|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
7-592 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 827.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 7 HFVNRFRLQAKKWLNRTALRFREQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAV 86
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 87 AVPIYATNTAKQVEYIVNDADIKILFVGDQEQLDQVCQIANNCPQLMKIVAMKAnMDLRDLPNACYWEDFLDV---VPNE 163
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDP-RGLRDDPRLLSLDELLALgreVADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 164 AEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAYVFHRGA 243
Cdd:COG1022 171 AELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 244 TNCYLEDTNHVRDALTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICVGEQHYQAEQ----PSQWLRLQY 319
Cdd:COG1022 251 TVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLagksPSLLLRLKH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 320 ALADKLVLTKLRALLGGRIKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVK 399
Cdd:COG1022 331 ALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 400 IGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDK 479
Cdd:COG1022 411 IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASP 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 480 FIEQIAVIADAKKYVSALIVPCFDSLEEYAKQLNIKYQDRIELIKHSDIIQMFERRIHELQKELPSFEQVKKFTLLPQAF 559
Cdd:COG1022 491 LIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYTSYAELAQDPEVRALIQEEVDRANAGLSRAEQIKRFRLLPKEF 570
|
570 580 590
....*....|....*....|....*....|...
gi 2490830388 560 STTMEEITPTLKLRRKVIMQRYREQIEEMYNER 592
Cdd:COG1022 571 TIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
32-577 |
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: 579.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 32 QWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKIL 111
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 112 FVGDqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqLSDLFTLIYTSGTTGEP 191
Cdd:cd05907 82 FVED-----------------------------------------------------------PDDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 192 KGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFE-RAWVAYVFHRGATNCYLEDTNHVRDALTTLKPTVMCAVP 270
Cdd:cd05907 103 KGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVFLAVP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 271 RFYEKIYTAVwdKVEKALAHRRALFNWAIcvgeqhyqaeqpsqwlrlqyaladklvltklrallGGRIKMMPCGGAKLEA 350
Cdd:cd05907 183 RVWEKVYAAI--KVKAVPGLKRKLFDLAV-----------------------------------GGRLRFAASGGAPLPA 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 351 SIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTE 430
Cdd:cd05907 226 ELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDGEILVRGPNVMLGYYKNPEATAEALDA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 431 DGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIADAKKYVSALIVPCFDSLEEYAK 510
Cdd:cd05907 306 DGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEALEAWAE 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490830388 511 QLNIKYQDRIELIKHSDIIQMFERRIHELQKELPSFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVI 577
Cdd:cd05907 386 EHGIAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
34-589 |
2.35e-132 |
|
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: 397.74 E-value: 2.35e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQ---EIDRFSYALIAQHIDI--QDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADI 108
Cdd:cd05927 1 GPYEWISYKEvaeRADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 109 KILFVGDQeqldqvcqianncpqlMKIVAMKANMDLrdlpnacYWEDFLDVVPNEAEfekrlnskqlsDLFTLIYTSGTT 188
Cdd:cd05927 81 SIVFCDAG----------------VKVYSLEEFEKL-------GKKNKVPPPPPKPE-----------DLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 189 GEPKGVMLDYANLAHQLNAHDLALNV----NEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLE-DTNHVRDALTTLKP 263
Cdd:cd05927 127 GNPKGVMLTHGNIVSNVAGVFKILEIlnkiNPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgDIRLLLDDIKALKP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 264 TVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICVGEQHYQA--EQPSQWLrlqyalaDKLVLTKLRALLGGRIKMM 341
Cdd:cd05927 207 TVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSgvVRASPFW-------DKLVFNKIKQALGGNVRLM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 342 PCGGAKLEASIGSFFHSI-GINIKLGYGMTETTA--TVSCWQDKgfNPNSIGTLMPNAEVKIGE-------------ENE 405
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVAlGCPVLEGYGQTECTAgaTLTLPGDT--SVGHVGGPLPCAEVKLVDvpemnydakdpnpRGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 406 ILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIA 485
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 486 VIADAKK-YVSALIVPCFDSLEEYAKQLNIKYQDRIELIKHSDIIQMFERRIHELQKE--LPSFEQVKKFTLLPQAFSTT 562
Cdd:cd05927 438 VYGDSLKsFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLVRLGKEngLKGFEQVKAIHLEPEPFSVE 517
|
570 580
....*....|....*....|....*..
gi 2490830388 563 MEEITPTLKLRRKVIMQRYREQIEEMY 589
Cdd:cd05927 518 NGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
25-581 |
4.80e-115 |
|
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: 354.04 E-value: 4.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 25 LRFREQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVN 104
Cdd:cd17641 1 LREKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 105 DADIKILFVGDQEQLDQVCQIANNCPQLMKIVAM-KANMDLRDLPNACYWEDFLDVVPNEA-----EFEKRLNSKQLSDL 178
Cdd:cd17641 81 YTGARVVIAEDEEQVDKLLEIADRIPSVRYVIYCdPRGMRKYDDPRLISFEDVVALGRALDrrdpgLYEREVAAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 179 FTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWV--AYVFHRGATNCYLEDTNHVRD 256
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSvgQALVCGFIVNFPEEPETMMED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 257 aLTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICVG----EQHYQAEQPSQWLRLQYALADKLVLTKLRA 332
Cdd:cd17641 241 -LREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGlralDRGKRGRPVSLWLRLASWLADALLFRPLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 333 LLG-GRIKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKIGEENEILVRGG 411
Cdd:cd17641 320 RLGfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILVRSP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 412 MVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIADAK 491
Cdd:cd17641 400 GVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 492 KYVSALIVPCFDSLEEYAKQLNIKYQDRIELIKHSDIIQMFERRIHELQKELPSFEQVKKFTLLPQAFSTTMEEITPTLK 571
Cdd:cd17641 480 PYLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELTRTRK 559
|
570
....*....|
gi 2490830388 572 LRRKVIMQRY 581
Cdd:cd17641 560 VRRGVIAEKY 569
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
37-577 |
1.10e-107 |
|
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: 331.63 E-value: 1.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 37 SWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVGDQ 116
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEND 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 117 EqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlSDLFTLIYTSGTTGEPKGVML 196
Cdd:cd17640 87 S----------------------------------------------------------DDLATIIYTSGTTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 197 DYANLAHQLnaHDLALNVNED--DVSLSFLPLSHIFERAWVAYVFHRGATNCYledTN--HVRDALTTLKPTVMCAVPRF 272
Cdd:cd17640 109 THANLLHQI--RSLSDIVPPQpgDRFLSILPIWHSYERSAEYFIFACGCSQAY---TSirTLKDDLKRVKPHYIVSVPRL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 273 YEKIYTAVWDKVEKALAHRRALFnwaicvgeqhyqaeqpsqwlrlqyaladklvltkLRALLGGRIKMMPCGGAKLEASI 352
Cdd:cd17640 184 WESLYSGIQKQVSKSSPIKQFLF----------------------------------LFFLSGGIFKFGISGGGALPPHV 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 353 GSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKP 421
Cdd:cd17640 230 DTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIvdpegnvvlppGEKGIVWVRGPQVMKGYYKNP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 422 EETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIADAKKYVSALIVPC 501
Cdd:cd17640 310 EATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPN 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 502 FDSLEEYAKQLNIKY-QDRIELIKHSDIIQMFERRIHELQKELP---SFEQVKKFTLLPQAFsTTMEEITPTLKLRRKVI 577
Cdd:cd17640 390 FEELEKWAKESGVKLaNDRSQLLASKKVLKLYKNEIKDEISNRPgfkSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
28-589 |
3.96e-103 |
|
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: 323.93 E-value: 3.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 28 REQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDAD 107
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 108 IKILFVGDQEQLDQVCQIANNCPQLMKIVAMKANMDLRdLPNACYWEDFLDV---VPNEaEFEKRLNSKQLSDLFTLIYT 184
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEK-EPNLYSWDEFMELgrsIPDE-QLDAIISSQKPNQCCTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 185 SGTTGEPKGVMLDYANL---AHQLNAH-DLALNVNEDDVSLSFLPLSHIFER---AWVAyVFHRGATncYLEDtnhvRDA 257
Cdd:cd05933 159 SGTTGMPKGVMLSHDNItwtAKAASQHmDLRPATVGQESVVSYLPLSHIAAQildIWLP-IKVGGQV--YFAQ----PDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 258 L-----TTLK---PTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICVGEQHYQAEQPSQW-LRLQYALADKLVLT 328
Cdd:cd05933 232 LkgtlvKTLRevrPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESpSPLFYRLAKKLVFK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 KLRALLG-GRIKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTA--TVScwQDKGFNPNSIGTLMPNAEVKIGEEN- 404
Cdd:cd05933 312 KVRKALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGphTIS--NPQAYRLLSCGKALPGCKTKIHNPDa 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 ----EILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKD-K 479
Cdd:cd05933 390 dgigEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 480 FIEQIAVIADAKKYVSALI-VPC---------FDSLE----EYAKQLNIKYQDRIELIKHSD--IIQMFERRIHELQKEL 543
Cdd:cd05933 470 IISNAMLIGDKRKFLSMLLtLKCevnpetgepLDELTeeaiEFCRKLGSQATRVSEIAGGKDpkVYEAIEEGIKRVNKKA 549
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2490830388 544 PSFEQ-VKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMY 589
Cdd:cd05933 550 ISNAQkIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
12-461 |
7.21e-99 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 307.32 E-value: 7.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREqaqWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:pfam00501 1 LERQAARTPDKTALEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILFVGDQEQLDQVCQIANNCPQLMKIVAMKANMDLRDlpnacywEDFLDVVPNEAEFEKRLN 171
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKE-------EPLPEEAKPADVPPPPPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 172 SKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAH----DLALNVNEDDVSLSFLPLSHIFERAWVAY-VFHRGATNC 246
Cdd:pfam00501 151 PPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGATVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 247 YLE-----DTNHVRDALTTLKPTVMCAVPRFYEKIytavwdkvekaLAHRRalfnwaicvgeqhyqaeqpsqwlrlqyal 321
Cdd:pfam00501 231 LPPgfpalDPAALLELIERYKVTVLYGVPTLLNML-----------LEAGA----------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 322 adklvltkLRALLGGRIKMMPCGGAKLEASIGSFFHSIGIN-IKLGYGMTETTATVSC---WQDKGFNPNSIGTLMPNAE 397
Cdd:pfam00501 271 --------PKRALLSSLRLVLSGGAPLPPELARRFRELFGGaLVNGYGLTETTGVVTTplpLDEDLRSLGSVGRPLPGTE 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 398 VKI-----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTS 461
Cdd:pfam00501 343 VKIvddetgepvppGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
32-581 |
7.38e-95 |
|
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: 299.77 E-value: 7.38e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 32 QWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKIL 111
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 112 FVGdqeQLDQVCQIANNCPQLMKIVAMKanmdLRDLPNACY-WEDFLDVVPNEAEFEKRLNSKqlsdLFTLIYTSGTTGE 190
Cdd:cd05932 83 FVG---KLDDWKAMAPGVPEGLISISLP----PPSAANCQYqWDDLIAQHPPLEERPTRFPEQ----LATLIYTSGTTGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 191 PKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLEDT--NHVRDaLTTLKPTVMCA 268
Cdd:cd05932 152 PKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESldTFVED-VQRARPTLFFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 269 VPRFYEKIYTAVWDKVekalahrralfnwaicvgeqhyqaeqPSQWLR--LQYALADKLVLTKLRALLG-GRIKMMPCGG 345
Cdd:cd05932 231 VPRLWTKFQQGVQDKI--------------------------PQQKLNllLKIPVVNSLVKRKVLKGLGlDQCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 346 AKLEASIGSFFHSIGINIKLGYGMTETTAtVSCWQDKGFNP-NSIGTLMPNAEVKIGEENEILVRGGMVMRGYYKKPEET 424
Cdd:cd05932 285 APVPPALLEWYRSLGLNILEAYGMTENFA-YSHLNYPGRDKiGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 425 AKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIADAKKYVSALIVPcfdS 504
Cdd:cd05932 364 AEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVL---S 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490830388 505 LEEYAKQLNikyQDRIELIKHsdiiqmFERRIHELQKELPSFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRY 581
Cdd:cd05932 441 EEARLRADA---FARAELEAS------LRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
26-591 |
8.73e-93 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 298.55 E-value: 8.73e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 26 RFREQAQWQEMSWQTFQQEIDR---FSYALIAQHIDIQDKIGIFANNMPRWTIADFgAMQARA-VAVPIYATNTAKQVEY 101
Cdd:PLN02736 66 RIRVDGTVGEYKWMTYGEAGTArtaIGSGLVQHGIPKGACVGLYFINRPEWLIVDH-ACSAYSyVSVPLYDTLGPDAVKF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 102 IVNDADIKILFVGDQeQLDQVCQIANNCPQLMKIVAMK-ANMDLRDLPNACYWEdfldVVP-NEAEFEKRLNSKQL---- 175
Cdd:PLN02736 145 IVNHAEVAAIFCVPQ-TLNTLLSCLSEIPSVRLIVVVGgADEPLPSLPSGTGVE----IVTySKLLAQGRSSPQPFrppk 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 -SDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERA-WVAYVFHRGATNCYLEDTNH 253
Cdd:PLN02736 220 pEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVnQIVMLHYGVAVGFYQGDNLK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 254 VRDALTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICVGEQHY-QAEQPSqwlrlqyALADKLVLTKLRA 332
Cdd:PLN02736 300 LMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALeNGKNPS-------PMWDRLVFNKIKA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 333 LLGGRIKMMPCGGAKLEASIGSFFH-SIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVK---IGEEN---- 404
Cdd:PLN02736 373 KLGGRVRFMSSGASPLSPDVMEFLRiCFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKlvdVPEMNytse 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 -------EILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGK 477
Cdd:PLN02736 453 dqpyprgEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAK 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 478 DKFIEQIAVIADA-KKYVSALIVPCFDSLEEYAKQLNIKYQDRIELIKHSDIIQMFERRIHELQKE--LPSFEQVKKFTL 554
Cdd:PLN02736 533 CKFVAQCFVYGDSlNSSLVAVVVVDPEVLKAWAASEGIKYEDLKQLCNDPRVRAAVLADMDAVGREaqLRGFEFAKAVTL 612
|
570 580 590
....*....|....*....|....*....|....*..
gi 2490830388 555 LPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMYNE 591
Cdd:PLN02736 613 VPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
162-577 |
2.53e-89 |
|
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: 285.26 E-value: 2.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 162 NEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNA--HDLALNVNEDDVSLSFLPLSHIFERAWVAYVF 239
Cdd:cd17639 74 NETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGlgDRVPELLGPDDRYLAYLPLAHIFELAAENVCL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 240 HRGATNCY-----LEDTNHVR---DaLTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAicvgeqhYQAEqp 311
Cdd:cd17639 154 YRGGTIGYgsprtLTDKSKRGckgD-LTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTA-------YQSK-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 312 SQWLRLQY--ALADKLVLTKLRALLGGRIKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTA--TVSCWQDkgFNPN 387
Cdd:cd17639 224 LKALKEGPgtPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAggTVQDPGD--LETG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 388 SIGTLMPNAEVKIGE-------------ENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRL 454
Cdd:cd17639 302 RVGPPLPCCEIKLVDweeggystdkpppRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 455 KELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIAD-AKKYVSALIVPCFDSLEEYAKQLNIKYQDRIELIKHSDIIQMFE 533
Cdd:cd17639 382 KDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADpDKSYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVL 461
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2490830388 534 RRIHELQKE--LPSFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVI 577
Cdd:cd17639 462 KSLAETARAagLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
35-574 |
4.38e-87 |
|
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: 278.17 E-value: 4.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 35 EMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVG 114
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 115 DQEqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlsDLFTLIYTSGTTGEPKGV 194
Cdd:cd05914 87 DED-----------------------------------------------------------DVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 195 MLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAW-VAYVFHRGATNCYLEDTNHVR-DALTTLKPTVMCAVPRF 272
Cdd:cd05914 108 MLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFtLLLPLLNGAHVVFLDKIPSAKiIALAFAQVTPTLGVPVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 273 YEKIYTAVWDKVEKaLAHRRALFNWAICVGEQHYQaeqpsqwlrlqyaladKLVLTKLRALLGGRIKMMPCGGAKLEASI 352
Cdd:cd05914 188 LVIEKIFKMDIIPK-LTLKKFKFKLAKKINNRKIR----------------KLAFKKVHEAFGGNIKEFVIGGAKINPDV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 353 GSFFHSIGINIKLGYGMTETTATVScwqdkgFNP------NSIGTLMPNAEVKI------GEENEILVRGGMVMRGYYKK 420
Cdd:cd05914 251 EEFLRTIGFPYTIGYGMTETAPIIS------YSPpnrirlGSAGKVIDGVEVRIdspdpaTGEGEIIVRGPNVMKGYYKN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 421 PEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIADAKKYVsALIVP 500
Cdd:cd05914 325 PEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLV-ALAYI 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 501 CFDSLEEYAKQLnikyQDRIELIKhsdiiqmfERRIHELQKELPSFEQVKKFTLLPQAFsttmeEITPTLKLRR 574
Cdd:cd05914 404 DPDFLDVKALKQ----RNIIDAIK--------WEVRDKVNQKVPNYKKISKVKIVKEEF-----EKTPKGKIKR 460
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
12-589 |
7.58e-85 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 277.85 E-value: 7.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFRE--QAQWQEMSWQTFQQ---EIDRFSYALIAQHIDIQDKIGIFANNMPRWTIAdfgaMQARA- 85
Cdd:PLN02430 48 FSKSVEKYPDNKMLGWRRivDGKVGPYMWKTYKEvyeEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA----MEACAa 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 86 ---VAVPIYATNTAKQVEYIVNDADIKILFVGD---QEQLDQVCQIANncpQLMKIVAMKANMD-----LRDLPNACY-W 153
Cdd:PLN02430 124 hslICVPLYDTLGPGAVDYIVDHAEIDFVFVQDkkiKELLEPDCKSAK---RLKAIVSFTSVTEeesdkASQIGVKTYsW 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 154 EDFLDVvpnEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNED-----DVSLSFLPLSH 228
Cdd:PLN02430 201 IDFLHM---GKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDkmthdDVYLSFLPLAH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 229 IFERAWVAYVFHRGATNCYLE-DTNHVRDALTTLKPTVMCAVPRFYEKIYtavwDKVEKALAH----RRALFNwaicVGE 303
Cdd:PLN02430 278 ILDRMIEEYFFRKGASVGYYHgDLNALRDDLMELKPTLLAGVPRVFERIH----EGIQKALQElnprRRLIFN----ALY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 304 QHYQAeqpsqWLRLQYA------LADKLVLTKLRALLGGRIKMMPCGGAKLEASIGSFFH--SIGINIKlGYGMTETTAT 375
Cdd:PLN02430 350 KYKLA-----WMNRGYShkkaspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRvtSCAFVVQ-GYGLTETLGP 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 376 VS-CWQDKGFNPNSIGTLMPNAEVKIGE-------------ENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGE 441
Cdd:PLN02430 424 TTlGFPDEMCMLGTVGAPAVYNELRLEEvpemgydplgeppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGE 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 442 MDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIADA-KKYVSALIVPCFDSLEEYAKQLNIKyqDRI 520
Cdd:PLN02430 503 ILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSfKSMLVAVVVPNEENTNKWAKDNGFT--GSF 580
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 521 ELIKHSDiiQMFERRIHELQ-----KELPSFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMY 589
Cdd:PLN02430 581 EELCSLP--ELKEHILSELKstaekNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
12-587 |
3.73e-77 |
|
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: 251.65 E-value: 3.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFreqaQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:COG0318 5 LRRAAARHPDRPALVF----GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILFVgdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrln 171
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 172 skqlsdlFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFerAWVAYVF---HRGATNCYL 248
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVF--GLTVGLLaplLAGATLVLL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 249 E--DTNHVRDALTTLKPTVMCAVPRFYEKIytavwdkvekalahrralfnwaicvgeqhyqaeqpsqwlrLQYALADKLV 326
Cdd:COG0318 174 PrfDPERVLELIERERVTVLFGVPTMLARL----------------------------------------LRHPEFARYD 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 327 LTKLRALLggrikmmpCGGAKL-EASIGSFFHSIGINIKLGYGMTETTATVSC-WQDKGFN-PNSIGTLMPNAEVKI--- 400
Cdd:COG0318 214 LSSLRLVV--------SGGAPLpPELLERFEERFGVRIVEGYGLTETSPVVTVnPEDPGERrPGSVGRPLPGVEVRIvde 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNGKYIAPQYIEG 473
Cdd:COG0318 286 dgrelppGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMII-SGGENVYPAEVEE 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 474 KIGKDKFIEQIAVIA--DAKKY--VSALIVPCFDSLEeyakqlnikyqDRIELIKHsdiiqmferriheLQKELPSFEQV 549
Cdd:COG0318 364 VLAAHPGVAEAAVVGvpDEKWGerVVAFVVLRPGAEL-----------DAEELRAF-------------LRERLARYKVP 419
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2490830388 550 KKFTLLpqafsttmEEI--TPTLKLRRKVIMQRYREQIEE 587
Cdd:COG0318 420 RRVEFV--------DELprTASGKIDRRALRERYAAGALE 451
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
38-591 |
2.93e-76 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 255.15 E-value: 2.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 38 WQTFQQEID---RFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVg 114
Cdd:PLN02861 77 WLTYKEVYDaaiRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFV- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 115 DQEQLDQVCQIANNCPQLMKI------VAMKANMDLRDLPNACY-WEDFldvvPNEAEFEKRLNSKQLSDLFTLIYTSGT 187
Cdd:PLN02861 156 QESKISSILSCLPKCSSNLKTivsfgdVSSEQKEEAEELGVSCFsWEEF----SLMGSLDCELPPKQKTDICTIMYTSGT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 188 TGEPKGVMLDYANLAHQLNAHDLALNVN-----EDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLE-DTNHVRDALTTL 261
Cdd:PLN02861 232 TGEPKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQgDIRYLMEDVQAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 262 KPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAIcvgeqHYQAEQPSQWLRLQYA--LADKLVLTKLRALLGGRIK 339
Cdd:PLN02861 312 KPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAY-----NYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 340 MMPCGGAKLEASIGSFFHSIGI-NIKLGYGMTETTAtvSCWQDKGFNPNSIGTL---MPNAEVKIGE------------- 402
Cdd:PLN02861 387 LLLSGAAPLPRHVEEFLRVTSCsVLSQGYGLTESCG--GCFTSIANVFSMVGTVgvpMTTIEARLESvpemgydalsdvp 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 403 ENEILVRGGMVMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIE 482
Cdd:PLN02861 465 RGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIA 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 483 QIAVIADA-KKYVSALIVPCFDSLEEYAKQLNiKYQDRIELIKHSDIIQMFERRIHELQKE--LPSFEQVKKFTLLPQAF 559
Cdd:PLN02861 544 SIWVYGNSfESFLVAVVVPDRQALEDWAANNN-KTGDFKSLCKNLKARKYILDELNSTGKKlqLRGFEMLKAIHLEPNPF 622
|
570 580 590
....*....|....*....|....*....|..
gi 2490830388 560 STTMEEITPTLKLRRKVIMQRYREQIEEMYNE 591
Cdd:PLN02861 623 DIERDLITPTFKLKRPQLLKYYKDCIDQLYSE 654
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
12-589 |
1.83e-71 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 242.62 E-value: 1.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFRE--QAQWQEMSWQTFQQEID---RFSYALIAQHIDIQDKIGIFANNMPRWTIAdFGAMQARAV 86
Cdd:PLN02614 51 FRMSVEKYPNNPMLGRREivDGKPGKYVWQTYQEVYDiviKLGNSLRSVGVKDEAKCGIYGANSPEWIIS-MEACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 87 -AVPIYATNTAKQVEYIVNDADIKILFVgDQEQLDQVCQIANNCPQLMKIVAMKANMDLRDLPNA-------CYWEDFLD 158
Cdd:PLN02614 130 yCVPLYDTLGAGAVEFIISHSEVSIVFV-EEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAetfglviYAWDEFLK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 159 VVPNEaefEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLD-------YANLAHQLNAHDLALNvnEDDVSLSFLPLSHIFE 231
Cdd:PLN02614 209 LGEGK---QYDLPIKKKSDICTIMYTSGTTGDPKGVMISnesivtlIAGVIRLLKSANAALT--VKDVYLSYLPLAHIFD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 232 RAWV-AYVFHRGATNCYLEDTNHVRDALTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICV-------GE 303
Cdd:PLN02614 284 RVIEeCFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYkfgnmkkGQ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 304 QHYQAEqpsqwlrlqyALADKLVLTKLRALLGGRIKMMPCGGAKLEASIGSFFHSIGI-NIKLGYGMTETTA-TVSCWQD 381
Cdd:PLN02614 364 SHVEAS----------PLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACcHVLQGYGLTESCAgTFVSLPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 382 KGFNPNSIGTLMPNAEVKIGE-------------ENEILVRGGMVMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNL 448
Cdd:PLN02614 434 ELDMLGTVGPPVPNVDIRLESvpemeydalastpRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSM 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 449 FITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIADA-KKYVSALIVPCFDSLEEYAKQ--LNIKYQDRIELIKH 525
Cdd:PLN02614 513 KIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSfESFLVAIANPNQQILERWAAEngVSGDYNALCQNEKA 592
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 526 SDIIqMFERRIHELQKELPSFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMY 589
Cdd:PLN02614 593 KEFI-LGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
12-511 |
5.69e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 232.00 E-value: 5.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIy 91
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGR----RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 atNT---AKQVEYIVNDADIKILFVgDQEQLDQVCQIANNCPQLMKIVAMKANMDLRDLPNACYWEDFLDVVPNEAEF-E 167
Cdd:PRK06187 87 --NIrlkPEEIAYILNDAEDRVVLV-DSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEELLAAASDTFDFpD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 168 KRLNskqlsDLFTLIYTSGTTGEPKGVMLDYANL-AHQLNAHDlALNVNEDDVSLSFLPLSHIFerAW-VAYV-FHRGAT 244
Cdd:PRK06187 164 IDEN-----DAAAMLYTSGTTGHPKGVVLSHRNLfLHSLAVCA-WLKLSRDDVYLVIVPMFHVH--AWgLPYLaLMAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 245 NCYLE--DTNHVRDALTTLKPTVMCAVPrfyeKIYTAVwdkvekaLAHRRAlfnwaicvgeqhyqaeqPSQWLRlqyala 322
Cdd:PRK06187 236 QVIPRrfDPENLLDLIETERVTFFFAVP----TIWQML-------LKAPRA-----------------YFVDFS------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 323 dklvltklrallggRIKMMPCGGAKL-EASIGSFFHSIGINIKLGYGMTETTATVSC----WQDKGFNP--NSIGTLMPN 395
Cdd:PRK06187 282 --------------SLRLVIYGGAALpPALLREFKEKFGIDLVQGYGMTETSPVVSVlppeDQLPGQWTkrRSAGRPLPG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 396 AEVKI------------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNG 463
Cdd:PRK06187 348 VEARIvdddgdelppdgGEVGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYITDRIKDVII-SGG 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2490830388 464 KYIAPQYIEGKIGKDKFIEQIAVIA--DAK--KYVSALIVPC------FDSLEEYAKQ 511
Cdd:PRK06187 426 ENIYPRELEDALYGHPAVAEVAVIGvpDEKwgERPVAVVVLKpgatldAKELRAFLRG 483
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
35-589 |
1.22e-66 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 230.00 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 35 EMSWQTFQQEIDR---FSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKIL 111
Cdd:PLN02387 103 EYEWITYGQVFERvcnFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 112 fVGDQEQLDQVCQIANNCPQLMKIVAMKANMDLRD--LPNACYW--EDFLDV--VPNEAEFEKRLNSKqlSDLFTLIYTS 185
Cdd:PLN02387 183 -ICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDssLSGSSNWtvSSFSEVekLGKENPVDPDLPSP--NDIAVIMYTS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 186 GTTGEPKGVMLDYANLAHQLNAHDLAL-NVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCY-----LEDT-NHVR--- 255
Cdd:PLN02387 260 GSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYgspltLTDTsNKIKkgt 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 256 --DAlTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNwaicVGEQHYQAEQPSQWL---RLQYALADKLVLTKL 330
Cdd:PLN02387 340 kgDA-SALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFD----IAYKRRLAAIEGSWFgawGLEKLLWDALVFKKI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 331 RALLGGRIKMMPCGGAKLEASIGSFFH-SIGINIKLGYGMTETTA--TVSCWQDKgfNPNSIGTLMPNAEVKI--GEE-- 403
Cdd:PLN02387 415 RAVLGGRIRFMLSGGAPLSGDTQRFINiCLGAPIGQGYGLTETCAgaTFSEWDDT--SVGRVGPPLPCCYVKLvsWEEgg 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 404 ----------NEILVRGGMVMRGYYKKPEETAKAFTEDG----FLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQ 469
Cdd:PLN02387 493 ylisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLG 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 470 YIEGKIGKDKFIEQIAVIADA-KKYVSALIVPCFDSLEEYAKQLNIKYQDRIELIKHSDIIQMFERRIHELQKE--LPSF 546
Cdd:PLN02387 573 KVEAALSVSPYVDNIMVHADPfHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCEKEEAVKEVQQSLSKAAKAarLEKF 652
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2490830388 547 EQVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMY 589
Cdd:PLN02387 653 EIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
34-487 |
5.28e-61 |
|
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: 210.15 E-value: 5.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFV 113
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 114 gDQEQLDQVCQIANNCPQLMKIVAMkanmdlRDLPNACYWEDFLDVVPNEAEFEKRLNSKQLS--DLFTLIYTSGTTGEP 191
Cdd:cd05911 89 -DPDGLEKVKEAAKELGPKDKIIVL------DDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGkdDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 192 KGVMLDYANL---AHQLNAHdLALNVNEDDVSLSFLPLSHIFerawvayvfhrGATNCYLedtnhvrdALTTLKPTVMCa 268
Cdd:cd05911 162 KGVCLSHRNLianLSQVQTF-LYGNDGSNDVILGFLPLYHIY-----------GLFTTLA--------SLLNGATVIIM- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 269 vPRFYekiyTAVW-DKVEKalaHRralFNWAICVgeqhyqaeqPSQWLRL-QYALADKLVLTKLRALLggrikmmpCGGA 346
Cdd:cd05911 221 -PKFD----SELFlDLIEK---YK---ITFLYLV---------PPIAAALaKSPLLDKYDLSSLRVIL--------SGGA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 347 KLEASIGSFFHSIGIN--IKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI-----------GEENEILVRGGMV 413
Cdd:cd05911 273 PLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIvdddgkdslgpNEPGEICVRGPQV 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 414 MRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:cd05911 353 MKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVI 425
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
20-487 |
1.91e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 208.99 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 20 LNRTALRFREQAQWQEM----SWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNT 95
Cdd:PRK07656 11 LARAARRFGDKEAYVFGdqrlTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 96 AKQVEYIVNDADIKILFVGDQeQLDQVCQIANNCPQLMKIVAMKANMDLRDLPNACYWEDFLDvVPNEAEFEKRLNSKQL 175
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGL-FLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLA-AGDPAERAPEVDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDlftLIYTSGTTGEPKGVMLDYANLAhqLNAHDLA--LNVNEDDVSLSFLPLSHIF--ERAWVAyVFHRGATnCYLEDT 251
Cdd:PRK07656 169 AD---ILFTSGTTGRPKGAMLTHRQLL--SNAADWAeyLGLTEGDRYLAANPFFHVFgyKAGVNA-PLMRGAT-ILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 NHVRDALTTL---KPTVMCAVPRFYEKIYTAVwDKVEKALAHRRalfnwaICV-GeqhyQAEQPSQWL-RLQYALADKLV 326
Cdd:PRK07656 242 FDPDEVFRLIeteRITVLPGPPTMYNSLLQHP-DRSAEDLSSLR------LAVtG----AASMPVALLeRFESELGVDIV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 327 LTklrallggrikmmpcggakleasigsffhsiginiklGYGMTETTATVS-CWQDKGFN--PNSIGTLMPNAEVKI--- 400
Cdd:PRK07656 311 LT-------------------------------------GYGLSEASGVTTfNRLDDDRKtvAGTIGTAIAGVENKIvne 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEG 473
Cdd:PRK07656 354 lgeevpvGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKD-MFIVGGFNVYPAEVEE 432
|
490
....*....|....
gi 2490830388 474 KIGKDKFIEQIAVI 487
Cdd:PRK07656 433 VLYEHPAVAEAAVI 446
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
27-591 |
6.47e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 209.06 E-value: 6.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 27 FREQaqwQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDA 106
Cdd:PTZ00216 116 FNET---RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRET 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 107 DIKILfvgdqeqldqVCQIAN--NCPQLMKIVAMKANM--DLRDLPNAC--------YWEDFLDVVPNEAEFEKrLNSKQ 174
Cdd:PTZ00216 193 ECKAI----------VCNGKNvpNLLRLMKSGGMPNTTiiYLDSLPASVdtegcrlvAWTDVVAKGHSAGSHHP-LNIPE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 175 LSDLFTLI-YTSGTTGEPKGVMLDYANLAHQLNAHDLALN-----VNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCY- 247
Cdd:PTZ00216 262 NNDDLALImYTSGTTGDPKGVMHTHGSLTAGILALEDRLNdligpPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGFg 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 248 -----LEDTNHVRDALTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAicvgeqhYQAeqpsqwlRLQyALA 322
Cdd:PTZ00216 342 sprtlTDTFARPHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHA-------YQS-------RLR-ALK 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 323 D--------KLVLTKLRALLGGRIKMMPCGGAKLEASIGSFFHSI-GINIKlGYGMTETTAtVSCWQDKG-FNPNSIGTL 392
Cdd:PTZ00216 407 EgkdtpywnEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVfGMVIQ-GWGLTETVC-CGGIQRTGdLEPNAVGQL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 393 MPNAEVKI--GEE----------NEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKT 460
Cdd:PTZ00216 485 LKGVEMKLldTEEykhtdtpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKN 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 461 SNGKYIAPQYIEGKIGKDKFI--EQIAVIAD-AKKYVSALIVPCFDSLEEYAKQLNIK------YQDRIELIKHSDIIQM 531
Cdd:PTZ00216 565 CLGEYIALEALEALYGQNELVvpNGVCVLVHpARSYICALVLTDEAKAMAFAKEHGIEgeypaiLKDPEFQKKATESLQE 644
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 532 FERRIHElqkelPSFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMYNE 591
Cdd:PTZ00216 645 TARAAGR-----KSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-487 |
2.15e-57 |
|
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: 199.71 E-value: 2.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 15 QAKKWLNRTALRFREQaqwqemsWQTFQQ---EIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:cd05936 8 AARRFPDKTALIFMGR-------KLTYREldaLAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILFVGdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywEDFLDVV-PNEAEFEKRL 170
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVA---------------------------------------VSFTDLLaAGAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 171 NSKQlsDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVN--EDDVSLSFLPLSHIFerAWVA---YVFHRGATN 245
Cdd:cd05936 122 LTPE--DVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLleGDDVVLAALPLFHVF--GLTVallLPLALGATI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 246 cYLEDTNHVRDALTTL---KPTVMCAVPRFYEkiytavwdkvekALAHRRALfnwaicvgeqhyqaeqpsqwlrlqyala 322
Cdd:cd05936 198 -VLIPRFRPIGVLKEIrkhRVTIFPGVPTMYI------------ALLNAPEF---------------------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 323 DKLVLTKLRALLggrikmmpCGGAKLEASIGSFFHSI-GINIKLGYGMTETTATVSC----WQDKgfnPNSIGTLMPNAE 397
Cdd:cd05936 237 KKRDFSSLRLCI--------SGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVnpldGPRK---PGSIGIPLPGTE 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 398 VKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIA 467
Cdd:cd05936 306 VKIvdddgeelppGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKD-MIIVGGFNVY 383
|
490 500
....*....|....*....|
gi 2490830388 468 PQYIEGKIGKDKFIEQIAVI 487
Cdd:cd05936 384 PREVEEVLYEHPAVAEAAVV 403
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
177-501 |
1.19e-55 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 191.34 E-value: 1.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLEDTN--HV 254
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDpeAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 255 RDALTTLKPTVMCAVPRFYEKIytavwdkvekalahrralfnwaicvgeqhyqaeqpsqwlrLQYALADKLVLTKLRALL 334
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARL----------------------------------------LKAPESAGYDLSSLRALV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 335 ggrikmmpCGGAKLEASIGSFFHSI-GINIKLGYGMTETTATVSCWQ--DKGFNPNSIGTLMPNAEVKI----------G 401
Cdd:cd04433 121 --------SGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPpdDDARKPGSVGRPVPGVEVRIvdpdggelppG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 402 EENEILVRGGMVMRGYYKKPEETAkAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNGKYIAPQYIEGKIGKDKFI 481
Cdd:cd04433 193 EIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGV 270
|
330 340
....*....|....*....|....
gi 2490830388 482 EQIAVIA--DAKK--YVSALIVPC 501
Cdd:cd04433 271 AEAAVVGvpDPEWgeRVVAVVVLR 294
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
21-500 |
1.80e-53 |
|
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: 188.20 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:cd17631 10 DRTALVFGGR----SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFvgdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlSDLFT 180
Cdd:cd17631 86 YILADSGAKVLF---------------------------------------------------------------DDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFE-RAWVAYVFHRGATNCYLE--DTNHVRDA 257
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGlGVFTLPTLLRGGTVVILRkfDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 258 LTTLKPTVMCAVPrfyekiytAVWDKVekalahrralfnwaicvgeqhyqaeqpsqwlrLQYALADKLVLTKLRALLggr 337
Cdd:cd17631 183 IERHRVTSFFLVP--------TMIQAL--------------------------------LQHPRFATTDLSSLRAVI--- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 338 ikmmpCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVsCW------QDKgfnPNSIGTLMPNAEVKI----------G 401
Cdd:cd17631 220 -----YGGAPMPERLLRALQARGVKFVQGYGMTETSPGV-TFlspedhRRK---LGSAGRPVFFVEVRIvdpdgrevppG 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 402 EENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIGKDKFI 481
Cdd:cd17631 291 EVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKD-MIISGGENVYPAEVEDVLYEHPAV 368
|
490 500
....*....|....*....|...
gi 2490830388 482 EQIAVIA--DAK--KYVSALIVP 500
Cdd:cd17631 369 AEVAVIGvpDEKwgEAVVAVVVP 391
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
47-468 |
1.32e-45 |
|
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: 168.57 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 47 RFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgdqeqldqVCQIA 126
Cdd:cd05904 44 RLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT--------TAELA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 127 NNCPQL-MKIVAMkanmdlRDLPNACYWEDFLDVVPNEAEFeKRLNSKQlSDLFTLIYTSGTTGEPKGVMLDYANL---A 202
Cdd:cd05904 116 EKLASLaLPVVLL------DSAEFDSLSFSDLLFEADEAEP-PVVVIKQ-DDVAALLYSSGTTGRSKGVMLTHRNLiamV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 203 HQLNAhDLALNVNEDDVSLSFLPLSHIFERAWVAY-VFHRGATNCYLE--DTNHVRDALTTLKPTVMCAVPrfyekiyta 279
Cdd:cd05904 188 AQFVA-GEGSNSDSEDVFLCVLPMFHIYGLSSFALgLLRLGATVVVMPrfDLEELLAAIERYKVTHLPVVP--------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 280 vwdKVEKALAHRralfnwaicvgeqhyqaeqpsqwlrlqyALADKLVLTKLRALLggrikmmpCGGAKLEASIGSFFHSI 359
Cdd:cd05904 258 ---PIVLALVKS----------------------------PIVDKYDLSSLRQIM--------SGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 360 --GINIKLGYGMTETTA-TVSCWQDKGF--NPNSIGTLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKPEE 423
Cdd:cd05904 299 fpNVDLGQGYGMTESTGvVAMCFAPEKDraKYGSVGRLVPNVEAKIvdpetgeslppNQTGELWIRGPSIMKGYLNNPEA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2490830388 424 TAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAP 468
Cdd:cd05904 379 TAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAP 422
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
16-500 |
1.41e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 166.29 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 16 AKKWLNRTALRFREQAqwqeMSWQTFQQEIDRFSyALIAQHIDIQ--DKIGIFANNMPRWTIADFGAMQARAVAVPIYAT 93
Cdd:PRK08314 20 ARRYPDKTAIVFYGRA----ISYRELLEEAERLA-GYLQQECGVRkgDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 94 NTAKQVEYIVNDADIKILFVGdQEQLDQVCQIANNCPQLMKIVAMKANMD-----------LR--------DLPNACYWE 154
Cdd:PRK08314 95 NREEELAHYVTDSGARVAIVG-SELAPKVAPAVGNLRLRHVIVAQYSDYLpaepeiavpawLRaepplqalAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 155 DFLD--VVPNEAEfekrlnsKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHI--F 230
Cdd:PRK08314 174 EALAagLAPPPHT-------AGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVtgM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 231 ERAWVAYVFhRGATncyledtnhvrdalttlkpTVMcaVPRfyekiytavWDKvekALAHRralfnwAIcvgeQHYQAeq 310
Cdd:PRK08314 247 VHSMNAPIY-AGAT-------------------VVL--MPR---------WDR---EAAAR------LI----ERYRV-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 311 pSQWLRLQYALADKLV--------LTKLRaLLGGrikmmpcGGAKLEASIGSFFHSI-GINIKLGYGMTETTATVScwqd 381
Cdd:PRK08314 281 -THWTNIPTMVVDFLAspglaerdLSSLR-YIGG-------GGAAMPEAVAERLKELtGLDYVEGYGLTETMAQTH---- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 382 kgFNP------NSIG--------------TLmpnAEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTE-DG--FLRTGD 438
Cdd:PRK08314 348 --SNPpdrpklQCLGiptfgvdarvidpeTL---EELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGD 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2490830388 439 VGEMDSCGNLFITDRLKELMKTSNGKyIAPQYIEGKIGKDKFIEQIAVIA--DAKK--YVSALIVP 500
Cdd:PRK08314 423 LGRMDEEGYFFITDRLKRMINASGFK-VWPAEVENLLYKHPAIQEACVIAtpDPRRgeTVKAVVVL 487
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
35-499 |
3.79e-42 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 157.26 E-value: 3.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 35 EMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVG 114
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 115 dqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnsKQLSDLFTLIYTSGTTGEPKGV 194
Cdd:cd05935 81 ----------------------------------------------------------SELDDLALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 195 MLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIferawvayvfhrgatncyledtnhvrdalTTLKPTVMCAVPRFYE 274
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPSDVILACLPLFHV-----------------------------TGFVGSLNTAVYVGGT 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 275 KIYTAVWDK--VEKALAHRRALFNWAIcvgeqhyqaeqPSQWLRLQYALADKLV-LTKLRALLGGRIKMMPCGGAKLEAS 351
Cdd:cd05935 154 YVLMARWDRetALELIEKYKVTFWTNI-----------PTMLVDLLATPEFKTRdLSSLKVLTGGGAPMPPAVAEKLLKL 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 352 IGSFFHSiginiklGYGMTETTATV----------SCWQDKGFNPNS-IGTLMPNAEVKIGEENEILVRGGMVMRGYYKK 420
Cdd:cd05935 223 TGLRFVE-------GYGLTETMSQThtnpplrpklQCLGIP*FGVDArVIDIETGRELPPNEVGEIVVRGPQIFKGYWNR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 421 PEETAKAFTEDG---FLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVIADAKKY---- 493
Cdd:cd05935 296 PEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVISVPDERvgee 374
|
....*.
gi 2490830388 494 VSALIV 499
Cdd:cd05935 375 VKAFIV 380
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
34-488 |
3.23e-39 |
|
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: 148.98 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFV 113
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 114 gdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlsDLFTLIYTSGTTGEPKG 193
Cdd:cd05934 82 ---------------------------------------------------------------DPASILYTSGTTGPPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 194 VMLDYANLAH--QLNAHDLALNvnEDDVSLSFLPLSHIFERAWVAYV-FHRGATnCYLEDTNHVRdalttlkptvmcavp 270
Cdd:cd05934 99 VVITHANLTFagYYSARRFGLG--EDDVYLTVLPLFHINAQAVSVLAaLSVGAT-LVLLPRFSAS--------------- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 271 RFyekiytavWDKVEKalaHRRALFNwaiCVGEQ-HYQAEQPSQWLRLQYaladklvltKLRALlggrikmmpCGGAKLE 349
Cdd:cd05934 161 RF--------WSDVRR---YGATVTN---YLGAMlSYLLAQPPSPDDRAH---------RLRAA---------YGAPNPP 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 350 ASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI----------GEENEILVRG----GMvMR 415
Cdd:cd05934 209 ELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIvdddgqelpaGEPGELVIRGlrgwGF-FK 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2490830388 416 GYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:cd05934 288 GYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAAVVA 358
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
21-472 |
8.38e-39 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 150.26 E-value: 8.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFR-EQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQV 99
Cdd:COG0365 24 DKVALIWEgEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 100 EYIVNDADIKILFVGD--------QEQLDQVCQIANNCPQLMKIVAMKANMDLRDLPNACYWEDFLDVVPNEAEFEkRLN 171
Cdd:COG0365 104 ADRIEDAEAKVLITADgglrggkvIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAEFEPE-PTD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 172 SkqlSDLFTLIYTSGTTGEPKGVMLDYAN-LAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAY-VFHRGATNCYLE 249
Cdd:COG0365 183 A---DDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYgPLLNGATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 DTNHVRDALTTL------KPTVMCAVPRFYekiytavwdkvekalahrRALFNWAICVGEQHyqaeqpsqwlrlqyalaD 323
Cdd:COG0365 260 GRPDFPDPGRLWeliekyGVTVFFTAPTAI------------------RALMKAGDEPLKKY-----------------D 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 324 klvLTKLRALLggrikmmpCGGAKLEASIGSFFHS-IGINIKLGYGMTETTAT-VSCWQDKGFNPNSIGTLMPNAEVKI- 400
Cdd:COG0365 305 ---LSSLRLLG--------SAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVAVv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 ---------GEENEILVRG---GMvMRGYYKKPEETAKAF--TEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYI 466
Cdd:COG0365 374 dedgnpvppGEEGELVIKGpwpGM-FRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRI 451
|
....*.
gi 2490830388 467 APQYIE 472
Cdd:COG0365 452 GTAEIE 457
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
37-488 |
1.71e-37 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 145.85 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 37 SWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQ 116
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV-DR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 117 EQLDQVCQIANNCPQLMKIVAM--KANMDLRDLPNACYWEDFLDVVPNEAEFeKRLNSKQLSdlfTLIYTSGTTGEPKGV 194
Cdd:cd12119 106 DFLPLLEAIAPRLPTVEHVVVMtdDAAMPEPAGVGVLAYEELLAAESPEYDW-PDFDENTAA---AICYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 195 MLDYANLAHQ---LNAHDlALNVNEDDVSLSFLPLSHIfeRAW-VAYV-FHRGA----TNCYLeDTNHVRDALTTLKPTV 265
Cdd:cd12119 182 VYSHRSLVLHamaALLTD-GLGLSESDVVLPVVPMFHV--NAWgLPYAaAMVGAklvlPGPYL-DPASLAELIEREGVTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 266 MCAVPrfyekiytAVWDKVekalahrralfnwaicvgeqhyqaeqpsqwlrLQYALADKLVLTKLRALLggrikmmpCGG 345
Cdd:cd12119 258 AAGVP--------TVWQGL--------------------------------LDHLEANGRDLSSLRRVV--------IGG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 346 AKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPN-----------SIGTLMPNAEVKIGEEN---------- 404
Cdd:cd12119 290 SAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNlsedeqlalraKQGRPVPGVELRIVDDDgrelpwdgka 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 --EILVRGGMVMRGYYKKPEETAkAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNGKYIAPQYIEGKIGKDKFIE 482
Cdd:cd12119 370 vgELQVRGPWVTKSYYKNDEESE-ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWISSVELENAIMAHPAVA 447
|
....*.
gi 2490830388 483 QIAVIA 488
Cdd:cd12119 448 EAAVIG 453
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
21-516 |
3.12e-37 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 143.58 E-value: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQ-DKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQV 99
Cdd:cd05941 1 DRIAIVDDGD----SITYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 100 EYIVNDADIKILFvgdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlsDLF 179
Cdd:cd05941 77 EYVITDSEPSLVL----------------------------------------------------------------DPA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 180 TLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIferawvayvfH-----------RGATNCYL 248
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHV----------HglvnallcplfAGASVEFL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 249 EDTNHVRDALTTLKP--TVMCAVPRFYEKIytavwdkvekalahrralfnwaicvgeqhyqaeqpsqwlrLQYALADKLV 326
Cdd:cd05941 163 PKFDPKEVAISRLMPsiTVFMGVPTIYTRL----------------------------------------LQYYEAHFTD 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 327 LTKLRALLGGRIKMMPCGGAKLEASIGSFFHSIGINIKLG-YGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKIGEEN- 404
Cdd:cd05941 203 PQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLErYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEEt 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 ----------EILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYIAPQYIEGK 474
Cdd:cd05941 283 geplprgevgEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERV 362
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2490830388 475 IGKDKFIEQIAVI----ADAKKYVSALIVP-------CFDSLEEYAKQLNIKY 516
Cdd:cd05941 363 LLAHPGVSECAVIgvpdPDWGERVVAVVVLragaaalSLEELKEWAKQRLAPY 415
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
180-466 |
3.96e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 147.17 E-value: 3.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 180 TLIYTSGTTGEPKGVMLDYANLAHQ---LNAHDLALNVNEDDvSLSFLPLSHIFERAWVAYVFHRGAT-NCYLEDTNHVR 255
Cdd:PTZ00342 308 SIVYTSGTSGKPKGVMLSNKNLYNTvvpLCKHSIFKKYNPKT-HLSYLPISHIYERVIAYLSFMLGGTiNIWSKDINYFS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 256 DALTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICVGEQHYQAEQpSQWLrlqyalaDKL--VLTKLRAL 333
Cdd:PTZ00342 387 KDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGF-SKFL-------EGIthISSKIKDK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 334 LGGRIKMMPCGGAKLEASIGSFFhSIGINIKL--GYGMTETTATVSCWQDKGFNPNSIG-TLMPNAEVKIGE-------- 402
Cdd:PTZ00342 459 VNPNLEVILNGGGKLSPKIAEEL-SVLLNVNYyqGYGLTETTGPIFVQHADDNNTESIGgPISPNTKYKVRTwetykatd 537
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490830388 403 ---ENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKYI 466
Cdd:PTZ00342 538 tlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYI 604
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
37-579 |
3.15e-34 |
|
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: 135.90 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 37 SWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVGDQ 116
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 117 EQLDqvCQIAnncpqlmkivAMKANMDLRDLpnacYWEDFLDVVPNEAE------FEKRLNSKQL----SDLFTLIYTSG 186
Cdd:cd05926 96 ELGP--ASRA----------ASKLGLAILEL----ALDVGVLIRAPSAEslsnllADKKNAKSEGvplpDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 187 TTGEPKGVMLDYANLA---------HQLNAHDLALNVneddvslsfLPLSHIferawvayvfhrgatncyledtnH--VR 255
Cdd:cd05926 160 TTGRPKGVPLTHRNLAasatnitntYKLTPDDRTLVV---------MPLFHV-----------------------HglVA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 256 DALTTL--KPTVMCAvPRFYEkiyTAVWDKVEKALAhrralfNWAICVGEQHyqaeqpsQWLrLQYALADKL-VLTKLRA 332
Cdd:cd05926 208 SLLSTLaaGGSVVLP-PRFSA---STFWPDVRDYNA------TWYTAVPTIH-------QIL-LNRPEPNPEsPPPKLRF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 333 LLGGRIKMMPCGGAKLEAsigsFFhsiGINIKLGYGMTETTATVSC-----WQDKgfnPNSIGtlMPN-AEVKI------ 400
Cdd:cd05926 270 IRSCSASLPPAVLEALEA----TF---GAPVLEAYGMTEAAHQMTSnplppGPRK---PGSVG--KPVgVEVRIldedge 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 ----GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIG 476
Cdd:cd05926 338 ilppGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 477 KDKFIEQIAVIA--DAkKY---VSALIVPCFDSleeyakqlnikYQDRIELIKHsdiiqmferriheLQKELPSFEQVKK 551
Cdd:cd05926 417 SHPAVLEAVAFGvpDE-KYgeeVAAAVVLREGA-----------SVTEEELRAF-------------CRKHLAAFKVPKK 471
|
570 580 590
....*....|....*....|....*....|.
gi 2490830388 552 FTL---LPQafsttmeeiTPTLKLRRKVIMQ 579
Cdd:cd05926 472 VYFvdeLPK---------TATGKIQRRKVAE 493
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
35-487 |
4.01e-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: 136.50 E-value: 4.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 35 EMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVg 114
Cdd:cd17642 44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 115 DQEQLDQVCQIANNCPQLMKIVAMKANMDLRDL--------PNACYWEDFLDVVPNEAEFEKrlnskqlsDLFTLIYTSG 186
Cdd:cd17642 123 SKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYqclytfitQNLPPGFNEYDFKPPSFDRDE--------QVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 187 TTGEPKGVMLDYANLAHQLN-AHD--LALNVNEDDVSLSFLPLSHIFerawvayvfhrgatncyledtnhvrdALTTLKP 263
Cdd:cd17642 195 STGLPKGVQLTHKNIVARFShARDpiFGNQIIPDTAILTVIPFHHGF--------------------------GMFTTLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 264 TVMCA-----VPRFYEKIY-TAVWD-KVEKAL--AHRRALFNwaicvgeqhyqaeqpsqwlrlQYALADKLVLTKLRALL 334
Cdd:cd17642 249 YLICGfrvvlMYKFEEELFlRSLQDyKVQSALlvPTLFAFFA---------------------KSTLVDKYDLSNLHEIA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 335 ggrikmmpCGGAKLEASIGSFF-HSIGIN-IKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI-----------G 401
Cdd:cd17642 308 --------SGGAPLSKEVGEAVaKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVvdldtgktlgpN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 402 EENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGKIGKDKFI 481
Cdd:cd17642 380 ERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKI 458
|
....*.
gi 2490830388 482 EQIAVI 487
Cdd:cd17642 459 FDAGVA 464
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
21-512 |
6.33e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 136.06 E-value: 6.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQAQwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:PRK12583 33 DREALVVRHQAL--RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFVGD----------------QEQLDQVCQIAN-NCPQLMKIVAMkanmDLRDLPNACYWEDFL---DVV 160
Cdd:PRK12583 111 YALGQSGVRWVICADafktsdyhamlqellpGLAEGQPGALACeRLPELRGVVSL----APAPPPGFLAWHELQargETV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 161 PNEAEFEkRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFER--AWVAYV 238
Cdd:PRK12583 187 SREALAE-RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMvlANLGCM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 239 FHrGATNCYledTNHVRDALTTLKP------TVMCAVPRFYekiytavwdkvekaLAhrralfnwaicvgeqhyQAEQPs 312
Cdd:PRK12583 266 TV-GACLVY---PNEAFDPLATLQAveeercTALYGVPTMF--------------IA-----------------ELDHP- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 313 qwlrlQYALADklvLTKLR-ALLGGrikmMPCGGAKLEASIGSFFHSigiNIKLGYGMTETT--ATVSCWQDK-GFNPNS 388
Cdd:PRK12583 310 -----QRGNFD---LSSLRtGIMAG----APCPIEVMRRVMDEMHMA---EVQIAYGMTETSpvSLQTTAADDlERRVET 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 389 IGTLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKElM 458
Cdd:PRK12583 375 VGRTQPHLEVKVvdpdgatvprGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKD-M 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 459 KTSNGKYIAPQYIEgkigkDKFIEQIAVIAdakkyVSALIVPCfdslEEYAKQL 512
Cdd:PRK12583 454 IIRGGENIYPREIE-----EFLFTHPAVAD-----VQVFGVPD----EKYGEEI 493
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
75-501 |
9.79e-34 |
|
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: 134.38 E-value: 9.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 75 IADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVGDQ--EQLDQvcqianncPQLMKIVAMKANMDLRDLPNACY 152
Cdd:cd05909 46 LANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQfiEKLKL--------HHLFDVEYDARIVYLEDLRAKIS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 153 WED----FLD--VVPNEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPL 226
Cdd:cd05909 118 KADkckaFLAgkFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 227 SHIFERA---W------VAYVFHRGATNcYLEDTNHVRDAlttlKPTVMCAVPRFYeKIYTavwdkvekalahRRAlfnw 297
Cdd:cd05909 198 FHSFGLTgclWlpllsgIKVVFHPNPLD-YKKIPELIYDK----KATILLGTPTFL-RGYA------------RAA---- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 298 aicvgeqhyqaeQPSQWLRLQYALadklvltklrallggrikmmpCGGAKLEASIGSFFHS-IGINIKLGYGMTETTATV 376
Cdd:cd05909 256 ------------HPEDFSSLRLVV---------------------AGAEKLKDTLRQEFQEkFGIRILEGYGTTECSPVI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 377 SCWQDK-GFNPNSIGTLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDS 444
Cdd:cd05909 303 SVNTPQsPNKEGTVGRPLPGMEVKIvsvetheevpiGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDG 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2490830388 445 CGNLFITDRLKELMKtsngkyiapqyIEGKIGKDKFIEQIA-VIADAKKYVSALIVPC 501
Cdd:cd05909 382 EGFLTITGRLSRFAK-----------IAGEMVSLEAIEDILsEILPEDNEVAVVSVPD 428
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
23-472 |
4.03e-33 |
|
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: 132.98 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 23 TALRFREQAqwqeMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYI 102
Cdd:TIGR03098 17 TALVHHDRT----LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 103 VNDADIKILfVGDQEQLDQVCQIANNCPQLMKIVAMKANMDLRDLP---NACYWEDFLDVVPneaefEKRLNSKQLSDLF 179
Cdd:TIGR03098 93 LADCNVRLL-VTSSERLDLLHPALPGCHDLRTLIIVGDPAHASEGHpgeEPASWPKLLALGD-----ADPPHPVIDSDMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 180 TLIYTSGTTGEPKGVMLDYANLAhqLNAHDLA--LNVNEDDVSLSFLPLSHIFERAWVAYVFHRGATnCYLEDTNHVRDA 257
Cdd:TIGR03098 167 AILYTSGSTGRPKGVVLSHRNLV--AGAQSVAtyLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGAT-VVLHDYLLPRDV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 258 LTTLKP---TVMCAVPRFYEKIYTAVWDkvEKALAHRRALFNwaicvgeqhyqaeqpsqwlrlqyaladklvltklralL 334
Cdd:TIGR03098 244 LKALEKhgiTGLAAVPPLWAQLAQLDWP--ESAAPSLRYLTN-------------------------------------S 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 335 GGRikmMPcggAKLEASIGSFFHSigINIKLGYGMTEttATVSCWQDKGF---NPNSIGTLMPNAEVKI----------G 401
Cdd:TIGR03098 285 GGA---MP---RATLSRLRSFLPN--ARLFLMYGLTE--AFRSTYLPPEEvdrRPDSIGKAIPNAEVLVlredgsecapG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 402 EENEILVRGGMVMRGYYKKPEETAKAFT-----EDGFLRT------GDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQY 470
Cdd:TIGR03098 355 EEGELVHRGALVAMGYWNDPEKTAERFRplppfPGELHLPelavwsGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTE 433
|
..
gi 2490830388 471 IE 472
Cdd:TIGR03098 434 VE 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
2-499 |
8.17e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.93 E-value: 8.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 2 ASLDFHfvnrfrlqAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAM 81
Cdd:PRK06145 6 ASIAFH--------ARRTPDRAALVYRDQ----EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 82 QARAVAVPIYATNTAKQVEYIVNDADIKILFVgdQEQLDQVcqIANNCPQLmkIVAMKANMDLRDLPNAcywedFLDVVP 161
Cdd:PRK06145 74 YLGAVFLPINYRLAADEVAYILGDAGAKLLLV--DEEFDAI--VALETPKI--VIDAAAQADSRRLAQG-----GLEIPP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 162 NEAEFEkrlnskqlSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHI--FERAWVAYVF 239
Cdd:PRK06145 143 QAAVAP--------TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVgaFDLPGIAVLW 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 240 HRGATNCYLE-DTNHVRDALTTLKPTVMCAVPRFYEKIYTaVWDKVEKALAHrralFNWAICVGEQhyqaeQPSQWLRlq 318
Cdd:PRK06145 215 VGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVLT-VPDRDRFDLDS----LAWCIGGGEK-----TPESRIR-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 319 yaladklvltklrallggrikmmpcggakleaSIGSFFHsiGINIKLGYGMTETTATvSCWQDKGFNPNSIGTL---MPN 395
Cdd:PRK06145 283 --------------------------------DFTRVFT--RARYIDAYGLTETCSG-DTLMEAGREIEKIGSTgraLAH 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 396 AEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKY 465
Cdd:PRK06145 328 VEIRIadgagrwlppNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKD-MIISGGEN 405
|
490 500 510
....*....|....*....|....*....|....*...
gi 2490830388 466 IAPQYIEGKIGKDKFIEQIAVIA--DAK--KYVSALIV 499
Cdd:PRK06145 406 IASSEVERVIYELPEVAEAAVIGvhDDRwgERITAVVV 443
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
54-508 |
1.35e-32 |
|
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: 132.58 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 54 AQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQEQLDQVCQIANNCPQLM 133
Cdd:cd17632 87 EQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV-SAEHLDLAVEAVLEGGTPP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 134 KIV---------AMKANMD-----LRDLPNACYWEDFLDVVPNEAEFEKRLNSKQLSD-LFTLIYTSGTTGEPKGVMLDY 198
Cdd:cd17632 166 RLVvfdhrpevdAHRAALEsarerLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDpLALLIYTSGSTGTPKGAMYTE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 199 ANLAHQLnahdLALNVNEDD-----VSLSFLPLSHIFERAWVAYVFHRGATNCYL--EDTNHVRDALTTLKPTVMCAVPR 271
Cdd:cd17632 246 RLVATFW----LKVSSIQDIrppasITLNFMPMSHIAGRISLYGTLARGGTAYFAaaSDMSTLFDDLALVRPTELFLVPR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 272 fyekiytaVWDKVekalahrralfnwaicvgEQHYQAEQpsQWLRLQYALADKL---VLTKLRA-LLGGRIKMMPCGGAK 347
Cdd:cd17632 322 --------VCDML------------------FQRYQAEL--DRRSVAGADAETLaerVKAELRErVLGGRLLAAVCGSAP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 348 LEASIGSFFHS-IGINIKLGYGMTETtatvscwqdkgfnpnsiGTLMPNAEVK--------------IG--------EEN 404
Cdd:cd17632 374 LSAEMKAFMESlLDLDLHDGYGSTEA-----------------GAVILDGVIVrppvldyklvdvpeLGyfrtdrphPRG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 EILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVgeMDSCG--NLFITDRLKELMKTSNGKYIAPQYIEGKIGKDKFIE 482
Cdd:cd17632 437 ELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV--MAELGpdRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVR 514
|
490 500
....*....|....*....|....*..
gi 2490830388 483 QIAVIAD-AKKYVSALIVPCFDSLEEY 508
Cdd:cd17632 515 QIFVYGNsERAYLLAVVVPTQDALAGE 541
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
44-472 |
4.84e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 130.65 E-value: 4.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 44 EIDRFSYALIA---QHIDIQ--DKIGIFANNMPRWTIADFGAMQARAVAV---PIYatnTAKQVEYIVNDADIKILFV-G 114
Cdd:PRK05677 54 ELYKLSGAFAAwlqQHTDLKpgDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY---TAREMEHQFNDSGAKALVClA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 115 DQEQLDQ------------VCQIANNCPQLMKIVA------MKANMDLRDLPNACyweDFLDVVPNEAEFEKRLNSKQLS 176
Cdd:PRK05677 131 NMAHLAEkvlpktgvkhviVTEVADMLPPLKRLLInavvkhVKKMVPAYHLPQAV---KFNDALAKGAGQPVTEANPQAD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANL-AHQLNAHDL-ALNVNED-DVSLSFLPLSHIFerawvAYVFHRGATncyLEDTNH 253
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRNLvANMLQCRALmGSNLNEGcEILIAPLPLYHIY-----AFTFHCMAM---MLIGNH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 254 vrdalttlkpTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNwAICVGEqhyqaeqpsqwlrlqyaladklvltKLRAL 333
Cdd:PRK05677 280 ----------NILISNPRDLPAMVKELGKWKFSGFVGLNTLFV-ALCNNE-------------------------AFRKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 334 LGGRIKMMPCGGAKLEASIGSFFHSI-GINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI----------GE 402
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVidddgnelplGE 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 403 ENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIE 472
Cdd:PRK05677 404 VGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS-GFNVYPNELE 472
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
46-453 |
7.42e-32 |
|
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: 127.77 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 46 DRFSYALIAQH-IDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVGDQEQLDQVCq 124
Cdd:TIGR01733 10 NRLARHLRAAGgVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 125 ianncpqlmkivamkanMDLRDLPNACYWEDFLDVVPNEAEFEKRLNSkqlSDLFTLIYTSGTTGEPKGVMLDYANLAHQ 204
Cdd:TIGR01733 89 -----------------LVLPVILLDPLELAALDDAPAPPPPDAPSGP---DDLAYVIYTSGSTGRPKGVVVTHRSLVNL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 205 LNAHDLALNVNEDDVSLSFLPLSH---IFERAWVAYVfhrGATNCYLEDT------NHVRDALTTLKPTVMCAVPrfyek 275
Cdd:TIGR01733 149 LAWLARRYGLDPDDRVLQFASLSFdasVEEIFGALLA---GATLVVPPEDeerddaALLAALIAEHPVTVLNLTP----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 276 iytAVWDKVEKALAHRRALFNWAICVGEqhyqaeqpsqWLRLQyaladklVLTKLRAllggrikmmPCGGAKLeasigsf 355
Cdd:TIGR01733 221 ---SLLALLAAALPPALASLRLVILGGE----------ALTPA-------LVDRWRA---------RGPGARL------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 356 fhsigINiklGYGMTETTATVSCWQ-----DKGFNPNSIGTLMPNAE----------VKIGEENEILVRGGMVMRGYYKK 420
Cdd:TIGR01733 265 -----IN---LYGPTETTVWSTATLvdpddAPRESPVPIGRPLANTRlyvldddlrpVPVGVVGELYIGGPGVARGYLNR 336
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2490830388 421 PEETAKAFTEDGFL--------RTGDVGEMDSCGNLFITDR 453
Cdd:TIGR01733 337 PELTAERFVPDPFAggdgarlyRTGDLVRYLPDGNLEFLGR 377
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
84-489 |
9.72e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 128.33 E-value: 9.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 84 RAVAVPIYATNTAKQVEYIVNDADIKILfvgdqeqldqvcqianncpqlmkIVAMKANMDLRDLPNACY----WEDFLDV 159
Cdd:cd05922 46 GLVFVPLNPTLKESVLRYLVADAGGRIV-----------------------LADAGAADRLRDALPASPdpgtVLDADGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 160 VPNEAEFEKRLNSKQlsDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAYVF 239
Cdd:cd05922 103 RAARASAPAHEVSHE--DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 240 HRGAT----NCYLEDTNHVrDALTTLKPTVMCAVPRFYEKIYTAVWDKVEkaLAHRRALFNWAicvgeqhyqAEQPSQWL 315
Cdd:cd05922 181 LRGATlvltNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAK--LPSLRYLTQAG---------GRLPQETI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 316 RlqyALADKLVltklrallGGRIKMMpcggakleasigsffhsiginiklgYGMTETTATVSCW--QDKGFNPNSIGTLM 393
Cdd:cd05922 249 A---RLRELLP--------GAQVYVM-------------------------YGQTEATRRMTYLppERILEKPGSIGLAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 394 PNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnG 463
Cdd:cd05922 293 PGGEFEIldddgtptppGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-G 371
|
410 420
....*....|....*....|....*.
gi 2490830388 464 KYIAPQYIEGKIGKDKFIEQIAVIAD 489
Cdd:cd05922 372 NRISPTEIEAAARSIGLIIEAAAVGL 397
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-575 |
1.84e-31 |
|
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: 127.26 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:cd05930 2 DAVAVVDGDQ----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFVgdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskQLSDLFT 180
Cdd:cd05930 78 YILEDSGAKLVLT------------------------------------------------------------DPDDLAY 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLS---HIFErAWVAYVfhRGATnCYLEDTNHVRD- 256
Cdd:cd05930 98 VIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSfdvSVWE-IFGALL--AGAT-LVVLPEEVRKDp 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 257 -----ALTTLKPTVMCAVPrfyekiytavwdkvekalAHRRALFNWAicvgeqhyqaeqpsqwlrlqyalaDKLVLTKLR 331
Cdd:cd05930 174 ealadLLAEEGITVLHLTP------------------SLLRLLLQEL------------------------ELAALPSLR 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 332 ALLggrikmmpCGGAKLEASIGSFFHSIGINIKL--GYGMTETTATVSCW----QDKGFNPNSIGTLMPNAE-------- 397
Cdd:cd05930 212 LVL--------VGGEALPPDLVRRWRELLPGARLvnLYGPTEATVDATYYrvppDDEEDGRVPIGRPIPNTRvyvldenl 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 398 --VKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFL------RTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQ 469
Cdd:cd05930 284 rpVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVKI-RGYRIELG 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 470 YIEGKIGKDKFIEQIAVIA----DAKKYVSALIVPcfdsleeyakqlnikyqDRIELIKHSDIIQmferrihELQKELPS 545
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAredgDGEKRLVAYVVP-----------------DEGGELDEEELRA-------HLAERLPD 418
|
570 580 590
....*....|....*....|....*....|..
gi 2490830388 546 FeqvkkftLLPQAFsTTMEEI--TPTLKLRRK 575
Cdd:cd05930 419 Y-------MVPSAF-VVLDALplTPNGKVDRK 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
21-499 |
8.89e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 127.04 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAV---PIYatnTAK 97
Cdd:PRK05605 47 DRPALDFFGA----TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLY---TAH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 98 QVEYIVNDADIKILFVGDQeQLDQVCQIANNCPqLMKIV------AMKANMDL------------RD-----LPNACYWE 154
Cdd:PRK05605 120 ELEHPFEDHGARVAIVWDK-VAPTVERLRRTTP-LETIVsvnmiaAMPLLQRLalrlpipalrkaRAaltgpAPGTVPWE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 155 DFLDVVPNEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANL---AHQLNAHDLALnVNEDDVSLSFLPLSHIFE 231
Cdd:PRK05605 198 TLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLfanAAQGKAWVPGL-GDGPERVLAALPMFHAYG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 232 RAWV-AYVFHRGATNCYLE--DTNHVRDALTTLKPTVMCAVPRFYEKIytavwdkVEKALAHRralfnwaicvgeqhyqa 308
Cdd:PRK05605 277 LTLClTLAVSIGGELVLLPapDIDLILDAMKKHPPTWLPGVPPLYEKI-------AEAAEERG----------------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 309 eqpsqwlrlqyaladkLVLTKLRALLGGRIKMMPCGGAKLEASIGSFfhsiginIKLGYGMTETTATVSCwqdkgfNPNS 388
Cdd:PRK05605 333 ----------------VDLSGVRNAFSGAMALPVSTVELWEKLTGGL-------LVEGYGLTETSPIIVG------NPMS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 389 -------IGTLMPNAEVKI------------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLF 449
Cdd:PRK05605 384 ddrrpgyVGVPFPDTEVRIvdpedpdetmpdGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIR 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 450 ITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVI----ADAKKYVSALIV 499
Cdd:PRK05605 463 IVDRIKELIITG-GFNVYPAEVEEVLREHPGVEDAAVVglprEDGSEEVVAAVV 515
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
31-492 |
1.49e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 126.31 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 31 AQWQEMSwqtfqqeiDRFSyALIAQH-IDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIK 109
Cdd:PRK06178 62 AELDELS--------DRFA-ALLRQRgVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 110 ILFVGDQeQLDQVCQIANNCPQLMKIVAMKANM-----------DLRDLPNACY-WEDFLDVVPNEAEfEKRLNSKQLSD 177
Cdd:PRK06178 133 VLLALDQ-LAPVVEQVRAETSLRHVIVTSLADVlpaeptlplpdSLRAPRLAAAgAIDLLPALRACTA-PVPLPPPALDA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 178 LFTLIYTSGTTGEPKGVMLDYANLAHQLNA-HDLALNVNEDDVSLSFLPlshIFeraWVA-------YVFHRGATNCYLe 249
Cdd:PRK06178 211 LAALNYTGGTTGMPKGCEHTQRDMVYTAAAaYAVAVVGGEDSVFLSFLP---EF---WIAgenfgllFPLFSGATLVLL- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 dtnhVR-DALTtlkptVMCAVPRFYEKIYTAVWDKVEKALAHRRalfnwaicVGEQHYQAeqpsqwlrLQYALADKLVLt 328
Cdd:PRK06178 284 ----ARwDAVA-----FMAAVERYRVTRTVMLVDNAVELMDHPR--------FAEYDLSS--------LRQVRVVSFVK- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 KLRALLGGRIKMMpCGGAKLEASigsffhsiginiklgYGMTET-TA-TVSC-WQDKGFN----PNSIGTLMPNAEVKI- 400
Cdd:PRK06178 338 KLNPDYRQRWRAL-TGSVLAEAA---------------WGMTEThTCdTFTAgFQDDDFDllsqPVFVGLPVPGTEFKIc 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 ----------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQY 470
Cdd:PRK06178 402 dfetgellplGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSE 479
|
490 500
....*....|....*....|....
gi 2490830388 471 IEGKIGKDKFIEQIAVI--ADAKK 492
Cdd:PRK06178 480 VEALLGQHPAVLGSAVVgrPDPDK 503
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
18-587 |
1.84e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 125.92 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 18 KWLNRTALRFREQAQW----QEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYAT 93
Cdd:PRK06710 28 KYVEQMASRYPEKKALhflgKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 94 NTAKQVEYIVNDADIKILFVGD-----------QEQLDQ--VCQIANNCP---QLMKIVAMKANMDLRDLPNACYWEDFL 157
Cdd:PRK06710 108 YTERELEYQLHDSGAKVILCLDlvfprvtnvqsATKIEHviVTRIADFLPfpkNLLYPFVQKKQSNLVVKVSESETIHLW 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 158 DVVPNEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQ--LNAHDLALNVNEDDVSLSFLPLSHIFERAWV 235
Cdd:PRK06710 188 NSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtlMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 236 AyvfhrgatncyledtnhvrdALTTLKPTVMCAVPRFYEKIytaVWDKVEKalaHRRALFNWAicvgeqhyqaeqPSQWL 315
Cdd:PRK06710 268 M--------------------NLSIMQGYKMVLIPKFDMKM---VFEAIKK---HKVTLFPGA------------PTIYI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 316 RL-QYALADKLVLTKLRALLGGrikmmpcgGAKLEASIGSFFHSI-GINIKLGYGMTETTATVSC---WQDKgfNPNSIG 390
Cdd:PRK06710 310 ALlNSPLLKEYDISSIRACISG--------SAPLPVEVQEKFETVtGGKLVEGYGLTESSPVTHSnflWEKR--VPGSIG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 391 TLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKPEETAkAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMK 459
Cdd:PRK06710 380 VPWPDTEAMImsletgealppGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 460 TSnGKYIAPQYIEGKIGKDKFIEQIAVIADAKKY----VSALIVPCFDSL--EEYAKQLNIKYQDRIELIKhsdiiqmfe 533
Cdd:PRK06710 459 AS-GFNVYPREVEEVLYEHEKVQEVVTIGVPDPYrgetVKAFVVLKEGTEcsEEELNQFARKYLAAYKVPK--------- 528
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 534 rrIHELQKELPsfeqvkkftllpqafSTTMEEItptlkLRRKVIMQRYREQIEE 587
Cdd:PRK06710 529 --VYEFRDELP---------------KTTVGKI-----LRRVLIEEEKRKNEDE 560
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
34-487 |
6.36e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.43 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQEIDRFSYALIAQ-HIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILF 112
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 113 VGDQeqldqvcqIANNCPQLMKIVAMKANMDLRDLpnacywEDFLDVVPNEAEfekrlnSKQLSDLFTLIYTSGTTGEPK 192
Cdd:PRK06839 106 VEKT--------FQNMALSMQKVSYVQRVISITSL------KEIEDRKIDNFV------EKNESASFIICYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 193 GVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAY--VFHRGATNC--YLEDTNHVRdALTTLKPTVMCA 268
Cdd:PRK06839 166 GAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFptLFAGGVIIVprKFEPTKALS-MIEKHKVTVVMG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 269 VPRFYEKIYTAVwDKVEKALAHRRALFNwaicvgeqhyqaeqpsqwlrlqyaladklvltklrallggrikmmpcGGAKL 348
Cdd:PRK06839 245 VPTIHQALINCS-KFETTNLQSVRWFYN-----------------------------------------------GGAPC 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 349 EASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGF--NPNSIGTLMPNAEVKI----------GEENEILVRGGMVMRG 416
Cdd:PRK06839 277 PEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELidenknkvevGEVGELLIRGPNVMKE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2490830388 417 YYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:PRK06839 357 YWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKE-MIISGGENIYPLEVEQVINKLSDVYEVAVV 425
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
21-472 |
1.41e-29 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 123.12 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRF--REQAQWQEMSWQTFQQEIDRFSYALiaQHIDIQ-DKIGIFANNMPRWTIADFGAMQARAVAVPIYATN--- 94
Cdd:cd05931 8 DRPAYTFldDEGGREETLTYAELDRRARAIAARL--QAVGKPgDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTpgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 95 TAKQVEYIVNDADIKILFVgDQEQLDQVCQIANNCPQLMKIVAmkANMDLRDLPNACYWEDFldvvpneaefekrlnSKQ 174
Cdd:cd05931 86 HAERLAAILADAGPRVVLT-TAAALAAVRAFAASRPAAGTPRL--LVVDLLPDTSAADWPPP---------------SPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 175 LSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSH-------IFERAWVayvfhrGATnCY 247
Cdd:cd05931 148 PDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHdmgliggLLTPLYS------GGP-SV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 248 LEDTNH-VRD------ALTTLKPTVMcAVPRF-YEkiytavwdkvekaLAHRRAlfnwaicvgeqhyQAEQPSQwlrlqy 319
Cdd:cd05931 221 LMSPAAfLRRplrwlrLISRYRATIS-AAPNFaYD-------------LCVRRV-------------RDEDLEG------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 320 aladkLVLTKLRALLGG--RI----------KMMPCgGAKLEAsigsffhsiginIKLGYGMTETTATVSC-WQDKG--- 383
Cdd:cd05931 268 -----LDLSSWRVALNGaePVrpatlrrfaeAFAPF-GFRPEA------------FRPSYGLAEATLFVSGgPPGTGpvv 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 384 --FNPN--------------------SIGTLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKPEETAKAF-- 428
Cdd:cd05931 330 lrVDRDalagravavaaddpaarelvSCGRPLPDQEVRIvdpetgrelpdGEVGEIWVRGPSVASGYWGRPEATAETFga 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2490830388 429 ----TEDGFLRTGDVGEM-DscGNLFITDRLKELMkTSNGKYIAPQYIE 472
Cdd:cd05931 410 laatDEGGWLRTGDLGFLhD--GELYITGRLKDLI-IVRGRNHYPQDIE 455
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
12-500 |
6.31e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 120.81 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREQAqWqemSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:PRK08316 17 LRRSARRYPDKTALVFGDRS-W---TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILFVGDQ--EQLDQVCQIANNCPQLMKIVamkanMDLRDLPNAcyWEDFLDVVPNE--AEFE 167
Cdd:PRK08316 93 FMLTGEELAYILDHSGARAFLVDPAlaPTAEAALALLPVDTLILSLV-----LGGREAPGG--WLDFADWAEAGsvAEPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 168 KRLNSkqlSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSH-----IFERAWVaYVfhrG 242
Cdd:PRK08316 166 VELAD---DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHcaqldVFLGPYL-YV---G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 243 ATNCYLE--DTNHVRDALTTLKPTVMCAVPrfyekiytAVWdkveKALAhRRALFnwaicvgeqhyqaeqpsqwlrlqya 320
Cdd:PRK08316 239 ATNVILDapDPELILRTIEAERITSFFAPP--------TVW----ISLL-RHPDF------------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 321 laDKLVLTKLR-ALLGGRIkmMPcgGAKLEaSIGSFFHSIGI-NIklgYGMTET--TATVSCWQDKGFNPNSIGTLMPNA 396
Cdd:PRK08316 281 --DTRDLSSLRkGYYGASI--MP--VEVLK-ELRERLPGLRFyNC---YGQTEIapLATVLGPEEHLRRPGSAGRPVLNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 397 EVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYI 466
Cdd:PRK08316 351 ETRVvdddgndvapGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENV 428
|
490 500 510
....*....|....*....|....*....|....*...
gi 2490830388 467 APQYIEGKIGKDKFIEQIAVIA--DAK--KYVSALIVP 500
Cdd:PRK08316 429 ASREVEEALYTHPAVAEVAVIGlpDPKwiEAVTAVVVP 466
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
177-581 |
8.12e-29 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 117.05 E-value: 8.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIferAWVAYVfhrgatncyledtnhVRD 256
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHV---GGLAIL---------------VRS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 257 ALTTLKPTVMcavprfyekiyTAVWDKVEKALAHRRalfNWAICVgeqhyqaeqPSQwlrLQYALADKLV---LTKLRAL 333
Cdd:cd17630 63 LLAGAELVLL-----------ERNQALAEDLAPPGV---THVSLV---------PTQ---LQRLLDSGQGpaaLKSLRAV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 334 LggrikmmpCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKIGEENEILVRGGMV 413
Cdd:cd17630 117 L--------LGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIWVGGASL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 414 MRGYYKKPEEtaKAFTEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEgkigkdkfieqiAVIADAKKY 493
Cdd:cd17630 189 AMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADN-MIISGGENIQPEEIE------------AALAAHPAV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 494 VSALIVPCFDslEEYAKQLNIKYQDRIELIkHSDIIQMferriheLQKELPSFEQVKKFTLLPQAfsttmeEITPTLKLR 573
Cdd:cd17630 254 RDAFVVGVPD--EELGQRPVAVIVGRGPAD-PAELRAW-------LKDKLARFKLPKRIYPVPEL------PRTGGGKVD 317
|
....*...
gi 2490830388 574 RKVIMQRY 581
Cdd:cd17630 318 RRALRAWL 325
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
12-500 |
8.80e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 120.69 E-value: 8.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREQ-AQWqemSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI 90
Cdd:PRK08315 22 LDRTAARYPDREALVYRDQgLRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 91 yatNTA---KQVEYIVNDADIKILFVGDQ-------EQLDQV------CQI----ANNCPQLMKIVAMKANmDLRDLPNa 150
Cdd:PRK08315 99 ---NPAyrlSELEYALNQSGCKALIAADGfkdsdyvAMLYELapelatCEPgqlqSARLPELRRVIFLGDE-KHPGMLN- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 151 cyWEDFLD--VVPNEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHqlNAHDLALNVN---EDDVSLSfLP 225
Cdd:PRK08315 174 --FDELLAlgRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILN--NGYFIGEAMKlteEDRLCIP-VP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 226 LSHIFerAWV----AYVFHrGATNCYLEDtnhVRDALTTL------KPTVMCAVPrfyeKIYTAVwdkvekaLAH-RRAL 294
Cdd:PRK08315 249 LYHCF--GMVlgnlACVTH-GATMVYPGE---GFDPLATLaaveeeRCTALYGVP----TMFIAE-------LDHpDFAR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 295 FNwaicvgeqhyqaeqpsqwlrlqyaladklvLTKLRallGGrikMM---PCGGAKLEASIGSFfHSIGINIklGYGMTE 371
Cdd:PRK08315 312 FD------------------------------LSSLR---TG---IMagsPCPIEVMKRVIDKM-HMSEVTI--AYGMTE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 372 TtATVSCwQDKGFNP-----NSIGTLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLR 435
Cdd:PRK08315 353 T-SPVST-QTRTDDPlekrvTTVGRALPHLEVKIvdpetgetvprGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMH 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 436 TGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEgkigkdKFIEQIAVIADA-------KKY---VSALIVP 500
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKD-MIIRGGENIYPREIE------EFLYTHPKIQDVqvvgvpdEKYgeeVCAWIIL 498
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
161-491 |
9.55e-29 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 118.60 E-value: 9.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 161 PNEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANlaHQLNAHDLALN--VNEDDVSLSFLPLSHI-----FERA 233
Cdd:cd05912 62 PNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGN--HWWSAIGSALNlgLTEDDNWLCALPLFHIsglsiLMRS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 234 wVAYvfhrgATNCYLE---DTNHVRDALTTLKPTVMCAVPrfyekiytavwdkvekalahrrALFNWAICVGEQHYQAEq 310
Cdd:cd05912 140 -VIY-----GMTVYLVdkfDAEQVLHLINSGKVTIISVVP----------------------TMLQRLLEILGEGYPNN- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 311 psqwLRLqyaladklvltklrALLGGRikmmPCGGAKLEASigsffHSIGINIKLGYGMTETtatvsCWQDKGFNP---- 386
Cdd:cd05912 191 ----LRC--------------ILLGGG----PAPKPLLEQC-----KEKGIPVYQSYGMTET-----CSQIVTLSPedal 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 387 ---NSIGTLMPNAEVKI-------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKE 456
Cdd:cd05912 239 nkiGSAGKPLFPVELKIeddgqppYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSD 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 2490830388 457 LMkTSNGKYIAPQYIEGKIGKDKFIEQIAVIA--DAK 491
Cdd:cd05912 318 LI-ISGGENIYPAEIEEVLLSHPAIKEAGVVGipDDK 353
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
177-487 |
8.51e-28 |
|
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: 114.14 E-value: 8.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIF--ERAWVAYVFhRGATNCYLE--DTN 252
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFgyKAGIVACLL-TGATVVPVAvfDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 253 HVRDALTTLKPTVMCAVPRFYEKIytavwdkvekaLAHrralfnwaicvgeqhyqaeqPSQwlrlqyalaDKLVLTKLRA 332
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSL-----------LDH--------------------PGR---------KKFDLSSLRA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 333 LLggrikmmpCGGAKLEASIGSFFHS-IGI-NIKLGYGMTETTATVSCWQDKGFN--PNSIGTLMPNAEVKIGEENEILV 408
Cdd:cd17638 120 AV--------TGAATVPVELVRRMRSeLGFeTVLTAYGLTEAGVATMCRPGDDAEtvATTCGRACPGFEVRIADDGEVLV 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490830388 409 RGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:cd17638 192 RGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKD-MYIVGGFNVYPAEVEGALAEHPGVAQVAVI 269
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
176-493 |
1.05e-27 |
|
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: 114.28 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDLFTLIYTSGTTGEPKGVMLDYANL-AHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAY-VFHRGA--TNCYLEDT 251
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTcLIHGGLcvTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 NHVRDALTTLKPTVMCAVPRFYEKIYTAVWDkvekALAHRRALfNWAICVGEQHYQAEQpsqwlrlQYALADKLVltklr 331
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKS----ANATVPSL-RLIGYGGSRAIAADV-------RFIEATGLT----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 332 allggrikmmpcggakleasigsffhsigiNIKLGYGMTETTaTVSCWQ--DKGFNPNSIGTLMPNAEVKI--------- 400
Cdd:cd17635 144 ------------------------------NTAQVYGLSETG-TALCLPtdDDSIEINAVGRPYPGVDVYLaatdgiagp 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -GEENEILVRGGMVMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEgkigkdK 479
Cdd:cd17635 193 sASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDEVE------R 264
|
330
....*....|....
gi 2490830388 480 FIEQIAVIADAKKY 493
Cdd:cd17635 265 IAEGVSGVQECACY 278
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-487 |
1.31e-27 |
|
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: 114.30 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 183 YTSGTTGEPKGVMLDYANLAHqlNAHDLA--LNVNEDDVSLSFLPLSHIFER--AWVAYVFHrGATNCYLEDTNHVRDAL 258
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVN--NGYFIGerLGLTEQDRLCIPVPLFHCFGSvlGVLACLTH-GATMVFPSPSFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 259 TTL---KPTVMCAVPRFYEKIYtavwdkvekalahrralfnwaicvgeqhyqaEQPSQwlrlqyalaDKLVLTKLRallG 335
Cdd:cd05917 86 EAIekeKCTALHGVPTMFIAEL-------------------------------EHPDF---------DKFDLSSLR---T 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 336 GRIKMMPCGGAKLEASIgSFFHSIGINIklGYGMTETTATvsCWQDKGFNP-----NSIGTLMPNAEVKI---------- 400
Cdd:cd05917 123 GIMAGAPCPPELMKRVI-EVMNMKDVTI--AYGMTETSPV--STQTRTDDSiekrvNTVGRIMPHTEAKIvdpeggivpp 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIGKDK 479
Cdd:cd05917 198 vGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKD-MIIRGGENIYPREIEEFLHTHP 276
|
....*...
gi 2490830388 480 FIEQIAVI 487
Cdd:cd05917 277 KVSDVQVV 284
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
172-454 |
2.14e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 118.10 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 172 SKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFE---RAW------VAYVFHRG 242
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGltvTLWlpllegIKVVYHPD 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 243 ATncyledtnhvrDALTTLK------PTVMCAVPRFYeKIYTavwdKVEKAlahrralfnwaicvgeqhyqaeqpsqwlr 316
Cdd:PRK08633 858 PT-----------DALGIAKlvakhrATILLGTPTFL-RLYL----RNKKL----------------------------- 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 317 lqyalaDKLVLTKLRallggrikMMPCGGAKLEASIG-SFFHSIGINIKLGYGMTETTATVSC----------WQDKGFN 385
Cdd:PRK08633 893 ------HPLMFASLR--------LVVAGAEKLKPEVAdAFEEKFGIRILEGYGATETSPVASVnlpdvlaadfKRQTGSK 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 386 PNSIGTLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLR---TGDVGEMDSCGNLFIT 451
Cdd:PRK08633 959 EGSVGMPLPGVAVRIvdpetfeelppGEDGLILIGGPQVMKGYLGDPEKTAEVIKDIDGIGwyvTGDKGHLDEDGFLTIT 1038
|
...
gi 2490830388 452 DRL 454
Cdd:PRK08633 1039 DRY 1041
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
177-472 |
2.61e-27 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 116.23 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANL----AHQLNAHDLALNVNEDDVSLSFLPLSHIFE---------RAWVAYVFHRGA 243
Cdd:PLN02246 180 DVVALPYSSGTTGLPKGVMLTHKGLvtsvAQQVDGENPNLYFHSDDVILCVLPMFHIYSlnsvllcglRVGAAILIMPKF 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 244 tncyleDTNHVRDALTTLKPTVMCAVPrfyeKIYTAVwdkvekalahrralfnwaicvgeqhyqAEQPsqwlrlqyaLAD 323
Cdd:PLN02246 260 ------EIGALLELIQRHKVTIAPFVP----PIVLAI---------------------------AKSP---------VVE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 324 KLVLTKLRALLGGRIKMmpcgGAKLEASIGSFFHsigiNIKL--GYGMTETTATVS-CWqdkGF-------NPNSIGTLM 393
Cdd:PLN02246 294 KYDLSSIRMVLSGAAPL----GKELEDAFRAKLP----NAVLgqGYGMTEAGPVLAmCL---AFakepfpvKSGSCGTVV 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 394 PNAEVKI-----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTsN 462
Cdd:PLN02246 363 RNAELKIvdpetgaslprNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-K 441
|
330
....*....|
gi 2490830388 463 GKYIAPQYIE 472
Cdd:PLN02246 442 GFQVAPAELE 451
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
35-501 |
2.97e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.85 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 35 EMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVG 114
Cdd:PRK06188 37 RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 115 DQEQLDQVCQIANNCPQLMKIVAMKANMDLRDLPNACywedfldvvpneAEFE-KRLNSKQLS-DLFTLIYTSGTTGEPK 192
Cdd:PRK06188 117 PAPFVERALALLARVPSLKHVLTLGPVPDGVDLLAAA------------AKFGpAPLVAAALPpDIAGLAYTGGTTGKPK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 193 GVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIfERAWVAYVFHRGATncyledtnhvrdalttlkpTVMCavPRF 272
Cdd:PRK06188 185 GVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHA-GGAFFLPTLLRGGT-------------------VIVL--AKF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 273 YEKiytAVWDKVEKalaHRralFNWAICVgeqhyqaeqPSQWlrlqYALAD-----KLVLTKLRALLGGRIKMMPcggAK 347
Cdd:PRK06188 243 DPA---EVLRAIEE---QR---ITATFLV---------PTMI----YALLDhpdlrTRDLSSLETVYYGASPMSP---VR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 348 L-EA--SIGSFFHSIginiklgYGMTETTATVSCWQDKGFNPNSIGTL----MPNA------------EVKIGEENEILV 408
Cdd:PRK06188 298 LaEAieRFGPIFAQY-------YGQTEAPMVITYLRKRDHDPDDPKRLtscgRPTPglrvalldedgrEVAQGEVGEICV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 409 RGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:PRK06188 371 RGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKD-MIVTGGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
490
....*....|....*..
gi 2490830388 489 --DAK--KYVSALIVPC 501
Cdd:PRK06188 449 vpDEKwgEAVTAVVVLR 465
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
37-488 |
4.50e-27 |
|
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: 114.70 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 37 SWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQ 116
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV-DR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 117 EqLDQVCQIANNCPqlmkivamkanmdlrdlpnacyweDFLDVVPNEaEFekrlnskqlsDLFTLIYTSGTTGEPKGVMl 196
Cdd:cd12118 110 E-FEYEDLLAEGDP------------------------DFEWIPPAD-EW----------DPIALNYTSGTTGRPKGVV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 197 dYANLAHQLNAHDLAL--NVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLE--DTNHVRDALTTLKPTVMCAVPRF 272
Cdd:cd12118 153 -YHHRGAYLNALANILewEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRkvDAKAIYDLIEKHKVTHFCGAPTV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 273 YEKIytavwdkvekalahrralfnwaicvgeqhyqAEQPSQWLRLqyaladklvltklralLGGRIKMMpCGGAKLEASI 352
Cdd:cd12118 232 LNML-------------------------------ANAPPSDARP----------------LPHRVHVM-TAGAPPPAAV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 353 GSFFHSIGINIKLGYGMTETT--ATVSCWQDK---------------------------GFNPNSIGTLmPNAEVKIGEe 403
Cdd:cd12118 264 LAKMEELGFDVTHVYGLTETYgpATVCAWKPEwdelpteerarlkarqgvryvgleevdVLDPETMKPV-PRDGKTIGE- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 404 neILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEGKIGKDKFIEQ 483
Cdd:cd12118 342 --IVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLE 417
|
....*
gi 2490830388 484 IAVIA 488
Cdd:cd12118 418 AAVVA 422
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
21-491 |
6.76e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 114.29 E-value: 6.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:PRK03640 17 DRTAIEFEEK----KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFVGD--QEQLDQVCQIanncpqlmkivamkanmdlrdlpnacYWEDFLDVVPNEAEFEkrlNSKQLSDL 178
Cdd:PRK03640 93 WQLDDAEVKCLITDDdfEAKLIPGISV--------------------------KFAELMNGPKEEAEIQ---EEFDLDEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 179 FTLIYTSGTTGEPKGVMLDYANlaHQLNAHDLALN--VNEDDVSLSFLPLSHI-----FERAwVAYvfhrGATnCYLE-- 249
Cdd:PRK03640 144 ATIMYTSGTTGKPKGVIQTYGN--HWWSAVGSALNlgLTEDDCWLAAVPIFHIsglsiLMRS-VIY----GMR-VVLVek 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 -DTNHVRDALTTLKPTVMCAVPRFYEKIytavwdkVEKalahrralfnwaicVGEQHYqaeqPSqwlrlqyaladklvlt 328
Cdd:PRK03640 216 fDAEKINKLLQTGGVTIISVVSTMLQRL-------LER--------------LGEGTY----PS---------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 KLRA-LLGGRikmmPCGGAKLEASigsffHSIGINIKLGYGMTETTATVsCWQDKGFNPNSIGT----LMPnAEVKI--- 400
Cdd:PRK03640 255 SFRCmLLGGG----PAPKPLLEQC-----KEKGIPVYQSYGMTETASQI-VTLSPEDALTKLGSagkpLFP-CELKIekd 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 ------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEGK 474
Cdd:PRK03640 324 gvvvppFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEV 401
|
490
....*....|....*....
gi 2490830388 475 IGKDKFIEQIAVI--ADAK 491
Cdd:PRK03640 402 LLSHPGVAEAGVVgvPDDK 420
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
9-544 |
1.06e-26 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 114.59 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 9 VNRFRLQAKKWLNRTAlRFREQAQW----QEMSWQTFQQEIDRF-SYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQA 83
Cdd:PRK08751 21 LEQFRTVAEVFATSVA-KFADRPAYhsfgKTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 84 RAVAVPIYATNTAKQVEYIVNDADIKILFVGDQEQlDQVCQIANNCPqlMKIVAMKANMDLRDLPNACYWEDFLDVV--- 160
Cdd:PRK08751 100 GLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFG-TTVQQVIADTP--VKQVITTGLGDMLGFPKAALVNFVVKYVkkl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 161 ------PNEAEFEK--------RLNSKQLS--DLFTLIYTSGTTGEPKGVMLDYANL-AHQLNAHDLALNVNE----DDV 219
Cdd:PRK08751 177 vpeyriNGAIRFREalalgrkhSMPTLQIEpdDIAFLQYTGGTTGVAKGAMLTHRNLvANMQQAHQWLAGTGKleegCEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 220 SLSFLPLSHIFERAWVAYVFHR-GATNCYLEDTNHVRDALTTLKPTvmcavpRFyeKIYTAVwdkvekalahrRALFNWA 298
Cdd:PRK08751 257 VITALPLYHIFALTANGLVFMKiGGCNHLISNPRDMPGFVKELKKT------RF--TAFTGV-----------NTLFNGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 299 icvgeqhyqaeqpsqwlrLQYALADKLVLTKLRALLGGrikmmpcgGAKLEASIGSFFHSI-GINIKLGYGMTETT--AT 375
Cdd:PRK08751 318 ------------------LNTPGFDQIDFSSLKMTLGG--------GMAVQRSVAERWKQVtGLTLVEAYGLTETSpaAC 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 376 VSCWQDKGFNpNSIGTLMPNAEV----------KIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSC 445
Cdd:PRK08751 372 INPLTLKEYN-GSIGLPIPSTDAcikddagtvlAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 446 GNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVIA--DAK--KYVSALIV---PCFDSLEeyakqlnIKYQD 518
Cdd:PRK08751 451 GFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPGVLEVAAVGvpDEKsgEIVKVVIVkkdPALTAED-------VKAHA 522
|
570 580
....*....|....*....|....*.
gi 2490830388 519 RIELIKHSdiiqmfERRIHELQKELP 544
Cdd:PRK08751 523 RANLTGYK------QPRIIEFRKELP 542
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
22-591 |
2.54e-26 |
|
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: 113.30 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 22 RTALRFREQAQ-WQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI---YATNTAK 97
Cdd:cd05921 11 RTWLAEREGNGgWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 98 --QVEYIVNDADIKILFVGDQEQLDQVcqIANNCPQLMKIVAMKANMDLRDLPNacywedFLDVV--PNEAEFEKRLNSK 173
Cdd:cd05921 91 laKLKHLFELLKPGLVFAQDAAPFARA--LAAIFPLGTPLVVSRNAVAGRGAIS------FAELAatPPTAAVDAAFAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 174 QLSDLFTLIYTSGTTGEPKGVMLDYANLA--HQLNAHDLALNVNEDDVSLSFLPLSHIF-ERAWVAYVFHRGATnCYLED 250
Cdd:cd05921 163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCanQAMLEQTYPFFGEEPPVLVDWLPWNHTFgGNHNFNLVLYNGGT-LYIDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 --------TNHVRDaLTTLKPTVMCAVPRFYEKIYTAvwdkVEKALAHRRALFNwaiCVGEQHYQAEQPSQ--WLRLQyA 320
Cdd:cd05921 242 gkpmpggfEETLRN-LREISPTVYFNVPAGWEMLVAA----LEKDEALRRRFFK---RLKLMFYAGAGLSQdvWDRLQ-A 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 321 LADKLVltklrallGGRIKMMPcggakleasigsffhsiginiklGYGMTET--TATVSCW-QDKgfnPNSIGTLMPNAE 397
Cdd:cd05921 313 LAVATV--------GERIPMMA-----------------------GLGATETapTATFTHWpTER---SGLIGLPAPGTE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 398 VKI---GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEM----DSCGNLFITDRLKELMKTSNGKYIA--P 468
Cdd:cd05921 359 LKLvpsGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSvgP 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 469 QYIEGKIGKDKFIEQIAVIADAKKYVSALIVPCFDSLEEYAKqlnIKYQDRIELIKHSDIIQMFERRIHELQKEL-PSFE 547
Cdd:cd05921 439 LRARAVAACAPLVHDAVVAGEDRAEVGALVFPDLLACRRLVG---LQEASDAEVLRHAKVRAAFRDRLAALNGEAtGSSS 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2490830388 548 QVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMYNE 591
Cdd:cd05921 516 RIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
47-486 |
4.91e-26 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 112.15 E-value: 4.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 47 RFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQEQLDQVCQIA 126
Cdd:PRK06018 51 KVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DLTFVPILEKIA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 127 NNCPQLMKIVAM--KANMDLRDLPNACYWEDFLDVVPNE---AEFEKRLNSkqlsdlfTLIYTSGTTGEPKGVMLDY-AN 200
Cdd:PRK06018 130 DKLPSVERYVVLtdAAHMPQTTLKNAVAYEEWIAEADGDfawKTFDENTAA-------GMCYTSGTTGDPKGVLYSHrSN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 201 LAHQLNAHDL-ALNVNEDDVSLSFLPLSHifERAW-VAYVFHRGATNCYLE----DTNHVRDALTTLKPTVMCAVPrfye 274
Cdd:PRK06018 203 VLHALMANNGdALGTSAADTMLPVVPLFH--ANSWgIAFSAPSMGTKLVMPgaklDGASVYELLDTEKVTFTAGVP---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 275 kiytAVWdkvekalahrralfnwaicvgeqhyqaeqpsqWLRLQYALADKLVLTKLrallggriKMMPCGGAKLEASIGS 354
Cdd:PRK06018 277 ----TVW--------------------------------LMLLQYMEKEGLKLPHL--------KMVVCGGSAMPRSMIK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 355 FFHSIGINIKLGYGMTETT--ATVSCWQD----------------KGFNPNSIgtlmpnaEVKI----GEE--------N 404
Cdd:PRK06018 313 AFEDMGVEVRHAWGMTEMSplGTLAALKPpfsklpgdarldvlqkQGYPPFGV-------EMKItddaGKElpwdgktfG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 EILVRGGMVMRGYYKkpeETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNGKYIAPqyIEgkigkdkfIEQI 484
Cdd:PRK06018 386 RLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISS--ID--------LENL 451
|
..
gi 2490830388 485 AV 486
Cdd:PRK06018 452 AV 453
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
16-487 |
8.96e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 111.31 E-value: 8.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 16 AKKWLNRTALRFREQA-QWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATN 94
Cdd:PRK08008 17 ADVYGHKTALIFESSGgVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 95 TAKQVEYIVNDADIKILFVGDQ--EQLDQVCQIANNCPQLMKIvamkANMDLRDLPNACYWEDFLDVVPNEAEFEKRLNS 172
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSAQfyPMYRQIQQEDATPLRHICL----TRVALPADDGVSSFTQLKAQQPATLCYAPPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 173 kqlSDLFTLIYTSGTTGEPKGVMLDYANL--AHQLNAHDLALnvNEDDVSLSFLPLSHI-FERAWVAYVFHRGATNCYLE 249
Cdd:PRK08008 173 ---DDTAEILFTSGTTSRPKGVVITHYNLrfAGYYSAWQCAL--RDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFVLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 DtnhvrdalttlkptvmcavprfyekiYTA--VWDKVEKalahRRALFNWAICVGEQHYQAEQPSQWLRlQYALADKLVL 327
Cdd:PRK08008 248 K--------------------------YSAraFWGQVCK----YRATITECIPMMIRTLMVQPPSANDR-QHCLREVMFY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 328 tklrallggrikmMPCGGAKLEASIGSFfhsiGINIKLGYGMTETtaTVSCWQDKGFNPN---SIGTLMPNAEVKIGEEN 404
Cdd:PRK08008 297 -------------LNLSDQEKDAFEERF----GVRLLTSYGMTET--IVGIIGDRPGDKRrwpSIGRPGFCYEAEIRDDH 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 ----------EILVR---GGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYI 471
Cdd:PRK08008 358 nrplpageigEICIKgvpGKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVEL 436
|
490
....*....|....*.
gi 2490830388 472 EGKIGKDKFIEQIAVI 487
Cdd:PRK08008 437 ENIIATHPKIQDIVVV 452
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
11-448 |
1.23e-25 |
|
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: 112.64 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 11 RFRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFannMPR---WTIADFGAMQARAVA 87
Cdd:COG1020 481 LFEAQAARTPDAVAVVFGDQ----SLTYAELNARANRLAHHLRALGVGPGDLVGVC---LERsleMVVALLAVLKAGAAY 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 88 VPIYATNTAKQVEYIVNDADIKILfVGDQEQLDQVcqIANNCPQLmkivamkanmdlrdlpnacywedFLDVVPNEAEFE 167
Cdd:COG1020 554 VPLDPAYPAERLAYMLEDAGARLV-LTQSALAARL--PELGVPVL-----------------------ALDALALAAEPA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 168 KRLNSK-QLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSH------IFeRAWVAyvfh 240
Cdd:COG1020 608 TNPPVPvTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasvweIF-GALLS---- 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 241 rGATnCYLEDTNHVRDA------LTTLKPTVMCAVPRFYEKIYTAVWDkvekALAHRRalfnWAICVGEqhyqaeqpsqw 314
Cdd:COG1020 683 -GAT-LVLAPPEARRDPaalaelLARHRVTVLNLTPSLLRALLDAAPE----ALPSLR----LVLVGGE----------- 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 315 lrlqyALADKLVlTKLRALlggrikmmpCGGAKLeasigsffhsigINiklGYGMTETTATVSCWQ----DKGFNPNSIG 390
Cdd:COG1020 742 -----ALPPELV-RRWRAR---------LPGARL------------VN---LYGPTETTVDSTYYEvtppDADGGSVPIG 791
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 391 TLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFL-------RTGDVGEMDSCGNL 448
Cdd:COG1020 792 RPIANTRVYVldahlqpvpvGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfpgarlyRTGDLARWLPDGNL 866
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
176-486 |
1.68e-24 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 107.83 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDLFTLIYTSGTTGEPKGVMLDY----ANLAHQLNAHDLALNVNEDDVSLSfLPLSHIFERAWVAYVF-HRGATNcyLED 250
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHrnmlANLEQAKAAYGPLLHPGKELVVTA-LPLYHIFALTVNCLLFiELGGQN--LLI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 TNHvRDalttlkptvmcaVPRFYEKI----YTAvwdkvekaLAHRRALFNwAICVGEQHYQaeqpsqwlrlqyaladkLV 326
Cdd:PRK08974 283 TNP-RD------------IPGFVKELkkypFTA--------ITGVNTLFN-ALLNNEEFQE-----------------LD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 327 LTKLRALLGGrikmmpcgGAKLEASIGSFFHSI-GINIKLGYGMTETTATVSC--WQDKGFNpNSIGTLMPNAEVKI--- 400
Cdd:PRK08974 324 FSSLKLSVGG--------GMAVQQAVAERWVKLtGQYLLEGYGLTECSPLVSVnpYDLDYYS-GSIGLPVPSTEIKLvdd 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -------GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEG 473
Cdd:PRK08974 395 dgnevppGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIED 472
|
330
....*....|....
gi 2490830388 474 KIG-KDKFIEQIAV 486
Cdd:PRK08974 473 VVMlHPKVLEVAAV 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
176-487 |
1.77e-24 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 107.41 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDLFTLIYTSGTTGEPKGVMLDYAN-LAHQLNA---HDLALNVNEDDVSLSF---LPLSHIFERAWVAYVFHR-GATNCY 247
Cdd:PRK07059 204 DDVAFLQYTGGTTGVSKGATLLHRNiVANVLQMeawLQPAFEKKPRPDQLNFvcaLPLYHIFALTVCGLLGMRtGGRNIL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 248 LEDTnhvRDAlttlkPTVMCAVPRFYEKIYTAVwdkvekalahrRALFNwAIcvgeqhyqaeqpsqwlrLQYALADKLVL 327
Cdd:PRK07059 284 IPNP---RDI-----PGFIKELKKYQVHIFPAV-----------NTLYN-AL-----------------LNNPDFDKLDF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 328 TKLRALLGGrikmmpcGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCwqdkgfNP-------NSIGTLMPNAEVKI 400
Cdd:PRK07059 327 SKLIVANGG-------GMAVQRPVAERWLEMTGCPITEGYGLSETSPVATC------NPvdatefsGTIGLPLPSTEVSI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 ----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQY 470
Cdd:PRK07059 394 rdddgndlplGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS-GFNVYPNE 472
|
330
....*....|....*..
gi 2490830388 471 IEGKIGKDKFIEQIAVI 487
Cdd:PRK07059 473 IEEVVASHPGVLEVAAV 489
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
20-491 |
3.64e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 106.28 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 20 LNRTALRFRE-------QAQWqemSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYA 92
Cdd:PRK07470 13 LRQAARRFPDrialvwgDRSW---TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 93 TNTAKQVEYIVNDADIKiLFVGDQEQLDQVCQIANNCPQLMKIVAMKAnmdlrdlpnACYWEDFLDVVPNEAEFEKRLNS 172
Cdd:PRK07470 90 RQTPDEVAYLAEASGAR-AMICHADFPEHAAAVRAASPDLTHVVAIGG---------ARAGLDYEALVARHLGARVANAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 173 KQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAH--DLALNVNEDDVSLSFLPLSH---IFERAWVAyvfhRGATNCY 247
Cdd:PRK07470 160 VDHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHlaDLMPGTTEQDASLVVAPLSHgagIHQLCQVA----RGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 248 LE----DTNHVRDALTTLKPTVMCAVPrfyekiyTAVWDKVE--KALAHRRALFNWAICVGEQHYQAEQpsqwlrlQYAL 321
Cdd:PRK07470 236 LPserfDPAEVWALVERHRVTNLFTVP-------TILKMLVEhpAVDRYDHSSLRYVIYAGAPMYRADQ-------KRAL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 322 AdKL--VLTKLRAL--LGGRIKMMPcggakleasigSFFHSI--GINIKLGY-GMTETTATVSCWQDKGfnpnsigtlmp 394
Cdd:PRK07470 302 A-KLgkVLVQYFGLgeVTGNITVLP-----------PALHDAedGPDARIGTcGFERTGMEVQIQDDEG----------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 395 nAEVKIGEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGK 474
Cdd:PRK07470 359 -RELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASD-MYISGGSNVYPREIEEK 435
|
490
....*....|....*....
gi 2490830388 475 IGKDKFIEQIAV--IADAK 491
Cdd:PRK07470 436 LLTHPAVSEVAVlgVPDPV 454
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
37-535 |
7.42e-24 |
|
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: 104.38 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 37 SWQTFQQEIDRFSYALIAQHIDIQDKIgifANNMPRW---TIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFV 113
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVV---AFQLPNWwefAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 114 gdqeqldqvcqianncPQLMKivamkaNMDLRDLPNacywedfldvvpneaefekrlnskqlsDLFTLIYTSGTTGEPKG 193
Cdd:cd05903 80 ----------------PERFR------QFDPAAMPD---------------------------AVALLLFTSGTTGEPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 194 VMLDYANL---AHQLNAHdlaLNVNEDDVSLSFLPLSHIferawVAYVFhrGATNCYLEDTnhvrdalttlkPTVMCAVp 270
Cdd:cd05903 111 VMHSHNTLsasIRQYAER---LGLGPGDVFLVASPMAHQ-----TGFVY--GFTLPLLLGA-----------PVVLQDI- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 271 rfyekiytavWDKvekalahrralfNWAICVGEQHyqaeqpsqwlRLQYALADKLVLTKL-RALLGG-----RIKMMPCG 344
Cdd:cd05903 169 ----------WDP------------DKALALMREH----------GVTFMMGATPFLTDLlNAVEEAgeplsRLRTFVCG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 345 GAKLEASIGSFFHSIGINIKLG-YGMTET-TATVSCWQDK-GFNPNSIGTLMPNAEVKI----------GEENEILVRGG 411
Cdd:cd05903 217 GATVPRSLARRAAELLGAKVCSaYGSTECpGAVTSITPAPeDRRLYTDGRPLPGVEIKVvddtgatlapGVEGELLSRGP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 412 MVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEGKIGKDKFIEQIAVIA--D 489
Cdd:cd05903 297 SVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpD 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 490 AK--KYVSALIV------PCFDSLEEY------AKQlniKYQDRIELIKH-----SDIIQMFERR 535
Cdd:cd05903 375 ERlgERACAVVVtksgalLTFDELVAYldrqgvAKQ---YWPERLVHVDDlprtpSGKVQKFRLR 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
21-575 |
8.85e-24 |
|
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: 104.68 E-value: 8.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:cd12116 2 DATAVRDDDR----SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFVGDqeqldqvcqianncpqlmkivamkanmDLRDLPNACywedfLDVVPNEAE-----FEKRLNSKQL 175
Cdd:cd12116 78 YILEDAEPALVLTDD---------------------------ALPDRLPAG-----LPVLLLALAaaaaaPAAPRTPVSP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLS-------------FLPLSHiferawvayvfhrG 242
Cdd:cd12116 126 DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAvttyafdisllelLLPLLA-------------G 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 243 ATnCYLEDTNHVRDA------LTTLKPTVMCAVPRFYEKIYTAVWdkveKALAHRRALfnwaiCVGEQhyqaeqpsqwlr 316
Cdd:cd12116 193 AR-VVIAPRETQRDPealarlIEAHSITVMQATPATWRMLLDAGW----QGRAGLTAL-----CGGEA------------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 317 LQYALADKLVLTklrallGGRIKMMpcggakleasigsffhsiginiklgYGMTETTaTVSCWQ--DKGFNPNSIGTLMP 394
Cdd:cd12116 251 LPPDLAARLLSR------VGSLWNL-------------------------YGPTETT-IWSTAArvTAAAGPIPIGRPLA 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 395 NAE----------VKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFL-------RTGDVGEMDSCGNLFITDRLKEL 457
Cdd:cd12116 299 NTQvyvldaalrpVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgpgsrlyRTGDLVRRRADGRLEYLGRADGQ 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 458 MKTsNGKYIAPQYIEGKIGKDKFIEQIAVIA---DAKKYVSALIVPCFDSLeeyakqlnikyQDRIELIKHsdiiqmfer 534
Cdd:cd12116 379 VKI-RGHRIELGEIEAALAAHPGVAQAAVVVredGGDRRLVAYVVLKAGAA-----------PDAAALRAH--------- 437
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2490830388 535 riheLQKELPSFeqvkkftLLPQAFsTTMEEI--TPTLKLRRK 575
Cdd:cd12116 438 ----LRATLPAY-------MVPSAF-VRLDALplTANGKLDRK 468
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
149-487 |
1.19e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 105.06 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 149 NACYWEDFLDVVPNEAEfeKRLNSKQL-SDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNE--DDVSLSFLP 225
Cdd:PLN02330 158 GAVNWKELLEAADRAGD--TSDNEEILqTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMigQVVTLGLIP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 226 LSHIFerawvayvfhrGATNcyledtnhvrdalttlkptVMCAVPRFYEKIytAVWDKVEkalahRRALFNwAICVGEQH 305
Cdd:PLN02330 236 FFHIY-----------GITG-------------------ICCATLRNKGKV--VVMSRFE-----LRTFLN-ALITQEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 306 YQAEQPSQWLRL-QYALADKLVLTKLRallggrIKMMPCGGAKLEASIGSFFHSI--GINIKLGYGMTETTATVSCWQD- 381
Cdd:PLN02330 278 FAPIVPPIILNLvKNPIVEEFDLSKLK------LQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHSCITLTHGDp 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 382 -KGF---NPNSIGTLMPNAEVK-IGEEN----------EILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCG 446
Cdd:PLN02330 352 eKGHgiaKKNSVGFILPNLEVKfIDPDTgrslpkntpgELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDG 431
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2490830388 447 NLFITDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:PLN02330 432 DIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAVV 471
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
11-472 |
1.82e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 105.04 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 11 RFRLQAKKWLNRTALRF-REQAQWQE---MSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAmQARAV 86
Cdd:PRK07529 30 LLSRAAARHPDAPALSFlLDADPLDRpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EAAGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 87 AVPIYATNTAKQVEYIVNDADIKILF-VG---DQEQLDQVCQIANNCPQLMKIVAMKANmdlRDLPNACYWE-------- 154
Cdd:PRK07529 109 ANPINPLLEPEQIAELLRAAGAKVLVtLGpfpGTDIWQKVAEVLAALPELRTVVEVDLA---RYLPGPKRLAvplirrka 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 155 -----DFLDVVPNE----AEFEKRLNSKQLSDLFtliYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLP 225
Cdd:PRK07529 186 harilDFDAELARQpgdrLFSGRPIGPDDVAAYF---HTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 226 LSHIFerawVAYV-----FHRGATncyledtnhvrdalttlkptVMCAVPRFY--EKIYTAVWDKVEkalahrralfnwa 298
Cdd:PRK07529 263 LFHVN----ALLVtglapLARGAH--------------------VVLATPQGYrgPGVIANFWKIVE------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 299 icvgeqHYQAEQPSQwlrlqyaladklVLTKLRALL----GGR----IKMMPCGGAKLEASIG-SFFHSIGINIKLGYGM 369
Cdd:PRK07529 306 ------RYRINFLSG------------VPTVYAALLqvpvDGHdissLRYALCGAAPLPVEVFrRFEAATGVRIVEGYGL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 370 TETTATVSCwqdkgfNP-------NSIGTLMPNAEVKI---------------GEENEILVRGGMVMRGYYKkPEETAKA 427
Cdd:PRK07529 368 TEATCVSSV------NPpdgerriGSVGLRLPYQRVRVvilddagrylrdcavDEVGVLCIAGPNVFSGYLE-AAHNKGL 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2490830388 428 FTEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIE 472
Cdd:PRK07529 441 WLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRGGHNIDPAAIE 484
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
61-491 |
5.00e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 102.58 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 61 DKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILfVGDQeqldqvcQIANNCPQLMKIVAMKA 140
Cdd:PRK09088 48 ERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL-LGDD-------AVAAGRTDVEDLAAFIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 141 NMDlrdlpnacywedfldvvPNEAEFEKRLNSKQLSdlfTLIYTSGTTGEPKGVMLDYANLAHqlNAHDLALNVNEDDVS 220
Cdd:PRK09088 120 SAD-----------------ALEPADTPSIPPERVS---LILFTSGTSGQPKGVMLSERNLQQ--TAHNFGVLGRVDAHS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 221 lSFLPLSHIFerawvayvfhrgatncyledtnHVRDALTTLKPTVMCAVPrfyekiyTAVWDKVEKALAHRRaLFNWAIc 300
Cdd:PRK09088 178 -SFLCDAPMF----------------------HIIGLITSVRPVLAVGGS-------ILVSNGFEPKRTLGR-LGDPAL- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 301 vGEQHY-QAEQPSQWLRLQYALaDKLVLTKLRALLGGrikmmpcGGAKLEASIGSFFHSiGINIKLGYGMTETTATVSCW 379
Cdd:PRK09088 226 -GITHYfCVPQMAQAFRAQPGF-DAAALRHLTALFTG-------GAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 380 QDKGFNPN---SIGTLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCG 446
Cdd:PRK09088 296 VDCDVIRAkagAAGIPTPTVQTRVvddqgndcpaGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADG 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2490830388 447 NLFITDRLKElMKTSNGKYIAPQYIEGKIGKDKFIEQIAVI--ADAK 491
Cdd:PRK09088 376 FFWVVDRKKD-MFISGGENVYPAEIEAVLADHPGIRECAVVgmADAQ 421
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
17-591 |
6.55e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 103.20 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 17 KKWLNRtalRFREQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI---YA- 92
Cdd:PRK12582 65 RPWLAQ---REPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSl 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 93 --TNTAKqVEYIVNDADIKILFVGDQEQLDQVCQIAN-NCPQLmkIVAMKANMDLRDLPnacywedFLDVV--PNEAEFE 167
Cdd:PRK12582 142 msHDHAK-LKHLFDLVKPRVVFAQSGAPFARALAALDlLDVTV--VHVTGPGEGIASIA-------FADLAatPPTAAVA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 168 KRLNSKQLSDLFTLIYTSGTTGEPKGV-----MLdYANLAHQLNAHDLALNvNEDDVSLSFLPLSHIFE-RAWVAYVFHR 241
Cdd:PRK12582 212 AAIAAITPDTVAKYLFTSGSTGMPKAVintqrMM-CANIAMQEQLRPREPD-PPPPVSLDWMPWNHTMGgNANFNGLLWG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 242 GATnCYLED--------TNHVRdALTTLKPTVMCAVPrfyeKIYTAVWDKVEKALAHRRALFNwaicvgeqhyqaeqpsq 313
Cdd:PRK12582 290 GGT-LYIDDgkplpgmfEETIR-NLREISPTVYGNVP----AGYAMLAEAMEKDDALRRSFFK----------------- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 314 wlRLQY------ALADKLvLTKLRAL----LGGRIKMMPcggakleasigsffhsiginiklGYGMTET--TATVSCWQD 381
Cdd:PRK12582 347 --NLRLmayggaTLSDDL-YERMQALavrtTGHRIPFYT-----------------------GYGATETapTTTGTHWDT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 382 KgfNPNSIGTLMPNAEVK---IGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVG----EMDSCGNLFITDRL 454
Cdd:PRK12582 401 E--RVGLIGLPLPGVELKlapVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAArfvdPDDPEKGLIFDGRV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 455 KELMKTSNGKYIAPqyieGKIGKDKFIEQIAVIADA------KKYVSALIVPCFDSLEEYAKQLNIKYQDrieLIKHSDI 528
Cdd:PRK12582 479 AEDFKLSTGTWVSV----GTLRPDAVAACSPVIHDAvvagqdRAFIGLLAWPNPAACRQLAGDPDAAPED---VVKHPAV 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 529 IQMFERRIHELQKELP-SFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMYNE 591
Cdd:PRK12582 552 LAILREGLSAHNAEAGgSSSRIARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
181-591 |
1.12e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 102.26 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDD--VSLSFLPLSHIF-ERAWVAYVFHRGATnCYLED------- 250
Cdd:PRK08180 214 FLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFgGNHNLGIVLYNGGT-LYIDDgkptpgg 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 ---TnhVRDaLTTLKPTVMCAVPRFYEKIYTAVwdKVEKALAHR-----RALFnwaicvgeqhYQAEQPSQ--WLRLQyA 320
Cdd:PRK08180 293 fdeT--LRN-LREISPTVYFNVPKGWEMLVPAL--ERDAALRRRffsrlKLLF----------YAGAALSQdvWDRLD-R 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 321 LAdklvltklRALLGGRIKMMPcggakleasigsffhsiginiklGYGMTET--TATVSCWQDKGfnPNSIGTLMPNAEV 398
Cdd:PRK08180 357 VA--------EATCGERIRMMT-----------------------GLGMTETapSATFTTGPLSR--AGNIGLPAPGCEV 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 399 KI---GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGD----VGEMD-SCGNLFitD-RLKELMKTSNGKYIApq 469
Cdd:PRK08180 404 KLvpvGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDavrfVDPADpERGLMF--DgRIAEDFKLSSGTWVS-- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 470 yiegkIG--KDKFIEQIA-VIADA------KKYVSALIVPCFDSLEEYAKQLniKYQDRIELIKHSDIIQMFERRIHELQ 540
Cdd:PRK08180 480 -----VGplRARAVSAGApLVQDVvitghdRDEIGLLVFPNLDACRRLAGLL--ADASLAEVLAHPAVRAAFRERLARLN 552
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2490830388 541 KELP-SFEQVKKFTLLPQAFSTTMEEITPTLKLRRKVIMQRYREQIEEMYNE 591
Cdd:PRK08180 553 AQATgSSTRVARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVEALYAD 604
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
21-499 |
1.24e-22 |
|
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: 101.17 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:cd05945 6 DRPAVVEGGR----TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFV-GDqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlsDLF 179
Cdd:cd05945 82 EILDAAKPALLIAdGD-------------------------------------------------------------DNA 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 180 TLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiFERAwVAYVF----HRGATNCYLED-TNHV 254
Cdd:cd05945 101 YIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFS--FDLS-VMDLYpalaSGATLVPVPRDaTADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 255 RDALTTLKP---TVMCAVPRFYEkiytavwdkvekaLAHRRALFNwaicvgeqhyQAEQPSqwLRLQYALADKLVLTKLR 331
Cdd:cd05945 178 KQLFRFLAEhgiTVWVSTPSFAA-------------MCLLSPTFT----------PESLPS--LRHFLFCGEVLPHKTAR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 332 ALLggriKMMPcggaklEASIgsffhsigINIklgYGMTETTATVSCWQ-----DKGFNPNSIGTLMPNAEVKI------ 400
Cdd:cd05945 233 ALQ----QRFP------DARI--------YNT---YGPTEATVAVTYIEvtpevLDGYDRLPIGYAKPGAKLVIldedgr 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 ----GEENEILVRGGMVMRGYYKKPEETAKAFTED---GFLRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEG 473
Cdd:cd05945 292 pvppGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEA 370
|
490 500
....*....|....*....|....*..
gi 2490830388 474 KIGKDKFIEQIAVIADAKK-YVSALIV 499
Cdd:cd05945 371 ALRQVPGVKEAVVVPKYKGeKVTELIA 397
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
177-457 |
1.52e-22 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 101.59 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIferawVAYVFHrgatncyledtnHVRd 256
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHV-----GGLVEL------------HLR- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 257 alttlkptvmcavprfyekiytavwdkvekalahrralfnwAICVGEQHYQA------EQPSQWLRL------QYALADK 324
Cdd:cd05906 230 -----------------------------------------AVYLGCQQVHVpteeilADPLRWLDLidryrvTITWAPN 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 325 LVLTKLRALLG---------GRIKMMPCGGAKLEASIGSFFHSI----GIN---IKLGYGMTETTA----TVSCWQDKGF 384
Cdd:cd05906 269 FAFALLNDLLEeiedgtwdlSSLRYLVNAGEAVVAKTIRRLLRLlepyGLPpdaIRPAFGMTETCSgviySRSFPTYDHS 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 385 NPN---SIGTLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDScGNLFIT 451
Cdd:cd05906 349 QALefvSLGRPIPGVSMRIvddegqllpeGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTIT 427
|
....*.
gi 2490830388 452 DRLKEL 457
Cdd:cd05906 428 GRTKDT 433
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
173-472 |
4.06e-22 |
|
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: 99.87 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 173 KQLSDLFTLI-YTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAwvayVFH-----RGATNC 246
Cdd:cd05908 102 CELADELAFIqFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLI----AFHlapliAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 247 YLEDTNHVRDALTTL------KPTVMCAvPRFYEKIYTAVWdKVEKA----LAHRRALFNWAicvgeqhyqaeQPsqwlr 316
Cdd:cd05908 178 LMPTRLFIRRPILWLkkasehKATIVSS-PNFGYKYFLKTL-KPEKAndwdLSSIRMILNGA-----------EP----- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 317 LQYALADKLvLTKLRALLGGRIKMMPCGGAKlEASIGSFFHSIGINIK----------LGYGMTETTATVScwqdKGFNP 386
Cdd:cd05908 240 IDYELCHEF-LDHMSKYGLKRNAILPVYGLA-EASVGASLPKAQSPFKtitlgrrhvtHGEPEPEVDKKDS----ECLTF 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 387 NSIGTLMPNAEVKI-GEENEIL---------VRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDScGNLFITDRLKE 456
Cdd:cd05908 314 VEVGKPIDETDIRIcDEDNKILpdgyighiqIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKD 392
|
330
....*....|....*.
gi 2490830388 457 LMKTsNGKYIAPQYIE 472
Cdd:cd05908 393 IIFV-NGQNVYPHDIE 407
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
177-491 |
5.26e-22 |
|
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: 97.34 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANL---AHQLNahdLALNVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLE--DT 251
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLiaaNLQLI---HAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEkfDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 NHVRDALTTLKPTVMCAVPrfyeKIYTAVWDKVEKalahrralfnwaicvgeqhyqaeQPSQWlrlqyaladklvlTKLR 331
Cdd:cd17637 78 AEALELIEEEKVTLMGSFP----PILSNLLDAAEK-----------------------SGVDL-------------SSLR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 332 ALLGGRikmMPCGGAKLEASIGSFFHSiginiklGYGMTETT--ATVSCWQDKgfnPNSIGTLMPNAEVKI--------- 400
Cdd:cd17637 118 HVLGLD---APETIQRFEETTGATFWS-------LYGQTETSglVTLSPYRER---PGSAGRPGPLVRVRIvddndrpvp 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -GEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRL--KELMKTSnGKYIAPQYIEGKIGK 477
Cdd:cd17637 185 aGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPG-GENVYPAEVEKVILE 262
|
330
....*....|....*.
gi 2490830388 478 DKFIEQIAVI--ADAK 491
Cdd:cd17637 263 HPAIAEVCVIgvPDPK 278
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
50-500 |
5.27e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 99.56 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 50 YALIAQHIDIQDKIGIFANNMPRWTIADFGAMQAR----------------AV-------AVPIY-AT----------NT 95
Cdd:PRK07514 6 FDALRAAFADRDAPFIETPDGLRYTYGDLDAASARlanllvalgvkpgdrvAVqvekspeALALYlATlragavflplNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 96 AKQ---VEYIVNDADIKiLFVGDQEQLDQVCQIANNC--PQLMKIVAmKANMDLRDLPNACYwEDFlDVVPNEAEfekrl 170
Cdd:PRK07514 86 AYTlaeLDYFIGDAEPA-LVVCDPANFAWLSKIAAAAgaPHVETLDA-DGTGSLLEAAAAAP-DDF-ETVPRGAD----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 171 nskqlsDLFTLIYTSGTTGEPKGVMLDYANLAHqlNAhdLALN----VNEDDVSLSFLPlshiferawvayVFH-RG--- 242
Cdd:PRK07514 157 ------DLAAILYTSGTTGRSKGAMLSHGNLLS--NA--LTLVdywrFTPDDVLIHALP------------IFHtHGlfv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 243 ATNCYLedTNHVR---------DALTTLKP--TVMCAVPRFYEKIytavwdkvekaLAHRRalfnwaicvgeqhyqaeqp 311
Cdd:PRK07514 215 ATNVAL--LAGASmiflpkfdpDAVLALMPraTVMMGVPTFYTRL-----------LQEPR------------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 312 sqwlrlqyaladklvLTKLRAllgGRIKMMPCGGAKLEASI-GSFFHSIGINIKLGYGMTETTATVScwqdkgfNP---- 386
Cdd:PRK07514 263 ---------------LTREAA---AHMRLFISGSAPLLAEThREFQERTGHAILERYGMTETNMNTS-------NPydge 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 387 ---NSIGTLMPNAEVKI-----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITD 452
Cdd:PRK07514 318 rraGTVGFPLPGVSLRVtdpetgaelppGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVG 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2490830388 453 RLKELMkTSNGKYIAPQYIEGkigkdkFIEQI------AVI----ADAKKYVSALIVP 500
Cdd:PRK07514 398 RGKDLI-ISGGYNVYPKEVEG------EIDELpgvvesAVIgvphPDFGEGVTAVVVP 448
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
47-488 |
1.01e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 99.05 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 47 RFSYALIAQHIDIQDKIgifANNMPRW---TIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVGDQEQ----L 119
Cdd:PRK06087 61 RLANWLLAKGIEPGDRV---AFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKqtrpV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 120 DQVCQIANNCPQLMKIVAM-KANMDLRDLPNACYWEDF--LDVVPNEAEfekrlnskqlSDLFTLIYTSGTTGEPKGVML 196
Cdd:PRK06087 138 DLILPLQNQLPQLQQIVGVdKLAPATSSLSLSQIIADYepLTTAITTHG----------DELAAVLFTSGTEGLPKGVML 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 197 DYANLAHQLNAHDLALNVNEDDVSLSFLPLSHiferawvAYVFHRGATNCY-------LEDTNHVRDALTTL---KPT-V 265
Cdd:PRK06087 208 THNNILASERAYCARLNLTWQDVFMMPAPLGH-------ATGFLHGVTAPFligarsvLLDIFTPDACLALLeqqRCTcM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 266 MCAVPRFYEkiytavwdkvekalahrraLFNwaiCVGEQHYQaeqpsqwlrlqyaladklvLTKLRALLggrikmmpCGG 345
Cdd:PRK06087 281 LGATPFIYD-------------------LLN---LLEKQPAD-------------------LSALRFFL--------CGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 346 AKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQDK--GFNPNSIGTLMPNAEVKI----------GEENEILVRGGMV 413
Cdd:PRK06087 312 TTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDplSRFMHTDGYAAAGVEIKVvdearktlppGCEGEEASRGPNV 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 414 MRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:PRK06087 392 FMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHDACVVA 465
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
7-491 |
1.11e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 98.70 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 7 HFVNRFRLQAKKWLNRTALRFREQAqwqeMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAV 86
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRFLGNT----TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 87 AVPIYATNTAKQVEYIVNDADIKILFVGDQEQlDQVCQIANNCPQLMKIVAMKANMDLRDLPnacyWEDFLDV------- 159
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVPLLSTVVVAGGSSDDSVLG----YEDLLAEagpahap 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 160 --VPNEAEfekrlnskqlsdlfTLI-YTSGTTGEPKGVMLDYANLAHQLNAHDLALNVN-EDDVSLSFLPLSHIFERAWV 235
Cdd:PRK07786 169 vdIPNDSP--------------ALImYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGIGSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 236 AYVFHRGATNCYLE----DTNHVRDALTTLKPTVMCAVPrfyekiytAVWDkvekalahrralfnwAICvgeqhyqAEQP 311
Cdd:PRK07786 235 LPGLLLGAPTVIYPlgafDPGQLLDVLEAEKVTGIFLVP--------AQWQ---------------AVC-------AEQQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 312 SQWLRLqyaladklvltKLRALLGGrikMMPCGGAKLEASIGSFfhsIGINIKLGYGMTETTAtVSCW---QDKGFNPNS 388
Cdd:PRK07786 285 ARPRDL-----------ALRVLSWG---AAPASDTLLRQMAATF---PEAQILAAFGQTEMSP-VTCMllgEDAIRKLGS 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 389 IGTLMPNA----------EVKIGEENEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKElM 458
Cdd:PRK07786 347 VGKVIPTVaarvvdenmnDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKD-M 424
|
490 500 510
....*....|....*....|....*....|....*
gi 2490830388 459 KTSNGKYIAPQYIEGKIGKDKFIEQIAVI--ADAK 491
Cdd:PRK07786 425 IISGGENIYCAEVENVLASHPDIVEVAVIgrADEK 459
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
85-580 |
6.38e-21 |
|
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: 96.41 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 85 AVAVPIYATNTAKQVEYIVNDADIKILFVGDQEQLDQVCQIAN-NCPQLMKIVAMKAnmdlrDLPNAcyWEDFLDVVPNE 163
Cdd:cd05970 97 AIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAApECPSKPKLVWVGD-----PVPEG--WIDFRKLIKNA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 164 AEFEKR--LNSKQLSDLFTLIY-TSGTTGEPKGVMLDYA-NLAHQLNAHdLALNVNEDDVSLSflplshIFERAWVAYVF 239
Cdd:cd05970 170 SPDFERptANSYPCGEDILLVYfSSGTTGMPKMVEHDFTyPLGHIVTAK-YWQNVREGGLHLT------VADTGWGKAVW 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 240 HR------GATNCYLEDTN-----HVRDALTTLKPTVMCAVPRFYekiytavwdkvekalahrRALFNWAIcvgeQHYQa 308
Cdd:cd05970 243 GKiygqwiAGAAVFVYDYDkfdpkALLEKLSKYGVTTFCAPPTIY------------------RFLIREDL----SRYD- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 309 eqpsqwlrlqyaladklvLTKLRallggriKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETT---ATVSCWQDKgfn 385
Cdd:cd05970 300 ------------------LSSLR-------YCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTltiATFPWMEPK--- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 386 PNSIGTLMPN----------AEVKIGEENEILVRG------GMvMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLF 449
Cdd:cd05970 352 PGSMGKPAPGyeidlidregRSCEAGEEGEIVIRTskgkpvGL-FGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 450 ITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAV--IADAKK--YVSALIVpcfdsleeyakqLNIKYQDRIELIKH 525
Cdd:cd05970 430 FVGRTDDLIKSS-GYRIGPFEVESALIQHPAVLECAVtgVPDPIRgqVVKATIV------------LAKGYEPSEELKKE 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 526 sdiIQMFERRIHELQKELPSFEQVKKftlLPQAFSTtmeeitptlKLRRKVIMQR 580
Cdd:cd05970 497 ---LQDHVKKVTAPYKYPRIVEFVDE---LPKTISG---------KIRRVEIRER 536
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
11-575 |
1.07e-20 |
|
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: 95.47 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 11 RFRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI 90
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQ----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 91 YATNTAKQVEYIVNDADIKILFVgdQEQLDQvcqianncpqlmKIVAMKANMDLRDLPNACYWEDFLDVVPNEaefekrl 170
Cdd:cd17655 78 DPDYPEERIQYILEDSGADILLT--QSHLQP------------PIAFIGLIDLLDEDTIYHEESENLEPVSKS------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 171 nskqlSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiferawvayvFhrgatncyled 250
Cdd:cd17655 137 -----DDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS-----------F----------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 tnhvrDAlttlkptvmcavprFYEKIYTAVwdkvekalahrraLFNWAICV--GEQHYQAEQPSQWLRLQYALADKL--- 325
Cdd:cd17655 190 -----DA--------------SVTEIFASL-------------LSGNTLYIvrKETVLDGQALTQYIRQNRITIIDLtpa 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 326 ---VLTKLRALLGGRIKMMPCGGAKLEAS-IGSFFHSIGINIKL--GYGMTETTATVSCWQ-----DKGFNPnSIGTLMP 394
Cdd:cd17655 238 hlkLLDAADDSEGLSLKHLIVGGEALSTElAKKIIELFGTNPTItnAYGPTETTVDASIYQyepetDQQVSV-PIGKPLG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 395 NAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFL------RTGDVGEMDSCGNLFITDRLKELM 458
Cdd:cd17655 317 NTRIYIldqygrpqpvGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQV 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 459 KTsNGKYIAPQYIEGKIGKDKFIEQIAVIA----DAKKYVSALIVpcFDsleeyakqlnikyqdrieliKHSDIIQMFER 534
Cdd:cd17655 397 KI-RGYRIELGEIEARLLQHPDIKEAVVIArkdeQGQNYLCAYIV--SE--------------------KELPVAQLREF 453
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2490830388 535 riheLQKELPSFeqvkkftLLPqAFSTTMEEI--TPTLKLRRK 575
Cdd:cd17655 454 ----LARELPDY-------MIP-SYFIKLDEIplTPNGKVDRK 484
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
22-472 |
1.83e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 95.27 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 22 RTALRFREQAQWQEMSWQTFQQEIDRFSYALIA---QHIDIQ--DKIGIFANNMPRWTIADFGAMQARAVAV---PIYat 93
Cdd:PRK12492 32 RSCKKFADRPAFSNLGVTLSYAELERHSAAFAAylqQHTDLVpgDRIAVQMPNVLQYPIAVFGALRAGLIVVntnPLY-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 94 nTAKQVEYIVNDADIKILFVGD------QEQLDQV-------CQIANNCPQ----LMKIVAMKANMDLRD--LPNACywe 154
Cdd:PRK12492 110 -TAREMRHQFKDSGARALVYLNmfgklvQEVLPDTgieylieAKMGDLLPAakgwLVNTVVDKVKKMVPAyhLPQAV--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 155 DFLDVVPNEAEFEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLA----------HQLNAHDLALNVNEDDVSLSFL 224
Cdd:PRK12492 186 PFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVanmlqvraclSQLGPDGQPLMKEGQEVMIAPL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 225 PLSHIFerAWVAYVFhrgatnCYLEDTNHvrdalttlkpTVMCAVPRfyeKIYTAVwdkvekalahrRALFNWaicvgeq 304
Cdd:PRK12492 266 PLYHIY--AFTANCM------CMMVSGNH----------NVLITNPR---DIPGFI-----------KELGKW------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 305 hyqaeQPSQWLRLQYALADKLVLTKLRALLGGRIKMMPCGGAKLEASIGSFFHSI-GINIKLGYGMTETTATVSCwqdkg 383
Cdd:PRK12492 307 -----RFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLtGCTIVEGYGLTETSPVAST----- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 384 fNP-------NSIGTLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCG 446
Cdd:PRK12492 377 -NPygelarlGTVGIPVPGTALKVidddgnelplGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDG 455
|
490 500
....*....|....*....|....*.
gi 2490830388 447 NLFITDRLKELMKTSnGKYIAPQYIE 472
Cdd:PRK12492 456 FVRIVDRKKDLIIVS-GFNVYPNEIE 480
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
46-489 |
6.89e-20 |
|
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: 92.79 E-value: 6.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 46 DRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVGDQEQLDQvcqi 125
Cdd:cd17651 31 NRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGEL---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 126 anncpqlmkivamkanmDLRDLPNACyWEDFLDVVPNEAEFEKRLnskQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQL 205
Cdd:cd17651 107 -----------------AVELVAVTL-LDQPGAAAGADAEPDPAL---DADDLAYVIYTSGSTGRPKGVVMPHRSLANLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 206 NAHDLALNVNEDDVSLSFLPLSH--IFERAWVAYVFhrGATNCYLedTNHVRDALTTLkptvmcavprfyekiyTAVWD- 282
Cdd:cd17651 166 AWQARASSLGPGARTLQFAGLGFdvSVQEIFSTLCA--GATLVLP--PEEVRTDPPAL----------------AAWLDe 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 283 -KVEKALAHRRALFNWAicvgEQHYQAEQPSQWLRLQYALADKLVLTK-LRALLGGRikmmpcGGAKLeasigsFFHsig 360
Cdd:cd17651 226 qRISRVFLPTVALRALA----EHGRPLGVRLAALRYLLTGGEQLVLTEdLREFCAGL------PGLRL------HNH--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 361 iniklgYGMTETTaTVSCWQDKGFN-----PNSIGTLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETA 425
Cdd:cd17651 287 ------YGPTETH-VVTALSLPGDPaawpaPPPIGRPIDNTRVYVldaalrpvppGVPGELYIGGAGLARGYLNRPELTA 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 426 KAFTEDGFL------RTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVIAD 489
Cdd:cd17651 360 ERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALARHPGVREAVVLAR 428
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
21-472 |
7.37e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 94.46 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRF--REQAQWQEMSWQTFQQEIdRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQ 98
Cdd:PRK05691 24 DRLALRFlaDDPGEGVVLSYRDLDLRA-RTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 99 -----VEYIVNDADIKILFVGD--QEQLDQVCQI-ANNCPQLMKIvamkanmdlrdlpnacyweDFLDVVPNEAEFEKRL 170
Cdd:PRK05691 103 hhqerLLSIIADAEPRLLLTVAdlRDSLLQMEELaAANAPELLCV-------------------DTLDPALAEAWQEPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 171 nskQLSDLFTLIYTSGTTGEPKGVMLDYANLA--HQLNAHDLALNVNEDDVSLSFLPLSH-----------IFErawvay 237
Cdd:PRK05691 164 ---QPDDIAFLQYTSGSTALPKGVQVSHGNLVanEQLIRHGFGIDLNPDDVIVSWLPLYHdmgliggllqpIFS------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 238 vfhrgATNCYLedtnhvrdalttLKPTVMCAVP-RFYEkiytavwdkvekALAHRRAL------FNWAIC---VGEQHYQ 307
Cdd:PRK05691 235 -----GVPCVL------------MSPAYFLERPlRWLE------------AISEYGGTisggpdFAYRLCserVSESALE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 308 AEQPSQWlRLQYALADKLVLTKLRALLGgriKMMPCGgakLEASigSFFHSiginiklgYGMTETTATVSCWQ------- 380
Cdd:PRK05691 286 RLDLSRW-RVAYSGSEPIRQDSLERFAE---KFAACG---FDPD--SFFAS--------YGLAEATLFVSGGRrgqgipa 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 381 ----DKGFNPN-----------SIGTLMPNAEVKIGEEN-----------EILVRGGMVMRGYYKKPEETAKAFTE-DG- 432
Cdd:PRK05691 349 leldAEALARNraepgtgsvlmSCGRSQPGHAVLIVDPQslevlgdnrvgEIWASGPSIAHGYWRNPEASAKTFVEhDGr 428
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2490830388 433 -FLRTGDVGEMDScGNLFITDRLKElMKTSNGKYIAPQYIE 472
Cdd:PRK05691 429 tWLRTGDLGFLRD-GELFVTGRLKD-MLIVRGHNLYPQDIE 467
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
42-511 |
1.52e-19 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 92.05 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 42 QQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQEQLDQ 121
Cdd:cd05959 36 EAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV-SGELAPV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 122 VCQIANN-CPQLMKIVAMKANMDLRDLPnacyweDFLDVVPNEAEFEKRLNSKQLSDLFTLiYTSGTTGEPKGVMLDYAN 200
Cdd:cd05959 115 LAAALTKsEHTLVVLIVSGGAGPEAGAL------LLAELVAAEAEQLKPAATHADDPAFWL-YSSGSTGRPKGVVHLHAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 201 LAHQLN--AHDLaLNVNEDDVSLSFLPLSHiferawvAY--------VFHRGATnCYLE----DTNHVRDALTTLKPTVM 266
Cdd:cd05959 188 IYWTAElyARNV-LGIREDDVCFSAAKLFF-------AYglgnsltfPLSVGAT-TVLMperpTPAAVFKRIRRYRPTVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 267 CAVPRFYEkiytavwdkvekalahrrALFNwaicvgeqhyqAEQPSQwlrlqyaladklvltklRALLggRIKMMPCGGA 346
Cdd:cd05959 259 FGVPTLYA------------------AMLA-----------APNLPS-----------------RDLS--SLRLCVSAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 347 KLEASIGSFFHS-IGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI----------GEENEILVRGGMVMR 415
Cdd:cd05959 291 ALPAEVGERWKArFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELrdedggdvadGEPGELYVRGPSSAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 416 GYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVIA----DAK 491
Cdd:cd05959 371 MYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVESALVQHPAVLEAAVVGvedeDGL 448
|
490 500
....*....|....*....|....*....
gi 2490830388 492 KYVSALIVP---------CFDSLEEYAKQ 511
Cdd:cd05959 449 TKPKAFVVLrpgyedseaLEEELKEFVKD 477
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
176-472 |
2.83e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 89.85 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFErawvAYV-----FHRGATncyled 250
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNG----SVVtlltpLASGAH------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 tnhvrdalttlkptVMCAVPRFY--EKIYTAVWDKVEkalahrralfnwaicvgeqHYQAEQPSQwlrlqyaladklVLT 328
Cdd:cd05944 72 --------------VVLAGPAGYrnPGLFDNFWKLVE-------------------RYRITSLST------------VPT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 KLRALLG-------GRIKMMPCGGAKLEASIGSFFH-SIGINIKLGYGMTETTATVSC-WQDKGFNPNSIGTLMPNAEVK 399
Cdd:cd05944 107 VYAALLQvpvnadiSSLRFAMSGAAPLPVELRARFEdATGLPVVEGYGLTEATCLVAVnPPDGPKRPGSVGLRLPYARVR 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 400 I---------------GEENEILVRGGMVMRGYYKKpEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGK 464
Cdd:cd05944 187 IkvldgvgrllrdcapDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGH 264
|
....*...
gi 2490830388 465 YIAPQYIE 472
Cdd:cd05944 265 NIDPALIE 272
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
177-488 |
3.72e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.06 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANLAHQLNAH-----DLALNVNEDDVSLSFLPLSHIFERA-WVAYVFHRGATNCYLE- 249
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeaSQYEYPGSDNVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRr 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 -DTNHVRDALTTLKPTVMCAVPrfyekiytavwdKVEKALAHRRAlfnwAICvgeqhyqaeqpsqwlrlqyaladklvlt 328
Cdd:PLN02574 279 fDASDMVKVIDRFKVTHFPVVP------------PILMALTKKAK----GVC---------------------------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 klrALLGGRIKMMPCGGAKL-EASIGSFFHSIG-INIKLGYGMTETTATVScwqdKGFNP------NSIGTLMPNAEVKI 400
Cdd:PLN02574 315 ---GEVLKSLKQVSCGAAPLsGKFIQDFVQTLPhVDFIQGYGMTESTAVGT----RGFNTeklskySSVGLLAPNMQAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQ 469
Cdd:PLN02574 388 vdwstgcllppGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPA 466
|
330
....*....|....*....
gi 2490830388 470 YIEGKIGKDKFIEQIAVIA 488
Cdd:PLN02574 467 DLEAVLISHPEIIDAAVTA 485
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
367-500 |
1.15e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 89.56 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 367 YGMTETTATVSC----WQDKGFNPN-SIGTLMPNAEVKI------------GEENEILVRGGMVMRGYYKKPEETAKAFT 429
Cdd:PRK05852 327 FGMTEATHQVTTtqieGIGQTENPVvSTGLVGRSTGAQIrivgsdglplpaGAVGEVWLRGTTVVRGYLGDPTITAANFT 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 430 eDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVIADAKKY----VSALIVP 500
Cdd:PRK05852 407 -DGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLygeaVAAVIVP 479
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
119-577 |
5.33e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.55 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 119 LDQVCQ------IANNCPQLMKIVAMkanmdlrDLPNACYWEDFLDVVPNEAEFEKRLNSKQL-----SDLFTLI-YTSG 186
Cdd:PLN02860 110 TDETCSswyeelQNDRLPSLMWQVFL-------ESPSSSVFIFLNSFLTTEMLKQRALGTTELdyawaPDDAVLIcFTSG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 187 TTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLE--DTNHVRDALTTLKPT 264
Cdd:PLN02860 183 TTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPkfDAKAALQAIKQHNVT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 265 VMCAVPRFYEKIytavwdkvekaLAHRRALFNWAicvgeqhyqaEQPSqwlrlqyaladklVLTKLRA-------LLGGR 337
Cdd:PLN02860 263 SMITVPAMMADL-----------ISLTRKSMTWK----------VFPS-------------VRKILNGggslssrLLPDA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 338 IKMMPCggakleASIGSffhsiginiklGYGMTETTATVS--------------CWQDKGFNPNS---------IGTLMP 394
Cdd:PLN02860 309 KKLFPN------AKLFS-----------AYGMTEACSSLTfmtlhdptlespkqTLQTVNQTKSSsvhqpqgvcVGKPAP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 395 NAEVKIG-----EENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQ 469
Cdd:PLN02860 372 HVELKIGldessRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTG-GENVYPE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 470 YIEGKIGKDKFIEQIAVIADAKKYVSALIVPCFdSLEEYAKQLNIKYQDRieliKHSDIIQMFERRIHELQKELPSFEQV 549
Cdd:PLN02860 451 EVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV-RLRDGWIWSDNEKENA----KKNLTLSSETLRHHCREKNLSRFKIP 525
|
490 500
....*....|....*....|....*...
gi 2490830388 550 KKFTLLPQAFSTtmeeiTPTLKLRRKVI 577
Cdd:PLN02860 526 KLFVQWRKPFPL-----TTTGKIRRDEV 548
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
43-459 |
9.31e-18 |
|
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: 85.82 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 43 QEIDRFSYAL---IAQHIDIQ-DKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILfvgdqeq 118
Cdd:cd17653 26 GELDAASNALanrLLQLGVVPgDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 119 ldqvcqIANNCPQlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlsDLFTLIYTSGTTGEPKGVMLDY 198
Cdd:cd17653 99 ------LTTDSPD---------------------------------------------DLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 199 ANLAHQLNAHDLALNVNEDDVSLSFLPLShiFErAWVAYVFH---RGATNCYLEDTNHVRDALTTLkpTVMCAVPRFYEK 275
Cdd:cd17653 128 RGVLNYVSQPPARLDVGPGSRVAQVLSIA--FD-ACIGEIFStlcNGGTLVLADPSDPFAHVARTV--DALMSTPSILST 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 276 IYTAVWDKVEKalahrralfnwaICVGeqhyqAEQPSQWLrlqyaladklvltkLRALLGGRikmmpcggakleasigSF 355
Cdd:cd17653 203 LSPQDFPNLKT------------IFLG-----GEAVPPSL--------------LDRWSPGR----------------RL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 356 FHsiginiklGYGMTETTATVSCWQDKGFNPNSIGTLMPNA----------EVKIGEENEILVRGGMVMRGYYKKPEETA 425
Cdd:cd17653 236 YN--------AYGPTECTISSTMTELLPGQPVTIGKPIPNStcyildadlqPVPEGVVGEICISGVQVARGYLGNPALTA 307
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2490830388 426 KAFTEDGF------LRTGDVGEMDSCGNLFITDRLKELMK 459
Cdd:cd17653 308 SKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVK 347
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
176-488 |
1.48e-17 |
|
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: 85.47 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDLFTLIYTSGTTGEPKGVMLDY-ANLAHQLNAHDlALNVNEDDVSLSflplshIFERAWVAYVFHR-------GATN-- 245
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHsYPLGHIPTAAY-WLGLRPDDIHWN------IADPGWAKGAWSSffgpwllGATVfv 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 246 CYLE--DTNHVRDALTTLKPTVMCAVPrfyekiytAVWDKVEKALAHRRALfnwaicvgeqhyqaeqpsqwLRLQYALad 323
Cdd:cd05972 154 YEGPrfDAERILELLERYGVTSFCGPP--------TAYRMLIKQDLSSYKF--------------------SHLRLVV-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 324 klvltklrallggrikmmpCGGAKL-EASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI-- 400
Cdd:cd05972 204 -------------------SAGEPLnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIid 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 --------GEENEILVRGGMV--MRGYYKKPEETAKAFTEDgFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQY 470
Cdd:cd05972 265 ddgrelppGEEGDIAIKLPPPglFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFE 342
|
330
....*....|....*...
gi 2490830388 471 IEGKIGKDKFIEQIAVIA 488
Cdd:cd05972 343 VESALLEHPAVAEAAVVG 360
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
11-448 |
1.81e-17 |
|
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: 85.33 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 11 RFRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI 90
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDR----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 91 YATNTAKQVEYIVNDADIKILfVGDQEQLDQVcqianncPQLMKIVAMKANMDLRDLPNAcywedfldVVPNEAEfekrl 170
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVL-LTDRSLAGRA-------GGLEVAVVIDEALDAGPAGNP--------AVPVSPD----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 171 nskqlsDLFTLIYTSGTTGEPKGVMLDYANLAhqlnahDLALNVN-----EDDVSLSFLPLShiFERA----WVAYVFhr 241
Cdd:cd12117 137 ------DLAYVMYTSGSTGRPKGVAVTHRGVV------RLVKNTNyvtlgPDDRVLQTSPLA--FDAStfeiWGALLN-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 242 GATnCYLEDTNHVRD------ALTTLKPTVMCAvprfyekiyTAvwdkvekalahrrALFNwaicvgeqhyqaeqpsqwl 315
Cdd:cd12117 201 GAR-LVLAPKGTLLDpdalgaLIAEEGVTVLWL---------TA-------------ALFN------------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 316 rlQYALADKLVLTKLRALL-GG--------RIKMMPCGGAKLeasigsffhsigINiklGYGMTETTaTVSCW---QDKG 383
Cdd:cd12117 239 --QLADEDPECFAGLRELLtGGevvspphvRRVLAACPGLRL------------VN---GYGPTENT-TFTTShvvTELD 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 384 FNPNS--IGTLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFL------RTGDVGEMDSC 445
Cdd:cd12117 301 EVAGSipIGRPIANTRVYVldedgrpvppGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPD 380
|
...
gi 2490830388 446 GNL 448
Cdd:cd12117 381 GRL 383
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
12-500 |
2.86e-17 |
|
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: 84.53 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREQAqwqeMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQS----LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILFvgdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrln 171
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILL----------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 172 sKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiFErAWVAYVFhrgaTNCYLEDT 251
Cdd:cd17645 101 -TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFS--FD-ASAWEIF----PHLTAGAA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 NHVRDALTTLKptvMCAVPRFYEKiytavwdkvekalaHRRALFNWAICVGEQHYQAEQPSqwlrlqyaladklvltkLR 331
Cdd:cd17645 173 LHVVPSERRLD---LDALNDYFNQ--------------EGITISFLPTGAAEQFMQLDNQS-----------------LR 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 332 ALLggrikmmpCGGAKLEAsigsfFHSIGINIKLGYGMTETTATVSCWQ-DKGFNPNSIGTLMPNAEVKI---------- 400
Cdd:cd17645 219 VLL--------TGGDKLKK-----IERKGYKLVNNYGPTENTVVATSFEiDKPYANIPIGKPIDNTRVYIldealqlqpi 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 GEENEILVRGGMVMRGYYKKPEETAKAFTEDGFL------RTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGK 474
Cdd:cd17645 286 GVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPF 364
|
490 500 510
....*....|....*....|....*....|
gi 2490830388 475 IGKDKFIEQIAVIA----DAKKYVSALIVP 500
Cdd:cd17645 365 LMNHPLIELAAVLAkedaDGRKYLVAYVTA 394
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
37-491 |
3.70e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 84.61 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 37 SWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVavpIYATNT---AKQVEYIVNDADIKILFV 113
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAV---LNTLNTrldAASIAFMLRHGEAKVLIV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 114 gDQEQLDQVCQIANNCPQLMKIV---AMKANMDLRDLPNACYwEDFLDvvPNEAEFEKRLNSKQLsDLFTLIYTSGTTGE 190
Cdd:PRK08162 122 -DTEFAEVAREALALLPGPKPLVidvDDPEYPGGRFIGALDY-EAFLA--SGDPDFAWTLPADEW-DAIALNYTSGTTGN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 191 PKGVMldYANLAHQLNA--HDLALNVNEDDVSLSFLPLSHI----FerAWVayVFHRGATNCYLE--DTNHVRDALTTLK 262
Cdd:PRK08162 197 PKGVV--YHHRGAYLNAlsNILAWGMPKHPVYLWTLPMFHCngwcF--PWT--VAARAGTNVCLRkvDPKLIFDLIREHG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 263 PTVMCAVPrfyekIytavwdkVEKALAHrralfnwaicvgeqhyqaeQPSQWlrlqyaladklvltklRALLGGRIKMMP 342
Cdd:PRK08162 271 VTHYCGAP-----I-------VLSALIN-------------------APAEW----------------RAGIDHPVHAMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 343 CGGAKLEASIGSFfHSIGINIKLGYGMTET--TATVSCWQD-------------KG--------------FNPNSiGTLM 393
Cdd:PRK08162 304 AGAAPPAAVIAKM-EEIGFDLTHVYGLTETygPATVCAWQPewdalplderaqlKArqgvryplqegvtvLDPDT-MQPV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 394 PNAEVKIGEeneILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEG 473
Cdd:PRK08162 382 PADGETIGE---IMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVED 456
|
490 500
....*....|....*....|
gi 2490830388 474 KIGKDKFIEQIAVIA--DAK 491
Cdd:PRK08162 457 VLYRHPAVLVAAVVAkpDPK 476
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
51-472 |
9.31e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 83.60 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 51 ALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQEQLDQVCQIANNCP 130
Cdd:PRK07008 55 ALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLF-DLTFLPLVDALAPQCP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 131 QLMKIVAM--KANMDLRDLPNACYwEDFLDVVPNEAEFeKRLNSKQLSdlfTLIYTSGTTGEPKGVMldYANLAHQLNAH 208
Cdd:PRK07008 134 NVKGWVAMtdAAHLPAGSTPLLCY-ETLVGAQDGDYDW-PRFDENQAS---SLCYTSGTTGNPKGAL--YSHRSTVLHAY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 209 DLAL----NVNEDDVSLSFLPLSHIfeRAW-VAYVFhrgatncyledtnhvrdALTTLKptVMCAVPRFYEKiytAVWDK 283
Cdd:PRK07008 207 GAALpdamGLSARDAVLPVVPMFHV--NAWgLPYSA-----------------PLTGAK--LVLPGPDLDGK---SLYEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 284 VEkalahrralfnwaicvGEQ-HYQAEQPSQWLR-LQYALADKLVLTKLRALLGGrikmmpcGGAKLEASIGSFFHSIGI 361
Cdd:PRK07008 263 IE----------------AERvTFSAGVPTVWLGlLNHMREAGLRFSTLRRTVIG-------GSACPPAMIRTFEDEYGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 362 NIKLGYGMTE-----TTATVScWQDKGFNPNSI-------GTLMPNAEVKI----GEE--------NEILVRGGMVMRGY 417
Cdd:PRK07008 320 EVIHAWGMTEmsplgTLCKLK-WKHSQLPLDEQrkllekqGRVIYGVDMKIvgddGRElpwdgkafGDLQVRGPWVIDRY 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 418 YKKPEETakafTEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNGKYIAPQYIE 472
Cdd:PRK07008 399 FRGDASP----LVDGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
182-453 |
1.61e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 82.35 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 182 IYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIferawvayvfH-----------RGATNCYL-- 248
Cdd:PRK07787 134 VYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHV----------HglvlgvlgplrIGNRFVHTgr 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 249 EDTNHVRDALTTlKPTVMCAVPrfyekiytAVWDKVEKALAHRRALfnwaicvgeqhyqaeQPSQWLRLQYALADKLVLT 328
Cdd:PRK07787 204 PTPEAYAQALSE-GGTLYFGVP--------TVWSRIAADPEAARAL---------------RGARLLVSGSAALPVPVFD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 KLRALLGGRIkmmpcggakLEAsigsffhsiginiklgYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKIGEEN---- 404
Cdd:PRK07787 260 RLAALTGHRP---------VER----------------YGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDggpv 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2490830388 405 --------EILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDR 453
Cdd:PRK07787 315 phdgetvgELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGR 371
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
13-562 |
2.49e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 82.11 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 13 RLQAKKWLNRTALRFREQaqwqemsWQTFQQEIDRFS---YALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVP 89
Cdd:PRK06155 28 ARQAERYPDRPLLVFGGT-------RWTYAEAARAAAaaaHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 90 IyatNTA---KQVEYIVNDADIKiLFVGDQEQLDQVcqianncpqlmkivamkANMDLRDLPNACYWedFLDVVPnEAEF 166
Cdd:PRK06155 101 I---NTAlrgPQLEHILRNSGAR-LLVVEAALLAAL-----------------EAADPGDLPLPAVW--LLDAPA-SVSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 167 EKRLNSKQL--------------SDLFTLIYTSGTTGEPKGVMLDYA-------NLAHQLNahdlalnVNEDDVSLSFLP 225
Cdd:PRK06155 157 PAGWSTAPLppldapapaaavqpGDTAAILYTSGTTGPSKGVCCPHAqfywwgrNSAEDLE-------IGADDVLYTTLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 226 LshiferawvayvFHRGATNCYLEdtnhvrdALttLKPTVMCAVPRFYEKIYtavWDkvekALAHRRALFNWAICVGEQH 305
Cdd:PRK06155 230 L------------FHTNALNAFFQ-------AL--LAGATYVLEPRFSASGF---WP----AVRRHGATVTYLLGAMVSI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 306 YQAEQPSQwlrlqyalADKLvlTKLRALLGgrikmmPCGGAKLEASigsFFHSIGINIKLGYGMTETTATVSC-WQDKgf 384
Cdd:PRK06155 282 LLSQPARE--------SDRA--HRVRVALG------PGVPAALHAA---FRERFGVDLLDGYGSTETNFVIAVtHGSQ-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 385 NPNSIGTLMPNAEVKIGEEN----------EILVRG---GMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFIT 451
Cdd:PRK06155 341 RPGSMGRLAPGFEARVVDEHdqelpdgepgELLLRAdepFAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 452 DRLKELMKtSNGKYIAPQYIEGKIGKDKFIEQIAVIAD----AKKYVSALIVPcfdsleEYAKQLnikyqDRIELIKHSD 527
Cdd:PRK06155 420 DRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAVFPVpselGEDEVMAAVVL------RDGTAL-----EPVALVRHCE 487
|
570 580 590
....*....|....*....|....*....|....*....
gi 2490830388 528 -IIQMFE-RRIHELQKELPSFE--QVKKFTLLPQAFSTT 562
Cdd:PRK06155 488 pRLAYFAvPRYVEFVAALPKTEngKVQKFVLREQGVTAD 526
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
21-195 |
2.93e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 81.86 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:PRK07798 18 DRVALVCGDR----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILfVGDQEQLDQVCQIANNCPQLMKIVAMKANMDLRDLPNACYWEDFLDVVPNEAEFEKRlnskqlS--DL 178
Cdd:PRK07798 94 YLLDDSDAVAL-VYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERDFGER------SpdDL 166
|
170
....*....|....*..
gi 2490830388 179 FtLIYTSGTTGEPKGVM 195
Cdd:PRK07798 167 Y-LLYTGGTTGMPKGVM 182
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
21-488 |
3.21e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.99 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:PLN03102 29 NRTSIIYGKT----RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFVgDQEQLDQVCQIanncpqLMKIVAMKANMDLRDlpnacywedfldVVPNEAEFEKRLNSKQLS---- 176
Cdd:PLN03102 105 AILRHAKPKILFV-DRSFEPLAREV------LHLLSSEDSNLNLPV------------IFIHEIDFPKRPSSEELDyecl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 ---------------------DLFTLIYTSGTTGEPKGVMLDyanlahqlnahdlalnvneddvslsflplshiferawv 235
Cdd:PLN03102 166 iqrgeptpslvarmfriqdehDPISLNYTSGTTADPKGVVIS-------------------------------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 236 ayvfHRGAtncYLEDTNHVRDALTTLKPTVMCAVPRFYEKIYTAVWdkvekALAHRRALfnwAICVgeQHYQAEQPSQWL 315
Cdd:PLN03102 208 ----HRGA---YLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTW-----GTAARGGT---SVCM--RHVTAPEIYKNI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 316 RLQYALADKLVLTKLRALL-GGRIKMMP--------CGGAKLEASIGSFFHSIGINIKLGYGMTETTATV-SC-WQD--- 381
Cdd:PLN03102 271 EMHNVTHMCCVPTVFNILLkGNSLDLSPrsgpvhvlTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVlFCeWQDewn 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 382 ----------KGFNPNSIGTLMpNAEVKIGEE-----------NEILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVG 440
Cdd:PLN03102 351 rlpenqqmelKARQGVSILGLA-DVDVKNKETqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVG 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2490830388 441 EMDSCGNLFITDRLKELMkTSNGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:PLN03102 429 VIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYPKVLETAVVA 475
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
23-500 |
1.71e-15 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 79.71 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 23 TALRfREQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYI 102
Cdd:PRK13295 44 TAVR-LGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 103 VNDADIKILFVG------DQEQLdqVCQIANNCPQLMKIVAMKAnmdlrDLPNAcyWEDFLdvvpNEAEFEKRLNSKQLS 176
Cdd:PRK13295 123 LKHAESKVLVVPktfrgfDHAAM--ARRLRPELPALRHVVVVGG-----DGADS--FEALL----ITPAWEQEPDAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 --------DLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFErawvayvFHRGAtncyl 248
Cdd:PRK13295 190 arlrpgpdDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTG-------FMYGL----- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 249 edtnhvrdalttLKPTVMCAvprfyEKIYTAVWDKVEKALAHRRALFNWAIcvgeqhyqAEQPsqwlrlqyALADKLVLT 328
Cdd:PRK13295 258 ------------MMPVMLGA-----TAVLQDIWDPARAAELIRTEGVTFTM--------ASTP--------FLTDLTRAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 KLRALLGGRIKMMPCGGAKLE-ASIGSFFHSIGINIKLGYGMTETTA-TVSCWQD---KGFNpnSIGTLMPNAEVKI--- 400
Cdd:PRK13295 305 KESGRPVSSLRTFLCAGAPIPgALVERARAALGAKIVSAWGMTENGAvTLTKLDDpdeRAST--TDGCPLPGVEVRVvda 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -------GEENEILVRGGMVMRGYYKKPEETAKAFteDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEG 473
Cdd:PRK13295 383 dgaplpaGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
490 500 510
....*....|....*....|....*....|.
gi 2490830388 474 KIGKDKFIEQIAVIA--DAK--KYVSALIVP 500
Cdd:PRK13295 460 LLYRHPAIAQVAIVAypDERlgERACAFVVP 490
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
36-491 |
2.36e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 79.02 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 36 MSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAmqARaVAVPIYATNT---AKQVEYIVNDADIKILF 112
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC--AR-LGATVIAVNTryrSHEVAHILGRGRARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 113 VGDQ-------EQLDQVCQIANncPQLMKIVAMKANMDLRDLPNACYWEDFLDVVPNEAEFEKRLNSKQLSDLFTLIYTS 185
Cdd:PRK06164 113 VWPGfkgidfaAILAAVPPDAL--PPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTTS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 186 GTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLE--DTNHVRDALTTLKP 263
Cdd:PRK06164 191 GTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPvfDAARTARALRRHRV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 264 TVMCAVPRFYEKIYtavwdkvekALAHRRALFNWAICVGeqhYQAEQPSQWLRLQYALADKLVLTKLrallggrikmmpc 343
Cdd:PRK06164 271 THTFGNDEMLRRIL---------DTAGERADFPSARLFG---FASFAPALGELAALARARGVPLTGL------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 344 ggakleasigsffhsiginiklgYGMTETTATVSCWQ---DKGFNPNSIGTLM-PNAEVKI-----------GEENEILV 408
Cdd:PRK06164 326 -----------------------YGSSEVQALVALQPatdPVSVRIEGGGRPAsPEARVRArdpqdgallpdGESGEIEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 409 RGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEgkigkdKFIEQIAVIA 488
Cdd:PRK06164 383 RAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIE------HALEALPGVA 455
|
...
gi 2490830388 489 DAK 491
Cdd:PRK06164 456 AAQ 458
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
36-472 |
2.69e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 78.59 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 36 MSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILfVGd 115
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL-IA- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 116 qeQLDQVCQIANNCPQLMKIV----------AMKANMDLRDLP-NACYWEDFLdvvpneAEFEKrLNSKQLSDLFTLIYT 184
Cdd:PRK12406 90 --HADLLHGLASALPAGVTVLsvptppeiaaAYRISPALLTPPaGAIDWEGWL------AQQEP-YDGPPVPQPQSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 185 SGTTGEPKGVMLDYANLAHQLNAHD---LALNVNEDDVSLSFLPLSHiferawvayvfhrGATNCYledtnhvrdALTTL 261
Cdd:PRK12406 161 SGTTGHPKGVRRAAPTPEQAAAAEQmraLIYGLKPGIRALLTGPLYH-------------SAPNAY---------GLRAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 262 K-PTVMCAVPRFYEKiytAVWDKVEKalaHRralfnwaicVGEQHYQAEQPSQWLRLQYALADKLVLTKLRALLGGrikM 340
Cdd:PRK12406 219 RlGGVLVLQPRFDPE---ELLQLIER---HR---------ITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHA---A 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 341 MPCGGAKLEASIGSFfhsiGINIKLGYGMTETTATVSCWQDKGFN-PNSIGTLMPNAEVKI----------GEENEILVR 409
Cdd:PRK12406 281 APCPADVKRAMIEWW----GPVIYEYYGSTESGAVTFATSEDALShPGTVGKAAPGAELRFvdedgrplpqGEIGEIYSR 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 410 -GGMVMRGYYKKPEETAKAfTEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIE 472
Cdd:PRK12406 357 iAGNPDFTYHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRD-MVISGGVNIYPAEIE 418
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-512 |
3.00e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.00 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:PRK12316 3063 FEEQVERTPDAVALAFGEQ----RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILFVGDQEQLDQVCQIANNCPQLMKIVAMKANMDLRDLPNacywedfldvvpneaefekrln 171
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPE---------------------- 3196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 172 skqlsDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiferawvayvFHRGATNCYLEDT 251
Cdd:PRK12316 3197 -----NLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS-----------FDVFVEELFWPLM 3260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 NHVRDALTTlkptvmcavprfyekiyTAVWDKVEKA--LAHRRALfnwaicvgeqhyqAEQPSQWLRLQYALADKlvltk 329
Cdd:PRK12316 3261 SGARVVLAG-----------------PEDWRDPALLveLINSEGV-------------DVLHAYPSMLQAFLEEE----- 3305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 330 lRALLGGRIKMMPCGGAKLEASIGSFFHSIGINIKLgYGMTETTATVSCWQ--DKGFNPNSIGTLMPNAE---------- 397
Cdd:PRK12316 3306 -DAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNL-YGPTEATITVTHWQcvEEGKDAVPIGRPIANRAcyildgslep 3383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 398 VKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGF------LRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYI 471
Cdd:PRK12316 3384 VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEI 3462
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2490830388 472 EGKIGKDKFIEQIAVIADAKKYVSALIVPCF---DSLEEYAKQL 512
Cdd:PRK12316 3463 EARLLEHPWVREAVVLAVDGRQLVAYVVPEDeagDLREALKAHL 3506
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
34-488 |
4.77e-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: 77.50 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFV 113
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 114 GDQEqldqvcqianncpqlmkivamkanmdlrdlpnACYWedfldvvpneaefekrlnskqlsdlftlIYTSGTTGEPKG 193
Cdd:cd05919 89 SADD--------------------------------IAYL----------------------------LYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 194 VMLDYAN--LAHQLNAHDLaLNVNEDDVSLSflpLSHIFeRAW-----VAYVFHRGATnCYLEDTNHVRDA----LTTLK 262
Cdd:cd05919 109 VMHAHRDplLFADAMAREA-LGLTPGDRVFS---SAKMF-FGYglgnsLWFPLAVGAS-AVLNPGWPTAERvlatLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 263 PTVMCAVPRFYekiytavwdkvekalahRRALfnwAICVGEQHyqaeqpsqwlrlqyALADklvltklrallggrIKMMP 342
Cdd:cd05919 183 PTVLYGVPTFY-----------------ANLL---DSCAGSPD--------------ALRS--------------LRLCV 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 343 CGGAKLEASIGSFF-HSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI----------GEENEILVRGG 411
Cdd:cd05919 215 SAGEALPRGLGERWmEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLvdeeghtippGEEGDLLVRGP 294
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490830388 412 MVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:cd05919 295 SAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVVA 369
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
397-525 |
5.11e-15 |
|
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: 77.75 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 397 EVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEGKIG 476
Cdd:cd05920 329 PVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVENLLL 407
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2490830388 477 KDKFIEQIAVIADAKKY----VSALIV-----PCFDSLEEYAKQLNI---KYQDRIELIKH 525
Cdd:cd05920 408 RHPAVHDAAVVAMPDELlgerSCAFVVlrdppPSAAQLRRFLRERGLaayKLPDRIEFVDS 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-439 |
5.81e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.85 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 11 RFRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI 90
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEE----KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPL 4631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 91 YATNTAKQVEYIVNDADIKILFVgdQEQLDQVCQIAnncpqlmkivamkANMDLRDLPNACYWEDFLDVVPneaefEKRL 170
Cdd:PRK12316 4632 DPEYPRERLAYMMEDSGAALLLT--QSHLLQRLPIP-------------DGLASLALDRDEDWEGFPAHDP-----AVRL 4691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 171 NSKQLSdlfTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLS-HIFERAWVaYVFHRGATNcyle 249
Cdd:PRK12316 4692 HPDNLA---YVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSfDGSHEGLY-HPLINGASV---- 4763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 dtnHVRDAlttlkptvmcavprfyekiytAVWDKVekalAHRRAlfnwaicVGEQHYQAEQ--PSQWLRL-QYALADKLV 326
Cdd:PRK12316 4764 ---VIRDD---------------------SLWDPE----RLYAE-------IHEHRVTVLVfpPVYLQQLaEHAERDGEP 4808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 327 LTKLRALLGGRikmmPCGGAKLEASIGSFFHSIGINiklGYGMTETTATVSCWQDKGFNPNS-----IGTLMPN------ 395
Cdd:PRK12316 4809 PSLRVYCFGGE----AVAQASYDLAWRALKPVYLFN---GYGPTETTVTVLLWKARDGDACGaaympIGTPLGNrsgyvl 4881
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 396 ----AEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGDV 439
Cdd:PRK12316 4882 dgqlNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDL 4936
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
182-488 |
1.24e-14 |
|
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: 76.19 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 182 IYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDV-----SLSF--------LPLSHIFERAWVAYVFHRGATNCYl 248
Cdd:cd17643 99 IYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVwtlfhSYAFdfsvweiwGALLHGGRLVVVPYEVARSPEDFA- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 249 edtNHVRDAlttlKPTVMCAVPrfyekiyTAVwdkvekalahrRALFNWAICVGEQHyqaeqpsqwLRLQYaladkLVLt 328
Cdd:cd17643 178 ---RLLRDE----GVTVLNQTP-------SAF-----------YQLVEAADRDGRDP---------LALRY-----VIF- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 klrallggrikmmpcGGAKLE-ASIGSFFHSIG------INiklGYGMTETTATVScW-----QD-KGFNPNSIGTLMPN 395
Cdd:cd17643 218 ---------------GGEALEaAMLRPWAGRFGldrpqlVN---MYGITETTVHVT-FrpldaADlPAAAASPIGRPLPG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 396 ----------AEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGDVGEMDSCGNLFITDRLKELM 458
Cdd:cd17643 279 lrvyvldadgRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQV 358
|
330 340 350
....*....|....*....|....*....|
gi 2490830388 459 KTsNGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:cd17643 359 KI-RGFRIELGEIEAALATHPSVRDAAVIV 387
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-438 |
1.38e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.51 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREQAqwqeMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQV----LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLD 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILfVGDQEQLDQvcqianncpqlmkivaMKANMDLRDLPNAcyweDFLDVVPNEAEF--EKR 169
Cdd:PRK12467 594 PEYPQDRLAYMLDDSGVRLL-LTQSHLLAQ----------------LPVPAGLRSLCLD----EPADLLCGYSGHnpEVA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 170 LNSKQLSdlfTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFErAWVAYV-FHRGATnCYL 248
Cdd:PRK12467 653 LDPDNLA---YVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG-VTELFGaLASGAT-LHL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 249 EDTNHVRDA------LTTLKPTVMCAVPrfyekiytavwdkvekalAHRRALFnwaicvgeqhyQAEQPSQWLRLQYALa 322
Cdd:PRK12467 728 LPPDCARDAeafaalMADQGVTVLKIVP------------------SHLQALL-----------QASRVALPRPQRALV- 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 323 dklvltklrallggrikmmpCGGAKLEASIGSFFHSIGINIKL--GYGMTETTATVSCW----QDKGFNPNSIGTLMPNA 396
Cdd:PRK12467 778 --------------------CGGEALQVDLLARVRALGPGARLinHYGPTETTVGVSTYelsdEERDFGNVPIGQPLANL 837
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2490830388 397 EVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGD 438
Cdd:PRK12467 838 GLYIldhylnpvpvGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGD 896
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
397-488 |
1.44e-14 |
|
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: 76.72 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 397 EVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMktsN--GKYIAPQYIEGK 474
Cdd:COG1021 374 PVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQI---NrgGEKIAAEEVENL 450
|
90
....*....|....
gi 2490830388 475 IGKDKFIEQIAVIA 488
Cdd:COG1021 451 LLAHPAVHDAAVVA 464
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
181-488 |
3.64e-14 |
|
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: 75.10 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiFErawvayvfhrGATNCYLedtnhvrdaltt 260
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFN--FD----------GAHEQLL------------ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 261 lkPTVMCA---VPRFYEkiytaVWDKVEkalAHRRALFNWAICVGeqhyqAEQPSQWlrlqYALADKLVLTKLRAllGGR 337
Cdd:cd17649 155 --PPLICGacvVLRPDE-----LWASAD---ELAEMVRELGVTVL-----DLPPAYL----QQLAEEADRTGDGR--PPS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 338 IKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQ---DKGFNPNS--IGTLMPN----------AEVKIGE 402
Cdd:cd17649 214 LRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKceaGAARAGASmpIGRPLGGrsayildadlNPVPVGV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 403 ENEILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGKI 475
Cdd:cd17649 294 TGELYIGGEGLARGYLGRPELTAERFVPDPFgapgsrlYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAAL 372
|
330
....*....|...
gi 2490830388 476 GKDKFIEQIAVIA 488
Cdd:cd17649 373 LEHPGVREAAVVA 385
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
174-500 |
6.14e-14 |
|
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: 74.04 E-value: 6.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 174 QLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDV------SLSFLPLSHIFERAWVA----YVFHRGA 243
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVrllqmaSFSFDVFAGDFARSLLNggtlVICPDEV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 244 tncyLEDTNHVRDALTTLKPTVMCAVPrfyekiytavwdkvekalahrralfnwAICVGEQHYQAEQpsqwlrlqyalad 323
Cdd:cd17650 171 ----KLDPAALYDLILKSRITLMESTP---------------------------ALIRPVMAYVYRN------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 324 KLVLTKLRALLGGRIKMMPCGGAKLEASIGSffHSIGINiklGYGMTETTATVSCWQ-------DKGFNPnsIGTLMPNA 396
Cdd:cd17650 207 GLDLSAMRLLIVGSDGCKAQDFKTLAARFGQ--GMRIIN---SYGVTEATIDSTYYEegrdplgDSANVP--IGRPLPNT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 397 E----------VKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGF------LRTGDVGEMDSCGNLFITDRLKELMKT 460
Cdd:cd17650 280 AmyvlderlqpQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2490830388 461 sNGKYIAPQYIEGKIGKDKFIEQIAVIA--DAK--KYVSALIVP 500
Cdd:cd17650 360 -RGFRIELGEIESQLARHPAIDEAVVAVreDKGgeARLCAYVVA 402
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
21-498 |
3.40e-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: 71.92 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:cd12114 2 DATAVICGDG----TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKiLFVGDQEQLDQVcqIANNCPQLMKIVAMKAnmdlrdlpnacyWEDFLDVVPneaefekrlnskQLSDLFT 180
Cdd:cd12114 78 AILADAGAR-LVLTDGPDAQLD--VAVFDVLILDLDALAA------------PAPPPPVDV------------APDDLAY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYA---NLAHQLNAHdlaLNVNEDDVSLSFLPLSH------IFE--RAWVAYVFHRGATncyLE 249
Cdd:cd12114 131 VIFTSGSTGTPKGVMISHRaalNTILDINRR---FAVGPDDRVLALSSLSFdlsvydIFGalSAGATLVLPDEAR---RR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 DTNHVRDALTTLKPTVMCAVPrfyekiytavwdkvekalahrrALFNWAICVGEQHyQAEQPSqwLRLQYALADKLVLT- 328
Cdd:cd12114 205 DPAHWAELIERHGVTLWNSVP----------------------ALLEMLLDVLEAA-QALLPS--LRLVLLSGDWIPLDl 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 329 --KLRALL-GGRIKMMpcGGAKlEASIGSFFHSIG------INIKLGYGMTETTATVScwqdkgfnpNSIGTLMPnaevk 399
Cdd:cd12114 260 paRLRALApDARLISL--GGAT-EASIWSIYHPIDevppdwRSIPYGRPLANQRYRVL---------DPRGRDCP----- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 400 IGEENEILVRGGMVMRGYYKKPEETAKAFTEDG----FLRTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGKI 475
Cdd:cd12114 323 DWVPGELWIGGRGVALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAAL 401
|
490 500
....*....|....*....|...
gi 2490830388 476 GKDKFIEQIAVIADAKKYVSALI 498
Cdd:cd12114 402 QAHPGVARAVVVVLGDPGGKRLA 424
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
61-472 |
8.60e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.88 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 61 DKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILfVGDQEQLDQVCQIANNCPQLMKIVAMKA 140
Cdd:PRK13391 50 DHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARAL-ITSAAKLDVARALLKQCPGVRHRLVLDG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 141 NMDLRDlpnacyWEDFLDVVpnEAEFEKRLNSKQLSDLftLIYTSGTTGEPKGVM--LDYANLAHQLNAHDLALN---VN 215
Cdd:PRK13391 129 DGELEG------FVGYAEAV--AGLPATPIADESLGTD--MLYSSGTTGRPKGIKrpLPEQPPDTPLPLTAFLQRlwgFR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 216 EDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLEdtnhvrdalttlkptvmcavpRFyekiytavwdKVEKALAhrralf 295
Cdd:PRK13391 199 SDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME---------------------HF----------DAEQYLA------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 296 nwaiCVGEQHYQAEQ--P---SQWLRLQYALADKLVLTKLRALLGGrikMMPCGGAKLEASI---GSFFHSIginiklgY 367
Cdd:PRK13391 242 ----LIEEYGVTHTQlvPtmfSRMLKLPEEVRDKYDLSSLEVAIHA---AAPCPPQVKEQMIdwwGPIIHEY-------Y 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 368 GMTETTATVSC----WQDkgfNPNSIGTLM---------PNAEVKIGEENEILVRGGMVMRgYYKKPEETAKAFTEDGFL 434
Cdd:PRK13391 308 AATEGLGFTACdseeWLA---HPGTVGRAMfgdlhilddDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGTW 383
|
410 420 430
....*....|....*....|....*....|....*....
gi 2490830388 435 RT-GDVGEMDSCGNLFITDRlKELMKTSNGKYIAPQYIE 472
Cdd:PRK13391 384 STvGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAE 421
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
174-448 |
1.53e-12 |
|
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: 69.88 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 174 QLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLS---HIFErawVAYVFHRGATNCYLED 250
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTfdvSILE---IFTTLAAGGCLCIPSE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 ---TNHVRDALTTLKPTVMCAVPrfyekiytavwdkvekALAhrRALfnwaicvgeqhyqaeQPSQWLRLQYaladkLVL 327
Cdd:cd05918 181 edrLNDLAGFINRLRVTWAFLTP----------------SVA--RLL---------------DPEDVPSLRT-----LVL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 328 tklrallggrikmmpcGGAKLEASIGSFFHSigiNIKL--GYGMTETT-ATVSCWQDKGFNPNSIGTLM----------- 393
Cdd:cd05918 223 ----------------GGEALTQSDVDTWAD---RVRLinAYGPAECTiAATVSPVVPSTDPRNIGRPLgatcwvvdpdn 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2490830388 394 PNAEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDG-------------FLRTGDVGEMDSCGNL 448
Cdd:cd05918 284 HDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegsgrgrrLYRTGDLVRYNPDGSL 351
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
11-438 |
1.97e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.58 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 11 RFRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI 90
Cdd:PRK12467 1579 LIEDQAAATPEAVALVFGEQ----ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPL 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 91 YATNTAKQVEYIVNDADIKILFVgdQEQLDQVCQIANNCPQLmkivamkanmdLRDLPNacyweDFLDVVPnEAEFEKRL 170
Cdd:PRK12467 1655 DPEYPRERLAYMIEDSGIELLLT--QSHLQARLPLPDGLRSL-----------VLDQED-----DWLEGYS-DSNPAVNL 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 171 NSKQLSdlfTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLS---HIFERAW----------VAY 237
Cdd:PRK12467 1716 APQNLA---YVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAfdvSVWELFWplingarlviAPP 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 238 VFHRGAtncylEDTNHVrdaLTTLKPTVMCAVPRFYEKIYTAVwDKVEKALAHRRalfnwaICVGEQHYQAEQPSQWLRl 317
Cdd:PRK12467 1793 GAHRDP-----EQLIQL---IERQQVTTLHFVPSMLQQLLQMD-EQVEHPLSLRR------VVCGGEALEVEALRPWLE- 1856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 318 qyaladKLVLTKLrallggrikmmpcggakleasigsffhsigINiklGYGMTETTATVSCW-----QDKGFNPNSIGTL 392
Cdd:PRK12467 1857 ------RLPDTGL------------------------------FN---LYGPTETAVDVTHWtcrrkDLEGRDSVPIGQP 1897
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2490830388 393 MPN----------AEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGD 438
Cdd:PRK12467 1898 IANlstyildaslNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGD 1960
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-446 |
2.60e-12 |
|
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: 69.23 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 12 FRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIY 91
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGR----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 92 ATNTAKQVEYIVNDADIKILFVGDQEQldqvcqianncpqlmkivAMKANMDLRDLPNACYWEDFLDVVPNEAEfekrln 171
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLA------------------ARLPAGGDVALLGDEALAAPPATPPLVPP------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 172 skQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLS---HIFERAWVayvFHRGATNCYL 248
Cdd:cd17646 136 --RPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSfdvSVWELFWP---LVAGARLVVA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 249 E-----DTNHVRDALTTLKPTVMCAVPR----FYEkiytavWDKVEKALAHRRAlfnwaICVGEqhyqaeqpsqwlrlqy 319
Cdd:cd17646 211 RpgghrDPAYLAALIREHGVTTCHFVPSmlrvFLA------EPAAGSCASLRRV-----FCSGE---------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 320 ALADKLVlTKLRALLGGRikmmpcggakleasigsfFHSiginiklGYGMTETTATVSCWQ---DKGFNPNSIGTLMPNA 396
Cdd:cd17646 264 ALPPELA-ARFLALPGAE------------------LHN-------LYGPTEAAIDVTHWPvrgPAETPSVPIGRPVPNT 317
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2490830388 397 EVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGF------LRTGDV------GEMDSCG 446
Cdd:cd17646 318 RLYVlddalrpvpvGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLarwrpdGALEFLG 389
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1-493 |
3.70e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 68.88 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 1 MASLDFHFVNRFRLQAKKWLNRTALRFREQAQwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGA 80
Cdd:PRK05857 9 MPQLPSTVLDRVFEQARQQPEAIALRRCDGTS--ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 81 MQARAVAVPIYATNTAKQVEYIVNDADIKILFVGDQEQLDqvcqiANNCPQ-LMKIVAMKANMDLRDLPNACYWE-DFLD 158
Cdd:PRK05857 87 AKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMA-----SSAVPEaLHSIPVIAVDIAAVTRESEHSLDaASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 159 VVPNEAEfekrlnskqlSDLFTLIYTSGTTGEPKGVML---DYANLAHQLNAHDLA-LNVNEDDVSLSFLPLSHIFERAW 234
Cdd:PRK05857 162 GNADQGS----------EDPLAMIFTSGTTGEPKAVLLanrTFFAVPDILQKEGLNwVTWVVGETTYSPLPATHIGGLWW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 235 VAYVFHRGATnCYL--EDTNHVRDALTTLKPTVMCAVPRFYEKIYTAVwdkvekalahrralfnwaicvgeqhyqaeqps 312
Cdd:PRK05857 232 ILTCLMHGGL-CVTggENTTSLLEILTTNAVATTCLVPTLLSKLVSEL-------------------------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 313 qwlrlqyaladKLVLTKLRALlggriKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCW-QDKG----FNPN 387
Cdd:PRK05857 279 -----------KSANATVPSL-----RLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALCLpTDDGsivkIEAG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 388 SIGTLMPNAEVKIGEEN----------------EILVRGGMVMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNLFIT 451
Cdd:PRK05857 343 AVGRPYPGVDVYLAATDgigptapgagpsasfgTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERREDGFFYIK 421
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2490830388 452 DRLKElMKTSNGKYIAPQYIegkigkDKFIEQIAVIADAKKY 493
Cdd:PRK05857 422 GRSSE-MIICGGVNIAPDEV------DRIAEGVSGVREAACY 456
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-500 |
5.86e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 7 HFVN-RFRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARA 85
Cdd:PRK12316 2003 PGVHqRIAEQAARAPEAIAVVFGDQ----HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 86 VAVPIYATNTAKQVEYIVNDADIKILFV--GDQEQLDqvcqiannCPQLMKIVAMKANMDLRDLPNacywedfldvvpne 163
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTqrHLLERLP--------LPAGVARLPLDRDAEWADYPD-------------- 2136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 164 aefEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLS-HIFERAWV------A 236
Cdd:PRK12316 2137 ---TAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSfDGAHEQWFhpllngA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 237 YVFHRGATncyLEDTNHVRDALTTLKPTVMCAVPRFYEKIytavwdkVEKALAHRRALFNWAICVGEQHYQAEQPSQWlr 316
Cdd:PRK12316 2214 RVLIRDDE---LWDPEQLYDEMERHGVTILDFPPVYLQQL-------AEHAERDGRPPAVRVYCFGGEAVPAASLRLA-- 2281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 317 lqyaladklvltkLRALLGGRIkmmpcggakleasigsffhsigINiklGYGMTETTATVS----CWQDK-GFNPNSIGT 391
Cdd:PRK12316 2282 -------------WEALRPVYL----------------------FN---GYGPTEAVVTPLlwkcRPQDPcGAAYVPIGR 2323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 392 LMPNAEVKIGEENEILVRGGM----------VMRGYYKKPEETAKAFTEDGF-------LRTGDVGEMDSCGNLFITDRL 454
Cdd:PRK12316 2324 ALGNRRAYILDADLNLLAPGMagelylggegLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRI 2403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2490830388 455 KELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVIADAK---KYVSALIVP 500
Cdd:PRK12316 2404 DHQVKI-RGFRIELGEIEARLQAHPAVREAVVVAQDGasgKQLVAYVVP 2451
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
177-500 |
6.22e-12 |
|
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: 67.88 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 177 DLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLS------HIFErAWVAyvfhrGATnCYLED 250
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSfdvcyqEIFS-TLLS-----GGT-LYIIR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 TNHVRD-----ALTTLKPTVMCAVPrfyekiyTAVWdkveKALAHRRALFN-WAICVGEQHYQAEQpsqwlrlqyaladk 324
Cdd:cd17656 202 EETKRDveqlfDLVKRHNIEVVFLP-------VAFL----KFIFSEREFINrFPTCVKHIITAGEQ-------------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 325 LVLTKLrallggrikmmpcggakleasIGSFFHSIGINIKLGYGMTETTATVSCwqdkGFNPNSIGTLMP-------NAE 397
Cdd:cd17656 257 LVITNE---------------------FKEMLHEHNVHLHNHYGPSETHVVTTY----TINPEAEIPELPpigkpisNTW 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 398 VKIGEEN----------EILVRGGMVMRGYYKKPEETAKAFTEDGF------LRTGDVGEMDSCGNLFITDRLKELMKTs 461
Cdd:cd17656 312 IYILDQEqqlqpqgivgELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2490830388 462 NGKYIAPQYIEGKIGKDKFIEQIAVIADA----KKYVSALIVP 500
Cdd:cd17656 391 RGYRIELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVM 433
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
170-575 |
8.30e-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: 67.46 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 170 LNSKQLSDLFT-------LIYTSGTTGEPKGVMLDYANLA-HQLNAHDLALNVNEDDV----SLSF-LPLSHIFErawva 236
Cdd:cd17644 93 LEDAQISVLLTqpenlayVIYTSGSTGKPKGVMIEHQSLVnLSHGLIKEYGITSSDRVlqfaSIAFdVAAEEIYV----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 237 yVFHRGATncyledtnhvrdalTTLKPTVMCAVPrfyekiyTAVWDKVEKalahrralfnWAICVGEQhyqaeQPSQWLR 316
Cdd:cd17644 168 -TLLSGAT--------------LVLRPEEMRSSL-------EDFVQYIQQ----------WQLTVLSL-----PPAYWHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 317 LQYALADKL--VLTKLRALLGGrikmmpcGGAKLEASIGSFFHSIGINIKL--GYGMTETTATVSCW---QDKGFNPNS- 388
Cdd:cd17644 211 LVLELLLSTidLPSSLRLVIVG-------GEAVQPELVRQWQKNVGNFIQLinVYGPTEATIAATVCrltQLTERNITSv 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 389 -IGTLMPNAEVKIGEEN----------EILVRGGMVMRGYYKKPEETAKAFTEDGFL--------RTGDVGEMDSCGNLF 449
Cdd:cd17644 284 pIGRPIANTQVYILDENlqpvpvgvpgELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlyKTGDLARYLPDGNIE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 450 ITDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVIA----DAKKYVSALIVPcfdsleeyakqlnikyqdrielikH 525
Cdd:cd17644 364 YLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVIVredqPGNKRLVAYIVP------------------------H 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2490830388 526 SDIIQMFERRIHELQKELPSFeqvkkftLLPQAFsTTMEE--ITPTLKLRRK 575
Cdd:cd17644 419 YEESPSTVELRQFLKAKLPDY-------MIPSAF-VVLEElpLTPNGKIDRR 462
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
184-487 |
1.10e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 66.61 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 184 TSGTTGEPKGVMLDYANLAHQLNA-HD---------LALnvneddvslsflPLSHIferAWVAYVfhrgatncyledtnh 253
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADAtHDrlggpgqwlLAL------------PAHHI---AGLQVL--------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 254 VRDALTTLKPTVMcAVPRFYEKiytavwdkveKALAhrRALfnwAICVGEQHYQAEQPSQWLRLQYALADKLVLTKLRAL 333
Cdd:PRK07824 93 VRSVIAGSEPVEL-DVSAGFDP----------TALP--RAV---AELGGGRRYTSLVPMQLAKALDDPAATAALAELDAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 334 LggrikmmpCGGAKLEASIGSFFHSIGINIKLGYGMTETTAtvSCWQDkgfnpnsiGTLMPNAEVKIgEENEILVRGGMV 413
Cdd:PRK07824 157 L--------VGGGPAPAPVLDAAAAAGINVVRTYGMSETSG--GCVYD--------GVPLDGVRVRV-EDGRIALGGPTL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 414 MRGYYKKPEEtaKAFTEDGFLRTGDVGEMDScGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:PRK07824 218 AKGYRNPVDP--DPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVF 287
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
18-193 |
1.30e-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: 67.52 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 18 KWL----NRTALRFR-EQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYA 92
Cdd:cd05968 69 KWLadtrTRPALRWEgEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 93 TNTAKQVEYIVNDADIKILFVGD-----------QEQLDQVCQianNCPQLMKIVAMK--ANMDLRDLPNACYWEDFLDV 159
Cdd:cd05968 149 GFGKEAAATRLQDAEAKALITADgftrrgrevnlKEEADKACA---QCPTVEKVVVVRhlGNDFTPAKGRDLSYDEEKET 225
|
170 180 190
....*....|....*....|....*....|....
gi 2490830388 160 VPNEAEfekRLNSKqlsDLFTLIYTSGTTGEPKG 193
Cdd:cd05968 226 AGDGAE---RTESE---DPLMIIYTSGTTGKPKG 253
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
181-500 |
1.43e-11 |
|
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: 65.79 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANL-AHQLNAHDLAlNVNEDDVSLSFLPLSHIFERAWVAYVFHRGATNCYLEDTNhvrdalt 259
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALlAQALVLAVLQ-AIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVD------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 260 tlkPTVMCAVprfyekiytavwdkvekaLAHRRAlfNWAICVGeqhyqaeqPSQWLRLQYALADKLVLTKLRALLGgrik 339
Cdd:cd17636 77 ---AEEVLEL------------------IEAERC--THAFLLP--------PTIDQIVELNADGLYDLSSLRSSPA---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 340 mMPCGGAKLEASIGSFFHSIGiniklGYGMTETTA-TVSCWQDKGFNPNSiGTLMPNAEVKI----------GEENEILV 408
Cdd:cd17636 122 -APEWNDMATVDTSPWGRKPG-----GYGQTEVMGlATFAALGGGAIGGA-GRPSPLVQVRIldedgrevpdGEVGEIVA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 409 RGGMVMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNL-FITDRLKelMKTSNGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:cd17636 195 RGPTVMAGYWNRPEVNARRTR-GGWHHTNDLGRREPDGSLsFVGPKTR--MIKSGAENIYPAEVERCLRQHPAVADAAVI 271
|
330
....*....|....*..
gi 2490830388 488 --ADAK--KYVSALIVP 500
Cdd:cd17636 272 gvPDPRwaQSVKAIVVL 288
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
19-544 |
3.21e-11 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 65.95 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 19 WLNRTAlrfreqaqwQEMSWqTFQQ--EIDRFSYALIAQHIDIQ--DKIGIFANNMPRWTIADFGAMQARAVAVPIYATN 94
Cdd:cd05928 32 WVNGKG---------DEVKW-SFRElgSLSRKAANVLSGACGLQrgDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 95 TAKQVEYIVNDADIKILFVGDqEQLDQVCQIANNCPQL-MKIVAMKANMDlrdlpnacYWEDFLDVVpNEAEFEKRLNSK 173
Cdd:cd05928 102 TAKDILYRLQASKAKCIVTSD-ELAPEVDSVASECPSLkTKLLVSEKSRD--------GWLNFKELL-NEASTEHHCVET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 174 QLSDLFTLIYTSGTTGEPKGVMLDYANLAH----------QLNAHDLALNVNedDVSLSFLPLSHIFErAWV--AYVF-H 240
Cdd:cd05928 172 GSQEPMAIYFTSGTTGSPKMAEHSHSSLGLglkvngrywlDLTASDIMWNTS--DTGWIKSAWSSLFE-PWIqgACVFvH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 241 RGATNcyleDTNHVRDALTTLKPTVMCAVPRFYEKIYTAVWDKVE-KALAHrralfnwAICVGEqhyqAEQPSqwlrlqy 319
Cdd:cd05928 249 HLPRF----DPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKfPSLQH-------CVTGGE----PLNPE------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 320 aladklVLTKLRallggrikmmpcggakleasigsffHSIGINIKLGYGMTETtaTVSCWQDKG--FNPNSIGTLMPNAE 397
Cdd:cd05928 307 ------VLEKWK-------------------------AQTGLDIYEGYGQTET--GLICANFKGmkIKPGSMGKASPPYD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 398 VKI----------GEENEILVRGGMV-----MRGYYKKPEETAKAFTEDgFLRTGDVGEMDSCGNLFITDRLKELMKTSn 462
Cdd:cd05928 354 VQIiddngnvlppGTEGDIGIRVKPIrpfglFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSS- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 463 GKYIAPQYIEGKIGKDKFIEQIAVIADAK----KYVSALIVPCFDSLEEYAKQLNIKYQDRielIKHSDIIQMFERRIhE 538
Cdd:cd05928 432 GYRIGPFEVESALIEHPAVVESAVVSSPDpirgEVVKAFVVLAPQFLSHDPEQLTKELQQH---VKSVTAPYKYPRKV-E 507
|
....*.
gi 2490830388 539 LQKELP 544
Cdd:cd05928 508 FVQELP 513
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
57-487 |
3.49e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 65.96 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 57 IDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILfVGDQEQLDQVCQIANNCPQLMKIV 136
Cdd:PRK05620 61 ITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVI-VADPRLAEQLGEILKECPCVRAVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 137 ------AMKANMDLRDLPNACYWEDFLD---VVPNEAEFEKRlnskqlsDLFTLIYTSGTTGEPKGVMLDYANL---AHQ 204
Cdd:PRK05620 140 figpsdADSAAAHMPEGIKVYSYEALLDgrsTVYDWPELDET-------TAAAICYSTGTTGAPKGVVYSHRSLylqSLS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 205 LNAHDlALNVNEDDVSLSFLPLSHIFE-----RAWVA---YVFhRGATncylEDTNHVRDALTTLKPTVMCAVPrfyeki 276
Cdd:PRK05620 213 LRTTD-SLAVTHGESFLCCVPIYHVLSwgvplAAFMSgtpLVF-PGPD----LSAPTLAKIIATAMPRVAHGVP------ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 277 ytAVWDKvekalahrraLFnwaicvgeQHYQAEQPSQwlrlqyaladklvlTKLRALLGGrikmmpcGGAKLEASIGSFF 356
Cdd:PRK05620 281 --TLWIQ----------LM--------VHYLKNPPER--------------MSLQEIYVG-------GSAVPPILIKAWE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 357 HSIGINIKLGYGMTETTA--TVS------CWQDKGFNPNSIGTLMPNAEVKI---GE--------ENEILVRGGMVMRGY 417
Cdd:PRK05620 320 ERYGVDVVHVWGMTETSPvgTVArppsgvSGEARWAYRVSQGRFPASLEYRIvndGQvmestdrnEGEIQVRGNWVTASY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 418 YKKP----------------EETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNGKYIAPQYIEGKIGKDKFI 481
Cdd:PRK05620 400 YHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEV 478
|
....*.
gi 2490830388 482 EQIAVI 487
Cdd:PRK05620 479 VECAVI 484
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
46-512 |
3.68e-11 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 65.53 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 46 DRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILfvgdqeqldqvcqi 125
Cdd:cd05971 17 NRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 126 anncpqlmkivamkanmdLRDLPNacywedfldvvpneaefekrlnskqlsDLFTLIYTSGTTGEPKGVmldyanlahqL 205
Cdd:cd05971 83 ------------------VTDGSD---------------------------DPALIIYTSGTTGPPKGA----------L 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 206 NAHDLAL-NVNEDDVSLSFLPLShiferawvAYVFHRGAtncyleDTNHVRDALTTLKPTVMCAVPrfyekiytavwdkv 284
Cdd:cd05971 108 HAHRVLLgHLPGVQFPFNLFPRD--------GDLYWTPA------DWAWIGGLLDVLLPSLYFGVP-------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 285 ekALAHRRALFN--WAICVGEQH--YQAEQPSQWLRLQYALADKLVLT--KLRALLggrikmmpCGGAKL-EASIGSFFH 357
Cdd:cd05971 160 --VLAHRMTKFDpkAALDLMSRYgvTTAFLPPTALKMMRQQGEQLKHAqvKLRAIA--------TGGESLgEELLGWARE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 358 SIGINIKLGYGMTETTATV-SCWQDKGFNPNSIGTLMPNAEVKI----------GEENEILVR--GGMVMRGYYKKPEET 424
Cdd:cd05971 230 QFGVEVNEFYGQTECNLVIgNCSALFPIKPGSMGKPIPGHRVAIvddngtplppGEVGEIAVElpDPVAFLGYWNNPSAT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 425 AKAFTEDgFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVIA--DAKK--YVSALIV- 499
Cdd:cd05971 310 EKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVVGipDPIRgeIVKAFVVl 387
|
490
....*....|....
gi 2490830388 500 -PCFDSLEEYAKQL 512
Cdd:cd05971 388 nPGETPSDALAREI 401
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
61-473 |
4.17e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 65.31 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 61 DKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQEQLDQVCQIANNCPQLMKIVAMka 140
Cdd:PRK08276 37 DVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV-SAALADTAAELAAELPAGVPLLLV-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 141 nmDLRDLPNACYWEDFLDVVPNEAEFEKRLNSkqlsdlfTLIYTSGTTGEPKGVM-------LDYANLAHqLNAHDLALN 213
Cdd:PRK08276 114 --VAGPVPGFRSYEEALAAQPDTPIADETAGA-------DMLYSSGTTGRPKGIKrplpgldPDEAPGMM-LALLGFGMY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 214 VNEDDVSLSFLPLSHIFERAWVAYVFHRGATncyledtnhvrdalttlkpTVMcavprfYEKiytavWDKvEKALAhrra 293
Cdd:PRK08276 184 GGPDSVYLSPAPLYHTAPLRFGMSALALGGT-------------------VVV------MEK-----FDA-EEALA---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 294 lfnwAIcvgeQHYQAEQpSQW--------LRLQYALADKLVLTKLR-ALLGGrikmMPCGGAKLEASI---GSFFHSIgi 361
Cdd:PRK08276 229 ----LI----ERYRVTH-SQLvptmfvrmLKLPEEVRARYDVSSLRvAIHAA----APCPVEVKRAMIdwwGPIIHEY-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 362 niklgYGMTE----TTATVSCWQDKgfnPNSIGTLMpNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKA 427
Cdd:PRK08276 294 -----YASSEgggvTVITSEDWLAH---PGSVGKAV-LGEVRIldedgnelppGEIGTVYFEMDGYPFEYHNDPEKTAAA 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2490830388 428 FTEDGFLRTGDVGEMDSCGNLFITDRlKELMKTSNGKYIAPQYIEG 473
Cdd:PRK08276 365 RNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIEN 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
22-487 |
4.60e-11 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 65.19 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 22 RTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQ-DKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:cd05958 1 RTCLRSPER----EWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILFVGDQE-QLDQVCQIAnncpqlmkivamkanmdlrdlpnacywedfldvvpneaefekrlnskqlsdlf 179
Cdd:cd05958 77 YILDKARITVALCAHALtASDDICILA----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 180 tliYTSGTTGEPKGVM---LDYANLAHQLNAHDLALnvNEDDVSLSFLPLSHIFERAWVA-YVFHRGATNCYLEDT--NH 253
Cdd:cd05958 104 ---FTSGTTGAPKATMhfhRDPLASADRYAVNVLRL--REDDRFVGSPPLAFTFGLGGVLlFPFGVGASGVLLEEAtpDL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 254 VRDALTTLKPTVMCAVPRFYEKIytavwdkvekaLAHRRAlfnwaicvGEQhyqaeqpsqwlrlqyaladklvltklraL 333
Cdd:cd05958 179 LLSAIARYKPTVLFTAPTAYRAM-----------LAHPDA--------AGP----------------------------D 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 334 LGGRIKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI----------GEE 403
Cdd:cd05958 212 LSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVvddegnpvpdGTI 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 404 NEILVRGGMvmrGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKtSNGKYIAPQYIEGKIGKDKFIEQ 483
Cdd:cd05958 292 GRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAE 367
|
....
gi 2490830388 484 IAVI 487
Cdd:cd05958 368 CAVV 371
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
311-487 |
5.78e-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: 63.96 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 311 PSQWLRL---QYALADKLVLTKLRALLG-----GRIKMMPCGGAKLEASIGSFFHSI--GINIKLGYGMTETT-ATVSCW 379
Cdd:cd17633 77 PKSWIRKinqYNATVIYLVPTMLQALARtlepeSKIKSIFSSGQKLFESTKKKLKNIfpKANLIEFYGTSELSfITYNFN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 380 QDKGfNPNSIGTLMPNAEVKI-----GEENEILVRGGMVMRGYYKkpeetAKAFTEDGFLRTGDVGEMDSCGNLFITDRL 454
Cdd:cd17633 157 QESR-PPNSVGRPFPNVEIEIrnadgGEIGKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRE 230
|
170 180 190
....*....|....*....|....*....|...
gi 2490830388 455 KElMKTSNGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:cd17633 231 SD-MIIIGGINIFPTEIESVLKAIPGIEEAIVV 262
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-500 |
7.54e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 23 TALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYI 102
Cdd:PRK12316 528 PALAFGEE----TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYM 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 103 VNDADIKIL----FVGDQEQLDQVCQianncpqlmkivamkaNMDLrDLPNAcywedFLDVVPNEAEfEKRLNSKQLSdl 178
Cdd:PRK12316 604 LEDSGVQLLlsqsHLGRKLPLAAGVQ----------------VLDL-DRPAA-----WLEGYSEENP-GTELNPENLA-- 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 179 fTLIYTSGTTGEPKGVMLDYANLAHQLNahdlalnvneddvslsflplshiferaWVAYVFHRGATNCYLEDTNHVRDAl 258
Cdd:PRK12316 659 -YVIYTSGSTGKPKGAGNRHRALSNRLC---------------------------WMQQAYGLGVGDTVLQKTPFSFDV- 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 259 ttlkptvmcAVPRFYEKIYTAVWDKVEKALAHRRALFNWAICVGEQ----HYqaeQPSQWLRLQYALADKLVLTKLRALL 334
Cdd:PRK12316 710 ---------SVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGvdtlHF---VPSMLQAFLQDEDVASCTSLRRIVC 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 335 GGRikmmPCGGAKLEASIGSFFHSIGINIklgYGMTETTATVSCWQ--DKGFNPNSIGTLMPNAE----------VKIGE 402
Cdd:PRK12316 778 SGE----ALPADAQEQVFAKLPQAGLYNL---YGPTEAAIDVTHWTcvEEGGDSVPIGRPIANLAcyildanlepVPVGV 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 403 ENEILVRGGMVMRGYYKKPEETAKAFTEDGFL------RTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGKIG 476
Cdd:PRK12316 851 LGELYLAGRGLARGYHGRPGLTAERFVPSPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLL 929
|
490 500
....*....|....*....|....
gi 2490830388 477 KDKFIEQIAVIADAKKYVSALIVP 500
Cdd:PRK12316 930 EHPWVREAAVLAVDGKQLVGYVVL 953
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
36-511 |
8.42e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 64.78 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 36 MSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgD 115
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIY-D 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 116 QEQLDQVCQIANNCPQLMKIVAmkanmdlrdlpnacyWEDFLDVVPNEAEFEKRLN-----SKQLSDlfTLIYTSGTTGE 190
Cdd:PRK13382 148 EEFSATVDRALADCPQATRIVA---------------WTDEDHDLTVEVLIAAHAGqrpepTGRKGR--VILLTSGTTGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 191 PKGVmldyanlahqlnahdlalnvnEDDVSLSFLPLSHIFERA-WVAYvfhrgatncyledtnhvrdalttlKPTVMCAv 269
Cdd:PRK13382 211 PKGA---------------------RRSGPGGIGTLKAILDRTpWRAE------------------------EPTVIVA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 270 PRFYekiytaVWDKVEKALAhrrALFNWAIcVGEQHYQAEQPSQWLRLQYALADKLVLTKLRallggRIKMMP------- 342
Cdd:PRK13382 245 PMFH------AWGFSQLVLA---ASLACTI-VTRRRFDPEATLDLIDRHRATGLAVVPVMFD-----RIMDLPaevrnry 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 343 -CGGAKLEASIGS---------FFHSIGINIKLGYGMTE----TTATVscwQDKGFNPNSIGTLMPNAEVKI-------- 400
Cdd:PRK13382 310 sGRSLRFAAASGSrmrpdvviaFMDQFGDVIYNNYNATEagmiATATP---ADLRAAPDTAGRPAEGTEIRIldqdfrev 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 --GEENEILVRGGMVMRGYYKKpeeTAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIGKD 478
Cdd:PRK13382 387 ptGEVGTIFVRNDTQFDGYTSG---STKDF-HDGFMASGDVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVEKTLATH 461
|
490 500 510
....*....|....*....|....*....|....*....
gi 2490830388 479 KFIEQIAVIA-DAKKY---VSALIVPCFDS--LEEYAKQ 511
Cdd:PRK13382 462 PDVAEAAVIGvDDEQYgqrLAAFVVLKPGAsaTPETLKQ 500
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
182-500 |
1.12e-10 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 64.07 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 182 IYTSGTTGEPKGVMLDYANLAHQ--LNAHDLALNVNEDDVSLSFLPLSH-IFERAWVAYVFHRGATNCYLEDTNHVrDAL 258
Cdd:cd05923 156 FYTSGTTGLPKGAVIPQRAAESRvlFMSTQAGLRHGRHNVVLGLMPLYHvIGFFAVLVAALALDGTYVVVEEFDPA-DAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 259 TTLKP---TVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAicvgeqhyqaeqpsqwlrlqyALADKlVLTKLRALLG 335
Cdd:cd05923 235 KLIEQervTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGA---------------------TMPDA-VLERVNQHLP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 336 GRIkmmpcggakleasigsffhsigINIklgYGMTETTATVscwqdkgFNPN-SIGTLMP---NAEVKI----------- 400
Cdd:cd05923 293 GEK----------------------VNI---YGTTEAMNSL-------YMRDaRTGTEMRpgfFSEVRIvriggspdeal 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 --GEENEILVR--GGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIG 476
Cdd:cd05923 341 anGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDD-MIISGGENIHPSEIERVLS 418
|
330 340
....*....|....*....|....*...
gi 2490830388 477 KDKFIEQIAVI--ADAK--KYVSALIVP 500
Cdd:cd05923 419 RHPGVTEVVVIgvADERwgQSVTACVVP 446
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
367-579 |
1.30e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 63.76 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 367 YGMTETTATVSCWQ------DKgFNPNSIGTLMPNAEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAF-T 429
Cdd:PRK04813 293 YGPTEATVAVTSIEitdemlDQ-YKRLPIGYAKPDSPLLIideegtklpdGEQGEIVISGPSVSKGYLNNPEKTAEAFfT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 430 EDG--FLRTGDVGEMDScGNLFITDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQiAVIADAKK-----YVSALIVPCF 502
Cdd:PRK04813 372 FDGqpAYHTGDAGYLED-GLLFYQGRIDFQIKL-NGYRIELEEIEQNLRQSSYVES-AVVVPYNKdhkvqYLIAYVVPKE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 503 DSLE-EYAKQLNIKyqdrielikhsdiiqmferriHELQKELPSFeqvkkftLLPQAFsTTMEEI--TPTLKLRRKVIMQ 579
Cdd:PRK04813 449 EDFErEFELTKAIK---------------------KELKERLMEY-------MIPRKF-IYRDSLplTPNGKIDRKALIE 499
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
17-490 |
1.44e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 63.74 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 17 KKWLNR----TALRFREQaQWqemSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIya 92
Cdd:PRK09029 10 RHWAQVrpqaIALRLNDE-VL---TWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 93 tNTAKQveyivndadikilfvgdQEQLDQVCqianncPQLmkivamkaNMDLRDLPNACYWEDFLDVVPNEAEFEKRLNS 172
Cdd:PRK09029 84 -NPQLP-----------------QPLLEELL------PSL--------TLDFALVLEGENTFSALTSLHLQLVEGAHAVA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 173 KQLSDLFTLIYTSGTTGEPKGVmldyanlAHQLNAHdLA-----LNV----NEDDVSLSfLPLSH-----IFERaWVAyv 238
Cdd:PRK09029 132 WQPQRLATMTLTSGSTGLPKAA-------VHTAQAH-LAsaegvLSLmpftAQDSWLLS-LPLFHvsgqgIVWR-WLY-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 239 fhRGATncyLedtnHVRDAlttlkptvmcavprfyekiytavwDKVEKALA---HrralfnwAICVgeqhyqaeqPSQWL 315
Cdd:PRK09029 200 --AGAT---L----VVRDK------------------------QPLEQALAgctH-------ASLV---------PTQLW 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 316 RLqyaLADKLVLTKLRALLggrikmmpCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCWQDKGFnpNSIGTLMPN 395
Cdd:PRK09029 231 RL---LDNRSEPLSLKAVL--------LGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAKRADGL--AGVGSPLPG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 396 AEVKIgEENEILVRGGMVMRGYYKKPEETakAFT-EDGFLRTGDVGEMDScGNLFITDRLKElMKTSNGKYIAPQYIEGK 474
Cdd:PRK09029 298 REVKL-VDGEIWLRGASLALGYWRQGQLV--PLVnDEGWFATRDRGEWQN-GELTILGRLDN-LFFSGGEGIQPEEIERV 372
|
490
....*....|....*...
gi 2490830388 475 IGKDKFIEQIAV--IADA 490
Cdd:PRK09029 373 INQHPLVQQVFVvpVADA 390
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-472 |
2.14e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 52 LIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI-YATNTAKQVEYIVN------DADIKILFVGDqEQLDQVCQ 124
Cdd:PRK09192 66 LLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLpLPMGFGGRESYIAQlrgmlaSAQPAAIITPD-ELLPWVNE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 125 IANNCPqlMKIVAMKANMDLRDLPNAcyweDFLDVVPNeaefekrlnskqlsDLFTLIYTSGTTGEPKGVMLDYANLAHQ 204
Cdd:PRK09192 145 ATHGNP--LLHVLSHAWFKALPEADV----ALPRPTPD--------------DIAYLQYSSGSTRFPRGVIITHRALMAN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 205 LNAHDL-ALNVNEDDVSLSFLPLSHifERAWVAYVFHRGATNC---YLEDTNHVRDALTTLK------------PTV--- 265
Cdd:PRK09192 205 LRAISHdGLKVRPGDRCVSWLPFYH--DMGLVGFLLTPVATQLsvdYLPTRDFARRPLQWLDlisrnrgtisysPPFgye 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 266 MCAVpRFYEKiytavwDKVEKALAHRRA------------LFNWAICVGEQHYQAEQ--PSqwlrlqYALADklvltklr 331
Cdd:PRK09192 283 LCAR-RVNSK------DLAELDLSCWRVagigadmirpdvLHQFAEAFAPAGFDDKAfmPS------YGLAE-------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 332 ALLGgrIKMMPCG-GAKLEASIGSFFHSIGINIKLGYGMTETTATVSCwqdkgfnpnsiGTLMPNAEVKIGEEN------ 404
Cdd:PRK09192 342 ATLA--VSFSPLGsGIVVEEVDRDRLEYQGKAVAPGAETRRVRTFVNC-----------GKALPGHEIEIRNEAgmplpe 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2490830388 405 ----EILVRGGMVMRGYYKKpEETAKAFTEDGFLRTGDVGEMdSCGNLFITDRLKELMkTSNGKYIAPQYIE 472
Cdd:PRK09192 409 rvvgHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
40-487 |
1.07e-09 |
|
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: 60.98 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 40 TFQQ---EIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgdq 116
Cdd:cd05969 2 TFAQlkvLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 117 eqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpNEAEFEKRlnskQLSDLFTLIYTSGTTGEPKGVML 196
Cdd:cd05969 79 ---------------------------------------------TEELYERT----DPEDPTLLHYTSGTTGTPKGVLH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 197 DYANLAHQLNAHDLALNVNEDDVslsflpLSHIFERAWVAYVFH-------RGATNCYLE---DTNHVRDALTTLKPTVM 266
Cdd:cd05969 110 VHDAMIFYYFTGKYVLDLHPDDI------YWCTADPGWVTGTVYgiwapwlNGVTNVVYEgrfDAESWYGIIERVKVTVW 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 267 CAVPrfyekiyTAVwdkvekalahrRALfnwaicvgeqhyqaeqpsqwLRLQYALADKLVLTKLRALLGGrikmmpcgGA 346
Cdd:cd05969 184 YTAP-------TAI-----------RML--------------------MKEGDELARKYDLSSLRFIHSV--------GE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 347 KLEASIGSFFHSI-GINIKLGYGMTETTATVSC-WQDKGFNPNSIGTLMPNAEVKI----------GEENEILVRGGM-- 412
Cdd:cd05969 218 PLNPEAIRWGMEVfGVPIHDTWWQTETGSIMIAnYPCMPIKPGSMGKPLPGVKAAVvdengnelppGTKGILALKPGWps 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 413 VMRGYYKKPEETAKAFTeDGFLRTGDVGEMDSCGNLFITDRLKELMKTSnGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:cd05969 298 MFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGVI 370
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
360-500 |
1.49e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 60.39 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 360 GINIKLGYGMTETTATVSCWQDKGF--NPNSIGTLMPNAEVKI--GEENEILVRGGMVMRGYYKKPEETAKAFTedgflr 435
Cdd:PRK07445 254 QLRLAPTYGMTETASQIATLKPDDFlaGNNSSGQVLPHAQITIpaNQTGNITIQAQSLALGYYPQILDSQGIFE------ 327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490830388 436 TGDVGEMDSCGNLFITDRLKELMkTSNGKYIAPQYIEGKIGKDKFIEQIAVIADAKKY----VSALIVP 500
Cdd:PRK07445 328 TDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwgevVTAIYVP 395
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
37-490 |
2.12e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 60.24 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 37 SWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILFVgDQ 116
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV-DQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 117 EQL---DQVCQI-----ANNCPQLMKIVAMKANMDLRDLPNA-----CYWEDFLDVvpNEAEFekrlNSKQLSDLFTLI- 182
Cdd:PLN02479 126 EFFtlaEEALKIlaekkKSSFKPPLLIVIGDPTCDPKSLQYAlgkgaIEYEKFLET--GDPEF----AWKPPADEWQSIa 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 183 --YTSGTTGEPKGVMLdyanlaHQLNAHDLALN------VNEDDVSLSFLPLSHIfeRAWV---AYVFHRGATNCYLE-D 250
Cdd:PLN02479 200 lgYTSGTTASPKGVVL------HHRGAYLMALSnaliwgMNEGAVYLWTLPMFHC--NGWCftwTLAALCGTNICLRQvT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 251 TNHVRDALTTLKPTVMCAVPRFYEKIYTAvwDKVEKALAHRRAlfnwaicvgeqhyqaeqpsqwlrlqyaladklvltkl 330
Cdd:PLN02479 272 AKAIYSAIANYGVTHFCAAPVVLNTIVNA--PKSETILPLPRV------------------------------------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 331 rallggrIKMMPCGGAKlEASIGSFFHSIGINIKLGYGMTET--TATVSCWQDK--GFNPNSIGTLMPNAEVK-IGEEN- 404
Cdd:PLN02479 313 -------VHVMTAGAAP-PPSVLFAMSEKGFRVTHTYGLSETygPSTVCAWKPEwdSLPPEEQARLNARQGVRyIGLEGl 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 -------------------EILVRGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNGKY 465
Cdd:PLN02479 385 dvvdtktmkpvpadgktmgEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGEN 462
|
490 500
....*....|....*....|....*
gi 2490830388 466 IAPQYIEGKIGKDKFIEQIAVIADA 490
Cdd:PLN02479 463 ISSLEVENVVYTHPAVLEASVVARP 487
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
182-465 |
2.98e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 59.53 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 182 IYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWvayvfhrGATncyledtnhvrdalttl 261
Cdd:PRK09274 180 LFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPAL-------GMT----------------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 262 kptvmCAVPRFyekiytavwDKVEKALAHRRALFNwAIcvgeQHYQAEQ----PSQWLRL-QYALADKLVLTKLRALLgg 336
Cdd:PRK09274 236 -----SVIPDM---------DPTRPATVDPAKLFA-AI----ERYGVTNlfgsPALLERLgRYGEANGIKLPSLRRVI-- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 337 rikmmpCGGAKLEASIGSFFHSI---GINIKLGYGMTET------------TATVSCWqDKGFNpNSIGTLMPNAEVKI- 400
Cdd:PRK09274 295 ------SAGAPVPIAVIERFRAMlppDAEILTPYGATEAlpissiesreilFATRAAT-DNGAG-ICVGRPVDGVEVRIi 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 ------------------GEENEILVRGGMVMRGYYKKPEETAKAFTEDG----FLRTGDVGEMDSCGNLFITDRLKELM 458
Cdd:PRK09274 367 aisdapipewddalrlatGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRV 446
|
....*..
gi 2490830388 459 KTSNGKY 465
Cdd:PRK09274 447 ETAGGTL 453
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
174-488 |
4.32e-09 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 58.80 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 174 QLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiFERA-W-VAYVFHRGATnCYLEDT 251
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS--FDASvWeLLMALLAGAT-LVLAPA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 N------HVRDALT-------TLKPTVMCAVPrfyekiytavwdkvEKALAHRRALfnwaICVGEqhyqaeqpsqwlrlq 318
Cdd:cd17652 168 EellpgePLADLLRehrithvTLPPAALAALP--------------PDDLPDLRTL----VVAGE--------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 319 yALADKLVltklRALLGGRiKMmpcggakleasigsffhsigINiklGYGMTETT--ATVS-CwqDKGFNPNSIGTLMPN 395
Cdd:cd17652 215 -ACPAELV----DRWAPGR-RM--------------------IN---AYGPTETTvcATMAgP--LPGGGVPPIGRPVPG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 396 AEVKI----------GEENEILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGDVGEMDSCGNLFITDRLKELM 458
Cdd:cd17652 264 TRVYVldarlrpvppGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQV 343
|
330 340 350
....*....|....*....|....*....|
gi 2490830388 459 KTsNGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:cd17652 344 KI-RGFRIELGEVEAALTEHPGVAEAVVVV 372
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
22-488 |
4.71e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 58.88 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 22 RTALRFREQaQWqemSWQTFQQEIDRFSYALIAQHI-DIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:PRK13388 17 TIAVRYGDR-TW---TWREVLAEAAARAAALIALADpDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILfVGDQEQLdqvcqianncPQLmkivamkANMDLRDLPnacywedFLDVvpNEAEFEKRLNSKQ------ 174
Cdd:PRK13388 93 ADIRRADCQLL-VTDAEHR----------PLL-------DGLDLPGVR-------VLDV--DTPAYAELVAAAGaltphr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 175 ---LSDLFTLIYTSGTTGEPKGVMLDYANLAhqLNAHDLA--LNVNEDDVSLSFLPLSH--IFERAWvAYVFHRGATNC- 246
Cdd:PRK13388 146 evdAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALTerFGLTRDDVCYVSMPLFHsnAVMAGW-APAVASGAAVAl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 247 --------YLEDTnhvrdalttlkptvmcavpRFYEKIYtavWDKVEKALAHRRAlfnwaicvgeqhyQAEQPSQwlrlq 318
Cdd:PRK13388 223 pakfsasgFLDDV-------------------RRYGATY---FNYVGKPLAYILA-------------TPERPDD----- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 319 yalADklvlTKLRALLGGrikmmpcggaklEAS---IGSFFHSIGINIKLGYGMTETTATVScwQDKGFNPNSIG----- 390
Cdd:PRK13388 263 ---AD----NPLRVAFGN------------EASprdIAEFSRRFGCQVEDGYGSSEGAVIVV--REPGTPPGSIGrgapg 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 391 -------TLMP-------------NAEVKIGEeneiLV--RGGMVMRGYYKKPEETAKAFtEDGFLRTGDVGEMDSCGNL 448
Cdd:PRK13388 322 vaiynpeTLTEcavarfdahgallNADEAIGE----LVntAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWI 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2490830388 449 FITDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:PRK13388 397 YFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
6-500 |
6.08e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 58.48 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 6 FHFVNRfrlQAKKWLNRTALRfreqAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARA 85
Cdd:cd12115 2 HDLVEA---QAARTPDAIALV----CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 86 VAVPIYATNTAKQVEYIVNDADIKILFVgdqeqldqvcqianncpqlmkivamkanmdlrdlpnacywedfldvvpneae 165
Cdd:cd12115 75 AYVPLDPAYPPERLRFILEDAQARLVLT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 166 fekrlnskQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLN-------AHDLA--LNVNEDDVSLS----FLPLSHifer 232
Cdd:cd12115 103 --------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQwaaaafsAEELAgvLASTSICFDLSvfelFGPLAT---- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 233 awvayvfhrGATNCYLEDTNHVRDALTTLKPTVMCAVPrfyekiyTAVwdkveKALAHRRALFNWAICV---GEqhyqae 309
Cdd:cd12115 171 ---------GGKVVLADNVLALPDLPAAAEVTLINTVP-------SAA-----AELLRHDALPASVRVVnlaGE------ 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 310 qpsqwlrlqyALADKLVLtKLRALLGG-RIkmmpcggakleasigsffhsigINIklgYGMTETT--ATVSCWQDKGFNP 386
Cdd:cd12115 224 ----------PLPRDLVQ-RLYARLQVeRV----------------------VNL---YGPSEDTtySTVAPVPPGASGE 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 387 NSIGTLMPN----------AEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGFL------RTGDVGEMDSCGNLFI 450
Cdd:cd12115 268 VSIGRPLANtqayvldralQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEF 347
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2490830388 451 TDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVI----ADAKKYVSALIVP 500
Cdd:cd12115 348 LGRADNQVKV-RGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVA 400
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-575 |
1.05e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.63 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVEYIVNDADIKILfV 113
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLL-L 3197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 114 GDQEQLDQVcqianncPQLMKIVAMkaNMDLRDlpnacyWEDFLDVVPNeaefekrlNSKQLSDLFTLIYTSGTTGEPKG 193
Cdd:PRK12467 3198 TQAHLLEQL-------PAPAGDTAL--TLDRLD------LNGYSENNPS--------TRVMGENLAYVIYTSGSTGKPKG 3254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 194 VMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiFERA-WVAY-VFHRGAtnCYLEDTNHVRDAlttlkptvmcavpr 271
Cdd:PRK12467 3255 VGVRHGALANHLCWIAEAYELDANDRVLLFMSFS--FDGAqERFLwTLICGG--CLVVRDNDLWDP-------------- 3316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 272 fyEKIYTAVwdkvekaLAHRRALFNWAicvgeqhyqaeqPSQwlrLQYALADKlvltKLRAllGGRIKMMPCGGAKL-EA 350
Cdd:PRK12467 3317 --EELWQAI-------HAHRISIACFP------------PAY---LQQFAEDA----GGAD--CASLDIYVFGGEAVpPA 3366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 351 SIGSFF-HSIGINIKLGYGMTETTATVSCW---QDKGFNPNS--IGTLMPNAE----------VKIGEENEILVRGGMVM 414
Cdd:PRK12467 3367 AFEQVKrKLKPRGLTNGYGPTEAVVTVTLWkcgGDAVCEAPYapIGRPVAGRSiyvldgqlnpVPVGVAGELYIGGVGLA 3446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 415 RGYYKKPEETAKAFTEDGFL-------RTGDVGEMDSCGNLFITDRLKELMKTsNGKYIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:PRK12467 3447 RGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLLQHPSVREAVVL 3525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 488 A---DAKKYVSALIVPcfdsleeyakqlNIKYQD-RIELIKHsdiiqmferriheLQKELPSFEQVKKFTLLPQAfsttm 563
Cdd:PRK12467 3526 ArdgAGGKQLVAYVVP------------ADPQGDwRETLRDH-------------LAASLPDYMVPAQLLVLAAM----- 3575
|
570
....*....|..
gi 2490830388 564 eEITPTLKLRRK 575
Cdd:PRK12467 3576 -PLGPNGKVDRK 3586
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
181-459 |
1.12e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.44 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANLahQLNAHDLALNV--NEDDVSLSFLPLSHIFerawvayvfhrGATNCYLedtnhvrdaL 258
Cdd:PRK06814 798 ILFTSGSEGTPKGVVLSHRNL--LANRAQVAARIdfSPEDKVFNALPVFHSF-----------GLTGGLV---------L 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 259 TTLK--PTVMCAVPRFYEKIYTAVWDKvekalahrralfNWAICVGEQHY-----QAEQPSQWLRLQYALAdklvltklr 331
Cdd:PRK06814 856 PLLSgvKVFLYPSPLHYRIIPELIYDT------------NATILFGTDTFlngyaRYAHPYDFRSLRYVFA--------- 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 332 allggrikmmpcGGAKLEASIGSFF-HSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVK------IGEEN 404
Cdd:PRK06814 915 ------------GAEKVKEETRQTWmEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRlepvpgIDEGG 982
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 EILVRGGMVMRGYYK--KP---EETakaftEDGFLRTGDVGEMDSCGNLFITDRLKELMK 459
Cdd:PRK06814 983 RLFVRGPNVMLGYLRaeNPgvlEPP-----ADGWYDTGDIVTIDEEGFITIKGRAKRFAK 1037
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
21-219 |
1.54e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 57.60 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFREQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE 100
Cdd:PRK04319 59 DKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 101 YIVNDADIKILfVGDQEQLDQVcqIANNCPQLMKIVAMKANMDLRDlpnacyweDFLDvvpneaeFEKRLN--SKQLS-- 176
Cdd:PRK04319 139 DRLEDSEAKVL-ITTPALLERK--PADDLPSLKHVLLVGEDVEEGP--------GTLD-------FNALMEqaSDEFDie 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2490830388 177 -----DLFTLIYTSGTTGEPKGVM-LDYANLAHQLNAHdLALNVNEDDV 219
Cdd:PRK04319 201 wtdreDGAILHYTSGSTGKPKGVLhVHNAMLQHYQTGK-YVLDLHEDDV 248
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
360-487 |
4.07e-08 |
|
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: 55.65 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 360 GINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVKI-------GEENEILV-----RGGMVMRGYYKKPEETAKA 427
Cdd:cd05974 225 GLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALldpdgapATEGEVALdlgdtRPVGLMKGYAGDPDKTAHA 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 428 FtEDGFLRTGDVGEMDSCGNLFITDRLKELMKTSNGKyIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:cd05974 305 M-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEAAVV 362
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
176-488 |
6.72e-08 |
|
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: 55.10 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 176 SDLFTLIYTSGTTGEPKGVMLDYANLAHQLNahDLA----LNVNEDDVSLSFlplshiferawVAYVFHrgatncyledt 251
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT--SLSeryfGRDNGDEAVLFF-----------SNYVFD----------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 NHVR---DALTT------LKPTVMCAVPRFYekiytavwdkvekALAHRRALfnwaicvgeqHYQAEQPSQWLRLQYALA 322
Cdd:cd17648 150 FFVEqmtLALLNgqklvvPPDEMRFDPDRFY-------------AYINREKV----------TYLSGTPSVLQQYDLARL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 323 DKLvltklrallggriKMMPCGGAKLEAS----IGSFFHSIGINiklGYGMTETTATVSCWQDKGFNP--NSIGTLMPNA 396
Cdd:cd17648 207 PHL-------------KRVDAAGEEFTAPvfekLRSRFAGLIIN---AYGPTETTVTNHKRFFPGDQRfdKSLGRPVRNT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 397 E----------VKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGF--------------LRTGDVGEMDSCGNLFITD 452
Cdd:cd17648 271 KcyvlndamkrVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLG 350
|
330 340 350
....*....|....*....|....*....|....*.
gi 2490830388 453 RlKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIA 488
Cdd:cd17648 351 R-NDFQVKIRGQRIEPGEVEAALASYPGVRECAVVA 385
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
391-458 |
1.01e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 54.95 E-value: 1.01e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490830388 391 TLMPNAEVKIGEeneILVRGGMVMRGYYKKPEETAKAF----------TEDG-FLRTGDVGEMdSCGNLFITDRLKELM 458
Cdd:PRK05850 388 TCIECPAGTVGE---IWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFI-SEGELFIVGRIKDLL 462
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
394-472 |
1.70e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 54.23 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 394 PNAEVKIGEEN-EILVRG--GMVM-------RGYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMkTSNG 463
Cdd:PRK10946 361 PDDEVWVADADgNPLPQGevGRLMtrgpytfRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQI-NRGG 439
|
....*....
gi 2490830388 464 KYIAPQYIE 472
Cdd:PRK10946 440 EKIAAEEIE 448
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
184-472 |
2.26e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.85 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 184 TSGTTGEPKGVMLDYANLAHQLNAHDLALNVN-EDDVSLSFLPLSHifERAWVAYV---FHRGATNCYLEDTNHVRDAL- 258
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFH--DMGMVGFLtvpMYFGAELVKVTPMDFLRDPLl 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 259 -----TTLKPTVMCAvPRF-YekiytavwdkvekALAHRRaLFNwaicvgeqhyQAEQPSQWLR-LQYAL--ADKLVLTK 329
Cdd:PRK07768 238 waeliSKYRGTMTAA-PNFaY-------------ALLARR-LRR----------QAKPGAFDLSsLRFALngAEPIDPAD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 330 LRALL--GGRIKMMPcgGAKLEAsigsffhsiginiklgYGMTETTATVScwqdkgFNP--------------------- 386
Cdd:PRK07768 293 VEDLLdaGARFGLRP--EAILPA----------------YGMAEATLAVS------FSPcgaglvvdevdadllaalrra 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 387 -----------NSIGTLMPNAEVKIGEEN----------EILVRGGMVMRGyYKKPEETAKAFTEDGFLRTGDVGEMDSC 445
Cdd:PRK07768 349 vpatkgntrrlATLGPPLPGLEVRVVDEDgqvlpprgvgVIELRGESVTPG-YLTMDGFIPAQDADGWLDTGDLGYLTEE 427
|
330 340
....*....|....*....|....*..
gi 2490830388 446 GNLFITDRLKELMKTSnGKYIAPQYIE 472
Cdd:PRK07768 428 GEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
11-228 |
2.66e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 53.72 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 11 RFRLQAKKWLNRTALRFREQaqwqEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPI 90
Cdd:PRK08279 42 VFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 91 YATNTAKQVEYIVNDADIKILFVGDqEQLDQVCQIANNCPQLMKIVAmkANMDLRDLPNAcyWEDFLDVVPNEAEFEKRL 170
Cdd:PRK08279 118 NTQQRGAVLAHSLNLVDAKHLIVGE-ELVEAFEEARADLARPPRLWV--AGGDTLDDPEG--YEDLAAAAAGAPTTNPAS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2490830388 171 NSK-QLSDLFTLIYTSGTTGEPKGV-------MLDYANLAHQLNAhdlalnvNEDDVSLSFLPLSH 228
Cdd:PRK08279 193 RSGvTAKDTAFYIYTSGTTGLPKAAvmshmrwLKAMGGFGGLLRL-------TPDDVLYCCLPLYH 251
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
34-500 |
1.82e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 50.88 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQEIdRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQVE---YIVNDADIKI 110
Cdd:PRK07769 54 RDLTWSQFGARN-RAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGrlhAVLDDCTPSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 111 LFVGDqEQLDQVCQIANNCP--QLMKIVAMKAnmdlrdLPNACyWEDFLDVVPNEaefekrlnskqlSDLFTLIYTSGTT 188
Cdd:PRK07769 133 ILTTT-DSAEGVRKFFRARPakERPRVIAVDA------VPDEV-GATWVPPEANE------------DTIAYLQYTSGST 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 189 GEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSH-------IFErawvAYVFHRgatncyledtnhvrdaLTTL 261
Cdd:PRK07769 193 RIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHdmglitvLLP----ALLGHY----------------ITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 262 KPTVMCAVPRFYEKIYTAVWDKVEKALAhrrALFNWAIcvgeQHYQA-------EQPsqwlrlqyaladkLVLTKLRALL 334
Cdd:PRK07769 253 SPAAFVRRPGRWIRELARKPGGTGGTFS---AAPNFAF----EHAAArglpkdgEPP-------------LDLSNVKGLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 335 GGRIKMMPcggakleASIGSFFHSIG------INIKLGYGMTETTATVSC--WQDKgfnPNSI---------GTLM---- 393
Cdd:PRK07769 313 NGSEPVSP-------ASMRKFNEAFApyglppTAIKPSYGMAEATLFVSTtpMDEE---PTVIyvdrdelnaGRFVevpa 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 394 --PNA------------------------EVKIGEENEILVRGGMVMRGYYKKPEETAKAF----------------TED 431
Cdd:PRK07769 383 daPNAvaqvsagkvgvsewavivdpetasELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDD 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2490830388 432 G-FLRTGDVGE-MDscGNLFITDRLKELMkTSNGKYIAPQYIEgkigkdkFIEQIAVIADAKKYVSALIVP 500
Cdd:PRK07769 463 AlWVRTGDYGVyFD--GELYITGRVKDLV-IIDGRNHYPQDLE-------YTAQEATKALRTGYVAAFSVP 523
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
397-472 |
1.82e-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: 50.84 E-value: 1.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2490830388 397 EVKIGEENEILVRGGMVMRgYYKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRlKELMKTSNGKYIAPQYIE 472
Cdd:cd05929 316 EVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIE 389
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
385-500 |
1.92e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.90 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 385 NPNSiGTLMPNAEVkigeeNEILVRGGMVMRGYYKKPEETAKAF----------------TEDG--FLRTGDVG-EMDsc 445
Cdd:PRK12476 417 DPDT-GAELPDGEV-----GEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgAADDgtWLRTGDLGvYLD-- 488
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 446 GNLFITDRLKELMkTSNGKYIAPQYIEgkigkdkfieqiAVIADA-----KKYVSALIVP 500
Cdd:PRK12476 489 GELYITGRIADLI-VIDGRNHYPQDIE------------ATVAEAspmvrRGYVTAFTVP 535
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
170-459 |
1.96e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.58 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 170 LNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHiferawvAYVFHrgatNCYLE 249
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFH-------AYGFN----SCTLF 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 250 dtnhvrdALTTLKPTVMCAVPRFYEKIYTAVWDKVEKALAHRRALFNWAicvgeqhyqaeqpsqwlrLQYALADKLVLTK 329
Cdd:PRK06334 246 -------PLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYI------------------LKTAKKQESCLPS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 330 LR-ALLGGRIkmmpCGGAKLEASIGSFFHsigINIKLGYGMTETTATVSC-WQDKGFNPNSIGTLMPNAEVKI------- 400
Cdd:PRK06334 301 LRfVVIGGDA----FKDSLYQEALKTFPH---IQLRQGYGTTECSPVITInTVNSPKHESCVGMPIRGMDVLIvseetkv 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2490830388 401 ----GEENEILVRGGMVMRGYYKkpEETAKAFTE---DGFLRTGDVGEMDSCGNLFITDRLKELMK 459
Cdd:PRK06334 374 pvssGETGLVLTRGTSLFSGYLG--EDFGQGFVElggETWYVTGDLGYVDRHGELFLKGRLSRFVK 437
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
21-237 |
2.27e-06 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 50.65 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFR--EQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYATNTAKQ 98
Cdd:cd17634 68 DRTAIIYEgdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 99 VEYIVNDADIKILFVGD-----------QEQLDQVCQiANNCPQLMKIVAMKANMDLRDLPNACYWEDFLDVVPNEAEFE 167
Cdd:cd17634 148 VAGRIIDSSSRLLITADggvragrsvplKKNVDDALN-PNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQP 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2490830388 168 KRLNSkqlSDLFTLIYTSGTTGEPKGVMLDYANLAHQLnAHDLA--LNVNEDDVSLSFLPLSHIFERAWVAY 237
Cdd:cd17634 227 EAMNA---EDPLFILYTSGTTGKPKGVLHTTGGYLVYA-ATTMKyvFDYGPGDIYWCTADVGWVTGHSYLLY 294
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
367-472 |
2.75e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 50.31 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 367 YGMTE-TTATVSCWQDKGFNPNSIGTLMPNAEVKIGEEN----------EILVRGGMVMRGYY--KKPEetakafTEDGF 433
Cdd:PRK07788 355 YGSTEvAFATIATPEDLAEAPGTVGRPPKGVTVKILDENgnevprgvvgRIFVGNGFPFEGYTdgRDKQ------IIDGL 428
|
90 100 110
....*....|....*....|....*....|....*....
gi 2490830388 434 LRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIE 472
Cdd:PRK07788 429 LSSGDVGYFDEDGLLFVDGRDDD-MIVSGGENVFPAEVE 466
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
61-500 |
4.75e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 49.71 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 61 DKIGIFannMPRWTI---ADFGA-MQARAVAVPIYaTNTAKQVEYIVNDADIKILFVGDQ-----------EQLDQVcqi 125
Cdd:PRK08043 256 ERIGLM---LPNATIsaaVIFGAsLRRRIPAMMNY-TAGVKGLTSAITAAEIKTIFTSRQfldkgklwhlpEQLTQV--- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 126 anncpQLMKIVAMKANMDLRDLpnacYWEDFLDVVPNEAEFekrlnSKQLSDLFTLIYTSGTTGEPKGVMLDYANLahql 205
Cdd:PRK08043 329 -----RWVYLEDLKDDVTTADK----LWIFAHLLMPRLAQV-----KQQPEDAALILFTSGSEGHPKGVVHSHKSL---- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 206 nahdLAlNVNE---------DDVSLSFLPLSHIFerawvayvfhrGATNCYLedTNHVRDALTTLKPTvmcavPRFYEKI 276
Cdd:PRK08043 391 ----LA-NVEQiktiadftpNDRFMSALPLFHSF-----------GLTVGLF--TPLLTGAEVFLYPS-----PLHYRIV 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 277 YTAVWDKvekalaHRRALFNWAICVGeqHY-QAEQPSQWLRLQYALAdklvltklrallggrikmmpcGGAKLEASIGS- 354
Cdd:PRK08043 448 PELVYDR------NCTVLFGTSTFLG--NYaRFANPYDFARLRYVVA---------------------GAEKLQESTKQl 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 355 FFHSIGINIKLGYGMTETTATVSCWQDKGFNPNSIGTLMPNAEVK------IGEENEILVRGGMVMRGYYK--KP----- 421
Cdd:PRK08043 499 WQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEQGGRLQLKGPNIMNGYLRveKPgvlev 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 422 --EETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKELMKtsngkyiapqyIEGKIGKDKFIEQIAVIADAKKYVSALIV 499
Cdd:PRK08043 579 ptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAK-----------IAGEMVSLEMVEQLALGVSPDKQHATAIK 647
|
.
gi 2490830388 500 P 500
Cdd:PRK08043 648 S 648
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-487 |
6.21e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.78 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 15 QAKKWLNRTALrfreqaQWQEMS--WQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIADFGAMQARAVAVPIYA 92
Cdd:PRK05691 1140 QARQTPERIAL------VWDGGSldYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDP 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 93 TNTAKQVEYIVNDADIKILF-----VGDQEQLDQVCQIAnncpqlmkivamkanMDLRDLPNacyWEDFLDVVPNEAEfe 167
Cdd:PRK05691 1214 DYPAERLAYMLADSGVELLLtqshlLERLPQAEGVSAIA---------------LDSLHLDS---WPSQAPGLHLHGD-- 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 168 krlnskqlsDLFTLIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiferawvayvFHRGATNCY 247
Cdd:PRK05691 1274 ---------NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIS-----------FDVSVWECF 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 248 LedtnhvrdALTTLKPTVMCAVPrfyekiytavwdkvEKALAHRRALFNWAICVGEQHYQAeqPSQWLRLQYALADKlvL 327
Cdd:PRK05691 1334 W--------PLITGCRLVLAGPG--------------EHRDPQRIAELVQQYGVTTLHFVP--PLLQLFIDEPLAAA--C 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 328 TKLRALLggrikmmpCGGAKLEASIGSFFHSIGINIKLG--YGMTETTATVSCWQ----DKGFNPnsIGTLMPNA--EVK 399
Cdd:PRK05691 1388 TSLRRLF--------SGGEALPAELRNRVLQRLPQVQLHnrYGPTETAINVTHWQcqaeDGERSP--IGRPLGNVlcRVL 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 400 IGEEN--------EILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGDVGEMDSCGNLFITDRLKELMKTsNGK 464
Cdd:PRK05691 1458 DAELNllppgvagELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNADGALEYLGRLDQQVKL-RGF 1536
|
490 500
....*....|....*....|...
gi 2490830388 465 YIAPQYIEGKIGKDKFIEQIAVI 487
Cdd:PRK05691 1537 RVEPEEIQARLLAQPGVAQAAVL 1559
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
179-493 |
1.11e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 48.24 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 179 FTLIYTSGTTGEPKGVMLDYANLAH--QLNAHDLALNvNEDDVSLSFLPLSHIFERAWVAyVFHRGATNCYLED--TNHV 254
Cdd:PRK07638 146 FYMGFTSGSTGKPKAFLRAQQSWLHsfDCNVHDFHMK-REDSVLIAGTLVHSLFLYGAIS-TLYVGQTVHLMRKfiPNQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 255 RDALTTLKPTVMCAVPRFYEKIYtavwdKVEKALahrralfnwaicvgeqhyqaEQPsqwlrlqyalaDKLVLTklrall 334
Cdd:PRK07638 224 LDKLETENISVMYTVPTMLESLY-----KENRVI--------------------ENK-----------MKIISS------ 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 335 ggrikmmpcgGAKLEASIGSFFHSIGINIKLG--YGMTE---TTATVScwQDKGFNPNSIGTLMPNAEVKI--------- 400
Cdd:PRK07638 262 ----------GAKWEAEAKEKIKNIFPYAKLYefYGASElsfVTALVD--EESERRPNSVGRPFHNVQVRIcneageevq 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 401 -GEENEILVRGGMVMRGYyKKPEETAKAFTEDGFLRTGDVGEMDSCGNLFITDRLKElMKTSNGKYIAPQYIEGKIGKDK 479
Cdd:PRK07638 330 kGEIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKN-MILFGGINIFPEEIESVLHEHP 407
|
330
....*....|....
gi 2490830388 480 FIEQIAVIADAKKY 493
Cdd:PRK07638 408 AVDEIVVIGVPDSY 421
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
181-465 |
1.63e-05 |
|
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: 47.46 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSHIFERAWvayvfhrgatncyledtnhvrdALTT 260
Cdd:cd05910 90 ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPAL----------------------GLTS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 261 LKPTVmcavprfyekiytavwDKVEKALAHRRALFNWAicvgeQHYQAEQ----PSQWLRL-QYALADKLVLTKLRALLG 335
Cdd:cd05910 148 VIPDM----------------DPTRPARADPQKLVGAI-----RQYGVSIvfgsPALLERVaRYCAQHGITLPSLRRVLS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 336 GrikmmpcgGAKLEASIGSFFHSI---GINIKLGYGMTE-------------TTATVSCWQDKGfnpNSIGTLMPNAEVK 399
Cdd:cd05910 207 A--------GAPVPIALAARLRKMlsdEAEILTPYGATEalpvssigsrellATTTAATSGGAG---TCVGRPIPGVRVR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 400 I-------------------GEENEILVRGGMVMRGYYKKPEETAKAFTED---GFL-RTGDVGEMDSCGNLFITDRLKE 456
Cdd:cd05910 276 IieiddepiaewddtlelprGEIGEITVTGPTVTPTYVNRPVATALAKIDDnseGFWhRMGDLGYLDDEGRLWFCGRKAH 355
|
....*....
gi 2490830388 457 LMKTSNGKY 465
Cdd:cd05910 356 RVITTGGTL 364
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
34-195 |
1.93e-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: 47.65 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 34 QEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIA----------------DFGAmqaRAVAvpiyatNTAK 97
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAmlatasigaiwsscspDFGV---PGVL------DRFG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 98 QVEyivndadIKILFVGD--------QEQLDQVCQIANNCPQLMKIVAM-----KANMDLRDLPNACYWEDFLDVVPN-E 163
Cdd:cd05943 168 QIE-------PKVLFAVDaytyngkrHDVREKVAELVKGLPSLLAVVVVpytvaAGQPDLSKIAKALTLEDFLATGAAgE 240
|
170 180 190
....*....|....*....|....*....|..
gi 2490830388 164 AEFEkRLNSKQLsdLFTLiYTSGTTGEPKGVM 195
Cdd:cd05943 241 LEFE-PLPFDHP--LYIL-YSSGTTGLPKCIV 268
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
21-205 |
2.04e-05 |
|
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: 47.63 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFR--EQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIAdfgaMQA--R--AVAVPIYATN 94
Cdd:TIGR02188 72 DKVAIIWEgdEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIA----MLAcaRigAIHSVVFGGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 95 TAKQVEYIVNDADIKILFVGDQ---------------EQLDQVCQIANNCpqlmkIVAMKANMDL------RDLpnacYW 153
Cdd:TIGR02188 148 SAEALADRINDAGAKLVITADEglrggkviplkaivdEALEKCPVSVEHV-----LVVRRTGNPVvpwvegRDV----WW 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2490830388 154 EDFLDVVPNEAEFEKrLNSKQLsdLFTLiYTSGTTGEPKGVM------LDYANLAHQL 205
Cdd:TIGR02188 219 HDLMAKASAYCEPEP-MDSEDP--LFIL-YTSGSTGKPKGVLhttggyLLYAAMTMKY 272
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
21-219 |
2.97e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.10 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 21 NRTALRFR-EQAQWQEMSWQTFQQEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIA----------------DFGAmqa 83
Cdd:PRK03584 99 DRPAIIFRgEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAmlataslgaiwsscspDFGV--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 84 RAVAvpiyatNTAKQVEyivndadIKILFVGD--------QEQLDQVCQIANNCPQLMKIVA---MKANMDLRDLPNACY 152
Cdd:PRK03584 176 QGVL------DRFGQIE-------PKVLIAVDgyryggkaFDRRAKVAELRAALPSLEHVVVvpyLGPAAAAAALPGALL 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 153 WEDFLDVVPNEA-EFEkRLNSKQlsDLFTLiYTSGTTGEPK-------GVMLDyanlahQLNAHDLALNVNEDDV 219
Cdd:PRK03584 243 WEDFLAPAEAAElEFE-PVPFDH--PLWIL-YSSGTTGLPKcivhghgGILLE------HLKELGLHCDLGPGDR 307
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
153-228 |
7.86e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 45.44 E-value: 7.86e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490830388 153 WEDFLDVVPNEaefEKRLNSKQLSDLFTLIYTSGTTGEPKGVMLDYANLA---HQLNAHdlaLNVNEDDVSLSFLPLSH 228
Cdd:PRK07867 132 WADELAAHRDA---EPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAsagVMLAQR---FGLGPDDVCYVSMPLFH 204
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
327-487 |
8.82e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 45.37 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 327 LTKLRALLGGRIKMMPCGGAKLEASIGSFFHSIGINIKLGYGMTETTATVSCWqdkgfnPNSIGTLMPNAEVKIGEEN-- 404
Cdd:PRK13383 291 LPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDA------PETVGKPVAGCPVRILDRNnr 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 405 --------EILVRGGMVMRGYykkPEETAKAFTeDGFLRTGDVGEMDSCGNLFITDRlKELMKTSNGKYIAPQYIEGKIG 476
Cdd:PRK13383 365 pvgprvtgRIFVGGELAGTRY---TDGGGKAVV-DGMTSTGDMGYLDNAGRLFIVGR-EDDMIISGGENVYPRAVENALA 439
|
170
....*....|.
gi 2490830388 477 KDKFIEQIAVI 487
Cdd:PRK13383 440 AHPAVADNAVI 450
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
136-204 |
1.03e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 45.13 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2490830388 136 VAMKANMDLrdlpnacYWEDFLDVVPNEAEFEkRLNSKQLsdLFTLiYTSGTTGEPKGVM------LDYANLAHQ 204
Cdd:PRK00174 216 VDWVEGRDL-------WWHELVAGASDECEPE-PMDAEDP--LFIL-YTSGSTGKPKGVLhttggyLVYAAMTMK 279
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
43-219 |
1.38e-04 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 44.86 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 43 QEIDRFSYALIAQHIDIQDKIGIFANNMPRWTIAdfgaMQA--R--AVAVPIYATNTAKQVEYIVNDADIKILFVGDQ-- 116
Cdd:cd05966 92 REVCRFANVLKSLGVKKGDRVAIYMPMIPELVIA----MLAcaRigAVHSVVFAGFSAESLADRINDAQCKLVITADGgy 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 117 --EQLDQVCQIAN----NCPQLMK-IVAMKAN-----MDLRDLpnacYWEDFLDVVPNEAEFEkRLNSKqlsD-LFTLiY 183
Cdd:cd05966 168 rgGKVIPLKEIVDealeKCPSVEKvLVVKRTGgevpmTEGRDL----WWHDLMAKQSPECEPE-WMDSE---DpLFIL-Y 238
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2490830388 184 TSGTTGEPKGVM------LDYANLAHQlnahdLALNVNEDDV 219
Cdd:cd05966 239 TSGSTGKPKGVVhttggyLLYAATTFK-----YVFDYHPDDI 275
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
417-516 |
2.37e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 417 YYKKPEETAKA-FTEDGFLRT-GDVGEMDSCGNLFITDRlKELMKTSNGKYIAPQYIEGKIGKDKFIEQIAVIA----DA 490
Cdd:PRK13390 362 YLNDPEKTAAAqHPAHPFWTTvGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQETENALTMHPAVHDVAVIGvpdpEM 440
|
90 100
....*....|....*....|....*...
gi 2490830388 491 KKYVSALI--VPCFDSLEEYAKQLnIKY 516
Cdd:PRK13390 441 GEQVKAVIqlVEGIRGSDELAREL-IDY 467
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
181-438 |
1.24e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.08 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 181 LIYTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLShiF----ERAWV-----AYVFHRGATNCYLEDt 251
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSIN--FdaasERLLVpllcgARVVLRAQGQWGAEE- 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 252 nhvrdalttlkptvMCAVPRfyekiytavwdkvekalAHRRALFNWAICVGEQHyqaeqpSQWLRLQYA-LADKLVLTKL 330
Cdd:PRK05691 2415 --------------ICQLIR-----------------EQQVSILGFTPSYGSQL------AQWLAGQGEqLPVRMCITGG 2457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 331 RALLGGRIKMMPCGGAKleasiGSFFHSiginiklgYGMTETT-------ATVSCWQDKGFNPnsIGTLMPN-------- 395
Cdd:PRK05691 2458 EALTGEHLQRIRQAFAP-----QLFFNA--------YGPTETVvmplaclAPEQLEEGAASVP--IGRVVGArvayilda 2522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2490830388 396 --AEVKIGEENEILVRGGMVMRGYYKKPEETAKAFTEDGF-------LRTGD 438
Cdd:PRK05691 2523 dlALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGD 2574
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
163-228 |
2.13e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 40.79 E-value: 2.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490830388 163 EAEFEKRLNSKQLSDLFTLI-YTSGTTGEPKGVMLDYANLAHQLNAHDLALNVNEDDVSLSFLPLSH 228
Cdd:PRK08308 87 ESDFTKLEAVNYLAEEPSLLqYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTH 153
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
361-447 |
4.26e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 39.81 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 361 INIKLGYGMTETTATVS------CWQDKGFNPN-----SIGTLMPNAEV------------KIGEENEILVRGGMVMRGY 417
Cdd:cd17647 250 VRIVNMYGTTETQRAVSyfevpsRSSDPTFLKNlkdvmPAGRGMLNVQLlvvnrndrtqicGIGEVGEIYVRAGGLAEGY 329
|
90 100 110
....*....|....*....|....*....|
gi 2490830388 418 YKKPEETAKAFTEDGFLRTGDVGEMDSCGN 447
Cdd:cd17647 330 RGLPELNKEKFVNNWFVEPDHWNYLDKDNN 359
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
119-199 |
8.66e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 39.16 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490830388 119 LDQVCQIANNCPQLMKIV----AMKANMDLRDLPNACYWEDFLD-VVPNEAefekrLNSKQLSdlfTLIYTSGTTGEPKG 193
Cdd:PRK10524 179 LDEAIALAQHKPRHVLLVdrglAPMARVAGRDVDYATLRAQHLGaRVPVEW-----LESNEPS---YILYTSGTTGKPKG 250
|
....*....
gi 2490830388 194 VMLD---YA 199
Cdd:PRK10524 251 VQRDtggYA 259
|
|
| |
