQQHTDLVpgDRIAVQMPNVLQYPIAVFGALRAGLIVVntnPLYT---AREMRHQFKDSGARALVyln 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 113 ---------VGDQE-EYNCTLEIIDACPQ-----IQKIV-TMKDNVDLKNHPKACDWQTFLLEGSPLQQTALQARLEqkq 176
Cdd:PRK12492 131 mfgklvqevLPDTGiEYLIEAKMGDLLPAakgwlVNTVVdKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLD--- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 177 ltDLFTLIYTSGTTGEPKGVMLDYANLA---HQLKA----HDEAFTTLNVSQYDSSLSFLPLSHIFerAWVAyvlhrgav 249
Cdd:PRK12492 208 --DIAVLQYTGGTTGLAKGAMLTHGNLVanmLQVRAclsqLGPDGQPLMKEGQEVMIAPLPLYHIY--AFTA-------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 250 NCyledtnrvrealseirptlMCA-VPRFYEKIYTAVWDkvqkAPLFRRMIFNWaiavgqkRFQFISQKKPIpFVlrqqy 328
Cdd:PRK12492 276 NC-------------------MCMmVSGNHNVLITNPRD----IPGFIKELGKW-------RFSALLGLNTL-FV----- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 329 ALADKlvlSKLRQLLGGRIRMMPCGGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSCWEEGhfEPNSIGTL-MP--- 403
Cdd:PRK12492 320 ALMDH---PGFKDLDFSALKLTNSGGTALVKATAERWEQLtGCTIVEGYGLTETSPVASTNPYG--ELARLGTVgIPvpg 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 ---------GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKY 474
Cdd:PRK12492 395 talkvidddGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS-GFN 473
|
490
....*....|
gi 1178481066 475 IAPQYIETKV 484
Cdd:PRK12492 474 VYPNEIEDVV 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
11-584 |
7.63e-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: 83.53 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 11 RIREQAKLLLNETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPI 90
Cdd:cd17655 2 LFEEQAEKTPDHTAVVF----EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 91 YATSAAKQVEYILNNADVKILfvgdqeeynCTLEIIDACPQIQKIVTMKDNVDLKNHPKAcdwqtfllegsplqqtalqa 170
Cdd:cd17655 78 DPDYPEERIQYILEDSGADIL---------LTQSHLQPPIAFIGLIDLLDEDTIYHEESE-------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 171 RLEQ-KQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAF---TTLNVSQYdSSLSF-LPLSHIFerawvAYVLH 245
Cdd:cd17655 129 NLEPvSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIyqgEHLRVALF-ASISFdASVTEIF-----ASLLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 246 RGAVNCYLEDTnrvrealseirptlmcavprfyekiytaVWDkvqkaplfrrmifnwaiavGQKRFQFISQK-----KPI 320
Cdd:cd17655 203 GNTLYIVRKET----------------------------VLD-------------------GQALTQYIRQNritiiDLT 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 321 PFVLrQQYALADKLVLSKLRQLLggrirmmpCGGAKLEPN-----IGLFFHSIGI-NVklgYGMTETT--ATVSCWEEGH 392
Cdd:cd17655 236 PAHL-KLLDAADDSEGLSLKHLI--------VGGEALSTElakkiIELFGTNPTItNA---YGPTETTvdASIYQYEPET 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 393 FEPNS--IGTlmPGAEVKI------------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFL------KTGDAGEFD 452
Cdd:cd17655 304 DQQVSvpIGK--PLGNTRIyildqygrpqpvGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWL 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 453 PQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIA----DAKKYVSALIVPcfnslEEYAKQLNIKYHdr 528
Cdd:cd17655 382 PDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEAVVIArkdeQGQNYLCAYIVS-----EKELPVAQLREF-- 453
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 529 lelikhsdilqmfeqrindLQKELPSFeqikkftLLPqAFTTKMEEI--TPTLKLRRK 584
Cdd:cd17655 454 -------------------LARELPDY-------MIP-SYFIKLDEIplTPNGKVDRK 484
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
61-500 |
1.09e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 82.93 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 61 DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILfVGDQEEYNCTLEIIDACPQIQKIvtmkD 140
Cdd:PRK09088 48 ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL-LGDDAVAAGRTDVEDLAAFIASA----D 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 141 NVDLKNHPKAcdwqtfllegsPLQQTALqarleqkqltdlftLIYTSGTTGEPKGVMLDYANLAHqlKAHDEAFTTlNVS 220
Cdd:PRK09088 123 ALEPADTPSI-----------PPERVSL--------------ILFTSGTSGQPKGVMLSERNLQQ--TAHNFGVLG-RVD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 221 QYDSSLSFLPLSHIFerawvayvlhrGAVncyledTNrvrealseIRPTLMCA----VPRFYEKIYTAVWDKVQkaplfr 296
Cdd:PRK09088 175 AHSSFLCDAPMFHII-----------GLI------TS--------VRPVLAVGgsilVSNGFEPKRTLGRLGDP------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 297 rmifnwaiAVGQKRFQFISQkkpIPFVLRQQYALaDKLVLSKLRQLLGGrirmmpcGGAKLEPNIgLFFHSIGINVKLGY 376
Cdd:PRK09088 224 --------ALGITHYFCVPQ---MAQAFRAQPGF-DAAALRHLTALFTG-------GAPHAAEDI-LGWLDDGIPMVDGF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 377 GMTET--------TATVSCWEEGhfepnSIGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFT 438
Cdd:PRK09088 284 GMSEAgtvfgmsvDCDVIRAKAG-----AAGIPTPTVQTRVvddqgndcpaGVPGELLLRGPNLSPGYWRRPQATARAFT 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 439 EDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIAVI--ADAK 500
Cdd:PRK09088 359 GDGWFRTGDIARRDADGFFWVVDRKKD-MFISGGENVYPAEIEAVLADHPGIRECAVVgmADAQ 421
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
52-552 |
2.03e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 82.49 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 52 LLANHIGVQDKIAIfahNMPRW---TIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGDQEEYN----CTLE 124
Cdd:PRK06087 66 LLAKGIEPGDRVAF---QLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTrpvdLILP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 125 IIDACPQIQKIVTmkdnVDlKNHPKACD--WQTFLLEGSPLQQTALQARleqkqlTDLFTLIYTSGTTGEPKGVMLDYAN 202
Cdd:PRK06087 143 LQNQLPQLQQIVG----VD-KLAPATSSlsLSQIIADYEPLTTAITTHG------DELAAVLFTSGTEGLPKGVMLTHNN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 203 LAhqlkAHDEAFT-TLNVSQYDSSLSFLPLSHiferawvAYVLHRGAVNCYLEDTNRVrealseirptlmcavprfYEKI 281
Cdd:PRK06087 212 IL----ASERAYCaRLNLTWQDVFMMPAPLGH-------ATGFLHGVTAPFLIGARSV------------------LLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 282 YTAVwdkvQKAPLFRRMIFNWAIAVgqkrfqfisqkkpIPFVlrqqYAL-----ADKLVLSKLRQLLggrirmmpCGGAK 356
Cdd:PRK06087 263 FTPD----ACLALLEQQRCTCMLGA-------------TPFI----YDLlnlleKQPADLSALRFFL--------CGGTT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 357 LEPNIGLFFHSIGINVKLGYGMTETT--ATVSCWEEGHFEPNSIGTLMPGAEVKI----------GENNEILVRGGMVMR 424
Cdd:PRK06087 314 IPKKVARECQQRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVvdearktlppGCEGEEASRGPNVFM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 425 GYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQYIETKVGKDKFIEQIAVIA--DAK-- 500
Cdd:PRK06087 394 GYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHDACVVAmpDERlg 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178481066 501 KYVSALIVPCFN----SLEEYAKQLNIK------YHDRLELIKHSDILQMFEQRINDLQKEL 552
Cdd:PRK06087 473 ERSCAYVVLKAPhhslTLEEVVAFFSRKrvakykYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
31-197 |
3.02e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 81.86 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 31 SGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPI---YATSaakQVEYILNNAD 107
Cdd:PRK07798 24 CGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYVED---ELRYLLDDSD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 108 VKILFVGDqeEY-NCTLEIIDACPQIQKIVTMKDNVDLKNHPKACDWQTFLLEGSPLQqtalqaRLEQKQLTDLFtLIYT 186
Cdd:PRK07798 101 AVALVYER--EFaPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPER------DFGERSPDDLY-LLYT 171
|
170
....*....|.
gi 1178481066 187 SGTTGEPKGVM 197
Cdd:PRK07798 172 GGTTGMPKGVM 182
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
7-543 |
4.15e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 81.36 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 7 HFVNRIREQAKLLLNETALRYHTPSgwenISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAV 86
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRFLGNT----TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 87 VVPIYATSAAKQVEYILNNADVKILFVGDQEEyNCTLEIIDACPQIQKIVTMKDNVDlknhPKACDWQTFLLEGSPLQQT 166
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVPLLSTVVVAGGSSD----DSVLGYEDLLAEAGPAHAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 167 ALQARleqkqltDLFTLI-YTSGTTGEPKGVMLDYANLAHQlkahdeAFTTLNVSQYD--SSLSFL--PLSHIFERAWVA 241
Cdd:PRK07786 169 VDIPN-------DSPALImYTSGTTGRPKGAVLTHANLTGQ------AMTCLRTNGADinSDVGFVgvPLFHIAGIGSML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 242 YVLHRGAVNCYLE----DTNRVREALSEIRPTLMCAVPRFYEKIYTAvwDKVQKAPLFRRMIfNWAIAVGQkrfqfisqk 317
Cdd:PRK07786 236 PGLLLGAPTVIYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVCAE--QQARPRDLALRVL-SWGAAPAS--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 318 kpiPFVLRQQYAladklvlsklrqllggrirMMPcggaklEPNIGLFFhsiginvklgyGMTETTAtVSCWEEGH---FE 394
Cdd:PRK07786 304 ---DTLLRQMAA-------------------TFP------EAQILAAF-----------GQTEMSP-VTCMLLGEdaiRK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 395 PNSIGTLMPGA----------EVKIGENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIK 464
Cdd:PRK07786 344 LGSVGKVIPTVaarvvdenmnDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKK 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 465 ElMKTSNGKYIAPQYIETKVGKDKFIEQIAVI--ADAK-KYVSALIVPCFN-----SLEEYAKQLNikyhDRLELIKHSD 536
Cdd:PRK07786 423 D-MIISGGENIYCAEVENVLASHPDIVEVAVIgrADEKwGEVPVAVAAVRNddaalTLEDLAEFLT----DRLARYKHPK 497
|
....*..
gi 1178481066 537 ILQMFEQ 543
Cdd:PRK07786 498 ALEIVDA 504
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
179-497 |
8.63e-16 |
|
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: 79.69 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVM---------LDYANLAHQLKAHDEAFTTLNVS-QYDSSLSFL-PLSHiferaWVAYVLHRG 247
Cdd:cd05972 82 DPALIYFTSGTTGLPKGVLhthsyplghIPTAAYWLGLRPDDIHWNIADPGwAKGAWSSFFgPWLL-----GATVFVYEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 248 AVNcyleDTNRVREALSEIRPTLMCAVPrfyekiyTAvwdkvqkaplFRRMIfnwaiAVGQKRFQFisqkkpipfvlrqq 327
Cdd:cd05972 157 PRF----DAERILELLERYGVTSFCGPP-------TA----------YRMLI-----KQDLSSYKF-------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 328 yaladklvlsklrqllgGRIRMMPCGGAKLEPN-IGLFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAE 406
Cdd:cd05972 197 -----------------SHLRLVVSAGEPLNPEvIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 407 VKI----------GENNEILVRGGMV--MRGYYKKPQETADSFTEDGFLkTGDAGEFDPQGNLYITDRIKELMKTSnGKY 474
Cdd:cd05972 260 VAIidddgrelppGEEGDIAIKLPPPglFLGYVGDPEKTEASIRGDYYL-TGDRAYRDEDGYFWFVGRADDIIKSS-GYR 337
|
330 340
....*....|....*....|...
gi 1178481066 475 IAPQYIETKVGKDKFIEQIAVIA 497
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVG 360
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
4-500 |
9.01e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 80.47 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 4 LNL-HFVnriREQAKLLLNETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQ 82
Cdd:PRK07470 7 MNLaHFL---RQAARRFPDRIALVW----GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 83 VRAVVVPIYATSAAKQVEYILNNADVK-ILFVGDQEEYnctLEII-DACPQIQKIVTMKDNvdlknhPKACDWQTFLLEG 160
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARaMICHADFPEH---AAAVrAASPDLTHVVAIGGA------RAGLDYEALVARH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 161 spLQQTALQARLEQKQLTDLFtliYTSGTTGEPKGVMLDYANLAHQLKAHdEAFTTLNVSQYDSSLSFLPLSH---IFER 237
Cdd:PRK07470 151 --LGARVANAAVDHDDPCWFF---FTSGTTGRPKAAVLTHGQMAFVITNH-LADLMPGTTEQDASLVVAPLSHgagIHQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 238 AWVAyvlhRGAVNCYLE----DTNRVREALSEIRPTLMCAVPRFYeKIYT---AVwDKVQKAPLfRRMIFNWAiavgqkr 310
Cdd:PRK07470 225 CQVA----RGAATVLLPserfDPAEVWALVERHRVTNLFTVPTIL-KMLVehpAV-DRYDHSSL-RYVIYAGA------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 311 fqfisqkkPIpFVLRQQYALAdklVLSK-LRQLLG-----GRIRMMPCGGAKLEPniglffhsiGINVKLGY-GMTETTA 383
Cdd:PRK07470 291 --------PM-YRADQKRALA---KLGKvLVQYFGlgevtGNITVLPPALHDAED---------GPDARIGTcGFERTGM 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 384 TVSCWEEghfepnsigtlmPGAEVKIGENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRI 463
Cdd:PRK07470 350 EVQIQDD------------EGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRA 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 1178481066 464 KElMKTSNGKYIAPQYIETKVGKDKFIEQIAV--IADAK 500
Cdd:PRK07470 417 SD-MYISGGSNVYPREIEEKLLTHPAVSEVAVlgVPDPV 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
169-497 |
1.02e-15 |
|
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: 79.81 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 169 QARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANL----------AHQLKAHDEAFTTLNV---SQYDSSLSFlPL---- 231
Cdd:cd05919 82 EARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPllfadamareALGLTPGDRVFSSAKMffgYGLGNSLWF-PLavga 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 232 SHIFERAWVayvlhrgavncyleDTNRVREALSEIRPTLMCAVPRFYekiytavwdkvqkaplfrrmifnwaiavgqkrf 311
Cdd:cd05919 161 SAVLNPGWP--------------TAERVLATLARFRPTVLYGVPTFY--------------------------------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 312 qfisqkkpipfvlrqqyalADKLVLSKLRQLLGGRIRMMPCGGAKLEPNIGLFF-HSIGINVKLGYGMTETTATVSCWEE 390
Cdd:cd05919 194 -------------------ANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWmEHFGGPILDGIGATEVGHIFLSNRP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 391 GHFEPNSIGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYIT 460
Cdd:cd05919 255 GAWRLGSTGRPVPGYEIRLvdeeghtippGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHA 333
|
330 340 350
....*....|....*....|....*....|....*..
gi 1178481066 461 DRIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:cd05919 334 GRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVVA 369
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
21-497 |
1.50e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.06 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 21 NETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVE 100
Cdd:PLN03102 29 NRTSIIY----GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 101 YILNNADVKILFVgDQEEYNCTLEIIDACP----QIQKIVTMKDNVDLKNHP--KACDWQTFLLEGSPLQQTALQARLEQ 174
Cdd:PLN03102 105 AILRHAKPKILFV-DRSFEPLAREVLHLLSsedsNLNLPVIFIHEIDFPKRPssEELDYECLIQRGEPTPSLVARMFRIQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 175 KQlTDLFTLIYTSGTTGEPKGVMLdyanlAHQlKAHDEAFTTL---NVSQYDSSLSFLPLSHIFERAWVAYVLHRGAVNC 251
Cdd:PLN03102 184 DE-HDPISLNYTSGTTADPKGVVI-----SHR-GAYLSTLSAIigwEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 252 YLEDTN--RVREALSEIRPTLMCAVPRFYEKIYTAvwDKVQKAPlfrrmifnwaiavGQKRFQFISQKKPIPFVLrqqya 329
Cdd:PLN03102 257 CMRHVTapEIYKNIEMHNVTHMCCVPTVFNILLKG--NSLDLSP-------------RSGPVHVLTGGSPPPAAL----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 330 ladklvLSKLRQLlggrirmmpcggaklepniglffhsiGINVKLGYGMTETTATV-SC-WE-EGHFEPN---------- 396
Cdd:PLN03102 317 ------VKKVQRL--------------------------GFQVMHAYGLTEATGPVlFCeWQdEWNRLPEnqqmelkarq 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 397 --SIGTLmpgAEVKIGENN-------------EILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITD 461
Cdd:PLN03102 365 gvSILGL---ADVDVKNKEtqesvprdgktmgEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKD 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 1178481066 462 RIKELMkTSNGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:PLN03102 441 RSKDII-ISGGENISSVEVENVLYKYPKVLETAVVA 475
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
13-508 |
1.50e-15 |
|
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: 79.55 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 13 REQAKLLLNETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYA 92
Cdd:cd12117 4 EEQAARTPDAVAVVY----GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 93 TSAAKQVEYILNNADVKILfVGDQeeyncTLEIIDACPQiqkivtmkDNVDLKNHPKAcdwqtfllEGSPLQQTALQArl 172
Cdd:cd12117 80 ELPAERLAFMLADAGAKVL-LTDR-----SLAGRAGGLE--------VAVVIDEALDA--------GPAGNPAVPVSP-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 173 eqkqlTDLFTLIYTSGTTGEPKGVMLDYANLAhQLkAHDEAFTTLNVSqyDSSLSFLPLShiFERA----WVAyVLHRGA 248
Cdd:cd12117 136 -----DDLAYVMYTSGSTGRPKGVAVTHRGVV-RL-VKNTNYVTLGPD--DRVLQTSPLA--FDAStfeiWGA-LLNGAR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 249 VNCY----LEDTNRVREALSEIRPTLMcavprfyekiytavWdkvQKAPLFRrmifnwaiavgqkrfqfisqkkpipfvl 324
Cdd:cd12117 204 LVLApkgtLLDPDALGALIAEEGVTVL--------------W---LTAALFN---------------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 325 rqQYALADKLVLSKLRQLLGGRIRMMP---------CGGAKLepniglffhsigINvklGYGMTETTaTVSCW---EEGH 392
Cdd:cd12117 239 --QLADEDPECFAGLRELLTGGEVVSPphvrrvlaaCPGLRL------------VN---GYGPTENT-TFTTShvvTELD 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 393 FEPNS--IGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFL------KTGDAGEFDPQ 454
Cdd:cd12117 301 EVAGSipIGRPIANTRVYVldedgrpvppGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPD 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 455 GNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVSALIV 508
Cdd:cd12117 381 GRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLV 433
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
51-570 |
1.64e-15 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 79.80 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgdQEEYNCTLEIIDACP 130
Cdd:PRK06155 62 ALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV--EAALLAALEAADPGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 131 QIQKIVTMKDNVDLKNHPKAcdWQTfllegSPLQQTALQARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYA-------NL 203
Cdd:PRK06155 140 LPLPAVWLLDAPASVSVPAG--WST-----APLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 204 AHQL--KAHDEAFTTlnvsqydsslsfLPLSHIFERAWVAYVLHRGAVncyledtnrvrealseirptlMCAVPRFYEKI 281
Cdd:PRK06155 213 AEDLeiGADDVLYTT------------LPLFHTNALNAFFQALLAGAT---------------------YVLEPRFSASG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 282 YtavWDKVQKAplfrrmifnwaiavGQKRFQFISQKKPIpfVLRQQYALADKlvLSKLRQLLGGRIrmmpcGGAKLEPni 361
Cdd:PRK06155 260 F---WPAVRRH--------------GATVTYLLGAMVSI--LLSQPARESDR--AHRVRVALGPGV-----PAALHAA-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 362 glFFHSIGINVKLGYGMTETTATVSC-WEEGhfEPNSIGTLMPGAEVKI----------GENNEILVRG---GMVMRGYY 427
Cdd:PRK06155 312 --FRERFGVDLLDGYGSTETNFVIAVtHGSQ--RPGSMGRLAPGFEARVvdehdqelpdGEPGELLLRAdepFAFATGYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 428 KKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMKtSNGKYIAPQYIETKVGKDKFIEQIAVIAD----AKKYV 503
Cdd:PRK06155 388 GMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAVFPVpselGEDEV 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178481066 504 SALIVPcfnsleEYAKQLnikyhDRLELIKHSD-ILQMFE-QRINDLQKELPSFE--QIKKFTLLPQAFTT 570
Cdd:PRK06155 466 MAAVVL------RDGTAL-----EPVALVRHCEpRLAYFAvPRYVEFVAALPKTEngKVQKFVLREQGVTA 525
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
183-497 |
1.90e-15 |
|
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: 78.95 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLS-HIFERAWVAyVLHRGAvnCYLedtnrvre 261
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERY---GLTPGDRELQFASFNfDGAHEQLLP-PLICGA--CVV-------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 262 alseIRPTLMCAVPRFY-EKIYTAVWDKVQKAPLFRRMIFNWAIAVGQKRfqfisqkkPIPfvLRQQYALADKLVLSKLR 340
Cdd:cd17649 165 ----LRPDELWASADELaEMVRELGVTVLDLPPAYLQQLAEEADRTGDGR--------PPS--LRLYIFGGEALSPELLR 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 341 QLLGGRIRMmpcggaklepniglffhsigINvklGYGMTETTATVSCWE---EGHFEPNS--IGTLMPG----------A 405
Cdd:cd17649 231 RWLKAPVRL--------------------FN---AYGPTEATVTPLVWKceaGAARAGASmpIGRPLGGrsayildadlN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 406 EVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGF-------LKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQ 478
Cdd:cd17649 288 PVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgapgsrlYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELG 366
|
330
....*....|....*....
gi 1178481066 479 YIETKVGKDKFIEQIAVIA 497
Cdd:cd17649 367 EIEAALLEHPGVREAAVVA 385
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
183-509 |
2.02e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 79.16 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPL--SHIFERAWVAYVLHRGAVncyledtnrvr 260
Cdd:PRK05852 181 IMFTGGTTGLPKMVPWTHANIASSVRA---IITGYRLSPRDATVAVMPLyhGHGLIAALLATLASGGAV----------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 261 ealseirptLMCAVPRFYEKIYtavWDKVQKAPLfrrmifNWAIAVgqkrfqfisqkkpiPFVLRQQYALADKLVLSKLR 340
Cdd:PRK05852 247 ---------LLPARGRFSAHTF---WDDIKAVGA------TWYTAV--------------PTIHQILLERAATEPSGRKP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 341 QLLggriRMMPCGGAKLEPNIGLFFH-SIGINVKLGYGMTETT---ATVSCWEEGHFEPNSIGTLM----PGAEVKI--- 409
Cdd:PRK05852 295 AAL----RFIRSCSAPLTAETAQALQtEFAAPVVCAFGMTEAThqvTTTQIEGIGQTENPVVSTGLvgrsTGAQIRIvgs 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -------GENNEILVRGGMVMRGYYKKPQETADSFTeDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIET 482
Cdd:PRK05852 371 dglplpaGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEG 448
|
330 340 350
....*....|....*....|....*....|.
gi 1178481066 483 KVGKDKFIEQIAVIADAKKY----VSALIVP 509
Cdd:PRK05852 449 VLASHPNVMEAAVFGVPDQLygeaVAAVIVP 479
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
183-457 |
2.14e-15 |
|
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: 80.29 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLSH------IFeRAWVA----YVLHRGAvncy 252
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY---GLGPGDRVLQFASLSFdasvweIF-GALLSgatlVLAPPEA---- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LEDTNRVREALSEIRPTLMCAVPrfyekiytAVWdkvqkaplfrrmifnwaiavgqkrfqfisqkkpipfvlrQQYALAD 332
Cdd:COG1020 694 RRDPAALAELLARHRVTVLNLTP--------SLL---------------------------------------RALLDAA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 333 KLVLSKLRQLLggrirmmpCGGAKLEPNIGLFFHSIGINVKL--GYGMTETTATVSCWE----EGHFEPNSIGTLMPGAE 406
Cdd:COG1020 727 PEALPSLRLVL--------VGGEALPPELVRRWRARLPGARLvnLYGPTETTVDSTYYEvtppDADGGSVPIGRPIANTR 798
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 407 VKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFL-------KTGDAGEFDPQGNL 457
Cdd:COG1020 799 VYVldahlqpvpvGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfpgarlyRTGDLARWLPDGNL 866
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
176-520 |
3.94e-15 |
|
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: 77.89 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 176 QLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDE----AFTTLNVSQYdSSLSFLPLSHIFERAWVA----YVLHRG 247
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRReyelDSFPVRLLQM-ASFSFDVFAGDFARSLLNggtlVICPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 248 AVncylEDTNRVREALSEIRPTLMCAVPrfyekiytavwdkvqkaplfrrmifnwAIAvgqkrfqfisqkkpIPFVlrqQ 327
Cdd:cd17650 170 VK----LDPAALYDLILKSRITLMESTP---------------------------ALI--------------RPVM---A 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 328 YALADKLVLSKLRQLLGGRIRMMPCGGAKLEPNIGLffHSIGINvklGYGMTETTATVSCWEEG-------HFEPnsIGT 400
Cdd:cd17650 202 YVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQ--GMRIIN---SYGVTEATIDSTYYEEGrdplgdsANVP--IGR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 401 LMPGAE----------VKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGF------LKTGDAGEFDPQGNLYITDRIK 464
Cdd:cd17650 275 PLPNTAmyvlderlqpQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVD 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 465 ELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIA--DAK--KYVSALIVPC----FNSLEEYAKQ 520
Cdd:cd17650 355 HQVKI-RGFRIELGEIESQLARHPAIDEAVVAVreDKGgeARLCAYVVAAatlnTAELRAFLAK 417
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
36-500 |
4.61e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 78.07 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgD 115
Cdd:PRK08162 44 RTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV-D 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 116 QEEYNCTLEIIDACPQIQKIVTmkdNVDLKNHPKA-----CDWQTFLLEGSPlqqtALQARLEQKQLtDLFTLIYTSGTT 190
Cdd:PRK08162 123 TEFAEVAREALALLPGPKPLVI---DVDDPEYPGGrfigaLDYEAFLASGDP----DFAWTLPADEW-DAIALNYTSGTT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 191 GEPKGVMLdyanlaHQLKAHDEAFTTL---NVSQYDSSLSFLPLSHI----FerAWVayVLHRGAVNCYLE--DTNRVRE 261
Cdd:PRK08162 195 GNPKGVVY------HHRGAYLNALSNIlawGMPKHPVYLWTLPMFHCngwcF--PWT--VAARAGTNVCLRkvDPKLIFD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 262 ALSEIRPTLMCAVPRFYEKIYTAVWDKvqKAPLFRRMIFNWAIAvgqkrfqfisqkKPIPFVLrqqyaladklvlsklrq 341
Cdd:PRK08162 265 LIREHGVTHYCGAPIVLSALINAPAEW--RAGIDHPVHAMVAGA------------APPAAVI----------------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 342 llggrirmmpcggAKLEpniglffhSIGINVKLGYGMTET--TATVSCWEEG--------------------HFEpNSIG 399
Cdd:PRK08162 314 -------------AKME--------EIGFDLTHVYGLTETygPATVCAWQPEwdalplderaqlkarqgvryPLQ-EGVT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 400 TLMP--GAEV-KIGEN-NEILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYI 475
Cdd:PRK08162 372 VLDPdtMQPVpADGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENI 449
|
490 500
....*....|....*....|....*..
gi 1178481066 476 APQYIETKVGKDKFIEQIAVIA--DAK 500
Cdd:PRK08162 450 SSIEVEDVLYRHPAVLVAAVVAkpDPK 476
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
36-535 |
8.99e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 77.11 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgd 115
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIY-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 116 QEEYNCTLE-IIDACPQIQKIVTMKDNVDLKNHPKacdwqtflLEGSPLQQTaLQARLEQKQltdlfTLIYTSGTTGEPK 194
Cdd:PRK13382 147 DEEFSATVDrALADCPQATRIVAWTDEDHDLTVEV--------LIAAHAGQR-PEPTGRKGR-----VILLTSGTTGTPK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 195 GvmldyanlahqlkahdeafttlnvSQYDSSLSFLPLSHIFERA-WVAYvlhrgavncyledtnrvrealseiRPTLMCA 273
Cdd:PRK13382 213 G------------------------ARRSGPGGIGTLKAILDRTpWRAE------------------------EPTVIVA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 274 vPRFYekiytaVWDkvqkaplFRRMIFNWAIA---VGQKRF------QFISQKKP-----IPFVLRQQYALADKLvlskL 339
Cdd:PRK13382 245 -PMFH------AWG-------FSQLVLAASLActiVTRRRFdpeatlDLIDRHRAtglavVPVMFDRIMDLPAEV----R 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 340 RQLLGGRIRMMPCGGAKLEPNIGL-FFHSIGINVKLGYGMTE----TTATVscwEEGHFEPNSIGTLMPGAEVKI----- 409
Cdd:PRK13382 307 NRYSGRSLRFAAASGSRMRPDVVIaFMDQFGDVIYNNYNATEagmiATATP---ADLRAAPDTAGRPAEGTEIRIldqdf 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -----GENNEILVRGGMVMRGYykKPQETADsfTEDGFLKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKV 484
Cdd:PRK13382 384 revptGEVGTIFVRNDTQFDGY--TSGSTKD--FHDGFMASGDVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVEKTL 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1178481066 485 GKDKFIEQIAVIA-DAKKY---VSALIVPcfnSLEEYAKQLNIKYHDRLELIKHS 535
Cdd:PRK13382 459 ATHPDVAEAAVIGvDDEQYgqrLAAFVVL---KPGASATPETLKQHVRDNLANYK 510
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
76-481 |
3.74e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 75.12 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 76 ADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILF--------VGDQEEYNCTLEIIDACPQIQ---KIvtmkDNVDL 144
Cdd:PRK12406 52 AAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahadllhgLASALPAGVTVLSVPTPPEIAaayRI----SPALL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 145 KNHPKACDWQTFLLEGSPLQQTALQARLeqkqltdlfTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTTLNVSQYDS 224
Cdd:PRK12406 128 TPPAGAIDWEGWLAQQEPYDGPPVPQPQ---------SMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRALIYGLKPGIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 225 SLSFLPLSHiferawvayvlhrGAVNCYLEDTNRVREALseirpTLMcavPRFYEKIYTAVWDKVQKAPLFrrMIfnwai 304
Cdd:PRK12406 199 ALLTGPLYH-------------SAPNAYGLRAGRLGGVL-----VLQ---PRFDPEELLQLIERHRITHMH--MV----- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 305 avgqkrfqfisqkkPIPFV--LRQQYALADKLVLSKLRQLLGGrirMMPCGG----AKLE---PNIGLFfhsiginvklg 375
Cdd:PRK12406 251 --------------PTMFIrlLKLPEEVRAKYDVSSLRHVIHA---AAPCPAdvkrAMIEwwgPVIYEY----------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 376 YGMTETTATVSCWEEGHF-EPNSIGTLMPGAEVKI----------GENNEILVR-GGMVMRGYYKKPQETAdSFTEDGFL 443
Cdd:PRK12406 303 YGSTESGAVTFATSEDALsHPGTVGKAAPGAELRFvdedgrplpqGEIGEIYSRiAGNPDFTYHNKPEKRA-EIDRGGFI 381
|
410 420 430
....*....|....*....|....*....|....*...
gi 1178481066 444 KTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIE 481
Cdd:PRK12406 382 TSGDVGYLDADGYLFLCDRKRD-MVISGGVNIYPAEIE 418
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
179-509 |
1.03e-13 |
|
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: 73.66 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHdeaFTTLNVSQYDSSLSFLPLShiFERAW---VAYVLHRGAVNCYLED 255
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE---REKTNINFSDKVLQFATCS--FDVCYqeiFSTLLSGGTLYIIREE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 256 TNRvrealseirptlmcAVPRFYEKIYTAVWDKVQKAPLFRRMIFNwaiavgQKRFqfisqKKPIPFVLRQQYALADKLV 335
Cdd:cd17656 204 TKR--------------DVEQLFDLVKRHNIEVVFLPVAFLKFIFS------EREF-----INRFPTCVKHIITAGEQLV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 336 LSKLRQllggriRMMpcggakLEPNIGLFFHsiginvklgYGMTE----TTATVSCWEEGHFEP--------------NS 397
Cdd:cd17656 259 ITNEFK------EML------HEHNVHLHNH---------YGPSEthvvTTYTINPEAEIPELPpigkpisntwiyilDQ 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 398 IGTLMPgaevkIGENNEILVRGGMVMRGYYKKPQETADSFTEDGF------LKTGDAGEFDPQGNLYITDRIKELMKTsN 471
Cdd:cd17656 318 EQQLQP-----QGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-R 391
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1178481066 472 GKYIAPQYIETKVGKDKFIEQIAVIADA----KKYVSALIVP 509
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVM 433
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
335-481 |
1.98e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 72.13 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 335 VLSKLRQLLGGR----IRMMPCGGAKLEPNIGLFFH-SIGINVKLGYGMTETTATVSC-WEEGHFEPNSIGTLMPGAEVK 408
Cdd:cd05944 107 VYAALLQVPVNAdissLRFAMSGAAPLPVELRARFEdATGLPVVEGYGLTEATCLVAVnPPDGPKRPGSVGLRLPYARVR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 409 I---------------GENNEILVRGGMVMRGYYKKpQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGK 473
Cdd:cd05944 187 IkvldgvgrllrdcapDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGH 264
|
....*...
gi 1178481066 474 YIAPQYIE 481
Cdd:cd05944 265 NIDPALIE 272
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
404-481 |
3.49e-13 |
|
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: 71.98 E-value: 3.49e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 404 GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQYIE 481
Cdd:cd05920 327 GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVE 403
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
404-481 |
3.63e-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: 72.10 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMktsN--GKYIAPQYIE 481
Cdd:COG1021 372 GNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQI---NrgGEKIAAEEVE 448
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
36-500 |
3.95e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 72.08 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVGD 115
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 116 ---QEEYNCTLEII--DACPQIQKIVTMKDNVDLKNHPKACDWqtFLLEGSPLQQTALQARLEQKQLTDLFTLIYTSGTT 190
Cdd:PRK06164 116 gfkGIDFAAILAAVppDALPPLRAIAVVDDAADATPAPAPGAR--VQLFALPDPAPPAAAGERAADPDAGALLFTTSGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 191 GEPKGVMLDYANLAHQLKAHDEAfttLNVSQYDSSLSFLPLSHIFERAWVAYVLHRGAVNCYLE--DTNRVREALSEIRP 268
Cdd:PRK06164 194 SGPKLVLHRQATLLRHARAIARA---YGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPvfDAARTARALRRHRV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 269 TLMCAVPRFYEKIYtavwDKVQKAPLFRRMifnwaiavgqKRFQFISqkkpipFvlrqQYALADklVLSKLRQllggriR 348
Cdd:PRK06164 271 THTFGNDEMLRRIL----DTAGERADFPSA----------RLFGFAS------F----APALGE--LAALARA------R 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 349 MMPCGGAklepniglffhsiginvklgYGMTETTATVSCWEEGHFEPNSI---GTLM-PGAEVKI-----------GENN 413
Cdd:PRK06164 319 GVPLTGL--------------------YGSSEVQALVALQPATDPVSVRIeggGRPAsPEARVRArdpqdgallpdGESG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 414 EILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIEtkvgkdKFIEQI 493
Cdd:PRK06164 379 EIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIE------HALEAL 451
|
....*..
gi 1178481066 494 AVIADAK 500
Cdd:PRK06164 452 PGVAAAQ 458
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
184-497 |
7.16e-13 |
|
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: 70.80 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 184 IYTSGTTGEPKGVMLDYANLAHQLKA--------HDEAFTTLNVSQYDSSL--SFLPLSHIFERAWVAYvlhrgavncyl 253
Cdd:cd17643 99 IYTSGSTGRPKGVVVSHANVLALFAAtqrwfgfnEDDVWTLFHSYAFDFSVweIWGALLHGGRLVVVPY----------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 254 eDTNRVREAlseirptlmcavprfyekiytavwdkvqkaplFRRMIFNWAIAVgqkrfqfISQKkPIPFvlrqqYALADK 333
Cdd:cd17643 168 -EVARSPED--------------------------------FARLLRDEGVTV-------LNQT-PSAF-----YQLVEA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 334 LVLSKLRQLlggRIRMMPCGGAKLEPN-IGLFFHSIG------INvklGYGMTETTATVScweeghFEP----------- 395
Cdd:cd17643 202 ADRDGRDPL---ALRYVIFGGEALEAAmLRPWAGRFGldrpqlVN---MYGITETTVHVT------FRPldaadlpaaaa 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 396 NSIGTLMPG----------AEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGF-------LKTGDAGEFDPQGNLY 458
Cdd:cd17643 270 SPIGRPLPGlrvyvldadgRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELE 349
|
330 340 350
....*....|....*....|....*....|....*....
gi 1178481066 459 ITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:cd17643 350 YLGRADEQVKI-RGFRIELGEIEAALATHPSVRDAAVIV 387
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
51-507 |
8.04e-13 |
|
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: 70.76 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 51 ALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgdqEEYNCTLEIIDACP 130
Cdd:cd12114 28 ALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT---DGPDAQLDVAVFDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 131 QIQKIVtmkdnvdlknhpkacdwqtfLLEGSPLQQTALQArleqkqLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAH 210
Cdd:cd12114 105 LILDLD--------------------ALAAPAPPPPVDVA------PDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 211 DEAFttlNVSQYD-----SSLSF-LPLSHIFE--RAWVAYVLHRGAvncYLEDTNRVREALSEIRPTLMCAVPrfyekiy 282
Cdd:cd12114 159 NRRF---AVGPDDrvlalSSLSFdLSVYDIFGalSAGATLVLPDEA---RRRDPAHWAELIERHGVTLWNSVP------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 283 tAVWDkvqkaplfrrMIFNWAIAVGQkrfqfisqkkpipfvlrqqyaladklVLSKLR-QLLGG---------RIRmmpc 352
Cdd:cd12114 226 -ALLE----------MLLDVLEAAQA--------------------------LLPSLRlVLLSGdwipldlpaRLR---- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 353 ggaKLEPNIGlfFHSIGinvklgyGMTETtatvSCW------EEGHFEPNSIGTLMP------------GAEVKIGENNE 414
Cdd:cd12114 265 ---ALAPDAR--LISLG-------GATEA----SIWsiyhpiDEVPPDWRSIPYGRPlanqryrvldprGRDCPDWVPGE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 415 ILVRGGMVMRGYYKKPQETADSFTEDG----FLKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFI 490
Cdd:cd12114 329 LWIGGRGVALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGV 407
|
490
....*....|....*..
gi 1178481066 491 EQIAVIADAKKYVSALI 507
Cdd:cd12114 408 ARAVVVVLGDPGGKRLA 424
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
21-499 |
8.42e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 70.67 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 21 NETALRYHTpsgwENISWHQFQQDLDtfSYALLANHIGV--QDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQ 98
Cdd:PRK09029 18 QAIALRLND----EVLTWQQLCARID--QLAAGFAQQGVveGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 99 VEYILNNADVKILFVGDQEeynctleiidacPQIQKIVTmkDNVDLKNHPKACDWQtfllegspLQQTAlqarleqkqlt 178
Cdd:PRK09029 92 LEELLPSLTLDFALVLEGE------------NTFSALTS--LHLQLVEGAHAVAWQ--------PQRLA----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 dlfTLIYTSGTTGEPKGVmldyanlAHQLKAH-DEAFTTLNV---SQYDSSLSFLPLSH-----IFERaWvayvLHRGAV 249
Cdd:PRK09029 139 ---TMTLTSGSTGLPKAA-------VHTAQAHlASAEGVLSLmpfTAQDSWLLSLPLFHvsgqgIVWR-W----LYAGAT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 250 nCYLEDTNRVREALSeirptlMCA----VPrfyekiyTAVWdkvqkaplfrRMIFNWAIAVGQKRFqfisqkkpipfvlr 325
Cdd:PRK09029 204 -LVVRDKQPLEQALA------GCThaslVP-------TQLW----------RLLDNRSEPLSLKAV-------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 326 qqyaladklvlsklrqLLGGRirMMPcggAKLEPNIglffHSIGINVKLGYGMTETTATVsCWEEGHFEPNsIGTLMPGA 405
Cdd:PRK09029 246 ----------------LLGGA--AIP---VELTEQA----EQQGIRCWCGYGLTEMASTV-CAKRADGLAG-VGSPLPGR 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 406 EVKIgENNEILVRGGMVMRGYYKKPQETadSFT-EDGFLKTGDAGEFDpQGNLYITDRIKElMKTSNGKYIAPQYIETKV 484
Cdd:PRK09029 299 EVKL-VDGEIWLRGASLALGYWRQGQLV--PLVnDEGWFATRDRGEWQ-NGELTILGRLDN-LFFSGGEGIQPEEIERVI 373
|
490
....*....|....*..
gi 1178481066 485 GKDKFIEQIAV--IADA 499
Cdd:PRK09029 374 NQHPLVQQVFVvpVADA 390
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
170-509 |
9.21e-13 |
|
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: 70.66 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 170 ARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLShiFErawvAYVLhrgav 249
Cdd:cd17645 96 AKILLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYF---GVTPADKSLVYASFS--FD----ASAW----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 250 ncyledtnrvrealsEIRPTLMCAvprfyekiytavwdkvqkAPLFrrmIFNWAIAVGQKRFQ--FISQKKPIPFVLRQq 327
Cdd:cd17645 162 ---------------EIFPHLTAG------------------AALH---VVPSERRLDLDALNdyFNQEGITISFLPTG- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 328 yaladklVLSKLRQLLGGRIRMMPCGGAKLEPniglfFHSIGINVKLGYGMTETTATVSCWEEGHFEPN-SIGTLMPGAE 406
Cdd:cd17645 205 -------AAEQFMQLDNQSLRVLLTGGDKLKK-----IERKGYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPIDNTR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 407 VKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGFL------KTGDAGEFDPQGNLYITDRIKELMKTs 470
Cdd:cd17645 273 VYIldealqlqpiGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI- 351
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1178481066 471 NGKYIAPQYIETKVGKDKFIEQIAVIA----DAKKYVSALIVP 509
Cdd:cd17645 352 RGYRIEPGEIEPFLMNHPLIELAAVLAkedaDGRKYLVAYVTA 394
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
163-584 |
1.02e-12 |
|
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: 70.54 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 163 LQQTALQARLEQKQltDLFTLIYTSGTTGEPKGVMLDY---ANLAHQLKAHDEAFTTLNVSQYdSSLSF-LPLSHIFEra 238
Cdd:cd17644 93 LEDAQISVLLTQPE--NLAYVIYTSGSTGKPKGVMIEHqslVNLSHGLIKEYGITSSDRVLQF-ASIAFdVAAEEIYV-- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 239 wvayVLHRGAvncyledTNRVREAlsEIRPTLmcavprfyekiyTAVWDKVQKaplfrrmifnWAIAVgqkrfqfisqkk 318
Cdd:cd17644 168 ----TLLSGA-------TLVLRPE--EMRSSL------------EDFVQYIQQ----------WQLTV------------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 319 pIPFVLRQQYALADKLVLSKLRqlLGGRIRMMPCGGAKLEPN-IGLFFHSIGINVKL--GYGMTETTATVSCWE-----E 390
Cdd:cd17644 201 -LSLPPAYWHLLVLELLLSTID--LPSSLRLVIVGGEAVQPElVRQWQKNVGNFIQLinVYGPTEATIAATVCRltqltE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 391 GHFEPNSIGTLMPGAE----------VKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFL--------KTGDAGEFD 452
Cdd:cd17644 278 RNITSVPIGRPIANTQvyildenlqpVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlyKTGDLARYL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 453 PQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIA----DAKKYVSALIVPcfnsleEYAKQLNIKYhdr 528
Cdd:cd17644 358 PDGNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVIVredqPGNKRLVAYIVP------HYEESPSTVE--- 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 529 lelikhsdiLQMFeqrindLQKELPSFeqikkftLLPQAFTTkMEE--ITPTLKLRRK 584
Cdd:cd17644 428 ---------LRQF------LKAKLPDY-------MIPSAFVV-LEElpLTPNGKIDRR 462
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-484 |
1.16e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.35 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 4 LNLHFVNRIREQAKLLLNETALRYHTPSGWEN--ISWHQFQQDLDTFSYALLAnHIGVQDKIAIFAHNMPRWTIADIGTM 81
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGvvLSYRDLDLRARTIAAALQA-RASFGDRAVLLFPSGPDYVAAFFGCL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 82 QVRAVVVPIYATSAAKQveyilnNADVKILFVGDQEEYNCTLEIIDACPQIQKIVTMKDN-------VDLKNHPKACDWQ 154
Cdd:PRK05691 86 YAGVIAVPAYPPESARR------HHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAAnapellcVDTLDPALAEAWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 155 tfllegsplqQTALQArleqkqlTDLFTLIYTSGTTGEPKGVMLDYANLA--HQLKAHDEAfttLNVSQYDSSLSFLPLS 232
Cdd:PRK05691 160 ----------EPALQP-------DDIAFLQYTSGSTALPKGVQVSHGNLVanEQLIRHGFG---IDLNPDDVIVSWLPLY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 233 H-----------IFerAWVAYVLHrgAVNCYLEDTNRVREALSEIRPTLMCAvPRFyekIYTAVWDKVQKAPLFRRMIFN 301
Cdd:PRK05691 220 HdmgliggllqpIF--SGVPCVLM--SPAYFLERPLRWLEAISEYGGTISGG-PDF---AYRLCSERVSESALERLDLSR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 302 WAIAvgqkrfqfISQKKPIpfvlRQQY--ALADKLVlsklrqllggrirmmPCGgakLEPNIglFFHSiginvklgYGMT 379
Cdd:PRK05691 292 WRVA--------YSGSEPI----RQDSleRFAEKFA---------------ACG---FDPDS--FFAS--------YGLA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 380 ETTATVSCWEEG----------------HFEPN------SIGTLMPGAEVKI---------GENN--EILVRGGMVMRGY 426
Cdd:PRK05691 332 EATLFVSGGRRGqgipaleldaealarnRAEPGtgsvlmSCGRSQPGHAVLIvdpqslevlGDNRvgEIWASGPSIAHGY 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178481066 427 YKKPQETADSFTE-DG--FLKTGDAGeFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKV 484
Cdd:PRK05691 412 WRNPEASAKTFVEhDGrtWLRTGDLG-FLRDGELFVTGRLKD-MLIVRGHNLYPQDIEKTV 470
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
31-468 |
4.82e-12 |
|
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: 68.10 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 31 SGWENISWhqfqQDLDTFSYALlANHI---GVQ--DKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNN 105
Cdd:cd17653 18 SLGGSLTY----GELDAASNAL-ANRLlqlGVVpgDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 106 AdvkilfvgdqeeyNCTLEIIDACPQiqkivtmkdnvdlknhpkacdwqtfllegsplqqtalqarleqkqltDLFTLIY 185
Cdd:cd17653 93 S-------------GATLLLTTDSPD-----------------------------------------------DLAYIIF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 186 TSGTTGEPKGVMLDYANLAHQLkahDEAFTTLNVSQYDSSLSFLPLShiFER-AWVAYV-LHRGAVnCYLEDTNRVREAL 263
Cdd:cd17653 113 TSGSTGIPKGVMVPHRGVLNYV---SQPPARLDVGPGSRVAQVLSIA--FDAcIGEIFStLCNGGT-LVLADPSDPFAHV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 264 SEIRPTLMCAvPRFYEKIYTAVWDKVqkaplfrRMIFNWAIAVGQkrfqfisqkkpipfvlrqqyALADKLvlsklrqll 343
Cdd:cd17653 187 ARTVDALMST-PSILSTLSPQDFPNL-------KTIFLGGEAVPP--------------------SLLDRW--------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 344 GGRIRMmpcggaklepniglffhsigINvklGYGMTETTATVSCWEEGHFEPNSIGTLMPGA----------EVKIGENN 413
Cdd:cd17653 230 SPGRRL--------------------YN---AYGPTECTISSTMTELLPGQPVTIGKPIPNStcyildadlqPVPEGVVG 286
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1178481066 414 EILVRGGMVMRGYYKKPQETADSFTEDGF------LKTGDAGEFDPQGNLYITDRIKELMK 468
Cdd:cd17653 287 EICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVK 347
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
305-529 |
2.40e-11 |
|
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: 65.12 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 305 AVGQKRFQFISQKKpipfVLRQQYALADKLVLSKLRQLLG-----GRIRMMPCGGAKLEPNIGLFFHSIGINVKL--GYG 377
Cdd:cd17633 69 FIGQRKFNPKSWIR----KINQYNATVIYLVPTMLQALARtlepeSKIKSIFSSGQKLFESTKKKLKNIFPKANLieFYG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 378 MTETT-ATVSCWEEGHfEPNSIGTLMPGAEVKI-----GENNEILVRGGMVMRGYYKkpqetADSFTEDGFLKTGDAGEF 451
Cdd:cd17633 145 TSELSfITYNFNQESR-PPNSVGRPFPNVEIEIrnadgGEIGKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 452 DPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVSALIVPCFNSLEEYAKQLNIKYHDRL 529
Cdd:cd17633 219 DEEGYLYLVGRESD-MIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRFLKQKL 295
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1-502 |
2.72e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 66.19 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 1 MTNLNLHFVNRIREQAKLLLNETALRyhTPSGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGT 80
Cdd:PRK05857 9 MPQLPSTVLDRVFEQARQQPEAIALR--RCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 81 MQVRAVVVPIYATSAAKQVEYILNNADVKILFV--GDQEEYNCTLEIIDACPQIqkivtmKDNVDLKNHPKACDWQTFLL 158
Cdd:PRK05857 87 AKLGAIAVMADGNLPIAAIERFCQITDPAAALVapGSKMASSAVPEALHSIPVI------AVDIAAVTRESEHSLDAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 159 EGSPLQQTalqarleqkqlTDLFTLIYTSGTTGEPKGVML---DYANLAHQLKAHDEAFTTLNVSQydSSLSFLPLSHIF 235
Cdd:PRK05857 161 AGNADQGS-----------EDPLAMIFTSGTTGEPKAVLLanrTFFAVPDILQKEGLNWVTWVVGE--TTYSPLPATHIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 236 ERAWVAYVLHRGAVnCYL--EDTNRVREALSEIRPTLMCAVPRFYEKIytavwdkvqkaplfrrmifnwaiavgqkrfqf 313
Cdd:PRK05857 228 GLWWILTCLMHGGL-CVTggENTTSLLEILTTNAVATTCLVPTLLSKL-------------------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 314 ISQKKpipfvlrqqyaLADKLVLSklrqllggrIRMMPCGGAKLEPNIGLFFHSIGINVKLGYGMTETTATVSCWEE--- 390
Cdd:PRK05857 275 VSELK-----------SANATVPS---------LRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALCLPTddg 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 391 --GHFEPNSIGTLMPGAEVKIGENN----------------EILVRGGMVMRGYYKKPQETADSFTeDGFLKTGDAGEFD 452
Cdd:PRK05857 335 siVKIEAGAVGRPYPGVDVYLAATDgigptapgagpsasfgTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERR 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1178481066 453 PQGNLYITDRIKElMKTSNGKYIAPQYIetkvgkDKFIEQIAVIADAKKY 502
Cdd:PRK05857 414 EDGFFYIKGRSSE-MIICGGVNIAPDEV------DRIAEGVSGVREAACY 456
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
85-496 |
5.24e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 65.57 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 85 AVVVPIYATSAAKQVEYILNNADVKILfVGDQEEYNCTLEIIDACPQIQKIVTMKDN------VDLKNHPKACDWQTfLL 158
Cdd:PRK05620 89 AVFNPLNKQLMNDQIVHIINHAEDEVI-VADPRLAEQLGEILKECPCVRAVVFIGPSdadsaaAHMPEGIKVYSYEA-LL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 159 EGSP-------LQQTALQArleqkqltdlftLIYTSGTTGEPKGVMLDYANL---AHQLKAHDeaftTLNVSQYDSSLSF 228
Cdd:PRK05620 167 DGRStvydwpeLDETTAAA------------ICYSTGTTGAPKGVVYSHRSLylqSLSLRTTD----SLAVTHGESFLCC 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 229 LPLSHIFerAW-VAYVLHRGAVNCYLEDTNRVREALSEIRPTLMcavPRFYEKIYTaVWDKVqkaplfrrmifnwaiavg 307
Cdd:PRK05620 231 VPIYHVL--SWgVPLAAFMSGTPLVFPGPDLSAPTLAKIIATAM---PRVAHGVPT-LWIQL------------------ 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 308 qkrFQFISQKKPIPFVLRQQYAladklvlsklrqllggrirmmpcGGAKLEPN-IGLFFHSIGINVKLGYGMTETTA--T 384
Cdd:PRK05620 287 ---MVHYLKNPPERMSLQEIYV-----------------------GGSAVPPIlIKAWEERYGVDVVHVWGMTETSPvgT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 385 VSC----------W----EEGHFePNSI-------GTLMPGAEVKIGEnneILVRGGMVMRGYYKKPQET---------- 433
Cdd:PRK05620 341 VARppsgvsgearWayrvSQGRF-PASLeyrivndGQVMESTDRNEGE---IQVRGNWVTASYYHSPTEEgggaastfrg 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 434 ------ADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKtSNGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:PRK05620 417 edvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVI 484
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
37-496 |
5.37e-11 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 64.83 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 37 SWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILfvgdq 116
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 117 eeynctleiidacpqiqkIVTmkdnvdlknhpkacdwqtfllegsplqqtalQARLEQKQLTDLFTLIYTSGTTGEPKGV 196
Cdd:cd05969 77 ------------------ITT-------------------------------EELYERTDPEDPTLLHYTSGTTGTPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 197 mldyanlahqLKAHDEAfttlnVSQYDSSLSFLPLS------HIFERAWVAYVLH-------RGAVNCYLE---DTNRVR 260
Cdd:cd05969 108 ----------LHVHDAM-----IFYYFTGKYVLDLHpddiywCTADPGWVTGTVYgiwapwlNGVTNVVYEgrfDAESWY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 261 EALSEIRPTLMCAVPrfyekiyTAvwdkvqkaplFRRMifnwaiavgqkrfqfisqkkpipfvLRQQYALADKLVLSKLR 340
Cdd:cd05969 173 GIIERVKVTVWYTAP-------TA----------IRML-------------------------MKEGDELARKYDLSSLR 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 341 QLLGGrirmmpcgGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSC-WEEGHFEPNSIGTLMPGAEVKI--------- 409
Cdd:cd05969 211 FIHSV--------GEPLNPEAIRWGMEVfGVPIHDTWWQTETGSIMIAnYPCMPIKPGSMGKPLPGVKAAVvdengnelp 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 410 -GENNEILVRGGM--VMRGYYKKPQETADSFTeDGFLKTGDAGEFDPQGNLYITDRIKELMKTSnGKYIAPQYIETKVGK 486
Cdd:cd05969 283 pGTKGILALKPGWpsMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALME 360
|
490
....*....|
gi 1178481066 487 DKFIEQIAVI 496
Cdd:cd05969 361 HPAVAEAGVI 370
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-195 |
5.47e-11 |
|
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: 65.59 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 24 ALRYHTPSGW-ENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYI 102
Cdd:cd05968 79 ALRWEGEDGTsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 103 LNNADVKILFVGD-----QEEYNCTLEIIDA---CPQIQKIVTMKD-NVDLKNHPKACDWqtfllegSPLQQTALQARLE 173
Cdd:cd05968 159 LQDAEAKALITADgftrrGREVNLKEEADKAcaqCPTVEKVVVVRHlGNDFTPAKGRDLS-------YDEEKETAGDGAE 231
|
170 180
....*....|....*....|..
gi 1178481066 174 QKQLTDLFTLIYTSGTTGEPKG 195
Cdd:cd05968 232 RTESEDPLMIIYTSGTTGKPKG 253
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
369-509 |
6.95e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.63 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 369 GINVKLGYGMTETTATVSCWEEGHF--EPNSIGTLMPGAEVKIGENN--EILVRGGMVMRGYYkkPQetadSFTEDGFLK 444
Cdd:PRK07445 254 QLRLAPTYGMTETASQIATLKPDDFlaGNNSSGQVLPHAQITIPANQtgNITIQAQSLALGYY--PQ----ILDSQGIFE 327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 445 TGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKKY----VSALIVP 509
Cdd:PRK07445 328 TDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwgevVTAIYVP 395
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
169-509 |
7.20e-11 |
|
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: 64.65 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 169 QARLEQKQLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFT------TLNVSQYDSSLS----FLPLSHIFERA 238
Cdd:cd12115 96 QARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSaeelagVLASTSICFDLSvfelFGPLATGGKVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 239 WVAYVLHrgavncyLEDTnrvrEALSEIrpTLMCAVPrfyekiyTAVWDKVQKAPLFR--RMIfNWAiavGQkrfqfisq 316
Cdd:cd12115 176 LADNVLA-------LPDL----PAAAEV--TLINTVP-------SAAAELLRHDALPAsvRVV-NLA---GE-------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 317 kkPIPFVLRQQyaLADKLVLSKLRQLlggrirmmpcggaklepniglffhsiginvklgYGMTETT--ATVSCWEEGHFE 394
Cdd:cd12115 224 --PLPRDLVQR--LYARLQVERVVNL---------------------------------YGPSEDTtySTVAPVPPGASG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 395 PNSIGTLMPG----------AEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFL------KTGDAGEFDPQGNLY 458
Cdd:cd12115 267 EVSIGRPLANtqayvldralQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLE 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1178481066 459 ITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVI----ADAKKYVSALIVP 509
Cdd:cd12115 347 FLGRADNQVKV-RGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVA 400
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
399-481 |
7.52e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.03 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 399 GTLMPGAEVKI-GENNE---------ILVRGGMVMRGYYKKpQETADSFTEDGFLKTGDAGeFDPQGNLYITDRIKELMk 468
Cdd:PRK09192 388 GKALPGHEIEIrNEAGMplpervvghICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI- 464
|
90
....*....|...
gi 1178481066 469 TSNGKYIAPQYIE 481
Cdd:PRK09192 465 IINGRNIWPQDIE 477
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-499 |
8.46e-11 |
|
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: 64.60 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 12 IREQAKLLLNETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIY 91
Cdd:cd17646 4 VAEQAARTPDAPAVVD----EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 92 ATSAAKQVEYILNNADVKILFVGDQEEynctleiiDACPqiqkivtmkdnvDLKNHPKACDWQTFLLEGSPLQQTALQAr 171
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLA--------ARLP------------AGGDVALLGDEALAAPPATPPLVPPRPD- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 172 leqkqltDLFTLIYTSGTTGEPKGVMLDYANLAHQLK--AHDEAFTTLNVSQYDSSLSF--------LPLSHiferawva 241
Cdd:cd17646 139 -------NLAYVIYTSGSTGRPKGVMVTHAGIVNRLLwmQDEYPLGPGDRVLQKTPLSFdvsvwelfWPLVA-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 242 yvlhrGAvncyledtnrvrealseirpTLMCAVPrfyekiytavwDKVQKAPLFRRMIFNWAIAVgqkrFQFIsqkkpiP 321
Cdd:cd17646 204 -----GA--------------------RLVVARP-----------GGHRDPAYLAALIREHGVTT----CHFV------P 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 322 FVLRQQYALADKLVLSKLRQLLggrirmmpCGGAKLEPNIGLFFHSI-GINVKLGYGMTETTATVSCWE---EGHFEPNS 397
Cdd:cd17646 238 SMLRVFLAEPAAGSCASLRRVF--------CSGEALPPELAARFLALpGAELHNLYGPTEAAIDVTHWPvrgPAETPSVP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 398 IGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGF------LKTGDAGEFDPQGNLYITD 461
Cdd:cd17646 310 IGRPVPNTRLYVlddalrpvpvGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLG 389
|
490 500 510
....*....|....*....|....*....|....*...
gi 1178481066 462 RIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIADA 499
Cdd:cd17646 390 RSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVVARA 426
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
98-481 |
1.13e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 64.34 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 98 QVEYILNNADVKILFvgdqeeYNCT-LEIIDA----CPQIQKIVTMKDNVDL--KNHPKACdWQTfLLEGsplQQTALQ- 169
Cdd:PRK07008 102 QIAYIVNHAEDRYVL------FDLTfLPLVDAlapqCPNVKGWVAMTDAAHLpaGSTPLLC-YET-LVGA---QDGDYDw 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 170 ARLEQKQLTdlfTLIYTSGTTGEPKGVMldYANLAHQLKAHDEAF-TTLNVSQYDSSLSFLPLSHIfeRAW-VAYVLhrG 247
Cdd:PRK07008 171 PRFDENQAS---SLCYTSGTTGNPKGAL--YSHRSTVLHAYGAALpDAMGLSARDAVLPVVPMFHV--NAWgLPYSA--P 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 248 AVNCYLE------DTNRVREALSEIRPTLMCAVPrfyekiytAVWdkvqkaplfrRMIFnwaiavgqkrfqfisqkkpip 321
Cdd:PRK07008 242 LTGAKLVlpgpdlDGKSLYELIEAERVTFSAGVP--------TVW----------LGLL--------------------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 322 fvlrqQYALADKLVLSKLRQLLGGrirmmpcGGAKLEPNIGLFFHSIGINVKLGYGMTE-----TTATVScWEEGHFEPN 396
Cdd:PRK07008 283 -----NHMREAGLRFSTLRRTVIG-------GSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgTLCKLK-WKHSQLPLD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 397 SI-------GTLMPGAEVKI-GENN-----------EILVRGGMVMRGYYKKpqetADSFTEDGFLKTGDAGEFDPQGNL 457
Cdd:PRK07008 350 EQrkllekqGRVIYGVDMKIvGDDGrelpwdgkafgDLQVRGPWVIDRYFRG----DASPLVDGWFPTGDVATIDADGFM 425
|
410 420
....*....|....*....|....
gi 1178481066 458 YITDRIKELMKtSNGKYIAPQYIE 481
Cdd:PRK07008 426 QITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
21-197 |
1.29e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 64.15 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 21 NETALRYHTPSGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVE 100
Cdd:PRK04319 59 DKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 101 YILNNADVKILfVGDQEEYncTLEIIDACPQIQKIVTMKDNVDLKnhPKACDWQTFLLEGSPlqqtalQARLEQKQLTDL 180
Cdd:PRK04319 139 DRLEDSEAKVL-ITTPALL--ERKPADDLPSLKHVLLVGEDVEEG--PGTLDFNALMEQASD------EFDIEWTDREDG 207
|
170
....*....|....*..
gi 1178481066 181 FTLIYTSGTTGEPKGVM 197
Cdd:PRK04319 208 AILHYTSGSTGKPKGVL 224
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
179-509 |
1.77e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.59 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 179 DLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTTlnvSQYDSSLSFLPLS-HIFERAWVaYVLHRGAvnCYLedtn 257
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYEL---TPDDRVLQFMSFSfDGSHEGLY-HPLINGA--SVV---- 4764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 258 rvrealseIRPTLMCAVPRFYEKIYTAVWDKVQKAPLFRRMIFNWAIAVGQkrfqfisqkkpiPFVLRQQYALADKLVLS 337
Cdd:PRK12316 4765 --------IRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGE------------PPSLRVYCFGGEAVAQA 4824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 338 KLRQLLGGRirmmpcggaklePNIGLFfhsigiNvklGYGMTETTATVSCWEEGHFEPNS-----IGTLMPG-------- 404
Cdd:PRK12316 4825 SYDLAWRAL------------KPVYLF------N---GYGPTETTVTVLLWKARDGDACGaaympIGTPLGNrsgyvldg 4883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 405 --AEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGF-------LKTGDAGEFDPQGNLYITDRIKELMKTsNGKYI 475
Cdd:PRK12316 4884 qlNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRI 4962
|
330 340 350
....*....|....*....|....*....|....*..
gi 1178481066 476 APQYIETKVGKDKFIEQIAVIAD---AKKYVSALIVP 509
Cdd:PRK12316 4963 ELGEIEARLREHPAVREAVVIAQegaVGKQLVGYVVP 4999
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
183-463 |
2.79e-10 |
|
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: 62.95 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQLKAHDEAF---TTLNVSQYdSSLSF-LPLSHIFerawvaYVLHRGAVNCYLEDTNR 258
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEHRALSTSALAHGRALgltSESRVLQF-ASYTFdVSILEIF------TTLAAGGCLCIPSEEDR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 259 vREALSEirptlmcavprfyekiytavwdkvqkapLFRRMIFNWAIAVgqkrfqfisqkkpiPFVLRQqyaLADKLVLSk 338
Cdd:cd05918 184 -LNDLAG----------------------------FINRLRVTWAFLT--------------PSVARL---LDPEDVPS- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 339 LRQL-LGG-----RIRMMPCGGAKLepniglffhsigINvklGYGMTETT-ATVSCWEEGHFEPNSIGTLMPGA------ 405
Cdd:cd05918 217 LRTLvLGGealtqSDVDTWADRVRL------------IN---AYGPAECTiAATVSPVVPSTDPRNIGRPLGATcwvvdp 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 406 -----EVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDG-------------FLKTGDAGEFDPQGNLYITDRI 463
Cdd:cd05918 282 dnhdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegsgrgrrLYRTGDLVRYNPDGSLEYVGRK 357
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
40-481 |
1.06e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 61.10 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 40 QFQQDLDTFSYALLANHIGVQDKIAIFAHNMprwtiadigtmqvRAVVVPIYAT-------------SAAKQVEYILNNA 106
Cdd:PRK07788 79 ELDEQSNALARGLLALGVRAGDGVAVLARNH-------------RGFVLALYAAgkvgariillntgFSGPQLAEVAARE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 107 DVKILFVGDqeEYNCTLEiiDACPQIQKIVTMKDNVDlKNHPKACDWQTF--LLEGS---PLQQTALQARLeqkqltdlf 181
Cdd:PRK07788 146 GVKALVYDD--EFTDLLS--ALPPDLGRLRAWGGNPD-DDEPSGSTDETLddLIAGSstaPLPKPPKPGGI--------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 182 tLIYTSGTTGEPKGVM-------------LDY----ANLAHQLKAhdEAFTTLNVSQYDSSLSFlplshifeRAWVayVL 244
Cdd:PRK07788 212 -VILTSGTTGTPKGAPrpepsplaplaglLSRvpfrAGETTLLPA--PMFHATGWAHLTLAMAL--------GSTV--VL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 245 HRGAvncyleDTNRVREALSEIRPTLMCAVPRFyekiytavwdkvqkaplFRRMIfnwaiAVGQKrfqfisqkkpipfvL 324
Cdd:PRK07788 279 RRRF------DPEATLEDIAKHKATALVVVPVM-----------------LSRIL-----DLGPE--------------V 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 325 RQQYalaDklvLSKLRqllggrirMMPCGGAKLEPNIGLFFHSiginvKLG------YGMTE-TTATVSCWEEGHFEPNS 397
Cdd:PRK07788 317 LAKY---D---TSSLK--------IIFVSGSALSPELATRALE-----AFGpvlynlYGSTEvAFATIATPEDLAEAPGT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 398 IGTLMPGAEVKI----------GENNEILVRGGMVMRGYykkpQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKElM 467
Cdd:PRK07788 378 VGRPPKGVTVKIldengnevprGVVGRIFVGNGFPFEGY----TDGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDD-M 452
|
490
....*....|....
gi 1178481066 468 KTSNGKYIAPQYIE 481
Cdd:PRK07788 453 IVSGGENVFPAEVE 466
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
37-499 |
1.48e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 60.63 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 37 SWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgDQ 116
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV-DQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 117 EEYNCTLEIIDACPQIQK--------IVTMKDNVDLKNHPKA-----CDWQTFLLEGSPlqqtalqaRLEQKQLTDLFTL 183
Cdd:PLN02479 126 EFFTLAEEALKILAEKKKssfkppllIVIGDPTCDPKSLQYAlgkgaIEYEKFLETGDP--------EFAWKPPADEWQS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 184 I---YTSGTTGEPKGVMLdyanlaHQLKAHDEAFTTLNVSQYDSS---LSFLPLSHIfeRAWV---AYVLHRGAVNCYLE 254
Cdd:PLN02479 198 IalgYTSGTTASPKGVVL------HHRGAYLMALSNALIWGMNEGavyLWTLPMFHC--NGWCftwTLAALCGTNICLRQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 255 DTNR-VREALSEIRPTLMCAVPrfyekiytAVWDKVQKAPLFRRMIfnwaiavgqkrfqfisqkkPIPFVlrqqyaladk 333
Cdd:PLN02479 270 VTAKaIYSAIANYGVTHFCAAP--------VVLNTIVNAPKSETIL-------------------PLPRV---------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 334 lvlsklrqllggrIRMMPCGGAKlePNIGLFFHSI-GINVKLGYGMTET--TATVSCW--EEGHFEPNSIGTL------- 401
Cdd:PLN02479 313 -------------VHVMTAGAAP--PPSVLFAMSEkGFRVTHTYGLSETygPSTVCAWkpEWDSLPPEEQARLnarqgvr 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 402 ---MPGAEVKIGENN-----------EILVRGGMVMRGYYKKPQETADSFtEDGFLKTGDAGEFDPQGNLYITDRIKELM 467
Cdd:PLN02479 378 yigLEGLDVVDTKTMkpvpadgktmgEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII 456
|
490 500 510
....*....|....*....|....*....|..
gi 1178481066 468 kTSNGKYIAPQYIETKVGKDKFIEQIAVIADA 499
Cdd:PLN02479 457 -ISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
152-509 |
3.30e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.17 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 152 DWqtflLEGSPlqQTALQARLEQKQLTdlfTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAF---TTLNVSQ-----YD 223
Cdd:PRK12467 1701 DW----LEGYS--DSNPAVNLAPQNLA---YVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYqlsAADVVLQftsfaFD 1771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 224 SSLS--FLPLSHIFERAWVAYVLHRgavncyleDTNRVREALSEIRPTLMCAVPRFYEKIYTAVwDKVQKAPLFRRMIFN 301
Cdd:PRK12467 1772 VSVWelFWPLINGARLVIAPPGAHR--------DPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHPLSLRRVVCG 1842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 302 waiavgqkrfqfisqkkpipfvlrqqyalADKLVLSKLRQLLggrirmmpcggAKLePNIGLFfhsigiNvklGYGMTET 381
Cdd:PRK12467 1843 -----------------------------GEALEVEALRPWL-----------ERL-PDTGLF------N---LYGPTET 1872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 382 TATVSCW-------EEGHFEPnsIGTLMPG----------AEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGF-- 442
Cdd:PRK12467 1873 AVDVTHWtcrrkdlEGRDSVP--IGQPIANlstyildaslNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgt 1950
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 443 -----LKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIA----DAKKYVsALIVP 509
Cdd:PRK12467 1951 vgsrlYRTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLREQGGVREAVVIAqdgaNGKQLV-AYVVP 2024
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
353-496 |
7.16e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 57.75 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 353 GGAKLEPNIGLFFHSIGINVKLGYGMTETTAtvSCWEEGhfEPnsigtlMPGAEVKIgENNEILVRGGMVMRGYYKKPQE 432
Cdd:PRK07824 159 GGGPAPAPVLDAAAAAGINVVRTYGMSETSG--GCVYDG--VP------LDGVRVRV-EDGRIALGGPTLAKGYRNPVDP 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 433 taDSFTEDGFLKTGDAGEFDpQGNLYITDRIKELMKTSnGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:PRK07824 228 --DPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVF 287
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
178-521 |
7.28e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 58.30 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 178 TDLFTLIYTSGTTGEPKGVMLdyanlahqlkahdeafttlnvsqydsslsflPLSHIFerAWVAYV-----LHRGAVNCY 252
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPV-------------------------------PLRALA--AFGAYLrdavdLRPEDSFWN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LEDTNRVREALSEIRPTLMCAVPR-FYEKIYTA--VWDKVQkaplfRRMIFNWAIAVGQKRFqFISQKKPIPfvlrqqya 329
Cdd:cd05973 135 AADPGWAYGLYYAITGPLALGHPTiLLEGGFSVesTWRVIE-----RLGVTNLAGSPTAYRL-LMAAGAEVP-------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 330 ladklvlsklrQLLGGRIRMMPCGGAKLEPNIGLFFHS-IGINVKLGYGMTETTATVS-CWEEGH-FEPNSIGTLMPGAE 406
Cdd:cd05973 201 -----------ARPKGRLRRVSSAGEPLTPEVIRWFDAaLGVPIHDHYGQTELGMVLAnHHALEHpVHAGSAGRAMPGWR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 407 VKIGENNEILVRGG--------------MVMRGYYKKPQETADSftedGFLKTGDAGEFDPQGNLYITDRIKELMkTSNG 472
Cdd:cd05973 270 VAVLDDDGDELGPGepgrlaidiansplMWFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVI-TMSG 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1178481066 473 KYIAPQYIETKVGKDKFIEQIAVIA--DAKK--YVSALIVPC--FNSLEEYAKQL 521
Cdd:cd05973 345 YRIGPFDVESALIEHPAVAEAAVIGvpDPERteVVKAFVVLRggHEGTPALADEL 399
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
369-468 |
8.60e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.82 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 369 GINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVK------IGENNEILVRGGMVMRGYYK--KP---QEtadsf 437
Cdd:PRK06814 932 GIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRlepvpgIDEGGRLFVRGPNVMLGYLRaeNPgvlEP----- 1006
|
90 100 110
....*....|....*....|....*....|.
gi 1178481066 438 TEDGFLKTGDAGEFDPQGNLYITDRIKELMK 468
Cdd:PRK06814 1007 PADGWYDTGDIVTIDEEGFITIKGRAKRFAK 1037
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-509 |
1.04e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 7 HFVN-RIREQAKLLLNETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRA 85
Cdd:PRK12316 2003 PGVHqRIAEQAARAPEAIAVVF----GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 86 VVVPIYATSAAKQVEYILNNADVKILFVgdQEEYNCTLeiidACPQIQKIVTMKDNVDLKNHPkacdwqtfllEGSPLQQ 165
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLT--QRHLLERL----PLPAGVARLPLDRDAEWADYP----------DTAPAVQ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 166 TALQarleqkqltDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLS-HIFERAWVAYVL 244
Cdd:PRK12316 2143 LAGE---------NLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY---ELSPADCELQFMSFSfDGAHEQWFHPLL 2210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 245 HRGAVncyledtnrvrealsEIRPtlmcavprfyekiyTAVWDKVQKAPLFRRMifnwAIAVGQkrfqfisqkkpIPFVL 324
Cdd:PRK12316 2211 NGARV---------------LIRD--------------DELWDPEQLYDEMERH----GVTILD-----------FPPVY 2246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 325 RQQYA--LADKLVLSKLRQL-LGGriRMMPCGGAKLE----PNIGLFfhsigiNvklGYGMTETTATVSCWEEGHFEPNS 397
Cdd:PRK12316 2247 LQQLAehAERDGRPPAVRVYcFGG--EAVPAASLRLAwealRPVYLF------N---GYGPTEAVVTPLLWKCRPQDPCG 2315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 398 -----IGTLMPGAEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGF-------LKTGDAGEFDPQG 455
Cdd:PRK12316 2316 aayvpIGRALGNRRAYIldadlnllapGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADG 2395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1178481066 456 NLYITDRIKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIADAK---KYVSALIVP 509
Cdd:PRK12316 2396 VVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVVAQDGasgKQLVAYVVP 2451
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
183-584 |
2.26e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.48 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFttlNVSQYDSSLSFLPLShiFERA-WVAY-VLHRGA----VNCYLEDT 256
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIAEAY---ELDANDRVLLFMSFS--FDGAqERFLwTLICGGclvvRDNDLWDP 3316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 257 NRVREALSEIRPTLMCAVPRFYEKIytAVWDKVQKAPLFRRMIFNW-AIAVGqkrfqfisqkkpipfvlrqqyalADKLV 335
Cdd:PRK12467 3317 EELWQAIHAHRISIACFPPAYLQQF--AEDAGGADCASLDIYVFGGeAVPPA-----------------------AFEQV 3371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 336 LSKLrqllggrirmmpcggaklePNIGLffhsigINvklGYGMTETTATVSCWE---EGHFEPNS--IGTLMPGAEVKIG 410
Cdd:PRK12467 3372 KRKL-------------------KPRGL------TN---GYGPTEAVVTVTLWKcggDAVCEAPYapIGRPVAGRSIYVL 3423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 411 ENN----------EILVRGGMVMRGYYKKPQETADSFTEDGFL-------KTGDAGEFDPQGNLYITDRIKELMKTsNGK 473
Cdd:PRK12467 3424 DGQlnpvpvgvagELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIEYLGRIDHQVKI-RGF 3502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 474 YIAPQYIETKVGKDKFIEQIAVIAdakkyvsaliVPcfnslEEYAKQLnIKYhdrleLIKHSDILQMFEQRINDLQKELP 553
Cdd:PRK12467 3503 RIELGEIEARLLQHPSVREAVVLA----------RD-----GAGGKQL-VAY-----VVPADPQGDWRETLRDHLAASLP 3561
|
410 420 430
....*....|....*....|....*....|.
gi 1178481066 554 SFEQIKKFTLLPQAfttkmeEITPTLKLRRK 584
Cdd:PRK12467 3562 DYMVPAQLLVLAAM------PLGPNGKVDRK 3586
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
183-457 |
7.29e-08 |
|
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: 54.62 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQlkahdeAFTTLNVSQYDSSLSFL---PLSHIFERAWVAYVLHRGAVNCYLE--DTN 257
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQ------ALVLAVLQAIDEGTVFLnsgPLFHIGTLMFTLATFHAGGTNVFVRrvDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 258 RVREALSEIRPTLMCAVPRFYEKIYTAVWDkvqkaplfrrmifnwaiavgqkrfqfisqkkpipfvlrqqyalaDKLVLS 337
Cdd:cd17636 79 EVLELIEAERCTHAFLLPPTIDQIVELNAD--------------------------------------------GLYDLS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 338 KLRQLLGgrirmMPCGGAKLEPNIGLFFHSIGinvklGYGMTETTA-TVSCWEEGHFEPNSiGTLMPGAEVKI------- 409
Cdd:cd17636 115 SLRSSPA-----APEWNDMATVDTSPWGRKPG-----GYGQTEVMGlATFAALGGGAIGGA-GRPSPLVQVRIldedgre 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1178481066 410 ---GENNEILVRGGMVMRGYYKKPQETADSFTeDGFLKTGDAGEFDPQGNL 457
Cdd:cd17636 184 vpdGEVGEIVARGPTVMAGYWNRPEVNARRTR-GGWHHTNDLGRREPDGSL 233
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-534 |
7.33e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 55.94 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 31 SGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKI 110
Cdd:PRK12467 533 FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 111 LFvgDQEEyncTLEIIDACPQIQKIVTMKDNvdlknhpkacDWqtflLEGSPLQQTALqaRLEQKQLTdlfTLIYTSGTT 190
Cdd:PRK12467 613 LL--TQSH---LLAQLPVPAGLRSLCLDEPA----------DL----LCGYSGHNPEV--ALDPDNLA---YVIYTSGST 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 191 GEPKGVMLDYANLAHQLKAHDEAFTTL---NVSQYdSSLSFlPLSHiferaWVAYV-LHRGAvncyledtnrvrealsei 266
Cdd:PRK12467 669 GQPKGVAISHGALANYVCVIAERLQLAaddSMLMV-STFAF-DLGV-----TELFGaLASGA------------------ 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 267 rpTLMCAVPRfyekiytAVWDKVQKAPLFRRmifnwaiavgqkrfQFISQKKPIPFVLRQqyaladklVLSKLRQLLGGR 346
Cdd:PRK12467 724 --TLHLLPPD-------CARDAEAFAALMAD--------------QGVTVLKIVPSHLQA--------LLQASRVALPRP 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 347 IRMMPCGGAKLEPNIGLFFHSIGINVKL--GYGMTETTATVSCWE----EGHFEPNSIGTLMPGAEVKI----------G 410
Cdd:PRK12467 773 QRALVCGGEALQVDLLARVRALGPGARLinHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANLGLYIldhylnpvpvG 852
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 411 ENNEILVRGGMVMRGYYKKPQETADSFTEDGF-------LKTGDAGEFDPQGNLYITDRIKELMKTsNGKYIAPQYIETK 483
Cdd:PRK12467 853 VVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEAR 931
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1178481066 484 VGKDKFIEQIAVIA---DAKKYVSALIVPCF--NSLEEYAKQLNIKYHDRLELIKH 534
Cdd:PRK12467 932 LLAQPGVREAVVLAqpgDAGLQLVAYLVPAAvaDGAEHQATRDELKAQLRQVLPDY 987
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
327-474 |
9.17e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 54.90 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 327 QYALADKLVLSKLRQLLggrirmmpCGGAKLEPNIGLFFHSI---GINVKLGYGMTET------------TATVSCWEEG 391
Cdd:PRK09274 278 RYGEANGIKLPSLRRVI--------SAGAPVPIAVIERFRAMlppDAEILTPYGATEAlpissiesreilFATRAATDNG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 392 hfEPNSIGTLMPGAEVKI-------------------GENNEILVRGGMVMRGYYKKPQETADSFTEDG----FLKTGDA 448
Cdd:PRK09274 350 --AGICVGRPVDGVEVRIiaisdapipewddalrlatGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDL 427
|
170 180
....*....|....*....|....*.
gi 1178481066 449 GEFDPQGNLYITDRIKELMKTSNGKY 474
Cdd:PRK09274 428 GYLDAQGRLWFCGRKAHRVETAGGTL 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-509 |
1.04e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 12 IREQAKLLLNETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIY 91
Cdd:PRK12316 517 FEEQVERTPEAPALAF----GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 92 ATSAAKQVEYILNNADVKILFVGDQeeyncTLEIIDACPQIQKIvtmkdnvdlknhpkACDWQTFLLEGSPlqQTALQAR 171
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLSQSH-----LGRKLPLAAGVQVL--------------DLDRPAAWLEGYS--EENPGTE 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 172 LEQKQLTdlfTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAF------TTLNVSQYDSSLS----FLPLSHIFERAWVA 241
Cdd:PRK12316 652 LNPENLA---YVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYglgvgdTVLQKTPFSFDVSvwefFWPLMSGARLVVAA 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 242 YVLHRGAVNcYLEDTNRVREALSEIRPTLMCAVPRFyekiytavwDKVQKAPLFRRMIFNwaiavgqkrfqfisqKKPIP 321
Cdd:PRK12316 729 PGDHRDPAK-LVELINREGVDTLHFVPSMLQAFLQD---------EDVASCTSLRRIVCS---------------GEALP 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 322 FVLRQQyaladklVLSKLrqllggrirmmpcggaklePNIGLFFHsiginvklgYGMTETTATVSCW---EEGHFEPnSI 398
Cdd:PRK12316 784 ADAQEQ-------VFAKL-------------------PQAGLYNL---------YGPTEAAIDVTHWtcvEEGGDSV-PI 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 399 GTLMPGAE----------VKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFL------KTGDAGEFDPQGNLYITDR 462
Cdd:PRK12316 828 GRPIANLAcyildanlepVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVagermyRTGDLARYRADGVIEYAGR 907
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1178481066 463 IKELMKTsNGKYIAPQYIETKVGKDKFIEQIAVIADAKKYVSALIVP 509
Cdd:PRK12316 908 IDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVL 953
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
186-481 |
1.38e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 54.23 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 186 TSGTTGEPKGVMLDYANLAHQLKAHDEAfTTLNVsQYDSSLSFLPLSHifERAWVAYV---LHRGAvncyledtnrvrEA 262
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVA-AEFDV-ETDVMVSWLPLFH--DMGMVGFLtvpMYFGA------------EL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 263 LSeIRPTLMCAVPRFYEKIYTAVWDKVQKAPlfrrmifNWAIAVGQKRfqfisqkkpipfvLRQQyALADKLVLSKLRQL 342
Cdd:PRK07768 224 VK-VTPMDFLRDPLLWAELISKYRGTMTAAP-------NFAYALLARR-------------LRRQ-AKPGAFDLSSLRFA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 343 LggrirmmpCGGAKLEPNIGLFFHSIGINVKLG-------YGMTETTATVSCWE-----------------EGHFEPN-- 396
Cdd:PRK07768 282 L--------NGAEPIDPADVEDLLDAGARFGLRpeailpaYGMAEATLAVSFSPcgaglvvdevdadllaaLRRAVPAtk 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 397 -------SIGTLMPGAEVKIGENN----------EILVRGGMVMRGYYkkpqeTADSFT----EDGFLKTGDAGEFDPQG 455
Cdd:PRK07768 354 gntrrlaTLGPPLPGLEVRVVDEDgqvlpprgvgVIELRGESVTPGYL-----TMDGFIpaqdADGWLDTGDLGYLTEEG 428
|
330 340
....*....|....*....|....*.
gi 1178481066 456 NLYITDRIKELMKTSnGKYIAPQYIE 481
Cdd:PRK07768 429 EVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
169-497 |
1.50e-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: 53.94 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 169 QARLEQKQLTDLFTLIYTSGTTGEPKGVMLDY---ANLAHQLKAH-------DEAFTTLNVSQYDSSLSFLPLSHIFERA 238
Cdd:cd17648 85 GARVVITNSTDLAYAIYTSGTTGKPKGVLVEHgsvVNLRTSLSERyfgrdngDEAVLFFSNYVFDFFVEQMTLALLNGQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 239 WVayVLHRGAVNcyleDTNRVREALSEIRPTLMCAVPRFYEKIytavwdKVQKAPLFRRMIfnwaiAVGQkrfQFISQkk 318
Cdd:cd17648 165 LV--VPPDEMRF----DPDRFYAYINREKVTYLSGTPSVLQQY------DLARLPHLKRVD-----AAGE---EFTAP-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 319 pipfvlrqqyaladklVLSKLRQLLGGRIrmmpcggaklepniglffhsigINvklGYGMTET--TATVSCWEEGHFEPN 396
Cdd:cd17648 223 ----------------VFEKLRSRFAGLI----------------------IN---AYGPTETtvTNHKRFFPGDQRFDK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 397 SIGTLMPGAE----------VKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGF--------------LKTGDAGEFD 452
Cdd:cd17648 262 SLGRPVRNTKcyvlndamkrVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWL 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1178481066 453 PQGNLYITDRiKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:cd17648 342 PSGELEYLGR-NDFQVKIRGQRIEPGEVEAALASYPGVRECAVVA 385
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
346-509 |
2.51e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 53.95 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 346 RIRMMPCGGAKLEPNIG-LFFHSIGINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPGAEVK------IGENNEILVR 418
Cdd:PRK08043 480 RLRYVVAGAEKLQESTKqLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEQGGRLQLK 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 419 GGMVMRGYYK--------KPQ-ETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMKtsngkyIAPQYIETKVgkdkf 489
Cdd:PRK08043 560 GPNIMNGYLRvekpgvleVPTaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAK------IAGEMVSLEM----- 628
|
170 180
....*....|....*....|
gi 1178481066 490 IEQIAVIADAKKYVSALIVP 509
Cdd:PRK08043 629 VEQLALGVSPDKQHATAIKS 648
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
404-481 |
4.90e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 52.68 E-value: 4.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 404 GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQYIE 481
Cdd:PRK10946 372 GNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQI-NRGGEKIAAEEIE 448
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
382-509 |
6.11e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.44 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 382 TATVSCweeGHFEPNSIGTLM---PGAEVKIGENNEILVRGGMVMRGYYKKPQETADSF----------------TEDG- 441
Cdd:PRK12476 399 VAHVSC---GQVARSQWAVIVdpdTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgAADDg 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 442 -FLKTGDAGeFDPQGNLYITDRIKELMkTSNGKYIAPQYIETKVgkdkfieqiaviADA-----KKYVSALIVP 509
Cdd:PRK12476 476 tWLRTGDLG-VYLDGELYITGRIADLI-VIDGRNHYPQDIEATV------------AEAspmvrRGYVTAFTVP 535
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
404-481 |
1.70e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 50.67 E-value: 1.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 404 GAEVKIGENNEILVRGGMVMRGYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRiKELMKTSNGKYIAPQYIE 481
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIE 408
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
404-509 |
2.26e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 50.50 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 404 GAEVKIGENNEILVRGGMVMRGYYKKPQETADSF----------------TEDG-FLKTGDAGEFdPQGNLYITDRIKEL 466
Cdd:PRK07769 410 ASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDDAlWVRTGDYGVY-FDGELYITGRVKDL 488
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1178481066 467 MkTSNGKYIAPQYIEtkvgkdkFIEQIAVIADAKKYVSALIVP 509
Cdd:PRK07769 489 V-IIDGRNHYPQDLE-------YTAQEATKALRTGYVAAFSVP 523
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
414-467 |
3.11e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 49.94 E-value: 3.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1178481066 414 EILVRGGMVMRGYYKKPQETADSF----------TEDG-FLKTGDAGeFDPQGNLYITDRIKELM 467
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLG-FISEGELFIVGRIKDLL 462
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
369-496 |
3.27e-06 |
|
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: 49.87 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 369 GINVKLGYGMTETTATVSCWEEGHFEPNSIGTLMPG----------AEVKIGENNEIL--VRGGMVMRGYYKKPQETADS 436
Cdd:cd05974 225 GLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGyrvalldpdgAPATEGEVALDLgdTRPVGLMKGYAGDPDKTAHA 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 437 FtEDGFLKTGDAGEFDPQGNLYITDRIKELMKTSNGKyIAPQYIETKVGKDKFIEQIAVI 496
Cdd:cd05974 305 M-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEAAVV 362
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
404-482 |
3.31e-06 |
|
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: 50.07 E-value: 3.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1178481066 404 GAEVKIGENNEILVRGGMVMRgYYKKPQETADSFTEDGFLKTGDAGEFDPQGNLYITDRiKELMKTSNGKYIAPQYIET 482
Cdd:cd05929 314 GNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIEN 390
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
176-497 |
5.70e-06 |
|
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: 49.17 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 176 QLTDLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDEAFTTL---NVSQYdSSLSFlpLSHIFEraWVAYVLHRGAVncY 252
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGpgsRVLQF-ASPSF--DASVWE--LLMALLAGATL--V 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 253 LEDTNRV------REALSEIRPTLMCAVPrfyekiytAVWDKVQKAPLfrrmifnwaiavgQKRFQFISQKKPIPFVLRQ 326
Cdd:cd17652 164 LAPAEELlpgeplADLLREHRITHVTLPP--------AALAALPPDDL-------------PDLRTLVVAGEACPAELVD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 327 QYAladklvlsklrqllGGRiRMmpcggaklepniglffhsigINvklGYGMTETT--ATVSCWEEGHFEPnSIGTLMPG 404
Cdd:cd17652 223 RWA--------------PGR-RM--------------------IN---AYGPTETTvcATMAGPLPGGGVP-PIGRPVPG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 405 AEVKI----------GENNEILVRGGMVMRGYYKKPQETADSFTEDGF-------LKTGDAGEFDPQGNLYITDRIKELM 467
Cdd:cd17652 264 TRVYVldarlrpvppGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQV 343
|
330 340 350
....*....|....*....|....*....|
gi 1178481066 468 KTsNGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:cd17652 344 KI-RGFRIELGEVEAALTEHPGVAEAVVVV 372
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-474 |
7.54e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 48.61 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQLKAhdeAFTTLNVSQYDSSLSFLPLSHIFERAW-VAYVL----HRGAVNCyleDTN 257
Cdd:cd05910 90 ILFTSGSTGTPKGVVYRHGTFAAQIDA---LRQLYGIRPGEVDLATFPLFALFGPALgLTSVIpdmdPTRPARA---DPQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 258 RVREALSEIRPTLMCAVPrfyekiytAVWDKVQKA--------PLFRRMIFNWA---IAVGQKRFQFISQKKPIPFVlrq 326
Cdd:cd05910 164 KLVGAIRQYGVSIVFGSP--------ALLERVARYcaqhgitlPSLRRVLSAGApvpIALAARLRKMLSDEAEILTP--- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 327 qYALADKLVLSKL--RQLLGGRiRMMPCGGAKLepNIGLFFHsiGINVKLgygMTETTATVSCWEEGHfepnsigtlmpg 404
Cdd:cd05910 233 -YGATEALPVSSIgsRELLATT-TAATSGGAGT--CVGRPIP--GVRVRI---IEIDDEPIAEWDDTL------------ 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1178481066 405 aEVKIGENNEILVRGGMVMRGYYKKPQETADSFTED---GFL-KTGDAGEFDPQGNLYITDRIKELMKTSNGKY 474
Cdd:cd05910 292 -ELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDnseGFWhRMGDLGYLDDEGRLWFCGRKAHRVITTGGTL 364
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
320-496 |
1.99e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 47.30 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 320 IPFVLRQQYALADKLvlsKLRQLLGgRIRMMPCGGAKLEPNIGL-FFHSIGINVKLGYGMTE-------TTATVSCWeeg 391
Cdd:PRK13383 271 VPVVLARILELPPRV---RARNPLP-QLRVVMSSGDRLDPTLGQrFMDTYGDILYNGYGSTEvgigalaTPADLRDA--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 392 hfePNSIGTLMPGAEVKIGENN----------EILVRGGMVMRGYykkpQETADSFTEDGFLKTGDAGEFDPQGNLYITD 461
Cdd:PRK13383 344 ---PETVGKPVAGCPVRILDRNnrpvgprvtgRIFVGGELAGTRY----TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVG 416
|
170 180 190
....*....|....*....|....*....|....*
gi 1178481066 462 RiKELMKTSNGKYIAPQYIETKVGKDKFIEQIAVI 496
Cdd:PRK13383 417 R-EDDMIISGGENVYPRAVENALAAHPAVADNAVI 450
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
34-203 |
2.05e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.58 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 34 ENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFv 113
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLII- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 114 gDQEEYNCTLEIIdacpqiqKIVTMKDnvdlknhpkacdwqtflLEGSPLQQTALQArLEQKQLTDLFTLIYTSGTTGEP 193
Cdd:PRK04813 105 -ATEELPLEILGI-------PVITLDE-----------------LKDIFATGNPYDF-DHAVKGDDNYYIIFTSGTTGKP 158
|
170
....*....|
gi 1178481066 194 KGVMLDYANL 203
Cdd:PRK04813 159 KGVQISHDNL 168
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
36-197 |
3.64e-05 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 46.88 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 36 ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAV---VVPIYATSAA----KQVEyilnnadV 108
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIwssCSPDFGVPGVldrfGQIE-------P 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 109 KILFVGDQEEYNC--------TLEIIDACPQIQKIVTMKDNV-----DLKNHPKACDWQTFLLEGSPLQQTALQARLEQK 175
Cdd:cd05943 172 KVLFAVDAYTYNGkrhdvrekVAELVKGLPSLLAVVVVPYTVaagqpDLSKIAKALTLEDFLATGAAGELEFEPLPFDHP 251
|
170 180
....*....|....*....|..
gi 1178481066 176 qltdLFTLiYTSGTTGEPKGVM 197
Cdd:cd05943 252 ----LYIL-YSSGTTGLPKCIV 268
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
37-481 |
4.07e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 43.19 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 37 SWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAVVVPIYATSAAKQVEYILNNADVKILFVgDQ 116
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF-DP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 117 EEYNCTLEIIDACPQIQKIVTMKDNVDlknhpkacDWQTFLLEGSPLQQTalqarLEQKQLTDLFTLIYTSGTTGEPKGV 196
Cdd:cd05915 105 NLLPLVEAIRGELKTVQHFVVMDEKAP--------EGYLAYEEALGEEAD-----PVRVPERAACGMAYTTGTTGLPKGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 197 MldYANLAHQLKAhdEAFTTLNVSQYDSSLSFL---PLSHIFERAWVAYVLHRGAV-NCYLEDTNR--VREALSEIRPTL 270
Cdd:cd05915 172 V--YSHRALVLHS--LAASLVDGTALSEKDVVLpvvPMFHVNAWCLPYAATLVGAKqVLPGPRLDPasLVELFDGEGVTF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 271 MCAVPRFYEKIYTAVwDKVQKAplfrrmiFNWAIavgqkrfQFISQKKPIPFVLRQQYALADKLVLsklrqLLGGRIRMM 350
Cdd:cd05915 248 TAGVPTVWLALADYL-ESTGHR-------LKTLR-------RLVVGGSAAPRSLIARFERMGVEVR-----QGYGLTETS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 351 PCGGAKL-EPNIGLFFHSIGINVKLGYGMTETTATVSCweeghFEPNSIGTLMPGAEVKIgenneILVRGGMVMRGYYKK 429
Cdd:cd05915 308 PVVVQNFvKSHLESLSEEEKLTLKAKTGLPIPLVRLRV-----ADEEGRPVPKDGKALGE-----VQLKGPWITGGYYGN 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1178481066 430 PQETADSFTEDGFLKTGDAGEFDPQGNLYITDRIKELMkTSNGKYIAPQYIE 481
Cdd:cd05915 378 EEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI-KSGGEWISSVDLE 428
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
20-210 |
9.49e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 42.09 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 20 LN--ETALRYHTPSGW------EN-----ISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIADIGTMQVRAV 86
Cdd:PRK03584 86 LNyaENLLRHRRDDRPaiifrgEDgprreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 87 ---VVPIYATSAA----KQVEyilnnadVKILFVGDQEEYNCTL--------EIIDACPQIQKIV---TMKDNVDLKNHP 148
Cdd:PRK03584 166 wssCSPDFGVQGVldrfGQIE-------PKVLIAVDGYRYGGKAfdrrakvaELRAALPSLEHVVvvpYLGPAAAAAALP 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1178481066 149 KACDWQTFL--LEGSPLQQTALQArleqkqltD--LFTLiYTSGTTGEPK-------GVMLDyanlahQLKAH 210
Cdd:PRK03584 239 GALLWEDFLapAEAAELEFEPVPF--------DhpLWIL-YSSGTTGLPKcivhghgGILLE------HLKEL 296
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
376-502 |
1.13e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 41.69 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 376 YGMTE---TTATVScwEEGHFEPNSIG----------TLMPGAEVKIGENNEILVRGGMVMRGYyKKPQETADSFTEDGF 442
Cdd:PRK07638 286 YGASElsfVTALVD--EESERRPNSVGrpfhnvqvriCNEAGEEVQKGEIGTVYVKSPQFFMGY-IIGGVLARELNADGW 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 443 LKTGDAGEFDPQGNLYITDRIKElMKTSNGKYIAPQYIETKVGKDKFIEQIAVIADAKKY 502
Cdd:PRK07638 363 MTVRDVGYEDEEGFIYIVGREKN-MILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSY 421
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
376-497 |
2.45e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 40.90 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 376 YGMTETTATVSCWEEG---HFEPNS------------IGTLMPGAEVKIG-----------ENNEILVRGGMVMRGYYKk 429
Cdd:PRK05851 310 YGLAESTCAVTVPVPGiglRVDEVTtddgsgarrhavLGNPIPGMEVRISpgdgaagvagrEIGEIEIRGASMMSGYLG- 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1178481066 430 pqetADSFTEDGFLKTGDAGEFdPQGNLYITDRIKELMkTSNGKYIAPQYIETKVGKDKFIEQIAVIA 497
Cdd:PRK05851 389 ----QAPIDPDDWFPTGDLGYL-VDGGLVVCGRAKELI-TVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
176-204 |
3.53e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.43 E-value: 3.53e-03
10 20
....*....|....*....|....*....
gi 1178481066 176 QLTDLFTLIYTSGTTGEPKGVMLDYANLA 204
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCTHRKVA 178
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
183-214 |
4.20e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 4.20e-03
10 20 30
....*....|....*....|....*....|..
gi 1178481066 183 LIYTSGTTGEPKGVMLDYANLAHQLKAHDEAF 214
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF 2369
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
180-206 |
6.91e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 39.35 E-value: 6.91e-03
10 20 30
....*....|....*....|....*....|...
gi 1178481066 180 LFTLiYTSGTTGEPKGVM------LDYANLAHQ 206
Cdd:PRK00174 248 LFIL-YTSGSTGKPKGVLhttggyLVYAAMTMK 279
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
9-197 |
7.69e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 39.09 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 9 VNRIREQAKLLL------------NETALRYhtpsGWENISWHQFQQDLDTFSYALLANHIGVQDKIAIFAHNMPRWTIA 76
Cdd:PRK08279 28 TALITPDSKRSLgdvfeeaaarhpDRPALLF----EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481066 77 DIGTMQVRAVVVPIyATSAAKQV-EYILNNADVKILFVGdqEEYNCTLEIIDACPQIQKIVTMKDNVDLKNHPKACDWQT 155
Cdd:PRK08279 104 WLGLAKLGAVVALL-NTQQRGAVlAHSLNLVDAKHLIVG--EELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1178481066 156 fLLEGSPLQQTALQARLeqkQLTDLFTLIYTSGTTGEPK-GVM 197
Cdd:PRK08279 181 -AAAGAPTTNPASRSGV---TAKDTAFYIYTSGTTGLPKaAVM 219
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
180-207 |
9.46e-03 |
|
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: 38.77 E-value: 9.46e-03
10 20 30
....*....|....*....|....*....|....
gi 1178481066 180 LFTLiYTSGTTGEPKGVM------LDYANLAHQL 207
Cdd:TIGR02188 240 LFIL-YTSGSTGKPKGVLhttggyLLYAAMTMKY 272
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