|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
14-603 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 712.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 14 TDLDTIYSLLAKRCERDPDDlIAQWQDDETrQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFAC 93
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDR-VALREKEDG-IWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 94 ASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQILEQIRAHSESLRYVFNFKANG---------LDAVADFGE 164
Cdd:COG1022 86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGlrddprllsLDELLALGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 165 SV-SDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFARYIQY 243
Cdd:COG1022 166 EVaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP--LGPGDRTLSFLPLAHVFERTVSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 244 VAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEKVYNAASQKAGA--GLKGRLFAKAFDHFVQWSKDEMAGGHHS 321
Cdd:COG1022 244 YALAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEagGLKRKLFRWALAVGRRYARARLAGKSPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 322 LGARIQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGR 401
Cdd:COG1022 324 LLLRLKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRAL-GIPVLEGYGLTETSPVITVNRPGDNRIGTVGP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 402 P-GCISIRLADDDELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPM 480
Cdd:COG1022 403 PlPGVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 481 EDVINTCPIVAHAVVIGDGRPFIAALIELDAEMTRSWLASQNLDIdAPMSEIATNDAVRALVQQYIDKANGNVSRAESVR 560
Cdd:COG1022 483 ENALKASPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPY-TSYAELAQDPEVRALIQEEVDRANAGLSRAEQIK 561
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 489915853 561 KFVILDEEFNQEDGTLTPSMKVVRPKVLQRYADVIDNMiYAPK 603
Cdd:COG1022 562 RFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEAL-YAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
45-587 |
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: 610.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 45 QWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIA 124
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 125 FAGDdshaqileqirahseslryvfnfkangldavadfgesvsdeeldkaigrvrADDLFTIVYTSGSTGKPKGVMLSHR 204
Cdd:cd05907 82 FVED---------------------------------------------------PDDLATIIYTSGTTGRPKGVMLSHR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 205 NFNHTVYNGYEVLNDMlyQPSRLLLFLPLAHCFA-RYIQYVAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEKV 283
Cdd:cd05907 111 NILSNALALAERLPAT--EGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVFLAVPRVWEKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 284 YNAASQKAGAGLKGRLFAKAfdhfvqwskdemagghhslgariqhsfymqtvgssirsaLGPNMKWLACGGAPLNADLAH 363
Cdd:cd05907 189 YAAIKVKAVPGLKRKLFDLA---------------------------------------VGGRLRFAASGGAPLPAELLH 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 364 FFNGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPG-CISIRLADDDELMIKGPNVFLGYYKQPQRTAEALTSDGW 442
Cdd:cd05907 230 FFRAL-GIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLpGVEVRIADDGEILVRGPNVMLGYYKNPEATAEALDADGW 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 443 LHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDGRPFIAALIELDAEMTRSWLASQN 522
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEALEAWAEEHG 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 523 lDIDAPMSEIATNDAVRALVQQYIDKANGNVSRAESVRKFVILDEEFNQEDGTLTPSMKVVRPKV 587
Cdd:cd05907 389 -IAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
45-598 |
1.58e-109 |
|
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: 343.19 E-value: 1.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 45 QWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIA 124
Cdd:cd05933 5 KWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 125 FAGDDSHAQILEQIRAHSESLRYVFNF------KANGLDAVADF---GESVSDEELDKAIGRVRADDLFTIVYTSGSTGK 195
Cdd:cd05933 85 VVENQKQLQKILQIQDKLPHLKAIIQYkeplkeKEPNLYSWDEFmelGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 196 PKGVMLSHRNFNHTVYNGYEVLnDMLYQPSR---LLLFLPLAHCFARYIQ-YVAIgSHGVVGYIPSAKRL---LAD-LRG 267
Cdd:cd05933 165 PKGVMLSHDNITWTAKAASQHM-DLRPATVGqesVVSYLPLSHIAAQILDiWLPI-KVGGQVYFAQPDALkgtLVKtLRE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 268 FKPTYLLGVPRVFEKVYN---AASQKAGaGLKGRLFAKAFDHFVQWSKDEMAGGHHSLGariqhSFYM--QTVGSSIRSA 342
Cdd:cd05933 243 VRPTAFMGVPRVWEKIQEkmkAVGAKSG-TLKRKIASWAKGVGLETNLKLMGGESPSPL-----FYRLakKLVFKKVRKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 343 LG-PNMKWLACGGAPLNADLAHFFNGFDgITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGCIS-IRLADDD---EL 415
Cdd:cd05933 317 LGlDRCQKFFTGAAPISRETLEFFLSLN-IPIMELYGMSETSGPHTISNPQAYRLLSCGKalPGCKTkIHNPDADgigEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 416 MIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINT-CPIVAHAV 494
Cdd:cd05933 396 CFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKeLPIISNAM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 495 VIGDGRPFIAALIELDAEMT------RSWLAS------QNLDIDAP-MSEIAT--NDAVRALVQQYIDKANGN-VSRAES 558
Cdd:cd05933 476 LIGDKRKFLSMLLTLKCEVNpetgepLDELTEeaiefcRKLGSQATrVSEIAGgkDPKVYEAIEEGIKRVNKKaISNAQK 555
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 489915853 559 VRKFVILDEEFNQEDGTLTPSMKVVRPKVLQRYADVIDNM 598
Cdd:cd05933 556 IQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKL 595
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
50-601 |
1.12e-108 |
|
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: 339.19 E-value: 1.12e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 50 SAGQMNDRVREVAKGLLGLGVK--PGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIV--AEVEPVIAF 125
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILnhAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AGddshaqileqirahseslryvfnFKANGLDAVADFGEsvsdeeldKAIGRV---RADDLFTIVYTSGSTGKPKGVMLS 202
Cdd:cd05927 87 AG-----------------------VKVYSLEEFEKLGK--------KNKVPPpppKPEDLATICYTSGTTGNPKGVMLT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 203 HRNFNHTVYNGYEVLND--MLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIP-SAKRLLADLRGFKPTYLLGVPRV 279
Cdd:cd05927 136 HGNIVSNVAGVFKILEIlnKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgDIRLLLDDIKALKPTVFPGVPRV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 280 FEKVYNA--ASQKAGAGLKGRLFAKAFDHFVQWSKdemagghhsLGARIQHSFYMQTVGSSIRSALGPNMKWLACGGAPL 357
Cdd:cd05927 216 LNRIYDKifNKVQAKGPLKRKLFNFALNYKLAELR---------SGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 358 NADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPG-CISIRL---------ADDD----ELMIKGPNVF 423
Cdd:cd05927 287 SPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLpCAEVKLvdvpemnydAKDPnprgEVCIRGPNVF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 424 LGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDG-RPF 502
Cdd:cd05927 367 SGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSlKSF 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 503 IAALIELDAEMTRSWLASQNLdIDAPMSEIATNDAVRALVQQYID---KANGnVSRAESVRKFVILDEEFNQEDGTLTPS 579
Cdd:cd05927 447 LVAIVVPDPDVLKEWAASKGG-GTGSFEELCKNPEVKKAILEDLVrlgKENG-LKGFEQVKAIHLEPEPFSVENGLLTPT 524
|
570 580
....*....|....*....|..
gi 489915853 580 MKVVRPKVLQRYADVIDNMiYA 601
Cdd:cd05927 525 FKLKRPQLKKYYKKQIDEM-YK 545
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
23-470 |
4.53e-94 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 296.92 E-value: 4.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 23 LAKRCERDPDDlIAqWQDDETRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVP 102
Cdd:pfam00501 1 LERQAARTPDK-TA-LEVGEGRRL---TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 103 VYETDSPKQTGDIVAEVEPVIAFAGDDSHAQILEQIRAHSESLRYVFNFKANGLDAVADF-GESVSDEELDKAIGRVRAD 181
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLpEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQP--SRLLLFLPLAHCFAR-YIQYVAIGSHGVVGYIP-- 256
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpdDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPgf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 257 ---SAKRLLADLRGFKPTYLLGVPRVFEKVYNAASQKagaglkgrlfakafdhfvqwskdemagghhslgariqhsfymQ 333
Cdd:pfam00501 236 palDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPK------------------------------------------R 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 334 TVGSSIRsalgpnmkWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQ---DANEVGSVGRP-GCISIRL 409
Cdd:pfam00501 274 ALLSSLR--------LVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPldeDLRSLGSVGRPlPGTEVKI 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 410 ADDD-----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITA 470
Cdd:pfam00501 346 VDDEtgepvppgepgELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
49-587 |
1.21e-91 |
|
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: 292.34 E-value: 1.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPvyetdspkqtgdivaevepviafAGD 128
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV-----------------------RGS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQILEQIRAHSESlryvfnfkangldaVADFGESvsdeeldkaigrvRADDLFTIVYTSGSTGKPKGVMLSHRNFNH 208
Cdd:cd17640 63 DSSVEELLYILNHSES--------------VALVVEN-------------DSDDLATIIYTSGTTGNPKGVMLTHANLLH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 209 TVYNgyevLNDMLyQPS---RLLLFLPLAHCFARYIQYVAIgSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEKVYN 285
Cdd:cd17640 116 QIRS----LSDIV-PPQpgdRFLSILPIWHSYERSAEYFIF-ACGCSQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 286 AASQKAGAGLKGRLFakafdhfvqwskdemagghhslgarIQHSFymqtvgssirsALGPNMKWLACGGAPLNADLAHFF 365
Cdd:cd17640 190 GIQKQVSKSSPIKQF-------------------------LFLFF-----------LSGGIFKFGISGGGALPPHVDTFF 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 366 NGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGcISIRLADDD-----------ELMIKGPNVFLGYYKQPQR 432
Cdd:cd17640 234 EAI-GIEVLNGYGLTETSPVVSARRLKCNVRGSVGRplPG-TEIKIVDPEgnvvlppgekgIVWVRGPQVMKGYYKNPEA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 433 TAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDGRPFIAALIELDAE 512
Cdd:cd17640 312 TSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNFE 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489915853 513 MTRSWLASQNLDIDAPMSEIATNDAVRALVQQ----YIDKANGnVSRAESVRKFVILDEEFnQEDGTLTPSMKVVRPKV 587
Cdd:cd17640 392 ELEKWAKESGVKLANDRSQLLASKKVLKLYKNeikdEISNRPG-FKSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
47-587 |
3.40e-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: 287.19 E-value: 3.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSpkqtgdivaevEPVIAFA 126
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLG-----------EDALIHS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 127 GDDSHAQILeqirahseslryvfnfkangldavadfgesVSDEEldkaigrvrADDLFTIVYTSGSTGKPKGVMLSHRNF 206
Cdd:cd17639 73 LNETECSAI------------------------------FTDGK---------PDDLACIMYTSGSTGNPKGVMLTHGNL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 207 NHTVYNGYEVLNDMLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYiPSAKRLL--------ADLRGFKPTYLLGVPR 278
Cdd:cd17639 114 VAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY-GSPRTLTdkskrgckGDLTEFKPTLMVGVPA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 279 VFEKVYNAASQK--AGAGLKGRLFAKAFdhfvqWSKdeMAGGHHSLGAriqhSFYMQTVGSSIRSALGPNMKWLACGGAP 356
Cdd:cd17639 193 IWDTIRKGVLAKlnPMGGLKRTLFWTAY-----QSK--LKALKEGPGT----PLLDELVFKKVRAALGGRLRYMLSGGAP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 357 LNADLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGRP-GCISIRLADDD-------------ELMIKGPNV 422
Cdd:cd17639 262 LSADTQEFLNIV-LCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPlPCCEIKLVDWEeggystdkppprgEILIRGPNV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 423 FLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDG-RP 501
Cdd:cd17639 341 FKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPdKS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 502 FIAALIELDAEMTRSWlASQNLDIDAPMSEIATNDAVRALVQ---QYIDKANGnVSRAESVRKFVILDEEFNQEDGTLTP 578
Cdd:cd17639 421 YPVAIVVPNEKHLTKL-AEKHGVINSEWEELCEDKKLQKAVLkslAETARAAG-LEKFEIPQGVVLLDEEWTPENGLVTA 498
|
....*....
gi 489915853 579 SMKVVRPKV 587
Cdd:cd17639 499 AQKLKRKEI 507
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
19-593 |
2.80e-86 |
|
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: 277.85 E-value: 2.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 19 IYSLLAKRCERDPDDLIAqwqddeTRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGA 98
Cdd:COG0318 1 LADLLRRAAARHPDRPAL------VFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 99 VSVPVYETDSPKQTGDIVAEVEPVIAFAgddshaqileqirahseslryvfnfkangldavadfgesvsdeeldkaigrv 178
Cdd:COG0318 75 VVVPLNPRLTAEELAYILEDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 179 raddlFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFARYIQ---YVAIGSHGVVGYI 255
Cdd:COG0318 103 -----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPGDVVLVALPLFHVFGLTVGllaPLLAGATLVLLPR 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 256 PSAKRLLADLRGFKPTYLLGVPRVFEKVYNAAsQKAGAGLkgrlfakafdhfvqwskdemagghhslgariqhsfymqtv 335
Cdd:COG0318 176 FDPERVLELIERERVTVLFGVPTMLARLLRHP-EFARYDL---------------------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 336 gSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANE--VGSVGRP-GCISIRLADD 412
Cdd:COG0318 215 -SSLRLVV--------SGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGErrPGSVGRPlPGVEVRIVDE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 413 D----------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMED 482
Cdd:COG0318 286 DgrelppgevgEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEE 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 483 VINTCPIVAHAVVIGDGRPF----IAALIELDAemtrswlasqnldiDAPMSEiatnDAVRALVQQyidkangNVSRAES 558
Cdd:COG0318 364 VLAAHPGVAEAAVVGVPDEKwgerVVAFVVLRP--------------GAELDA----EELRAFLRE-------RLARYKV 418
|
570 580 590
....*....|....*....|....*....|....*..
gi 489915853 559 VRKFVILDEefnqedgtL--TPSMKVVRPKVLQRYAD 593
Cdd:COG0318 419 PRRVEFVDE--------LprTASGKIDRRALRERYAA 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
46-591 |
5.84e-84 |
|
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: 275.46 E-value: 5.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 46 WHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAF 125
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AGDDSHAQILEQIRAHSESLRYVFNFKANGL-----DAVADFGESVS---------DEELDKAIGRVRADDLFTIVYTSG 191
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYCDPRGMrkyddPRLISFEDVVAlgraldrrdPGLYEREVAAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 192 STGKPKGVMLSHRNFNHTVYNGYEVlnDMLYQPSRLLLFLPLAhcfarYI--QYVAIG----SHGVVGYIPSAKRLLADL 265
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGHCAAYLAA--DPLGPGDEYVSVLPLP-----WIgeQMYSVGqalvCGFIVNFPEEPETMMEDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 266 RGFKPTYLLGVPRVFEKVY-NAASQKAGAG-LKGRLFAKAFDHFVQWSKDEMAGGHHSLGARIQHSFYMQTVGSSIRSAL 343
Cdd:cd17641 242 REIGPTFVLLPPRVWEGIAaDVRARMMDATpFKRFMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPLRDRL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 344 G-PNMKWLACGGAPLNADLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGRP-GCISIRLADDDELMIKGPN 421
Cdd:cd17641 322 GfSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPfPGTEVRIDEVGEILVRSPG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 422 VFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDGRP 501
Cdd:cd17641 401 VFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 502 FIAALIELDAEMTRSWlASQNLDIDAPMSEIATNDAVRALVQQYIDKANGNVSRAESVRKFVILDEEFNQEDGTLTPSMK 581
Cdd:cd17641 481 YLTAFICIDYAIVGKW-AEQRGIAFTTYTDLASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELTRTRK 559
|
570
....*....|
gi 489915853 582 VVRPKVLQRY 591
Cdd:cd17641 560 VRRGVIAEKY 569
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
44-591 |
3.19e-83 |
|
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: 271.65 E-value: 3.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 44 RQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVI 123
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 124 AFAG--DDSHAQ---ILEQIRAHSESLRYVFNFKaNGLDAVADFGESVSDEELDKAigrvraDDLFTIVYTSGSTGKPKG 198
Cdd:cd05932 82 LFVGklDDWKAMapgVPEGLISISLPPPSAANCQ-YQWDDLIAQHPPLEERPTRFP------EQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 199 VMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFAR-YIQYVAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVP 277
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIG--TEENDRMLSYLPLAHVTERvFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTLFFSVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 278 RVfekvynaasqkagaglkgrlfakafdhfvqWSKDEMaGGHHSLG-ARIQHSFYMQTVGSSIR----SALGPN-MKWLA 351
Cdd:cd05932 233 RL------------------------------WTKFQQ-GVQDKIPqQKLNLLLKIPVVNSLVKrkvlKGLGLDqCRLAG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 352 CGGAPLNADLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGCiSIRLADDDELMIKGPNVFLGYYKQ 429
Cdd:cd05932 282 CGSAPVPPALLEWYRSL-GLNILEAYGMTENFAYSHLNYPGRDKIGTVGNagPGV-EVRISEDGEILVRSPALMMGYYKD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 430 PQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDGRPFIAALIEL 509
Cdd:cd05932 360 PEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 510 DAEMTRSWLASqnldidapmseiaTNDAVRALVQQYIDKANGNVSRAESVRKFVILDEEFNQEDGTLTPSMKVVRPKVLQ 589
Cdd:cd05932 440 SEEARLRADAF-------------ARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEK 506
|
..
gi 489915853 590 RY 591
Cdd:cd05932 507 AY 508
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
7-601 |
2.20e-79 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 265.42 E-value: 2.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 7 VDTIYQTTDLDTIYSLLAKRCERDPDD--LIAQWQDDET---RQWhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAA 81
Cdd:PLN02736 34 VSRFPDHPEIGTLHDNFVYAVETFRDYkyLGTRIRVDGTvgeYKW--MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 82 TCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIV--AEVEPViaFAGDDSHAQILEQIrAHSESLRYVFNFkaNGLDAV 159
Cdd:PLN02736 112 NRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVnhAEVAAI--FCVPQTLNTLLSCL-SEIPSVRLIVVV--GGADEP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 160 -----ADFG-ESVSDEELdKAIGRV--------RADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVyNGYEVLNDmLYQPS 225
Cdd:PLN02736 187 lpslpSGTGvEIVTYSKL-LAQGRSspqpfrppKPEDVATICYTSGTTGTPKGVVLTHGNLIANV-AGSSLSTK-FYPSD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 226 RLLLFLPLAHCFARYIQYVAIgSHGV-VG-YIPSAKRLLADLRGFKPTYLLGVPRVFEKVYNA--ASQKAGAGLKGRLFA 301
Cdd:PLN02736 264 VHISYLPLAHIYERVNQIVML-HYGVaVGfYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGitNAVKESGGLKERLFN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 302 KAFDHfvqwSKDEMAGGhhslgaRIQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTE 381
Cdd:PLN02736 343 AAYNA----KKQALENG------KNPSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 382 TAapCLVNFQDA--NEVGSVGRPG-CISIRLAD--------DD------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLH 444
Cdd:PLN02736 413 TS--CVISGMDEgdNLSGHVGSPNpACEVKLVDvpemnytsEDqpyprgEICVRGPIIFKGYYKDEVQTREVIDEDGWLH 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 445 TGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDG-RPFIAALIELDAEMTRSWLASQNL 523
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSlNSSLVAVVVVDPEVLKAWAASEGI 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 524 DIDApMSEIATNDAVRALVQQYIDkangNVSRAESVRKF-----VIL-DEEFNQEDGTLTPSMKVVRPKVLQRYADVIDN 597
Cdd:PLN02736 571 KYED-LKQLCNDPRVRAAVLADMD----AVGREAQLRGFefakaVTLvPEPFTVENGLLTPTFKVKRPQAKAYFAKAISD 645
|
....
gi 489915853 598 MiYA 601
Cdd:PLN02736 646 M-YA 648
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
18-519 |
5.97e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 242.01 E-value: 5.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIAQWQDDETrqwhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRT------TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVYETDSPKQTGDIVAEVEPVIAFAgDDSHAQILEQIRAHSESLRYV----FNFKANGLDAVADFGESVSDEELDK 173
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLV-DSEFVPLLAAILPQLPTVRTVivegDGPAAPLAPEVGEYEELLAAASDTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 174 AIGRVRADDLFTIVYTSGSTGKPKGVMLSHRN-FNHTVYngyeVLNDMLYQPS-RLLLFLPLAHCFARYIQYVAIGsHGV 251
Cdd:PRK06187 160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNlFLHSLA----VCAWLKLSRDdVYLVIVPMFHVHAWGLPYLALM-AGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 252 VGYIP---SAKRLLADLRGFKPTYLLGVPrvfeKVYNAasqkagaglkgrLFAKAFDHFVQWSKdemagghhslgariqh 328
Cdd:PRK06187 235 KQVIPrrfDPENLLDLIETERVTFFFAVP----TIWQM------------LLKAPRAYFVDFSS---------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 sfymqtvgssirsalgpnMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAaPCLV----NFQDANEV---GSVGR 401
Cdd:PRK06187 283 ------------------LRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETS-PVVSvlppEDQLPGQWtkrRSAGR 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 402 PGC-ISIRLADDD------------ELMIKGPNVFLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFITGRKKDIII 468
Cdd:PRK06187 344 PLPgVEARIVDDDgdelppdggevgEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVII 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915853 469 TaGGKNISPAPMEDVINTCPIVAHAVVIG------DGRPFiaALI------ELDAEMTRSWLA 519
Cdd:PRK06187 423 S-GGENIYPRELEDALYGHPAVAEVAVIGvpdekwGERPV--AVVvlkpgaTLDAKELRAFLR 482
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
69-584 |
2.05e-70 |
|
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: 236.18 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 69 GVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPvyetdspkqtgdIVAEvepviafagddSHAQILEQIRAHSESlRYV 148
Cdd:cd05914 28 GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVP------------ILAE-----------FTADEVHHILNHSEA-KAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 149 FnfkangldavadfgesVSDEeldkaigrvraDDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVlnDMLYQPSRLL 228
Cdd:cd05914 84 F----------------VSDE-----------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEV--VLLGKGDKIL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 229 LFLPLAH---CFARYIQYVAIGSHGV-VGYIPSAKRLLADLRGFKPTYLLGVPRVFEKVYNAA--SQKAGAGLKGRLFAK 302
Cdd:cd05914 135 SILPLHHiypLTFTLLLPLLNGAHVVfLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDiiPKLTLKKFKFKLAKK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 303 AFDHfvqwskdemagghhslgaRIQHsfymqTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFdGITFIQGYGMTET 382
Cdd:cd05914 215 INNR------------------KIRK-----LAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTET 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 383 AApcLVNFQDANEV--GSVGRP-GCISIRLADDD------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDD 453
Cdd:cd05914 271 AP--IISYSPPNRIrlGSAGKViDGVEVRIDSPDpatgegEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 454 RGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHA-VVIGDGRpfIAALIELDAEMTRSWLASQNLDIDAPMSEI 532
Cdd:cd05914 349 EGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESlVVVQEKK--LVALAYIDPDFLDVKALKQRNIIDAIKWEV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489915853 533 atndavralvqqyIDKANGNVSRAESVRKFVILDEEFNQedgtlTPSMKVVR 584
Cdd:cd05914 427 -------------RDKVNQKVPNYKKISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
15-598 |
1.05e-68 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 237.02 E-value: 1.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 15 DLDTIYSLLAKRCERDPDDLIAQWqddetRQWHDVSAG--------QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEW 86
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGW-----RRIVDGKVGpymwktykEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 87 GVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQILEQIRAHSESLRYVFNFKangldavadfgeSV 166
Cdd:PLN02430 115 IVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFT------------SV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 167 SDEELDKA---------------IGRVRADDLF--------TIVYTSGSTGKPKGVMLSHRN---FNHTVYNGYEVLNDM 220
Cdd:PLN02430 183 TEEESDKAsqigvktyswidflhMGKENPSETNppkpldicTIMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 221 LYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSAKRLLA-DLRGFKPTYLLGVPRVFEKVYNAAsQKAGAGL---K 296
Cdd:PLN02430 263 MTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRdDLMELKPTLLAGVPRVFERIHEGI-QKALQELnprR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 297 GRLFAKAFDHFVQWSKdemAGGHHSLGARIQHSFYMQTVgssiRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQG 376
Cdd:PLN02430 342 RLIFNALYKYKLAWMN---RGYSHKKASPMADFLAFRKV----KAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 377 YGMTETAAPCLVNFQD-ANEVGSVGRPG-CISIRLAD-------------DDELMIKGPNVFLGYYKQPQRTAEALtSDG 441
Cdd:PLN02430 415 YGLTETLGPTTLGFPDeMCMLGTVGAPAvYNELRLEEvpemgydplgeppRGEICVRGKCLFSGYYKNPELTEEVM-KDG 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 442 WLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDG-RPFIAALIELDAEMTRSWlaS 520
Cdd:PLN02430 494 WFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSfKSMLVAVVVPNEENTNKW--A 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 521 QNLDIDAPMSEIATNDavraLVQQYIDKANGNVSRAESVRKF-----VILDEE-FNQEDGTLTPSMKVVRPKVLQRYADV 594
Cdd:PLN02430 572 KDNGFTGSFEELCSLP----ELKEHILSELKSTAEKNKLRGFeyikgVILETKpFDVERDLVTATLKKRRNNLLKYYQVE 647
|
....
gi 489915853 595 IDNM 598
Cdd:PLN02430 648 IDEM 651
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
19-501 |
4.82e-68 |
|
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: 230.14 E-value: 4.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 19 IYSLLAKRCERDPDDlIAQWQDDETrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGA 98
Cdd:cd05936 1 LADLLEEAARRFPDK-TALIFMGRK-----LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 99 VSVPVyetdSPKQTGDivaEVEPVIafagDDSHAQILEQIRAhseslryvfnFKanglDAVADFGESVSDEELDkaigrv 178
Cdd:cd05936 75 VVVPL----NPLYTPR---ELEHIL----NDSGAKALIVAVS----------FT----DLLAAGAPLGERVALT------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 179 rADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRLLLFLPLAHCFAR---YIQYVAIGSHGVVGYI 255
Cdd:cd05936 124 -PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLtvaLLLPLALGATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 256 PSAKRLLADLRGFKPTYLLGVPRVFEKVYNAAsqkagaGLKGRLFakafdhfvqwskdemagghhslgariqhsfymqtv 335
Cdd:cd05936 203 FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAP------EFKKRDF----------------------------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 336 gSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVN-FQDANEVGSVGRP--GcISIRLADD 412
Cdd:cd05936 242 -SSLRLCI--------SGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNpLDGPRKPGSIGIPlpG-TEVKIVDD 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 413 D----------ELMIKGPNVFLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFITGRKKDIIItAGGKNISPAPMED 482
Cdd:cd05936 312 DgeelppgevgELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVEE 389
|
490
....*....|....*....
gi 489915853 483 VINTCPIVAHAVVIGDGRP 501
Cdd:cd05936 390 VLYEHPAVAEAAVVGVPDP 408
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
23-497 |
1.56e-67 |
|
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: 227.88 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 23 LAKRCERDPDdLIAQWQDDETRQWHdvsagQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVP 102
Cdd:cd17631 1 LRRRARRHPD-RTALVFGGRSLTYA-----ELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 103 VyetdspkqtgdivaevepviafagddshaqileQIRAHSESLRYVfnfkangldaVADFGesvsdeeldkaiGRVRADD 182
Cdd:cd17631 75 L---------------------------------NFRLTPPEVAYI----------LADSG------------AKVLFDD 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 183 LFTIVYTSGSTGKPKGVMLSHRNFNHTVYN---GYEVLNDmlyqpSRLLLFLPLAHCFARYIQYVAIGSHGVVGYI---P 256
Cdd:cd17631 100 LALLMYTSGTTGRPKGAMLTHRNLLWNAVNalaALDLGPD-----DVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIlrkF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 257 SAKRLLADLRGFKPTYLLGVPRVFEKVynaasqkagaglkgrlfakafdhfvqwskdemagghhslgarIQHSFYMQTVG 336
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQAL------------------------------------------LQHPRFATTDL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 337 SSIRsalgpnmkWLACGGAPLNADLAHFFNGFdGITFIQGYGMTETAAP-CLVNFQDANE-VGSVGRP--GCiSIRLADD 412
Cdd:cd17631 213 SSLR--------AVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGvTFLSPEDHRRkLGSAGRPvfFV-EVRIVDP 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 413 D----------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMED 482
Cdd:cd17631 283 DgrevppgevgEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVED 360
|
490
....*....|....*
gi 489915853 483 VINTCPIVAHAVVIG 497
Cdd:cd17631 361 VLYEHPAVAEVAVIG 375
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
36-497 |
8.61e-65 |
|
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: 222.09 E-value: 8.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 36 AQWQDDETRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSPKQTGDI 115
Cdd:cd05911 1 AQIDADTGKEL---TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA----NPIYTADE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 116 VA----EVEPVIAFagddSHAQILEQIRAHSESLR-----YVFNFKANGLDAVADFGESVSDEEL--DKAIGRVRADDLF 184
Cdd:cd05911 74 LAhqlkISKPKVIF----TDPDGLEKVKEAAKELGpkdkiIVLDDKPDGVLSIEDLLSPTLGEEDedLPPPLKDGKDDTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 185 TIVYTSGSTGKPKGVMLSHRNF--NHTVYNGYEVLNDmlYQPSRLLLFLPLAH--CFARYIQYVAIGSHGVVGYIPSAKR 260
Cdd:cd05911 150 AILYSSGTTGLPKGVCLSHRNLiaNLSQVQTFLYGND--GSNDVILGFLPLYHiyGLFTTLASLLNGATVIIMPKFDSEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 261 LLADLRGFKPTYLLGVPRvfekvynaasqkagaglkgrlfakafdHFVQWSKDEMAgghhslgarIQHSFymqtvgssir 340
Cdd:cd05911 228 FLDLIEKYKITFLYLVPP---------------------------IAAALAKSPLL---------DKYDL---------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 341 salgPNMKWLACGGAPLNADLAHFFNG-FDGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGCiSIRLADDD---- 413
Cdd:cd05911 262 ----SSLRVILSGGAPLSKELQELLAKrFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRllPNV-EAKIVDDDgkds 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 -------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINT 486
Cdd:cd05911 337 lgpnepgEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAVLLE 415
|
490
....*....|.
gi 489915853 487 CPIVAHAVVIG 497
Cdd:cd05911 416 HPGVADAAVIG 426
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
41-595 |
1.14e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 221.39 E-value: 1.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 41 DETRqwhDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVY-------------ETD 107
Cdd:PTZ00216 117 NETR---YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYanlgedalayalrETE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 108 SPKqtgdIV---AEVEPVIAFagddshaqiLEQIRAHSESLRYV----FNFKANGLDAVA-----DFGESvsdeELDKAI 175
Cdd:PTZ00216 194 CKA----IVcngKNVPNLLRL---------MKSGGMPNTTIIYLdslpASVDTEGCRLVAwtdvvAKGHS----AGSHHP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 176 GRV--RADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPS---RLLLFLPLAHC--FARYIQYVAIGS 248
Cdd:PTZ00216 257 LNIpeNNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEedeTYCSYLPLAHImeFGVTNIFLARGA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 249 HgvVGYiPSAKRLL-------ADLRGFKPTYLLGVPRVFEKVYNAASQK---AGAgLKGRLFAKAFDHFVQWSKDEMagg 318
Cdd:PTZ00216 337 L--IGF-GSPRTLTdtfarphGDLTEFRPVFLIGVPRIFDTIKKAVEAKlppVGS-LKRRVFDHAYQSRLRALKEGK--- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 319 hhslgariQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDGItFIQGYGMTETAAPCLVNFQDANEVGS 398
Cdd:PTZ00216 410 --------DTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVCCGGIQRTGDLEPNA 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 399 VGR--PGCiSIRLADDD------------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKK 464
Cdd:PTZ00216 481 VGQllKGV-EMKLLDTEeykhtdtpeprgEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 465 DIIITAGGKNISPAPMEDVINTCPIVAH---AVVIGDGRPFIAALIELDAEMTRSWlASQNlDIDAPMSEIATNDAVRAL 541
Cdd:PTZ00216 560 ALAKNCLGEYIALEALEALYGQNELVVPngvCVLVHPARSYICALVLTDEAKAMAF-AKEH-GIEGEYPAILKDPEFQKK 637
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 542 VQQYIDKANGNVSRA--ESVRKFVILDEEFNQEDGTLTPSMKVVRPKVLQRYADVI 595
Cdd:PTZ00216 638 ATESLQETARAAGRKsfEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLI 693
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
17-497 |
5.16e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 213.52 E-value: 5.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 17 DTIYSLLAKRCERDPDD--LIAQWQDdetRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACA 94
Cdd:PRK08315 16 QTIGQLLDRTAARYPDReaLVYRDQG---LRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 95 SIGAVSV---PVYETdspkqtgdivAEVEPVIAFAG-----------DDSHAQILEQIR---AHSE----------SLRY 147
Cdd:PRK08315 90 KIGAILVtinPAYRL----------SELEYALNQSGckaliaadgfkDSDYVAMLYELApelATCEpgqlqsarlpELRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 148 VF---NFKANGL---DAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFnhtVYNGYEVLNDML 221
Cdd:PRK08315 160 VIflgDEKHPGMlnfDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNI---LNNGYFIGEAMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 222 YQPS-RLLLFLPLAHCFARYIQYVAIGSHGVVGYIPsakrlladLRGFKP------------TYLLGVPRVFEkvynaas 288
Cdd:PRK08315 237 LTEEdRLCIPVPLYHCFGMVLGNLACVTHGATMVYP--------GEGFDPlatlaaveeercTALYGVPTMFI------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 289 qkagAGLKGRLFAKaFDHfvqwskdemagghhslgariqhsfymqtvgSSIRSALgpnMkwlacGGAP--------LNAD 360
Cdd:PRK08315 302 ----AELDHPDFAR-FDL------------------------------SSLRTGI---M-----AGSPcpievmkrVIDK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 361 LahffnGFDGITFiqGYGMTETaAPclVNFQ----DANE--VGSVGRPG-CISIRLADDD-----------ELMIKGPNV 422
Cdd:PRK08315 339 M-----HMSEVTI--AYGMTET-SP--VSTQtrtdDPLEkrVTTVGRALpHLEVKIVDPEtgetvprgeqgELCTRGYSV 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 423 FLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK08315 409 MKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIEEFLYTHPKIQDVQVVG 482
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
182-521 |
7.12e-61 |
|
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: 206.75 E-value: 7.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMlyQPSRLLLFLPLAHCFARYIQYVAIgSHG---VVGYIPSA 258
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT--EGDVFLSTLPLFHIGGLFGLLGAL-LAGgtvVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 259 KRLLADLRGFKPTYLLGVPRVFEkvynaasqkagaglkgRLFakafdhfvqwskDEMAGGHHSLgariqhsfymqtvgSS 338
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLA----------------RLL------------KAPESAGYDL--------------SS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 339 IRSalgpnmkwLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEV--GSVGRPG-CISIRLADDD-- 413
Cdd:cd04433 116 LRA--------LVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARkpGSVGRPVpGVEVRIVDPDgg 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 --------ELMIKGPNVFLGYYKQPQRTAEAlTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVIN 485
Cdd:cd04433 188 elppgeigELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVLL 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489915853 486 TCPIVAHAVVIG----DGRPFIAALIEL------DAEMTRSWLASQ 521
Cdd:cd04433 266 GHPGVAEAAVVGvpdpEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
14-598 |
5.37e-60 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 213.17 E-value: 5.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 14 TDLDTIYSLLAKRCERDPDD-LIAQwqddetRQWHDVSAG--------QMNDRVREVAKGLLGLGVKPGSMVVIYAATCY 84
Cdd:PLN02861 40 ADIDSPWQFFSDAVKKYPNNqMLGR------RQVTDSKVGpyvwltykEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 85 EWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQILEQIRAHSESLRYVFNF---------KANG 155
Cdd:PLN02861 114 EWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFgdvsseqkeEAEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 156 LdAVADFG--ESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLShrnfNHTVYNGYEVLNDMLYQPSRLLL---- 229
Cdd:PLN02861 194 L-GVSCFSweEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILT----NRAIIAEVLSTDHLLKVTDRVATeeds 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 230 ---FLPLAHCFARYIQYVAIGSHGVVGYIPSAKR-LLADLRGFKPTYLLGVPRVFEKVYNAASQK--AGAGLKGRLFAKA 303
Cdd:PLN02861 269 yfsYLPLAHVYDQVIETYCISKGASIGFWQGDIRyLMEDVQALKPTIFCGVPRVYDRIYTGIMQKisSGGMLRKKLFDFA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 304 FDHFVQ-----WSKDEMAgghhslgariqhSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYG 378
Cdd:PLN02861 349 YNYKLGnlrkgLKQEEAS------------PRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 379 MTETAAPCLVNFQDA-NEVGSVGRP-GCISIRLAD-------------DDELMIKGPNVFLGYYKQPQRTAEALtSDGWL 443
Cdd:PLN02861 417 LTESCGGCFTSIANVfSMVGTVGVPmTTIEARLESvpemgydalsdvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWF 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 444 HTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDG-RPFIAALIELDAEMTRSWLASQN 522
Cdd:PLN02861 496 HTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSfESFLVAVVVPDRQALEDWAANNN 575
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489915853 523 LDIDapMSEIATNDAVRALVQQYIDKANGNVS-RAESVRKFVILDEE-FNQEDGTLTPSMKVVRPKVLQRYADVIDNM 598
Cdd:PLN02861 576 KTGD--FKSLCKNLKARKYILDELNSTGKKLQlRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLKYYKDCIDQL 651
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
53-598 |
2.96e-59 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 211.03 E-value: 2.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHA 132
Cdd:PLN02614 84 EVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKIS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 133 QILEQIRAHSESLRYVFNF---KANGLDAVADFGESVS--DEELDKAIGRV------RADDLFTIVYTSGSTGKPKGVML 201
Cdd:PLN02614 164 ELFKTCPNSTEYMKTVVSFggvSREQKEEAETFGLVIYawDEFLKLGEGKQydlpikKKSDICTIMYTSGTTGDPKGVMI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 202 SHRNFNHTVYNGYEVL---NDMLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIP-SAKRLLADLRGFKPTYLLGVP 277
Cdd:PLN02614 244 SNESIVTLIAGVIRLLksaNAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRgDVKLLIEDLGELKPTIFCAVP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 278 RVFEKVYNAASQKAGAGlkGRLFAKAFDHFVQWSKDEMAGGHHSLGARiqhSFYMQTVGSSIRSALGPNMKWLACGGAPL 357
Cdd:PLN02614 324 RVLDRVYSGLQKKLSDG--GFLKKFVFDSAFSYKFGNMKKGQSHVEAS---PLCDKLVFNKVKQGLGGNVRIILSGAAPL 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 358 NADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDA-NEVGSVGRP-GCISIRLAD-------------DDELMIKGPNV 422
Cdd:PLN02614 399 ASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDElDMLGTVGPPvPNVDIRLESvpemeydalastpRGEICIRGKTL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 423 FLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDG-RP 501
Cdd:PLN02614 479 FSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSfES 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 502 FIAALIELDAEMTRSWLASQNLDIDapMSEIATNDAVRALV-QQYIDKANGNVSRAESVRKFVILDE-EFNQEDGTLTPS 579
Cdd:PLN02614 558 FLVAIANPNQQILERWAAENGVSGD--YNALCQNEKAKEFIlGELVKMAKEKKMKGFEIIKAIHLDPvPFDMERDLLTPT 635
|
570
....*....|....*....
gi 489915853 580 MKVVRPKVLQRYADVIDNM 598
Cdd:PLN02614 636 FKKKRPQLLKYYQSVIDEM 654
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
13-517 |
1.36e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 205.91 E-value: 1.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 13 TTDLDTIYSLLAKRCERDPDDlIAQWQDDETrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFA 92
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDK-EAYVFGDQR-----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 93 CASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDshaqILEQIRAHSES---LRYVFNFKANGLDAVAD----FGES 165
Cdd:PRK07656 75 ALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL----FLGVDYSATTRlpaLEHVVICETEEDDPHTEkmktFTDF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 166 VSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNfnhtVYNGYEVLNDML-YQPS-RLLLFLPLAHCFARYIQY 243
Cdd:PRK07656 151 LAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQ----LLSNAADWAEYLgLTEGdRYLAANPFFHVFGYKAGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 244 VAIGSHGVVGYI-P--SAKRLLADLRGFKPTYLLGVPRVFEKVYNAAsqkagaglkgrlfAKAFDHFvqwskdemagghh 320
Cdd:PRK07656 227 NAPLMRGATILPlPvfDPDEVFRLIETERITVLPGPPTMYNSLLQHP-------------DRSAEDL------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 321 slgariqhsfymqtvgSSIRSALgpnmkwlaCGGAPLNADLAHFFNG-FDGITFIQGYGMTEtAAP--CLVNFQDANEV- 396
Cdd:PRK07656 281 ----------------SSLRLAV--------TGAASMPVALLERFESeLGVDIVLTGYGLSE-ASGvtTFNRLDDDRKTv 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 397 -GSVGRPgC--ISIRLAD----------DDELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRK 463
Cdd:PRK07656 336 aGTIGTA-IagVENKIVNelgeevpvgeVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRK 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915853 464 KDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG--D------GRPFIAAL--IELDAEMTRSW 517
Cdd:PRK07656 415 KDMFIV-GGFNVYPAEVEEVLYEHPAVAEAAVIGvpDerlgevGKAYVVLKpgAELTEEELIAY 477
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
53-497 |
2.59e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 203.47 E-value: 2.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV---PVYETD----SPKQTGdiVAEVEPVIAF 125
Cdd:PRK12583 50 QLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRASeleyALGQSG--VRWVICADAF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AGDDSHAQILEQIRAHSES------------LRYVFNFKAN---GL---DAVADFGESVSDEELDKAIGRVRADDLFTIV 187
Cdd:PRK12583 128 KTSDYHAMLQELLPGLAEGqpgalacerlpeLRGVVSLAPApppGFlawHELQARGETVSREALAERQASLDRDDPINIQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 188 YTSGSTGKPKGVMLSHRNFnhtVYNGYEVLNDM-LYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSakrlladlR 266
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNI---LNNGYFVAESLgLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPN--------E 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 267 GFKPTYLLgvprvfekvyNAASQKAGAGLKG--RLFAKAFDHfVQWSKDEMagghhslgariqhsfymqtvgSSIRSALg 344
Cdd:PRK12583 277 AFDPLATL----------QAVEEERCTALYGvpTMFIAELDH-PQRGNFDL---------------------SSLRTGI- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 345 pnmkwlaCGGAPLNADLAHFFNGFDGITFIQ-GYGMTETAApclVNFQDANE------VGSVGR--PGcISIRLADDD-- 413
Cdd:PRK12583 324 -------MAGAPCPIEVMRRVMDEMHMAEVQiAYGMTETSP---VSLQTTAAddlerrVETVGRtqPH-LEVKVVDPDga 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 --------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVIN 485
Cdd:PRK12583 393 tvprgeigELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIR-GGENIYPREIEEFLF 471
|
490
....*....|..
gi 489915853 486 TCPIVAHAVVIG 497
Cdd:PRK12583 472 THPAVADVQVFG 483
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
20-497 |
9.90e-57 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 201.88 E-value: 9.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 20 YSLLAKRCERDPDD--LIAQWQDDETRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:COG0365 12 YNCLDRHAEGRGDKvaLIWEGEDGEERTL---TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDS--------HAQILEQIRAHSESLRYVFNFKANGLDAVA----DFGES 165
Cdd:COG0365 89 AVHSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidLKEKVDEALEELPSLEHVIVVGRTGADVPMegdlDWDEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 166 VSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNF-NHTVYNGYEVLNdmlYQPSRLLLflplahCFAR----- 239
Cdd:COG0365 169 LAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYlVHAATTAKYVLD---LKPGDVFW------CTADigwat 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 240 ---YIQYV--AIGS-----HGVVGYiPSAKRLLADLRGFKPTYLLGVPRVFekvynaasqkagaglkgRLFAKAFDHFVQ 309
Cdd:COG0365 240 ghsYIVYGplLNGAtvvlyEGRPDF-PDPGRLWELIEKYGVTVFFTAPTAI-----------------RALMKAGDEPLK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 310 wskdemaggHHSLgariqhsfymqtvgSSIRSalgpnmkwLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAApCLVN 389
Cdd:COG0365 302 ---------KYDL--------------SSLRL--------LGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGG-IFIS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 390 FQDANEV--GSVGR--PGcISIRLADDD----------ELMIKG--PNVFLGYYKQPQRTAEAL--TSDGWLHTGDLATI 451
Cdd:COG0365 350 NLPGLPVkpGSMGKpvPG-YDVAVVDEDgnpvppgeegELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 489915853 452 DDRGFVFITGRKKDIIITAgGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:COG0365 429 DEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAVVG 473
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
52-517 |
2.13e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 187.51 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV---PVY---ETDSPKQtgDIVAEVepVIAF 125
Cdd:PRK05605 61 AELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYtahELEHPFE--DHGARV--AIVW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 agdDSHAQILEQIRAHSeSLRYVFNF-----------------------KANGLDAVAD----FGESVSDEELDKAIG-- 176
Cdd:PRK05605 137 ---DKVAPTVERLRRTT-PLETIVSVnmiaampllqrlalrlpipalrkARAALTGPAPgtvpWETLVDAAIGGDGSDvs 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 177 --RVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRLLLFLPLAHC--------FAryiqyVAI 246
Cdd:PRK05605 213 hpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPERVLAALPMFHAygltlcltLA-----VSI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 247 GSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEKVYNAASQKaGAGLKGrlfakafdhfvqwskdemagghhslgari 326
Cdd:PRK05605 288 GGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEER-GVDLSG----------------------------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 327 qhsfymqtvgssIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGYGMTETAaPCLVnfqdANEVGSVGRPGCIS 406
Cdd:PRK05605 338 ------------VRNAF--------SGAMALPVSTVELWEKLTGGLLVEGYGLTETS-PIIV----GNPMSDDRRPGYVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 407 -------IRLADDD------------ELMIKGPNVFLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFITGRKKDII 467
Cdd:PRK05605 393 vpfpdteVRIVDPEdpdetmpdgeegELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELI 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 468 ITaGGKNISPAPMEDVINTCPIVAHAVVIG----DGRPFIAALI------ELDAEMTRSW 517
Cdd:PRK05605 472 IT-GGFNVYPAEVEEVLREHPGVEDAAVVGlpreDGSEEVVAAVvlepgaALDPEGLRAY 530
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
49-497 |
2.43e-51 |
|
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: 185.90 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPkqtGDIVAEVE---PVIAF 125
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP---AEIAKQVKdsgAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AgddsHAQILEQIRAHSESLRYVFNFKANGLDAVADfgeSVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRN 205
Cdd:cd05904 110 T----TAELAEKLASLALPVVLLDSAEFDSLSFSDL---LFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 206 F--NHTVYNGYEVLNDMLyqPSRLLLFLPLAHC-----FARYIqyVAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPR 278
Cdd:cd05904 183 LiaMVAQFVAGEGSNSDS--EDVFLCVLPMFHIyglssFALGL--LRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 279 VFekvynAASQKAGAGLKGRLfakafdhfvqwskdemagghhslgariqhsfymqtvgSSIRSALgpnmkwlaCGGAPLN 358
Cdd:cd05904 259 IV-----LALVKSPIVDKYDL-------------------------------------SSLRQIM--------SGAAPLG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 359 ADLAH-FFNGFDGITFIQGYGMTETAAPCLVNFQDANE---VGSVGR--PGcISIRLADDD-----------ELMIKGPN 421
Cdd:cd05904 289 KELIEaFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDrakYGSVGRlvPN-VEAKIVDPEtgeslppnqtgELWIRGPS 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 422 VFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05904 368 IMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKE-LIKYKGFQVAPAELEALLLSHPEILDAAVIP 442
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
53-497 |
6.64e-49 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 178.90 E-value: 6.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLG-LGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSP-------KQTGDIVAEVEPVIA 124
Cdd:PRK06839 32 QLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEnelifqlKDSGTTVLFVEKTFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 125 FAGDDSHAQILEQIRAHSESLRYVFNFKANGLDavaDFGEsvsdeeldkaigrvraDDLFTIVYTSGSTGKPKGVMLSHR 204
Cdd:PRK06839 112 NMALSMQKVSYVQRVISITSLKEIEDRKIDNFV---EKNE----------------SASFIICYTSGTTGKPKGAVLTQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 205 N-FNHTVYNgyeVLNDMLYQPSRLLLFLPLAHcfaryiqyvaIGSHGVVGYipsakrlladlrgfkPTYLLG----VPRV 279
Cdd:PRK06839 173 NmFWNALNN---TFAIDLTMHDRSIVLLPLFH----------IGGIGLFAF---------------PTLFAGgviiVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 280 FEKvynaasqkagaglkgrlfAKAFdHFVQWSKDEMAGG----HHSLgarIQHSFYMQTVGSSIRsalgpnmkWLACGGA 355
Cdd:PRK06839 225 FEP------------------TKAL-SMIEKHKVTVVMGvptiHQAL---INCSKFETTNLQSVR--------WFYNGGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 356 PLNADLAHFFNGfDGITFIQGYGMTETAAPCLVNFQD--ANEVGSVGRPGCIS-IRLADDD----------ELMIKGPNV 422
Cdd:PRK06839 275 PCPEELMREFID-RGFLFGQGFGMTETSPTVFMLSEEdaRRKVGSIGKPVLFCdYELIDENknkvevgevgELLIRGPNV 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 423 FLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK06839 354 MKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
43-497 |
3.10e-48 |
|
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: 176.73 E-value: 3.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 43 TRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPV 122
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 123 IAFAGDDSHAQILEQirAHSESLRYVfnfkANGLDaVADFGESVSDEEL---------DKAIGRVRADDLFTIVYTSGST 193
Cdd:cd05926 89 LVLTPKGELGPASRA--ASKLGLAIL----ELALD-VGVLIRAPSAESLsnlladkknAKSEGVPLPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 194 GKPKGVMLSHRNFNHTVYN---GYEvlndmLYQPSRLLLFLPLAHCfaryiqyvaigsHGVVG------------YIP-- 256
Cdd:cd05926 162 GRPKGVPLTHRNLAASATNitnTYK-----LTPDDRTLVVMPLFHV------------HGLVAsllstlaaggsvVLPpr 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 257 -SAKRLLADLRGFKPTYLLGVP---RVFEKVYNAASQKAGAGLKgrlfakafdhfvqwskdemagghhslgariqhsFym 332
Cdd:cd05926 225 fSASTFWPDVRDYNATWYTAVPtihQILLNRPEPNPESPPPKLR---------------------------------F-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 333 qtvgssIRSAlgpnmkwlacgGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVN--FQDANEVGSVGRPGCISIRLA 410
Cdd:cd05926 270 ------IRSC-----------SASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPVGVEVRIL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 411 DDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPM 480
Cdd:cd05926 333 DEDgeilppgvvgEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR-GGEKISPLEV 411
|
490
....*....|....*..
gi 489915853 481 EDVINTCPIVAHAVVIG 497
Cdd:cd05926 412 DGVLLSHPAVLEAVAFG 428
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
52-593 |
5.41e-48 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 179.93 E-value: 5.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFAC-----------ASIG--AVSVPVYETdspkqtgdivaE 118
Cdd:PLN02387 110 GQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCfrqnitvvtiyASLGeeALCHSLNET-----------E 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 119 VEPVIAfagDDSHAQILEQIRAHSESLRYVFNFKANGLDAVADFG-------ESVSD-EELDKAiGRVRAD-----DLFT 185
Cdd:PLN02387 179 VTTVIC---DSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSgssnwtvSSFSEvEKLGKE-NPVDPDlpspnDIAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 186 IVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDmLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYiPSA------- 258
Cdd:PLN02387 255 IMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPK-LGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY-GSPltltdts 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 259 ----KRLLADLRGFKPTYLLGVPRVFEKVYNAASQKAGAglKGRLFAKAFDhfVQWSKDEMAGGHHSLGAR-IQHSFYMQ 333
Cdd:PLN02387 333 nkikKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDA--KGGLAKKLFD--IAYKRRLAAIEGSWFGAWgLEKLLWDA 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 334 TVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRP-GCISIRLAD- 411
Cdd:PLN02387 409 LVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPlPCCYVKLVSw 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 412 --------DD-----ELMIKGPNVFLGYYKQPQRTAEALTSDG----WLHTGDLATIDDRGFVFITGRKKDIIITAGGKN 474
Cdd:PLN02387 489 eeggylisDKpmprgEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEY 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 475 ISPAPMEDVINTCPIVAHAVVIGDgrPF---IAALIELDAEMTRSWLASQNLDIdAPMSEIATNDAVRALVQQYIDKA-- 549
Cdd:PLN02387 569 VSLGKVEAALSVSPYVDNIMVHAD--PFhsyCVALVVPSQQALEKWAKKAGIDY-SNFAELCEKEEAVKEVQQSLSKAak 645
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 489915853 550 NGNVSRAESVRKFVILDEEFNQEDGTLTPSMKVVRPKVLQRYAD 593
Cdd:PLN02387 646 AARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKD 689
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
44-497 |
1.37e-47 |
|
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: 173.25 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 44 RQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYetdspkqtgdivaevepvI 123
Cdd:cd05934 2 RRW---TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPIN------------------T 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 124 AFAGDDSHAQIleqirAHSeslryvfnfkanglDAVADFGesvsdeeldkaigrvradDLFTIVYTSGSTGKPKGVMLSH 203
Cdd:cd05934 61 ALRGDELAYII-----DHS--------------GAQLVVV------------------DPASILYTSGTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 204 RNFNHTvynGYEVLNDM-LYQPSRLLLFLPLAHCFARYIQ-YVAIGSHGVVGYIP--SAKRLLADLRGFKPTYLlgvprv 279
Cdd:cd05934 104 ANLTFA---GYYSARRFgLGEDDVYLTVLPLFHINAQAVSvLAALSVGATLVLLPrfSASRFWSDVRRYGATVT------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 280 fekvynaasqkagaglkgrlfakafdhfvqwskdemagghHSLGARIqhSFYMQTVGSSIRSAlgpNMKWLACGGAPLNA 359
Cdd:cd05934 175 ----------------------------------------NYLGAML--SYLLAQPPSPDDRA---HRLRAAYGAPNPPE 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 360 DLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPG-CISIRLADDD----------ELMIK---GPNVFLG 425
Cdd:cd05934 210 LHEEFEERF-GVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPApGYEVRIVDDDgqelpagepgELVIRglrGWGFFKG 288
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 426 YYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05934 289 YYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVERAILRHPAVREAAVVA 358
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
181-497 |
2.45e-47 |
|
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: 170.54 E-value: 2.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFnhtVYNGYEVLNDMLYQPS-RLLLFLPLAHCFARYIQYVAIGSHGVVGYIPS-- 257
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNI---VNNGYFIGERLGLTEQdRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSps 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 258 --AKRLLADLRGFKPTYLLGVPRVFEkvynaasqkagAGLKGRLFAKaFDHfvqwskdemagghhslgariqhsfymqtv 335
Cdd:cd05917 79 fdPLAVLEAIEKEKCTALHGVPTMFI-----------AELEHPDFDK-FDL----------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 336 gSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQ-GYGMTETAAPCLVNFQDAN---EVGSVGRP--------- 402
Cdd:cd05917 118 -SSLRTGI--------MAGAPCPPELMKRVIEVMNMKDVTiAYGMTETSPVSTQTRTDDSiekRVNTVGRImphteakiv 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 ---GCISIRLADDDELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAP 479
Cdd:cd05917 189 dpeGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPRE 267
|
330
....*....|....*...
gi 489915853 480 MEDVINTCPIVAHAVVIG 497
Cdd:cd05917 268 IEEFLHTHPKVSDVQVVG 285
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
17-501 |
2.45e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 171.29 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 17 DTIYSLLAKRCERDPDD--LIAQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACA 94
Cdd:PRK07529 25 ASTYELLSRAAARHPDApaLSFLLDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 95 SIGAVsVPVYETDSPKQTGDIV--AEVEPVIA---FAGDDShAQILEQIRAHSESLRYVFnfKANGLDAVA--------- 160
Cdd:PRK07529 105 AAGIA-NPINPLLEPEQIAELLraAGAKVLVTlgpFPGTDI-WQKVAEVLAALPELRTVV--EVDLARYLPgpkrlavpl 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 161 ----------DFGESVSDEELDKAIG--RVRADDLFTIVYTSGSTGKPKGVMLSHRNfnhTVYNGYEVLNDMLYQPSRLL 228
Cdd:PRK07529 181 irrkaharilDFDAELARQPGDRLFSgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGN---EVANAWLGALLLGLGPGDTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 229 LF-LPLAHCFARYIQY---VAIGSHGVVGyIPSAKRLLADLRGF-------KPTYLLGVPrvfeKVYNAASQKAgaglkg 297
Cdd:PRK07529 258 FCgLPLFHVNALLVTGlapLARGAHVVLA-TPQGYRGPGVIANFwkiveryRINFLSGVP----TVYAALLQVP------ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 298 rlfakafdhfvqwskdemAGGHHSlgariqhsfymqtvgSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGY 377
Cdd:PRK07529 327 ------------------VDGHDI---------------SSLRYAL--------CGAAPLPVEVFRRFEAATGVRIVEGY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 378 GMTETAAPCLVNFQD-ANEVGSVGR--PGC-ISIRLADDD-------------ELMIKGPNVFLGYYkQPQRTAEALTSD 440
Cdd:PRK07529 366 GLTEATCVSSVNPPDgERRIGSVGLrlPYQrVRVVILDDAgrylrdcavdevgVLCIAGPNVFSGYL-EAAHNKGLWLED 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489915853 441 GWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIgdGRP 501
Cdd:PRK07529 445 GWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEALLRHPAVALAAAV--GRP 502
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
52-497 |
2.50e-43 |
|
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: 163.57 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIV--AEVEPVIAfagDD 129
Cdd:cd12119 29 AEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIInhAEDRVVFV---DR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 130 SHAQILEQIRAHSESLRYVFNFKAN------GLDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSH 203
Cdd:cd12119 106 DFLPLLEAIAPRLPTVEHVVVMTDDaampepAGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 204 R-NFNHTVYNgyeVLNDMLYQPSR--LLLFLPLAHCFARYIQYVA--IGSHGVV-GYIPSAKRLLADLRGFKPTYLLGVP 277
Cdd:cd12119 186 RsLVLHAMAA---LLTDGLGLSESdvVLPVVPMFHVNAWGLPYAAamVGAKLVLpGPYLDPASLAELIEREGVTFAAGVP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 278 RVFEKVYNAasqkaGAGLKGRLFAkafdhfvqwskdemagghhslgariqhsfymqtvgssirsalgpnMKWLACGGAPL 357
Cdd:cd12119 263 TVWQGLLDH-----LEANGRDLSS---------------------------------------------LRRVVIGGSAV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 358 NADLAHFFNGfDGITFIQGYGMTETAAPCLVNFQDANEVG-----------SVGRPGC-ISIRLADDD------------ 413
Cdd:cd12119 293 PRSLIEAFEE-RGVRVIHAWGMTETSPLGTVARPPSEHSNlsedeqlalraKQGRPVPgVELRIVDDDgrelpwdgkavg 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ELMIKGPNVFLGYYKQPqRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHA 493
Cdd:cd12119 372 ELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVELENAIMAHPAVAEA 449
|
....
gi 489915853 494 VVIG 497
Cdd:cd12119 450 AVIG 453
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
23-596 |
1.36e-42 |
|
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: 162.22 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 23 LAKRCERDPDDL-IAQWQDDEtrQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV 101
Cdd:cd05921 1 LAHWARQAPDRTwLAEREGNG--GWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 102 PV---YETDSPKQT--GDIVAEVEPVIAFAGD-DSHAQILEQIRAHSESLRYVFNfKANGLDAV--ADFGESVSDEELDK 173
Cdd:cd05921 79 PVspaYSLMSQDLAklKHLFELLKPGLVFAQDaAPFARALAAIFPLGTPLVVSRN-AVAGRGAIsfAELAATPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 174 AIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVG 253
Cdd:cd05921 158 AFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 254 YI----PSAKRL---LADLRGFKPTYLLGVPRVFEKVYNAASQKAGagLKGRLFAKAfdHFVQWSKDEMAgghHSLGARI 326
Cdd:cd05921 238 YIddgkPMPGGFeetLRNLREISPTVYFNVPAGWEMLVAALEKDEA--LRRRFFKRL--KLMFYAGAGLS---QDVWDRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 327 QhSFYMQTVGSSIRsalgpnmkwlacggaplnadlahffngfdgitFIQGYGMTETAAPCLVNFQDANEVGSVGRP--GC 404
Cdd:cd05921 311 Q-ALAVATVGERIP--------------------------------MMAGLGATETAPTATFTHWPTERSGLIGLPapGT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 405 iSIRLADDD---ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGD---LATIDD--RGFVFiTGRKKDIIITAGGKNIS 476
Cdd:cd05921 358 -ELKLVPSGgkyEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDaakLADPDDpaKGLVF-DGRVAEDFKLASGTWVS 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 477 PAPME-DVINTC-PIVAHAVVIGDGRPFIAALIELDAEMTRSWLASQNLDiDApmsEIATNDAVRALVQQYIDKANGNVS 554
Cdd:cd05921 436 VGPLRaRAVAACaPLVHDAVVAGEDRAEVGALVFPDLLACRRLVGLQEAS-DA---EVLRHAKVRAAFRDRLAALNGEAT 511
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 489915853 555 RAES-VRKFVILDEEFNQEDGTLTPSMKVVRPKVLQRYADVID 596
Cdd:cd05921 512 GSSSrIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVE 554
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
46-577 |
9.38e-42 |
|
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: 160.31 E-value: 9.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 46 WHDVSA--GQMNDRVREVAKGL-LGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPV 122
Cdd:cd17632 63 PRFETItyAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 123 IAFAGDDSHAQILEQIRAHSESLR-YVFNFKANG----------LDAVADFGESVSDEELDKAIGR-----------VRA 180
Cdd:cd17632 143 LLAVSAEHLDLAVEAVLEGGTPPRlVVFDHRPEVdahraalesaRERLAAVGIPVTTLTLIAVRGRdlppaplfrpePDD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFNHtVYNGYEVLNDMLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSA-- 258
Cdd:cd17632 223 DPLALLIYTSGSTGTPKGAMYTERLVAT-FWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASdm 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 259 KRLLADLRGFKPTYLLGVPRVFEKVYnaasQKAGAGLKGRLFAKAfdhfvqwskDEMAgghhsLGARiqhsfymqtVGSS 338
Cdd:cd17632 302 STLFDDLALVRPTELFLVPRVCDMLF----QRYQAELDRRSVAGA---------DAET-----LAER---------VKAE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 339 IRS-ALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAApCLVNfqdanevGSVGRPGCISIRLAD------ 411
Cdd:cd17632 355 LRErVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGA-VILD-------GVIVRPPVLDYKLVDvpelgy 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 412 --------DDELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGD-LATIDDRGFVFITgRKKDIIITAGGKNISPAPMED 482
Cdd:cd17632 427 frtdrphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDvMAELGPDRLVYVD-RRNNVLKLSQGEFVTVARLEA 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 483 VINTCPIVAHAVVIGDG-RPFIAALI--------ELDAEMTRSWLASQnldidapMSEIATNdavrALVQQYidkangnv 553
Cdd:cd17632 506 VFAASPLVRQIFVYGNSeRAYLLAVVvptqdalaGEDTARLRAALAES-------LQRIARE----AGLQSY-------- 566
|
570 580
....*....|....*....|....
gi 489915853 554 sraESVRKFVILDEEFNQEDGTLT 577
Cdd:cd17632 567 ---EIPRDFLIETEPFTIANGLLS 587
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
61-497 |
1.86e-41 |
|
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: 156.68 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 61 VAKGLLGLG-VKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYeTDSPkqtgdiVAEVEPVIafagDDSHAQILeqir 139
Cdd:cd05941 24 LANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLN-PSYP------LAELEYVI----TDSEPSLV---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 140 ahseslryvfnfkangldavadfgesvsdeeLDKAigrvraddlfTIVYTSGSTGKPKGVMLSHRNFNHTVyngyevlnD 219
Cdd:cd05941 89 -------------------------------LDPA----------LILYTSGTTGRPKGVVLTHANLAANV--------R 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 220 ML-----YQPS-RLLLFLPLAHcfaryiqyvaigSHGVVGYI---------------PSAKRLLADLRGFKPTYLLGVPR 278
Cdd:cd05941 120 ALvdawrWTEDdVLLHVLPLHH------------VHGLVNALlcplfagasveflpkFDPKEVAISRLMPSITVFMGVPT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 279 VFEKVynaasqkagaglkgrlfAKAFDHfvqwskdemagghhslgariqhsfyMQTVGSSIRSALGPNMKWLACGGAPLN 358
Cdd:cd05941 188 IYTRL-----------------LQYYEA-------------------------HFTDPQFARAAAAERLRLMVSGSAALP 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 359 ADLAHFFNGFDGITFIQGYGMTETAApCLVNFQDANEV-GSVGRP-GCISIRLADDD-----------ELMIKGPNVFLG 425
Cdd:cd05941 226 VPTLEEWEAITGHTLLERYGMTEIGM-ALSNPLDGERRpGTVGMPlPGVQARIVDEEtgeplprgevgEIQVRGPSVFKE 304
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 426 YYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05941 305 YWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIG 376
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
23-606 |
2.51e-41 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 159.27 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 23 LAKRCERDPDD-LIAQWQDDEtrQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV 101
Cdd:PRK08180 45 LVHWAQEAPDRvFLAERGADG--GWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 102 PV---YETDS--PKQTGDIVAEVEPVIAFAGD-DSHAQILEQIRahSESLRYVFNFKANGLDAVADFGESVSDEE---LD 172
Cdd:PRK08180 123 PVspaYSLVSqdFGKLRHVLELLTPGLVFADDgAAFARALAAVV--PADVEVVAVRGAVPGRAATPFAALLATPPtaaVD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 173 KAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNF--NHTVYNgyEVLNDMLYQPSRLLLFLPLAHCFAryiqyvaiGSH- 249
Cdd:PRK08180 201 AAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLcaNQQMLA--QTFPFLAEEPPVLVDWLPWNHTFG--------GNHn 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 250 -GVV---G---YI----PSAKRL---LADLRGFKPTYLLGVPRVFEKVYNAAsqKAGAGLKGRLFAKAfdHFVQWSKdem 315
Cdd:PRK08180 271 lGIVlynGgtlYIddgkPTPGGFdetLRNLREISPTVYFNVPKGWEMLVPAL--ERDAALRRRFFSRL--KLLFYAG--- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 316 AGGHHSLGARIQhSFYMQTVGSSIRsalgpnmkwlacggaplnadlahffngfdgitFIQGYGMTETAAPCL-VNFQdAN 394
Cdd:PRK08180 344 AALSQDVWDRLD-RVAEATCGERIR--------------------------------MMTGLGMTETAPSATfTTGP-LS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 395 EVGSVGRP--GCiSIRLADDD---ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGD---LATIDD--RGFVFiTGRkk 464
Cdd:PRK08180 390 RAGNIGLPapGC-EVKLVPVGgklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDavrFVDPADpeRGLMF-DGR-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 465 diiIT-----AGGKNISPAPME-DVINTC-PIVAHAVVIGDGRPFIAALIELDAEMTRSwLAsqNLDIDAPMSEIATNDA 537
Cdd:PRK08180 466 ---IAedfklSSGTWVSVGPLRaRAVSAGaPLVQDVVITGHDRDEIGLLVFPNLDACRR-LA--GLLADASLAEVLAHPA 539
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915853 538 VRALVQQYIDK----ANGNVSRaesVRKFVILDEEFNQEDGTLTPSMKVVRPKVLQRYADVIDnMIYAPKNAA 606
Cdd:PRK08180 540 VRAAFRERLARlnaqATGSSTR---VARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVE-ALYADEPDD 608
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
17-497 |
7.54e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 156.63 E-value: 7.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 17 DTIYSLLAKRCERDPDDLIAQWQDdetRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASI 96
Cdd:PRK08316 11 QTIGDILRRSARRYPDKTALVFGD---RSW---TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 97 GAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDshaqILEQIRAHSESLRYVF---------NFKANGLDAVADFGESVS 167
Cdd:PRK08316 85 GAVHVPVNFMLTGEELAYILDHSGARAFLVDPA----LAPTAEAALALLPVDTlilslvlggREAPGGWLDFADWAEAGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 168 DEELDKAIgrvRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTvYNGYEVLNDMlyQPS-RLLLFLPLAHCFARY---IQY 243
Cdd:PRK08316 161 VAEPDVEL---ADDDLAQILYTSGTESLPKGAMLTHRALIAE-YVSCIVAGDM--SADdIPLHALPLYHCAQLDvflGPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 244 VAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRVFekvynaasqkagAGLkgrLFAKAFDHfvqwskdemagghHSLG 323
Cdd:PRK08316 235 LYVGATNVILDAPDPELILRTIEAERITSFFAPPTVW------------ISL---LRHPDFDT-------------RDLS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 324 ArIQHSFYmqtvGSSI---------RSALgPNMKwlacggaplnadlahFFNGfdgitfiqgYGMTETA--APCLVNFQD 392
Cdd:PRK08316 287 S-LRKGYY----GASImpvevlkelRERL-PGLR---------------FYNC---------YGQTEIAplATVLGPEEH 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 393 ANEVGSVGRPGC-ISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITG 461
Cdd:PRK08316 337 LRRPGSAGRPVLnVETRVVDDDgndvapgevgEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVD 415
|
490 500 510
....*....|....*....|....*....|....*.
gi 489915853 462 RKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK08316 416 RKKDMIKT-GGENVASREVEEALYTHPAVAEVAVIG 450
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
18-497 |
1.19e-40 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 156.37 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIAQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVYETDSPKQTGDIVAEVEPVIA-----FAGDDsHAQILEQIRAHSESLRYVFNFKANGLDAVADFgESVSDEELD 172
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLvvpktFRGFD-HAAMARRLRPELPALRHVVVVGGDGADSFEAL-LITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 173 KAIG------RVRADDLFTIVYTSGSTGKPKGVMLSHrnfnHTVYNGYevlndmlyqpsrlllflplahcfARYIQYVAI 246
Cdd:PRK13295 183 PDAPailarlRPGPDDVTQLIYTSGTTGEPKGVMHTA----NTLMANI-----------------------VPYAERLGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 247 GSHGVVgYIPSAkrlLADLRGFK-----PTyLLGVPRVFEKVYNAAsqKAGAGLKgrlfakafDHFVQWSkdeMAGGhhs 321
Cdd:PRK13295 236 GADDVI-LMASP---MAHQTGFMyglmmPV-MLGATAVLQDIWDPA--RAAELIR--------TEGVTFT---MAST--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 322 lgariqhSFYMQTVGSSIRSALG-PNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVgSVG 400
Cdd:PRK13295 295 -------PFLTDLTRAVKESGRPvSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDER-AST 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 401 RPGC----ISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEAltSDGWLHTGDLATIDDRGFVFITGRKKDI 466
Cdd:PRK13295 367 TDGCplpgVEVRVVDADgaplpagqigRLQVRGCSNFGGYLKRPQLNGTD--ADGWFDTGDLARIDADGYIRISGRSKDV 444
|
490 500 510
....*....|....*....|....*....|.
gi 489915853 467 IITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK13295 445 IIR-GGENIPVVEIEALLYRHPAIAQVAIVA 474
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
52-497 |
1.21e-40 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 156.45 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPV---YETDSPKQTGDIV---AEVEPVIaF 125
Cdd:PRK06087 53 SALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLlpsWREAELVWVLNKCqakMFFAPTL-F 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AGDDSHAQILEqIRAHSESLRYVFNF----KANGLDAVADFGESvsDEELDKAIgRVRADDLFTIVYTSGSTGKPKGVML 201
Cdd:PRK06087 132 KQTRPVDLILP-LQNQLPQLQQIVGVdklaPATSSLSLSQIIAD--YEPLTTAI-TTHGDELAAVLFTSGTEGLPKGVML 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 202 SHRN--FNHTVYNGyeVLN----DMLYQPSrlllflPLAHC---FARYIQYVAIGSHGVVGYIPSAKRLLADLRGFKPTY 272
Cdd:PRK06087 208 THNNilASERAYCA--RLNltwqDVFMMPA------PLGHAtgfLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 273 LLG-VPRVFEKVYNAASQKAgaglkgrlfakafdHFvqwskdemagghhslgariqhsfymqtvgssirsalgPNMKWLA 351
Cdd:PRK06087 280 MLGaTPFIYDLLNLLEKQPA--------------DL-------------------------------------SALRFFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 352 CGGAPLNADLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANE--VGSVGRPGC-ISIRLADDD----------ELMIK 418
Cdd:PRK06087 309 CGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNLDDPLSrfMHTDGYAAAgVEIKVVDEArktlppgcegEEASR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489915853 419 GPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK06087 388 GPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSREVEDILLQHPKIHDACVVA 465
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
44-497 |
2.02e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 151.88 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 44 RQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVI 123
Cdd:PRK09088 21 RRW---TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 124 aFAGDDSHAqileqirahseslryvfnfkANGLD--AVADFGESVSDEELDKAiGRVRADDLFTIVYTSGSTGKPKGVML 201
Cdd:PRK09088 98 -LLGDDAVA--------------------AGRTDveDLAAFIASADALEPADT-PSIPPERVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 202 SHRNFNHTVYNgYEVLNDMLYQpSRLLLFLPLAHcfaryiqyvaigshgVVGYIPSAKRLLAD------LRGFKPTYLLG 275
Cdd:PRK09088 156 SERNLQQTAHN-FGVLGRVDAH-SSFLCDAPMFH---------------IIGLITSVRPVLAVggsilvSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 276 vprvfekvynaasqkagaglkgRLfakafdhfvqwskdemagGHHSLGarIQHSFYMQTVGSSIR-------SALGpNMK 348
Cdd:PRK09088 219 ----------------------RL------------------GDPALG--ITHYFCVPQMAQAFRaqpgfdaAALR-HLT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 349 WLACGGAP-LNADLAHFFNgfDGITFIQGYGMTET------AAPCLVnfqDANEVGSVGRPG-CISIRLADDD------- 413
Cdd:PRK09088 256 ALFTGGAPhAAEDILGWLD--DGIPMVDGFGMSEAgtvfgmSVDCDV---IRAKAGAAGIPTpTVQTRVVDDQgndcpag 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ---ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIV 490
Cdd:PRK09088 331 vpgELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPAEIEAVLADHPGI 409
|
....*..
gi 489915853 491 AHAVVIG 497
Cdd:PRK09088 410 RECAVVG 416
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
18-601 |
3.75e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 153.28 E-value: 3.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDD-LIAQwQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASI 96
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRpWLAQ-REPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 97 GAVSVPVYETDSPKQTG-----DIVAEVEPVIAFAGD-DSHAQILEQIRAHSESLRYVFNfKANGLDAV--ADFGESVSD 168
Cdd:PRK12582 129 GVPAAPVSPAYSLMSHDhaklkHLFDLVKPRVVFAQSgAPFARALAALDLLDVTVVHVTG-PGEGIASIafADLAATPPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 169 EELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNhTVYNGYEVLNDML--YQPSRLLLFLPLAHCFARYIQYVAI 246
Cdd:PRK12582 208 AAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMC-ANIAMQEQLRPREpdPPPPVSLDWMPWNHTMGGNANFNGL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 247 GSHGVVGYIPSAKRL-------LADLRGFKPTYLLGVPrvfekvynaasqkagAGLKgrLFAKAFDhfvqwsKDEmaggh 319
Cdd:PRK12582 287 LWGGGTLYIDDGKPLpgmfeetIRNLREISPTVYGNVP---------------AGYA--MLAEAME------KDD----- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 320 hslgariqhsfymqtvgsSIRSALGPNMKWLACGGAPLNAD-------LAHFFNGfDGITFIQGYGMTETAAPCLVNFQD 392
Cdd:PRK12582 339 ------------------ALRRSFFKNLRLMAYGGATLSDDlyermqaLAVRTTG-HRIPFYTGYGATETAPTTTGTHWD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 393 ANEVGSVGRP--GcISIRLA---DDDELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDD-----RGFVFiTGR 462
Cdd:PRK12582 400 TERVGLIGLPlpG-VELKLApvgDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDpddpeKGLIF-DGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 463 KKDIIITAGGKNISPAPME-DVINTC-PIVAHAVVIGDGRPFIAALIELDAEMTRSWLAsqnlDIDAPMSEIATNDAVRA 540
Cdd:PRK12582 478 VAEDFKLSTGTWVSVGTLRpDAVAACsPVIHDAVVAGQDRAFIGLLAWPNPAACRQLAG----DPDAAPEDVVKHPAVLA 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 541 LVQQYIDKANGNVSRAES-VRKFVILDEEFNQEDGTLTPSMKVVRPKVLQRYADVIDNMiYA 601
Cdd:PRK12582 554 ILREGLSAHNAEAGGSSSrIARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERL-YA 614
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
62-497 |
4.01e-39 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 149.91 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 62 AKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQILEQIRAH 141
Cdd:TIGR01923 13 AKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLLEEKDFQADSLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 142 SESLryvfnfkangldavadfgESVSDEELDKAIgrvRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmL 221
Cdd:TIGR01923 93 RIEA------------------AGRYETSLSASF---NMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--F 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 222 YQPSRLLLFLPLAHcfaryiqyvaIGshgvvgyipsakrlladlrgfkptyllGVPRVFEKVYNAASQKAGAGlkgrlFA 301
Cdd:TIGR01923 150 TEDDNWLLSLPLYH----------IS---------------------------GLSILFRWLIEGATLRIVDK-----FN 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 302 KAFdhfvqwskdEMAGGHhslgaRIQHSFYMQTVGSSIRSALGP--NMKWLACGGAPLNADLAHFFNGFdGITFIQGYGM 379
Cdd:TIGR01923 188 QLL---------EMIANE-----RVTHISLVPTQLNRLLDEGGHneNLRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGM 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 380 TETAAP-CLVNFQDANEVGSVGRP--GCiSIRLADDD-----ELMIKGPNVFLGYYKQPQRTaEALTSDGWLHTGDLATI 451
Cdd:TIGR01923 253 TETCSQvTTATPEMLHARPDVGRPlaGR-EIKIKVDNkeghgEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGEL 330
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489915853 452 DDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:TIGR01923 331 DGEGFLYVLGRRDDLIIS-GGENIYPEEIETVLYQHPGIQEAVVVP 375
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
20-497 |
8.64e-39 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 150.41 E-value: 8.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 20 YSLLAKRCErDPDDLIAQWQDDETRQWhdvsaGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAV 99
Cdd:PRK07514 6 FDALRAAFA-DRDAPFIETPDGLRYTY-----GDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 100 SVPVyetdspkQTGDIVAEVEpviAFAGD--------DSHAQilEQIRAHSESL--RYVFNFKANG----LDAVADFGES 165
Cdd:PRK07514 80 FLPL-------NTAYTLAELD---YFIGDaepalvvcDPANF--AWLSKIAAAAgaPHVETLDADGtgslLEAAAAAPDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 166 VSDEeldkaigRVRADDLFTIVYTSGSTGKPKGVMLSHRNfnhtVYNGYEVLNDmlY----QPSRLLLFLPLAHCFARYI 241
Cdd:PRK07514 148 FETV-------PRGADDLAAILYTSGTTGRSKGAMLSHGN----LLSNALTLVD--YwrftPDDVLIHALPIFHTHGLFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 242 Q-YVAIGSHGVVGYIPS--AKRLLADLRgfKPTYLLGVPRVFEkvynaasqkagaglkgRLFA-KAFDhfvqwsKDEMAg 317
Cdd:PRK07514 215 AtNVALLAGASMIFLPKfdPDAVLALMP--RATVMMGVPTFYT----------------RLLQePRLT------REAAA- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 318 ghhslgariqhsfymqtvgssirsalgpNMKWLACGGAPLnadLAHFFNGFD---GITFIQGYGMTETAapclVN----F 390
Cdd:PRK07514 270 ----------------------------HMRLFISGSAPL---LAETHREFQertGHAILERYGMTETN----MNtsnpY 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 391 QDANEVGSVGR--PGcISIRLADDDE-----------LMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFV 457
Cdd:PRK07514 315 DGERRAGTVGFplPG-VSLRVTDPETgaelppgeigmIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYV 393
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 489915853 458 FITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK07514 394 HIVGRGKDLIIS-GGYNVYPKEVEGEIDELPGVVESAVIG 432
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
53-497 |
1.47e-38 |
|
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: 147.49 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSPKQTgdivaevepviafagddsHA 132
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLL----NTRLT------------------PN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 133 QILEQIRahseslryvfnfkanglDAVADFgesvsdeeldkaigrvraDDLFTIVYTSGSTGKPKGVMLSHRN-FNHTVY 211
Cdd:cd05912 64 ELAFQLK-----------------DSDVKL------------------DDIATIMYTSGTTGKPKGVQQTFGNhWWSAIG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 212 NgyeVLNDMLYQPSRLLLFLPLAHcfaryIQYVAIGSHGVVGYIP-------SAKRLLADLRGFKPTYLLGVPRVfekvy 284
Cdd:cd05912 109 S---ALNLGLTEDDNWLCALPLFH-----ISGLSILMRSVIYGMTvylvdkfDAEQVLHLINSGKVTIISVVPTM----- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 285 naasqkagaglkgrlfakafdhfVQWSKDEMAGGHHslgariqhsfymqtvgssirsalgPNMKWLACGGAPLNADLAHF 364
Cdd:cd05912 176 -----------------------LQRLLEILGEGYP------------------------NNLRCILLGGGPAPKPLLEQ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 365 FNGFdGITFIQGYGMTETAAP-CLVNFQDA-NEVGSVGRP--GCiSIRLADDD-------ELMIKGPNVFLGYYKQPQRT 433
Cdd:cd05912 209 CKEK-GIPVYQSYGMTETCSQiVTLSPEDAlNKIGSAGKPlfPV-ELKIEDDGqppyevgEILLKGPNVTKGYLNRPDAT 286
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915853 434 AEAlTSDGWLHTGDLATIDDRGFVFITGRKKDIIItAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05912 287 EES-FENGWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPAIKEAGVVG 348
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
53-497 |
1.22e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 146.65 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPK----QTGDivAEVEPVIAfagD 128
Cdd:PRK03640 32 ELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREellwQLDD--AEVKCLIT---D 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQileqirAHSESLRYVFNFKANGLDAVADFGESVSDeeldkaigrvraDDLFTIVYTSGSTGKPKGVMLSHRN-FN 207
Cdd:PRK03640 107 DDFEA------KLIPGISVKFAELMNGPKEEAEIQEEFDL------------DEVATIMYTSGTTGKPKGVIQTYGNhWW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 HTVYNgyeVLNDMLYQPSRLLLFLPLAHcfaryIQYVAIGSHGVVGYIP-------SAKRLLADLRGFKPTYLLGVPRVF 280
Cdd:PRK03640 169 SAVGS---ALNLGLTEDDCWLAAVPIFH-----ISGLSILMRSVIYGMRvvlvekfDAEKINKLLQTGGVTIISVVSTML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 281 EkvynaasqkagaglkgRLFAkafdhfvqwskdEMAGGHHSlgariqhsfymqtvgSSIRSALgpnmkwlaCGGAPLNAD 360
Cdd:PRK03640 241 Q----------------RLLE------------RLGEGTYP---------------SSFRCML--------LGGGPAPKP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 361 L-----AHffngfdGITFIQGYGMTETAAP-CLVNFQDA-NEVGSVGRP--GCiSIRLADDD---------ELMIKGPNV 422
Cdd:PRK03640 270 LleqckEK------GIPVYQSYGMTETASQiVTLSPEDAlTKLGSAGKPlfPC-ELKIEKDGvvvppfeegEIVVKGPNV 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 423 FLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK03640 343 TKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
18-497 |
2.26e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 146.67 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYE-WGVVDFACASi 96
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPALVLGDTR------LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLMAIGAAQLA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 97 GAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQILEQIRAHSESLRYVFNFKAngLDAVADFGESVSDEELDKAIG 176
Cdd:PRK06188 86 GLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 177 RVRADDLFTIVYTSGSTGKPKGVMLSHRN---FNHTVYNGYEVLNDMlyqpsRLLLFLPLAHCfaryiqyvaigshGVVG 253
Cdd:PRK06188 164 AALPPDIAGLAYTGGTTGKPKGVMGTHRSiatMAQIQLAEWEWPADP-----RFLMCTPLSHA-------------GGAF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 254 YIPSAKR--LLADLRGFKPTYLLgvpRVFEKvynaasQKAGAGLkgrlfakafdhFVQwskdEMagghhsLGARIQHSfy 331
Cdd:PRK06188 226 FLPTLLRggTVIVLAKFDPAEVL---RAIEE------QRITATF-----------LVP----TM------IYALLDHP-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 332 mqtvgsSIRSALGPNMKWLACGGAPLNAD-LAHFFNGFdGITFIQGYGMTETAAPCLV------NFQDANEVGSVGRP-- 402
Cdd:PRK06188 274 ------DLRTRDLSSLETVYYGASPMSPVrLAEAIERF-GPIFAQYYGQTEAPMVITYlrkrdhDPDDPKRLTSCGRPtp 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 GCiSIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGG 472
Cdd:PRK06188 347 GL-RVALLDEDgrevaqgevgEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVT-GG 423
|
490 500
....*....|....*....|....*
gi 489915853 473 KNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK06188 424 FNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
49-497 |
2.66e-37 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 144.83 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdspkqtgdivaevepvIAFAGD 128
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI-------------------LPFFRE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQILEqiraHSESLRYVFNFKANGLDAVADfgesvsdeeldkaigrvrADDLFTIVYTSGSTGKPKGVMLSHRNFNH 208
Cdd:cd05903 63 HELAFILR----RAKAKVFVVPERFRQFDPAAM------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 209 TVYNgyEVLNDMLYQPSRLLLFLPLAHcfaryiqyvAIGShgvvgyipsakrlladLRGFKPTYLLGVPRVFEKVYNAAS 288
Cdd:cd05903 121 SIRQ--YAERLGLGPGDVFLVASPMAH---------QTGF----------------VYGFTLPLLLGAPVVLQDIWDPDK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 289 QKAGAGLKGRLFAKAFDHFV-QWSKDEMAGGHHSlgariqhsfymqtvgssirsalgPNMKWLACGGAPLNADLAHFFNG 367
Cdd:cd05903 174 ALALMREHGVTFMMGATPFLtDLLNAVEEAGEPL-----------------------SRLRTFVCGGATVPRSLARRAAE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 368 FDGITFIQGYGMTETAApCLVNFQDANE---VGSVGRPG-CISIRLADDD----------ELMIKGPNVFLGYYKQPQRT 433
Cdd:cd05903 231 LLGAKVCSAYGSTECPG-AVTSITPAPEdrrLYTDGRPLpGVEIKVVDDTgatlapgvegELLSRGPSVFLGYLDRPDLT 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915853 434 AEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05903 310 ADAA-PEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
49-497 |
6.76e-36 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 142.71 E-value: 6.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLG-LGVKPGSMVVIYAATCYEWGVVDFA--CASIGAVSV-PVYETDSPK-QTGDIVAEVEPVI 123
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGvlRAGLTVVNVnPLYTPRELKhQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 124 afagdDSHAQILEQIRAHSEsLRYVFNfkaNGLDAVADFGES-------------VSDEELDKAI--------GR----- 177
Cdd:PRK08751 131 -----DNFGTTVQQVIADTP-VKQVIT---TGLGDMLGFPKAalvnfvvkyvkklVPEYRINGAIrfrealalGRkhsmp 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 178 ---VRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVL---NDMLYQPSRLLLFLPLAHCFARYIQYVAIGSHGV 251
Cdd:PRK08751 202 tlqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLagtGKLEEGCEVVITALPLYHIFALTANGLVFMKIGG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 252 VGYIPSAKR----LLADLRGFKPTYLLGVPRVFEKVYNAAsqkagaglkgrlfakAFDhfvqwskdemagghhslgariQ 327
Cdd:PRK08751 282 CNHLISNPRdmpgFVKELKKTRFTAFTGVNTLFNGLLNTP---------------GFD---------------------Q 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 328 HSFymqtvgSSIRSALGpnmkwlacGGAPLNADLAHFFNGFDGITFIQGYGMTETA-APCL--VNFQDANevGSVGRP-- 402
Cdd:PRK08751 326 IDF------SSLKMTLG--------GGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACInpLTLKEYN--GSIGLPip 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 ---GCI------SIRLADDDELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAgGK 473
Cdd:PRK08751 390 stdACIkddagtVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-GF 468
|
490 500
....*....|....*....|....
gi 489915853 474 NISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEVAAVG 492
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
25-593 |
1.06e-35 |
|
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: 141.99 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 25 KRCERDPDDLIAQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGvKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVY 104
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 105 ETDSPK---QTGDIVAEVEPVIAFAGDDSHAQILEQIRAHSESLRyvfnFKANGLDAVADfgeSVSDEELDKAIGrvrAD 181
Cdd:cd05931 80 PPTPGRhaeRLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGT----PRLLVVDLLPD---TSAADWPPPSPD---PD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNgyeVLNDMLYQP-SRLLLFLPLAHCFaryiqyvaigshGVVGYIpsakr 260
Cdd:cd05931 150 DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQ---IRRAYGLDPgDVVVSWLPLYHDM------------GLIGGL----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 261 LLADLRGFkPTYLLGvPRVFekVYNAASQ-KAGAGLKGRLFAK---AFDHFVQWSKDEMAGGhhslgariqhsfymqTVG 336
Cdd:cd05931 210 LTPLYSGG-PSVLMS-PAAF--LRRPLRWlRLISRYRATISAApnfAYDLCVRRVRDEDLEG---------------LDL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 337 SSIRSALgpnmkwlaCGGAPLNAD-LAHFFN-----GFDGITFIQGYGMTET----------AAPCLVNF---------- 390
Cdd:cd05931 271 SSWRVAL--------NGAEPVRPAtLRRFAEafapfGFRPEAFRPSYGLAEAtlfvsggppgTGPVVLRVdrdalagrav 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 391 ------QDANEVGSVGRPGC-ISIRLADDD-----------ELMIKGPNVFLGYYKQPQRTAE------ALTSDGWLHTG 446
Cdd:cd05931 343 avaaddPAARELVSCGRPLPdQEVRIVDPEtgrelpdgevgEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 447 DLATIDDrGFVFITGRKKDIIITAgGKNISPAPMEDVI-NTCP------IVAHAVVIGDGRPFIAAlieldAEMTRSWLA 519
Cdd:cd05931 423 DLGFLHD-GELYITGRLKDLIIVR-GRNHYPQDIEATAeEAHPalrpgcVAAFSVPDDGEERLVVV-----AEVERGADP 495
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489915853 520 sqnldidAPMSEIAtnDAVRALvqqyidkangnVSRAE--SVRKFVILdeefnqEDGTL--TPSMKVVRPKVLQRYAD 593
Cdd:cd05931 496 -------ADLAAIA--AAIRAA-----------VAREHgvAPADVVLV------RPGSIprTSSGKIQRRACRAAYLD 547
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
185-498 |
1.35e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 143.71 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 185 TIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEvlNDML--YQPSRLLLFLPLAHCFARYIQYVAIGShGVVGYIPSA--KR 260
Cdd:PTZ00342 308 SIVYTSGTSGKPKGVMLSNKNLYNTVVPLCK--HSIFkkYNPKTHLSYLPISHIYERVIAYLSFML-GGTINIWSKdiNY 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 261 LLADLRGFKPTYLLGVPRVFEKVYNAASQKAG--AGLKGRLFAKAFdhfvQWSKDEMAGGHHSLGARIQHsfymqtVGSS 338
Cdd:PTZ00342 385 FSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLVKKIL----SLRKSNNNGGFSKFLEGITH------ISSK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 339 IRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPGCISIRL--------- 409
Cdd:PTZ00342 455 IKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPISPNTKYkvrtwetyk 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 410 ADDD----ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISPAPMEDVIN 485
Cdd:PTZ00342 535 ATDTlpkgELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYS 614
|
330
....*....|...
gi 489915853 486 TCPIVAHAVVIGD 498
Cdd:PTZ00342 615 QISFINFCVVYGD 627
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
17-497 |
2.35e-35 |
|
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: 140.67 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 17 DTIYSLLAKRCERDPDD--LIaqwqdDETRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACA 94
Cdd:COG1021 25 ETLGDLLRRRAERHPDRiaVV-----DGERRL---SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 95 SIGAVsvPVYETDSPKQT--GDIVAEVEPViAFAGDDSHA-----QILEQIRAHSESLRYVFnfkangldAVADFGESVS 167
Cdd:COG1021 97 RAGAI--PVFALPAHRRAeiSHFAEQSEAV-AYIIPDRHRgfdyrALARELQAEVPSLRHVL--------VVGDAGEFTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 168 DEEL-----DKAIGRVRADD--LFTIvyTSGSTGKPKGVMLSHrnfnhtvyngyevlNDMLY------------QPSRLL 228
Cdd:COG1021 166 LDALlaapaDLSEPRPDPDDvaFFQL--SGGTTGLPKLIPRTH--------------DDYLYsvrasaeicgldADTVYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 229 LFLPLAHCFAryiqyvaIGSHGVVGYI-----------PSAKRLLADLRGFKPTYLLGVPRVfekvynaasqkagaglkg 297
Cdd:COG1021 230 AALPAAHNFP-------LSSPGVLGVLyaggtvvlapdPSPDTAFPLIERERVTVTALVPPL------------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 298 rlfAKAFDHFVQWSKdemagghHSLgariqhsfymqtvgSSIRSalgpnmkwLACGGAPLNADLAH-----FfngfdGIT 372
Cdd:COG1021 285 ---ALLWLDAAERSR-------YDL--------------SSLRV--------LQVGGAKLSPELARrvrpaL-----GCT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 373 FIQGYGMTETaapcLVNF---QDANEV--GSVGRPgcIS----IRLADDD----------ELMIKGPNVFLGYYKQPQRT 433
Cdd:COG1021 328 LQQVFGMAEG----LVNYtrlDDPEEVilTTQGRP--ISpddeVRIVDEDgnpvppgevgELLTRGPYTIRGYYRAPEHN 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915853 434 AEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:COG1021 402 ARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIAAEEVENLLLAHPAVHDAAVVA 464
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
181-506 |
2.77e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 134.15 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKgvMLSHRNFNHtVYNGYEVLNDMLYQPSRLLLF-LPLAHCFARYIQYVAIGSHG--VVGYIPS 257
Cdd:cd05944 2 DDVAAYFHTGGTTGTPK--LAQHTHSNE-VYNAWMLALNSLFDPDDVLLCgLPLFHVNGSVVTLLTPLASGahVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 258 AKR---LLADLRG----FKPTYLLGVPrvfeKVYNAASQKAGaglkgrlfakafdhfvqwskdemagghhslGARIqhsf 330
Cdd:cd05944 79 GYRnpgLFDNFWKlverYRITSLSTVP----TVYAALLQVPV------------------------------NADI---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 331 ymqtvgSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQD-ANEVGSVGRP---GCIS 406
Cdd:cd05944 121 ------SSLRFAM--------SGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPDgPKRPGSVGLRlpyARVR 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 407 IRLADDD-------------ELMIKGPNVFLGYYKQpQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGK 473
Cdd:cd05944 187 IKVLDGVgrllrdcapdevgEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGH 264
|
330 340 350
....*....|....*....|....*....|...
gi 489915853 474 NISPAPMEDVINTCPIVAHAVVIGDGRPFIAAL 506
Cdd:cd05944 265 NIDPALIEEALLRHPAVAFAGAVGQPDAHAGEL 297
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
47-497 |
4.63e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 134.13 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFA 126
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 127 gDDSHAQILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNF 206
Cdd:PRK07786 121 -EAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 207 N-----HTVYNGYEVLNDMLYQPSrlllflPLAHCfaryiqyVAIGSHGVvGYIPSAKRLLADLRGFKPTYLLGVPRVfE 281
Cdd:PRK07786 200 TgqamtCLRTNGADINSDVGFVGV------PLFHI-------AGIGSMLP-GLLLGAPTVIYPLGAFDPGQLLDVLEA-E 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 282 KVynaasqkagaglkgrlfAKAFDHFVQWskdemagghhslgariqhsfymQTVGSSIRsALGPNMKW--LACGGAPL-N 358
Cdd:PRK07786 265 KV-----------------TGIFLVPAQW----------------------QAVCAEQQ-ARPRDLALrvLSWGAAPAsD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 359 ADLAHFFNGFDGITFIQGYGMTE-TAAPCLVNFQDA-NEVGSVGRP-GCISIRLADDD----------ELMIKGPNVFLG 425
Cdd:PRK07786 305 TLLRQMAATFPEAQILAAFGQTEmSPVTCMLLGEDAiRKLGSVGKViPTVAARVVDENmndvpvgevgEIVYRAPTLMSG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 426 YYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK07786 385 YWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
18-562 |
7.64e-33 |
|
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: 133.56 E-value: 7.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIAQWQDDETRQWhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:cd05906 11 TLLELLLRAAERGPTKGITYIDADGSEEF--QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPV-----YETDSPK--------QTGDivaevEPVIaFAGDDSHAQILEQI-RAHSESLRyvfnfkangldavADFG 163
Cdd:cd05906 89 FVPAPLtvpptYDEPNARlrklrhiwQLLG-----SPVV-LTDAELVAEFAGLEtLSGLPGIR-------------VLSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 164 ESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVyNGYEVLNDMLYQpSRLLLFLPLAHCFA---RY 240
Cdd:cd05906 150 EELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARS-AGKIQHNGLTPQ-DVFLNWVPLDHVGGlveLH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 241 IQYVAIGSHGVvgYIPSAKrLLADlrgfkPTYLLgvpRVFEKvYNAAsqkagaglkgRLFAK--AFDHFVQwSKDEMAGG 318
Cdd:cd05906 228 LRAVYLGCQQV--HVPTEE-ILAD-----PLRWL---DLIDR-YRVT----------ITWAPnfAFALLND-LLEEIEDG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 319 HHSLGA-RiqhsfYMQTVGSSIRSALGPN-MKWLACGGAPLNAdlahffngfdgitFIQGYGMTETAAPCLVN------- 389
Cdd:cd05906 285 TWDLSSlR-----YLVNAGEAVVAKTIRRlLRLLEPYGLPPDA-------------IRPAFGMTETCSGVIYSrsfptyd 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 390 FQDANEVGSVGR--PGCiSIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDrGFV 457
Cdd:cd05906 347 HSQALEFVSLGRpiPGV-SMRIVDDEgqllpegevgRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 458 FITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAvvigdgrpFIAALIELDAEMTRSWLA---SQNLDIDAPMSEiaT 534
Cdd:cd05906 425 TITGRTKDTIIV-NGVNYYSHEIEAAVEEVPGVEPS--------FTAAFAVRDPGAETEELAiffVPEYDLQDALSE--T 493
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 489915853 535 NDAVRALV---------------QQYIDK-ANGNVSRAESVRKF 562
Cdd:cd05906 494 LRAIRSVVsrevgvspayliplpKEEIPKtSLGKIQRSKLKAAF 537
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
18-496 |
1.85e-32 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 132.19 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIaqWQDDETRqWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:PRK06155 22 TLPAMLARQAERYPDRPL--LVFGGTR-W---TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVYETDSPKQTGDIVAEVEPViAFAGDDSHAQILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKAI-- 175
Cdd:PRK06155 96 AIAVPINTALRGPQLEHILRNSGAR-LLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPApa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 176 GRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVL----NDMLYQpsrlllFLPLAH--CFARYIQYVAIGSH 249
Cdd:PRK06155 175 AAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLeigaDDVLYT------TLPLFHtnALNAFFQALLAGAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 250 GVVGYIPSAKRLLADLR--GFKPTYLLGvprvfEKVYNAASQKAGAGLKGrlfakafdhfvqwskdemagghhslgariq 327
Cdd:PRK06155 249 YVLEPRFSASGFWPAVRrhGATVTYLLG-----AMVSILLSQPARESDRA------------------------------ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 328 hsfymqtvgSSIRSALGPnmkwlacGGAPlnADLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANEvGSVGR--PGcI 405
Cdd:PRK06155 294 ---------HRVRVALGP-------GVPA--ALHAAFRERF-GVDLLDGYGSTETNFVIAVTHGSQRP-GSMGRlaPG-F 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 406 SIRLADDD----------ELMIKG--PNVFL-GYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGG 472
Cdd:PRK06155 353 EARVVDEHdqelpdgepgELLLRAdePFAFAtGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKD-AIRRRG 430
|
490 500
....*....|....*....|....
gi 489915853 473 KNISPAPMEDVINTCPIVAHAVVI 496
Cdd:PRK06155 431 ENISSFEVEQVLLSHPAVAAAAVF 454
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
21-497 |
2.11e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.55 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 21 SLLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVS 100
Cdd:PRK06145 6 ASIAFHARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 101 VPVYETDSPKQTGDIVAEVEPVIAFAGDD-------SHAQILEQIRAHSESLRyvfnfkangldaVADFGESVSDEELdk 173
Cdd:PRK06145 80 LPINYRLAADEVAYILGDAGAKLLLVDEEfdaivalETPKIVIDAAAQADSRR------------LAQGGLEIPPQAA-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 174 aigrVRADDLFTIVYTSGSTGKPKGVMLSHRNF-----NHTVYNGyevlndmLYQPSRLLLFLPLAHCFARYIQYVAIGS 248
Cdd:PRK06145 146 ----VAPTDLVRLMYTSGTTDRPKGVMHSYGNLhwksiDHVIALG-------LTASERLLVVGPLYHVGAFDLPGIAVLW 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 249 HGvvgyipsakRLLADLRGFKPtyllgvprvfEKVYNAASQKAgagLKGRLFAKafdhfVQWSKdemagghhslgariqh 328
Cdd:PRK06145 215 VG---------GTLRIHREFDP----------EAVLAAIERHR---LTCAWMAP-----VMLSR---------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 sfyMQTVGSSIRSALGpNMKWLACGGAPL-NADLAHFFNGFDGITFIQGYGMTETAA--PCLVNFQDANEVGSVGRP-GC 404
Cdd:PRK06145 252 ---VLTVPDRDRFDLD-SLAWCIGGGEKTpESRIRDFTRVFTRARYIDAYGLTETCSgdTLMEAGREIEKIGSTGRAlAH 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 405 ISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKN 474
Cdd:PRK06145 328 VEIRIADGAgrwlppnmkgEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGEN 405
|
490 500
....*....|....*....|...
gi 489915853 475 ISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK06145 406 IASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
22-497 |
3.03e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 131.32 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 22 LLAKRCERDPDDlIAQWQDDETRQWhdvsaGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV 101
Cdd:PRK07470 12 FLRQAARRFPDR-IALVWGDRSWTW-----REIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 102 PVyetdSPKQTGDIVA---EVEPVIAFAGDDSHAQILEQIRAHSESLRYVFNFKAngldavADFGESVSD---EELDKAI 175
Cdd:PRK07470 86 PT----NFRQTPDEVAylaEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGG------ARAGLDYEAlvaRHLGARV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 176 --GRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRLLLFLPLAHcfARYIQYVAIGSHGVVG 253
Cdd:PRK07470 156 anAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEQDASLVVAPLSH--GAGIHQLCQVARGAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 254 YIPSAKRLLAD-----LRGFKPTYLLGVPRVFEKVYNAASqkagaglkgrlfAKAFDHfvqwskdemagghhslgariqh 328
Cdd:PRK07470 234 VLLPSERFDPAevwalVERHRVTNLFTVPTILKMLVEHPA------------VDRYDH---------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 sfymqtvgSSIRsalgpnmkWLACGGAPL-NADLAHFFNGFdGITFIQGYGMTETAA------PCLVNFQDANEV--GSV 399
Cdd:PRK07470 280 --------SSLR--------YVIYAGAPMyRADQKRALAKL-GKVLVQYFGLGEVTGnitvlpPALHDAEDGPDAriGTC 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 400 GRP--GcISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDII 467
Cdd:PRK07470 343 GFErtG-MEVQIQDDEgrelppgetgEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY 420
|
490 500 510
....*....|....*....|....*....|
gi 489915853 468 ITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK07470 421 IS-GGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
180-497 |
5.05e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 131.04 E-value: 5.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 180 ADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRLLLF-LPLAHCFARYIQYVA---IGSHGVVgyI 255
Cdd:PRK05677 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIApLPLYHIYAFTFHCMAmmlIGNHNIL--I 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 256 PSAKRLLA---DLRGFKPTYLLGVPRVFEKVYNAASqkagaglkgrlfAKAFDHfvqwskdemagghhslgariqhsfym 332
Cdd:PRK05677 284 SNPRDLPAmvkELGKWKFSGFVGLNTLFVALCNNEA------------FRKLDF-------------------------- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 333 qtvgssirSALgpnmKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRP-GCISIRLAD 411
Cdd:PRK05677 326 --------SAL----KLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPvPSTLCKVID 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 412 DD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAgGKNISPAPME 481
Cdd:PRK05677 394 DDgnelplgevgELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS-GFNVYPNELE 472
|
330
....*....|....*.
gi 489915853 482 DVINTCPIVAHAVVIG 497
Cdd:PRK05677 473 DVLAALPGVLQCAAIG 488
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
181-497 |
5.40e-32 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 130.94 E-value: 5.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRL-LLFLPLAHCFARYIQ---YVAIGSHGVVGY-- 254
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGKELvVTALPLYHIFALTVNcllFIELGGQNLLITnp 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 255 --IPSakrLLADLRGFKPTYLLGVPRVFEKVYNAasqkagaglkgrlfaKAFdhfvqwskdemagghHSLgariqhSFym 332
Cdd:PRK08974 286 rdIPG---FVKELKKYPFTAITGVNTLFNALLNN---------------EEF---------------QEL------DF-- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 333 qtvgSSIRSALGpnmkwlacGGAPLNADLAHFFNGFDGITFIQGYGMTETA---APCLVNFQDANevGSVGRP-GCISIR 408
Cdd:PRK08974 325 ----SSLKLSVG--------GGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDYYS--GSIGLPvPSTEIK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 409 LADDD----------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITAgGKNISPA 478
Cdd:PRK08974 391 LVDDDgnevppgepgELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPN 468
|
330
....*....|....*....
gi 489915853 479 PMEDVINTCPIVAHAVVIG 497
Cdd:PRK08974 469 EIEDVVMLHPKVLEVAAVG 487
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
49-497 |
8.78e-32 |
|
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: 129.80 E-value: 8.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGD 128
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQILEQIRAHSESLRYVFNFK-ANGLDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFN 207
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIVSGgAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 HTVYN-GYEVL----NDMLYQPSRLL--------LFLPLAhcfaryiqyvaIGSHGVV-GYIPSAKRLLADLRGFKPTYL 273
Cdd:cd05959 190 WTAELyARNVLgireDDVCFSAAKLFfayglgnsLTFPLS-----------VGATTVLmPERPTPAAVFKRIRRYRPTVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 274 LGVPRVFekvynaASQKAGAGLKGRLFakafdhfvqwskdemagghhslgariqhsfymqtvgSSIRSALGpnmkwlacG 353
Cdd:cd05959 259 FGVPTLY------AAMLAAPNLPSRDL------------------------------------SSLRLCVS--------A 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 354 GAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGcISIRLADDD----------ELMIKGPN 421
Cdd:cd05959 289 GEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKpvPG-YEVELRDEDggdvadgepgELYVRGPS 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 422 VFLGYYKQPQRTAEALTSdGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05959 368 SATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADD-MLKVSGIWVSPFEVESALVQHPAVLEAAVVG 441
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
49-524 |
2.53e-31 |
|
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: 127.19 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSPKQTgdivaevEPVIAFAGD 128
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVI----NPLLH-------PDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQILeqirahseslryvfnfkangldaVADfgesvsdeeldkaigrvrADDLFTIVYTSGSTGKPKGVMLSHRNFNH 208
Cdd:cd05919 80 DCEARLV-----------------------VTS------------------ADDIAYLLYSSGTTGPPKGVMHAHRDPLL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 209 TVYN-GYEVL----NDMLYQPSRLL--------LFLPLAhcfaryiqyvaIGSHGVV-GYIPSAKRLLADLRGFKPTYLL 274
Cdd:cd05919 119 FADAmAREALgltpGDRVFSSAKMFfgyglgnsLWFPLA-----------VGASAVLnPGWPTAERVLATLARFRPTVLY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 275 GVPRvfekvynaasqkagaglkgrLFAKAFDhfvqwskdemagghhsLGARIQHSFymqtvgSSIRSALGpnmkwlacGG 354
Cdd:cd05919 188 GVPT--------------------FYANLLD----------------SCAGSPDAL------RSLRLCVS--------AG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 355 APLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGcISIRLADDD----------ELMIKGPNV 422
Cdd:cd05919 218 EALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRpvPG-YEIRLVDEEghtippgeegDLLVRGPSA 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 423 FLGYYKQPQRTaEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG----D 498
Cdd:cd05919 297 AVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQHPAVAEAAVVAvpesT 374
|
490 500
....*....|....*....|....*.
gi 489915853 499 GRPFIAALIELDAEMTRSWLASQNLD 524
Cdd:cd05919 375 GLSRLTAFVVLKSPAAPQESLARDIH 400
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
18-497 |
6.14e-31 |
|
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: 127.24 E-value: 6.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDdliaQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:cd05923 2 TVFEMLRRAASRAPD----ACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDshAQILEQIR-AHSESLRyvfnfkangLDAVADFGESVSDEELDKAIG 176
Cdd:cd05923 78 AVPALINPRLKAAELAELIERGEMTAAVIAVD--AQVMDAIFqSGVRVLA---------LSDLVGLGEPESAGPLIEDPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 177 RVRADDLFtIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRLLLFLPLAHC---FARYIQYVAIGSHGVVG 253
Cdd:cd05923 147 REPEQPAF-VFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVigfFAVLVAALALDGTYVVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 254 YIPSAKRLLADLRGFKPTYLLGVPRVFEKVYnAASQKAGAGLkgrlfakafdhfvqwskdemagghhslgariqhsfymq 333
Cdd:cd05923 226 EEFDPADALKLIEQERVTSLFATPTHLDALA-AAAEFAGLKL-------------------------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 334 tvgSSIRSalgpnmkwLACGGAPLNADLAHFFNGFDGITFIQGYGMTETaapclVNF---QDANEvGSVGRPGCIS-IRL 409
Cdd:cd05923 267 ---SSLRH--------VTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA-----MNSlymRDART-GTEMRPGFFSeVRI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 410 A-------------DDDELMIK--GPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKN 474
Cdd:cd05923 330 VriggspdealangEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGEN 407
|
490 500
....*....|....*....|...
gi 489915853 475 ISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIG 430
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
182-521 |
1.01e-30 |
|
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: 123.21 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHC--FARYIQYVAIGSHGVVgyIPSAK 259
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG--FGGGDSWLLSLPLYHVggLAILVRSLLAGAELVL--LERNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 260 RLLADLRGFKPTYLLGVPRVFEKVYnAASQKAGAglkgrlfAKAFDHfvqwskdemagghhslgariqhsfymqtvgssi 339
Cdd:cd17630 77 ALAEDLAPPGVTHVSLVPTQLQRLL-DSGQGPAA-------LKSLRA--------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 340 rsalgpnmkwLACGGAPLNADLAHFFNGFdGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGcISIRLADDDELMI 417
Cdd:cd17630 116 ----------VLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATKRPDGFGRGGVGVllPG-RELRIVEDGEIWV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 418 KGPNVFLGYYKQPQRtaEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd17630 184 GGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAHPAVRDAFVVG 260
|
330 340 350
....*....|....*....|....*....|....
gi 489915853 498 DG------RPfiAALIELDAEMT----RSWLASQ 521
Cdd:cd17630 261 VPdeelgqRP--VAVIVGRGPADpaelRAWLKDK 292
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
182-497 |
1.18e-30 |
|
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: 122.99 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNfNHTVYNGYEVLNDmLYQPSRLLLFLPLAHCFARYIQYVAIGSHG------VVGYI 255
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQ-TLRAAAAWADCAD-LTEDDRYLIINPFFHTFGYKAGIVACLLTGatvvpvAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 256 PSAKRLLADLRgfkPTYLLGVPRVFEKVYNAASQKagaglKGRLfakafdhfvqwskdemagghhslgariqhsfymqtv 335
Cdd:cd17638 79 DAILEAIERER---ITVLPGPPTLFQSLLDHPGRK-----KFDL------------------------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 336 gSSIRSALgpnmkwlaCGGAPLNADLAHFFN---GFDGITfiQGYGMTETAAPCLVNFQDANEV--GSVGR--PGcISIR 408
Cdd:cd17638 115 -SSLRAAV--------TGAATVPVELVRRMRselGFETVL--TAYGLTEAGVATMCRPGDDAETvaTTCGRacPG-FEVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 409 LADDDELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIItAGGKNISPAPMEDVINTCP 488
Cdd:cd17638 183 IADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGALAEHP 261
|
....*....
gi 489915853 489 IVAHAVVIG 497
Cdd:cd17638 262 GVAQVAVIG 270
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
52-501 |
5.24e-30 |
|
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: 124.33 E-value: 5.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYA---ATCYEwgvVDFACASIGAVSVPV-YETDSPKqtgdivaevepvIAFag 127
Cdd:cd12118 33 RQTYDRCRRLASALAALGISRGDTVAVLApntPAMYE---LHFGVPMAGAVLNALnTRLDAEE------------IAF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 128 ddshaqILEqiraHSESlRYVF---NFKANGLDAVADfgesvSDEELDKAIGRvraDDLFTIVYTSGSTGKPKGVMLSHR 204
Cdd:cd12118 96 ------ILR----HSEA-KVLFvdrEFEYEDLLAEGD-----PDFEWIPPADE---WDPIALNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 205 N-FNHTVYNGYEvlNDMlYQPSRLLLFLPLAHC----FARYIqyVAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRV 279
Cdd:cd12118 157 GaYLNALANILE--WEM-KQHPVYLWTLPMFHCngwcFPWTV--AAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 280 FEKVYNAASQKAgaglkgrlfaKAFDHFVQwskdemagghhslgariqhsfyMQTVGSSIRSALGPNMKWLacggaplna 359
Cdd:cd12118 232 LNMLANAPPSDA----------RPLPHRVH----------------------VMTAGAPPPAAVLAKMEEL--------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 360 dlahffngfdGITFIQGYGMTETAAPCLVN-FQDA-NEVGS-----------VGRPGCISIRLADDD------------- 413
Cdd:cd12118 271 ----------GFDVTHVYGLTETYGPATVCaWKPEwDELPTeerarlkarqgVRYVGLEEVDVLDPEtmkpvprdgktig 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHA 493
Cdd:cd12118 341 EIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGVLYKHPAVLEA 418
|
....*...
gi 489915853 494 VVIgdGRP 501
Cdd:cd12118 419 AVV--ARP 424
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
48-567 |
9.45e-30 |
|
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: 124.18 E-value: 9.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 48 DVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAG 127
Cdd:cd17642 44 NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 128 DDShaqiLEQIRAHSESLRYVFNFKAngLDAVADFGESVSDEELD-------------KAIGRVRADDLFTIVYTSGSTG 194
Cdd:cd17642 124 KKG----LQKVLNVQKKLKIIKTIII--LDSKEDYKGYQCLYTFItqnlppgfneydfKPPSFDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 195 KPKGVMLSHRN----FNHTVYngyEVLNDMLYQPSRLLLFLPLAHCFARY--IQYVAIGSHGVVGYIPSAKRLLADLRGF 268
Cdd:cd17642 198 LPKGVQLTHKNivarFSHARD---PIFGNQIIPDTAILTVIPFHHGFGMFttLGYLICGFRVVLMYKFEEELFLRSLQDY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 269 KPTYLLGVPRVFEkvynaasqkagaglkgrLFAKafdhfvqwskdemagghHSLGARIQHSfymqtvgssirsalgpNMK 348
Cdd:cd17642 275 KVQSALLVPTLFA-----------------FFAK-----------------STLVDKYDLS----------------NLH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 349 WLACGGAPLNADLAHFFNGFDGITFI-QGYGMTETAAPCLVNFQDANEVGSVGR--PGcISIRLADDD-----------E 414
Cdd:cd17642 305 EIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKvvPF-FYAKVVDLDtgktlgpnergE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 415 LMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAV 494
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQHPKIFDAG 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489915853 495 VIG----DGRPFIAALIELDAEMTrswlasqnldidapMSEiatndavralvQQYIDKANGNVSRAESVRKFVI-LDE 567
Cdd:cd17642 463 VAGipdeDAGELPAAVVVLEAGKT--------------MTE-----------KEVMDYVASQVSTAKRLRGGVKfVDE 515
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
181-497 |
1.17e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 124.16 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFnhtVYNGYEVLNDMLYQ-PSRLLLF----------LPLAHCFARYIQYVAI--- 246
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNL---VANMLQVRACLSQLgPDGQPLMkegqevmiapLPLYHIYAFTANCMCMmvs 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 247 GSHGVVGYIP-SAKRLLADLRGFKPTYLLGVprvfekvynaasqkagaglkGRLFAKAFDHfvqwskdemagghhslgar 325
Cdd:PRK12492 284 GNHNVLITNPrDIPGFIKELGKWRFSALLGL--------------------NTLFVALMDH------------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 326 iqhsfymqtvgSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVN-FQDANEVGSVGRP-G 403
Cdd:PRK12492 325 -----------PGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNpYGELARLGTVGIPvP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 404 CISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAgGK 473
Cdd:PRK12492 394 GTALKVIDDDgnelplgergELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS-GF 472
|
330 340
....*....|....*....|....
gi 489915853 474 NISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK12492 473 NVYPNEIEDVVMAHPKVANCAAIG 496
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
178-501 |
3.63e-29 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 121.67 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 178 VRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVL----NDmlyqpsRLLLFLPLAHCFARYIQYVA---IGSHG 250
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFdpnpED------VVFGALPFFHSFGLTGCLWLpllSGIKV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 251 VVGYIPSAKRLLADL-RGFKPTYLLGVPrVFekvynaasqkagagLKGrlFAKAfdhfvqWSKDEMagghhslgariqhs 329
Cdd:cd05909 218 VFHPNPLDYKKIPELiYDKKATILLGTP-TF--------------LRG--YARA------AHPEDF-------------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 330 fymqtvgSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGYGMTEtAAPCL-VNF-QDANEVGSVGRP----- 402
Cdd:cd05909 261 -------SSLRLVV--------AGAEKLKDTLRQEFQEKFGIRILEGYGTTE-CSPVIsVNTpQSPNKEGTVGRPlpgme 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 -------GCISIRLADDDELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNI 475
Cdd:cd05909 325 vkivsveTHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMV 402
|
330 340
....*....|....*....|....*....
gi 489915853 476 SPAPMEDVINT-CPI-VAHAVV-IGDGRP 501
Cdd:cd05909 403 SLEAIEDILSEiLPEdNEVAVVsVPDGRK 431
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
48-502 |
4.04e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 122.45 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 48 DVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV---PVY-ETDSPKQTGDIVAEV---- 119
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYtERELEYQLHDSGAKVilcl 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 120 EPVIAFAGDDSHAQILEQI--------RAHSESLRYVF-NFKANGLDAVADFGESVS-----DEELDKAIGRV--RADDL 183
Cdd:PRK06710 129 DLVFPRVTNVQSATKIEHVivtriadfLPFPKNLLYPFvQKKQSNLVVKVSESETIHlwnsvEKEVNTGVEVPcdPENDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 184 FTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRLLLFLPLAHCFARyiqyvaigshgvvgyipSAKRLLA 263
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGM-----------------TAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 264 DLRGFKptyLLGVPRVFEKVYNAASQKAgaglKGRLFAKAFDHFVqwskdemagghhslgARIQHSFYMQTVGSSIRSAL 343
Cdd:PRK06710 272 IMQGYK---MVLIPKFDMKMVFEAIKKH----KVTLFPGAPTIYI---------------ALLNSPLLKEYDISSIRACI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 344 GpnmkwlacGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEV-GSVGRPGCIS------------IRLA 410
Cdd:PRK06710 330 S--------GSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTeamimsletgeaLPPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 411 DDDELMIKGPNVFLGYYKQPQRTAeALTSDGWLHTGDLATIDDRGFVFITGRKKDIIItAGGKNISPAPMEDVINTCPIV 490
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEEVLYEHEKV 479
|
490
....*....|..
gi 489915853 491 AHAVVIGDGRPF 502
Cdd:PRK06710 480 QEVVTIGVPDPY 491
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
182-497 |
9.16e-29 |
|
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: 117.37 E-value: 9.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFnhtVYNGYEVLNDM-LYQPSRLLLFLPLAH----CFARYIQYVaiGSHGVVGYIP 256
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNL---IAANLQLIHAMgLTEADVYLNMLPLFHiaglNLALATFHA--GGANVVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 257 SAKRLLADLRGFKPTYLLGVPRVFekvynaasqkagaglkGRLFAKAFDHFVQWSkdemagghhslgariqhsfymqtvg 336
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPIL----------------SNLLDAAEKSGVDLS------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 337 sSIRSALGPNM-----KWLACGGAplnadlahffngfdgiTFIQGYGMTETAapCLVNFQDANEV-GSVGRPGCIS-IRL 409
Cdd:cd17637 115 -SLRHVLGLDApetiqRFEETTGA----------------TFWSLYGQTETS--GLVTLSPYRERpGSAGRPGPLVrVRI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 410 ADDD----------ELMIKGPNVFLGYYKQPQRTAEAlTSDGWLHTGDLATIDDRGFVFITGRK--KDIIITaGGKNISP 477
Cdd:cd17637 176 VDDNdrpvpagetgEIVVRGPLVFQGYWNLPELTAYT-FRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYP 253
|
330 340
....*....|....*....|
gi 489915853 478 APMEDVINTCPIVAHAVVIG 497
Cdd:cd17637 254 AEVEKVILEHPAIAEVCVIG 273
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
49-513 |
1.35e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 120.45 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLG-LGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPV-----------YETDSPKQTGDIV 116
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVnpmnreeelahYVTDSGARVAIVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 117 AEVEPVIAFAGDDSH------AQILEQIRAHSESLRYVFNFKANGLDAVADFG----ESVSDEELDKAIGRVRADDLFTI 186
Cdd:PRK08314 116 SELAPKVAPAVGNLRlrhvivAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGGvvawKEALAAGLAPPPHTAGPDDLAVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 187 VYTSGSTGKPKGVMLSHRNFNHTVYNGyeVLNDMLYQPSRLLLFLPLAHCFAryIQYV---AIGSHGVVGYIP-----SA 258
Cdd:PRK08314 196 PYTSGTTGVPKGCMHTHRTVMANAVGS--VLWSNSTPESVVLAVLPLFHVTG--MVHSmnaPIYAGATVVLMPrwdreAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 259 KRLLADLR----GFKPTY---LLGVPRVfekvynaasqkagaglkgrlfaKAFDHfvqwskdemagghhslgariqhsfy 331
Cdd:PRK08314 272 ARLIERYRvthwTNIPTMvvdFLASPGL----------------------AERDL------------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 332 mqtvgSSIRSALGpnmkwlacGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANevgsvgRPGCISIRLAD 411
Cdd:PRK08314 305 -----SSLRYIGG--------GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRP------KLQCLGIPTFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 412 DD------------------ELMIKGPNVFLGYYKQPQRTAEA-LTSDG--WLHTGDLATIDDRGFVFITGRKKDiIITA 470
Cdd:PRK08314 366 VDarvidpetleelppgevgEIVVHGPQVFKGYWNRPEATAEAfIEIDGkrFFRTGDLGRMDEEGYFFITDRLKR-MINA 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489915853 471 GGKNISPAPMEDVINTCPIVAHAVVIGDGRPF----IAALIELDAEM 513
Cdd:PRK08314 445 SGFKVWPAEVENLLYKHPAIQEACVIATPDPRrgetVKAVVVLRPEA 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
52-495 |
1.38e-28 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 118.52 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGL-GVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPkqtgdivaevEPVIAFAGDDS 130
Cdd:TIGR01733 3 RELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-DPAYP----------AERLAFILEDA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 131 HAQILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKAigRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTV 210
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA--PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 211 yngyEVLNDM--LYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSA-----KRLLADL-RGFKPTYLLGVPRVFek 282
Cdd:TIGR01733 150 ----AWLARRygLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeerddAALLAALiAEHPVTVLNLTPSLL-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 283 vynaasqkagaglkgrlfakafdhfvqwskdemagghhslgariqhsfymQTVGSSIRSALgPNMKWLACGGAPLNADLA 362
Cdd:TIGR01733 224 --------------------------------------------------ALLAAALPPAL-ASLRLVILGGEALTPALV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 363 HFFNG-FDGITFIQGYGMTETAAPCLVNFQDANEVGS-----VGRP-GCISIRLADDD----------ELMIKGPNVFLG 425
Cdd:TIGR01733 253 DRWRArGPGARLINLYGPTETTVWSTATLVDPDDAPRespvpIGRPlANTRLYVLDDDlrpvpvgvvgELYIGGPGVARG 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489915853 426 YYKQPQRTAEALTSDG--------WLHTGDLATIDDRGFVFITGRkKDIIITAGGKNISPAPMEDVINTCPIVAHAVV 495
Cdd:TIGR01733 333 YLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLPDGNLEFLGR-IDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
182-495 |
3.63e-28 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 115.82 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNF----NHTVYNGYEVLN-DMLYQPsrlllfLPLAHCFAR-YIQYVAIGSHGVV--G 253
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFfavpDILQKEGLNWVVgDVTYLP------LPATHIGGLwWILTCLIHGGLCVtgG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 254 YIPSAKRLLADLRGFKPTYLLGVPRVFEKVYNaasqkagaglkgrlfakafdhfvqwskdemagghhslgariqhsFYMQ 333
Cdd:cd17635 76 ENTTYKSLFKILTTNAVTTTCLVPTLLSKLVS--------------------------------------------ELKS 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 334 TVGSSirsalgPNMKWLACGGA-PLNADLAhFFNGFDGITFIQGYGMTETAAPCLVNF-QDANEVGSVGR--PGcISIRL 409
Cdd:cd17635 112 ANATV------PSLRLIGYGGSrAIAADVR-FIEATGLTNTAQVYGLSETGTALCLPTdDDSIEINAVGRpyPG-VDVYL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 410 ADDD----------ELMIKGPNVFLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFITGRKKDIIItAGGKNISPAP 479
Cdd:cd17635 184 AATDgiagpsasfgTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESIN-CGGVKIAPDE 261
|
330
....*....|....*.
gi 489915853 480 MEDVINTCPIVAHAVV 495
Cdd:cd17635 262 VERIAEGVSGVQECAC 277
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
17-521 |
4.83e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 119.08 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 17 DTIYSLLAKRCERDPDDliAQWQDDETrqwhDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASI 96
Cdd:PRK06164 10 DTLASLLDAHARARPDA--VALIDEDR----PLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 97 GAVSVPVYETDSPKQTGDIVAEVEPVI-----AFAGDDsHAQILEQIrAHSE--SLRYVFNFKANGLDAVAD-FGESV-- 166
Cdd:PRK06164 84 GATVIAVNTRYRSHEVAHILGRGRARWlvvwpGFKGID-FAAILAAV-PPDAlpPLRAIAVVDDAADATPAPaPGARVql 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 167 ----SDEELDKAIGRVRADDLFTIVYT-SGSTGKPKGVMLSHRNF---NHTVYNGYEVLNDmlyqpSRLLLFLPLAhcfa 238
Cdd:PRK06164 162 falpDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLlrhARAIARAYGYDPG-----AVLLAALPFC---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 239 ryiqyvaigshGVVGYipsaKRLLADLRGfkptyllGVPRVFEKVYNAAsqkagaglkgRLFAKAFDHFVQ--WSKDEMA 316
Cdd:PRK06164 233 -----------GVFGF----STLLGALAG-------GAPLVCEPVFDAA----------RTARALRRHRVThtFGNDEML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 317 GGHHSLGARIQHSFYMQTVG-SSIRSALGPNMKWLACGGAPLNadlahffngfdGItfiqgYGMTETAApcLVNFQDANE 395
Cdd:PRK06164 281 RRILDTAGERADFPSARLFGfASFAPALGELAALARARGVPLT-----------GL-----YGSSEVQA--LVALQPATD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 396 VGSV-----GRP--GCISIRLADDD-----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLA-TIDDRGF 456
Cdd:PRK06164 343 PVSVrieggGRPasPEARVRARDPQdgallpdgesgEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGyTRGDGQF 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915853 457 VFITgRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVVIG---DGRPFIAALI------ELDAEMTRSWLASQ 521
Cdd:PRK06164 423 VYQT-RMGD-SLRLGGFLVNPAEIEHALEALPGVAAAQVVGatrDGKTVPVAFViptdgaSPDEAGLMAACREA 494
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
178-497 |
6.76e-28 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 118.58 E-value: 6.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 178 VRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNDMLYQPSRL--LLF---LPLAHCFARYIQY---VAIGSH 249
Cdd:PRK07059 201 LGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqLNFvcaLPLYHIFALTVCGllgMRTGGR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 250 GVVgyIPSAKR---LLADLRGFKPTYLLGVprvfEKVYNAASQKAGaglkgrlFAKafdhfVQWSKDEMA-GGhhslgar 325
Cdd:PRK07059 281 NIL--IPNPRDipgFIKELKKYQVHIFPAV----NTLYNALLNNPD-------FDK-----LDFSKLIVAnGG------- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 326 iqhsfymqtvGSSIRSALGPnmKWLACGGAPLnadlahffngfdgitfIQGYGMTETAaPCL-VNFQDANE-VGSVGRP- 402
Cdd:PRK07059 336 ----------GMAVQRPVAE--RWLEMTGCPI----------------TEGYGLSETS-PVAtCNPVDATEfSGTIGLPl 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 --GCISIRlaDDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITA 470
Cdd:PRK07059 387 psTEVSIR--DDDgndlplgepgEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
330 340
....*....|....*....|....*..
gi 489915853 471 gGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK07059 465 -GFNVYPNEIEEVVASHPGVLEVAAVG 490
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
53-497 |
1.16e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 117.48 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdspkQTGDIVAEVEPVI------AFA 126
Cdd:PRK08008 42 ELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI-------NARLLREESAWILqnsqasLLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 127 GDDSHAQILEQIRAH-SESLRYVFNFKANG--LDAVADFGESVSDE--ELDKAIGrVRADDLFTIVYTSGSTGKPKGVML 201
Cdd:PRK08008 115 TSAQFYPMYRQIQQEdATPLRHICLTRVALpaDDGVSSFTQLKAQQpaTLCYAPP-LSTDDTAEILFTSGTTSRPKGVVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 202 SHRNFNHTVYngYEVLNDMLYQPSRLLLFLPLAH----CFARYIQYVAiGSHGVVGYIPSAKRLLADLRGFKPTYLLGVP 277
Cdd:PRK08008 194 THYNLRFAGY--YSAWQCALRDDDVYLTVMPAFHidcqCTAAMAAFSA-GATFVLLEKYSARAFWGQVCKYRATITECIP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 278 rvfekvynaasqkagaglkgrlfakafdhfvqwskdeMagghhslgarIQHSFYMQTVGSSIRS-ALGPNMKWLACGGAP 356
Cdd:PRK08008 271 -------------------------------------M----------MIRTLMVQPPSANDRQhCLREVMFYLNLSDQE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 357 LNADLAHFfngfdGITFIQGYGMTETAAPCLVNFQ-DANEVGSVGRPG-CISIRLADDD----------ELMIKG---PN 421
Cdd:PRK08008 304 KDAFEERF-----GVRLLTSYGMTETIVGIIGDRPgDKRRWPSIGRPGfCYEAEIRDDHnrplpageigEICIKGvpgKT 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 422 VFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK08008 379 IFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCN-MIKRGGENVSCVELENIIATHPKIQDIVVVG 453
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
21-497 |
1.37e-27 |
|
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: 116.66 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 21 SLLAKRCERDPDDlIAQWQDDetRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVs 100
Cdd:cd05920 19 DLLARSAARHPDR-IAVVDGD--RRL---TYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 101 vpvyetdspkqtgdivaevePVIAFAGDDSHAqiLEQIRAHSESLRYVFNFKANGLDAVADFGESVSDeeldkaigrVRA 180
Cdd:cd05920 92 --------------------PVLALPSHRRSE--LSAFCAHAEAVAYIVPDRHAGFDHRALARELAES---------IPE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIvyTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFAryiqyvaIGSHGVVGyipsakr 260
Cdd:cd05920 141 VALFLL--SGGTTGTPKLIPRTHNDYAYNVRASAEVCG--LDQDTVYLAVLPAAHNFP-------LACPGVLG------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 261 lladlrgfkpTYLLGvprvfEKVYNAASQKAGAGLKgrLFAKafdhfvqwskdemaggHHSLGARIQHSFYMQTVGSSIR 340
Cdd:cd05920 203 ----------TLLAG-----GRVVLAPDPSPDAAFP--LIER----------------EGVTVTALVPALVSLWLDAAAS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 341 SALGP-NMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETaapcLVNF---QDANEV--GSVGRPGCI--SIRLADD 412
Cdd:cd05920 250 RRADLsSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEG----LLNYtrlDDPDEViiHTQGRPMSPddEIRVVDE 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 413 D----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMED 482
Cdd:cd05920 326 EgnpvppgeegELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVEN 404
|
490
....*....|....*
gi 489915853 483 VINTCPIVAHAVVIG 497
Cdd:cd05920 405 LLLRHPAVHDAAVVA 419
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
18-497 |
4.20e-27 |
|
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: 115.65 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIAQWQDdetrqwHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHD------RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVYETDSPKQTGDIVAevepviafagdDSHAQIL----EQIR------AHSESLRYVFNFKANGLDAVADFGESVS 167
Cdd:TIGR03098 75 GVFVPINPLLKAEQVAHILA-----------DCNVRLLvtssERLDllhpalPGCHDLRTLIIVGDPAHASEGHPGEEPA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 168 DEELDKAIG------RVRADDLFTIVYTSGSTGKPKGVMLSHRNfnhtVYNGYEVLNDMLYQPS--RLLLFLPLAhcF-A 238
Cdd:TIGR03098 144 SWPKLLALGdadpphPVIDSDMAAILYTSGSTGRPKGVVLSHRN----LVAGAQSVATYLENRPddRLLAVLPLS--FdY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 239 RYIQYVAIGSHGvvgyipsAKRLLADlrgfkptYLLgvPRvfeKVYNAASQKAGAGLKG--RLFAKAFDhfVQWskdema 316
Cdd:TIGR03098 218 GFNQLTTAFYVG-------ATVVLHD-------YLL--PR---DVLKALEKHGITGLAAvpPLWAQLAQ--LDW------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 317 gghhslgariqhsfymqtvgssiRSALGPNMKWLA-CGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPclvNFQDANE 395
Cdd:TIGR03098 271 -----------------------PESAAPSLRYLTnSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFRS---TYLPPEE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 396 VGSvgRPGCI-------SIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTS----DGWLH-------TGD 447
Cdd:TIGR03098 325 VDR--RPDSIgkaipnaEVLVLREDgsecapgeegELVHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGD 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489915853 448 LATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIG 497
Cdd:TIGR03098 403 TVRRDEEGFLYFVGRRDEMIKTSGYR-VSPTEVEEVAYATGLVAEAVAFG 451
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
175-462 |
8.91e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.95 E-value: 8.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 175 IGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFARYIQ--YVAIGSHGVV 252
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN--LRNDDVILSSLPFFHSFGLTVTlwLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 253 gYIPS---AKRLLADLRGFKPTYLLGVPrVFEKVYnAASQKAgaglkgrlfakafdhfvqwsKDEMagghhslgariqhs 329
Cdd:PRK08633 854 -YHPDptdALGIAKLVAKHRATILLGTP-TFLRLY-LRNKKL--------------------HPLM-------------- 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 330 FymqtvgSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVN----------FQDANEVGSV 399
Cdd:PRK08633 897 F------ASLRLVV--------AGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNlpdvlaadfkRQTGSKEGSV 962
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489915853 400 GR--PGcISIRLADDDE-----------LMIKGPNVFLGYYKQPQRTAEALT---SDGWLHTGDLATIDDRGFVFITGR 462
Cdd:PRK08633 963 GMplPG-VAVRIVDPETfeelppgedglILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
11-497 |
8.92e-27 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 115.37 E-value: 8.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 11 YQTTDLDTIYSLLAKRCERDPDDLIAQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVD 90
Cdd:cd17634 47 FEDATLNLAANALDRHLRENGDRTAIIYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 91 FACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGD---------DSHAQILEQIRAHSESLRYVFNFKANGLD---- 157
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDDALNPNVTSVEHVIVLKRTGSDidwq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 158 --AVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMlsHRNFNHTVYNGYEVLNDMLYQPSRLLLflplah 235
Cdd:cd17634 207 egRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMKYVFDYGPGDIYW------ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 236 CFARyIQYVAIGSHGVVG-YIPSAKRLLADlrgfkptyllGVPrvfekVYNAAsqkagaglkGRLFAKAFDHfvqwskde 314
Cdd:cd17634 279 CTAD-VGWVTGHSYLLYGpLACGATTLLYE----------GVP-----NWPTP---------ARMWQVVDKH-------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 315 magghhslgaRIQHSFYMQTVGSSIRSAlGPN---------MKWLACGGAPLNADLAHFFN---GFDGITFIQGYGMTET 382
Cdd:cd17634 326 ----------GVNILYTAPTAIRALMAA-GDDaiegtdrssLRILGSVGEPINPEAYEWYWkkiGKEKCPVVDTWWQTET 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 383 AAPCLVNFQDANEV--GSVGRP--GcISIRLADDD----------ELMIKG--PNVFLGYYKQPQRTAEAL--TSDGWLH 444
Cdd:cd17634 395 GGFMITPLPGAIELkaGSATRPvfG-VQPAVVDNEghpqpggtegNLVITDpwPGQTRTLFGDHERFEQTYfsTFKGMYF 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489915853 445 TGDLATIDDRGFVFITGRKKDIIITAgGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd17634 474 SGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
57-506 |
1.01e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 113.69 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 57 RVREVAKGLLGLGVKPGSMVVIYAATCYEW-----GVVDFACAsIGAVSVPVYETDSPKQTGDIVAEVEPVIAFA---GD 128
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYielsfAVAYAGGR-LGLVFVPLNPTLKESVLRYLVADAGGRIVLAdagAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQILEQIRAHSESLRyvfnfkangLDAVADFGESVSDEELDKaigrvraDDLFTIVYTSGSTGKPKGVMLSHRNFnh 208
Cdd:cd05922 81 DRLRDALPASPDPGTVLD---------ADGIRAARASAPAHEVSH-------EDLALLLYTSGSTGSPKLVRLSHQNL-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 209 tVYNGYEVLNDMLYQPS-RLLLFLPLAHCFARYI--QYVAIGSHGVV--GYIPSAKrLLADLRGFKPTYLLGVPRVFEKV 283
Cdd:cd05922 143 -LANARSIAEYLGITADdRALTVLPLSYDYGLSVlnTHLLRGATLVLtnDGVLDDA-FWEDLREHGATGLAGVPSTYAML 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 284 YNAASQKAGAglkgrlfakafdhfvqwskdemagghhslgariqhsfymqtvgssirsalgPNMKWLA-CGGAPLNADLA 362
Cdd:cd05922 221 TRLGFDPAKL---------------------------------------------------PSLRYLTqAGGRLPQETIA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 363 HFFNGFDGITFIQGYGMTETAAPclVNFQDANEV----GSVGR--PGC-ISIRlaDDD----------ELMIKGPNVFLG 425
Cdd:cd05922 250 RLRELLPGAQVYVMYGQTEATRR--MTYLPPERIlekpGSIGLaiPGGeFEIL--DDDgtptppgepgEIVHRGPNVMKG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 426 YYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIGDGRPFIAA 505
Cdd:cd05922 326 YWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNR-ISPTEIEAAARSIGLIIEAAAVGLPDPLGEK 404
|
.
gi 489915853 506 L 506
Cdd:cd05922 405 L 405
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-513 |
1.73e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 112.96 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdspkqtgdivaevEPVIAfagd 128
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPI----------------NPMLK---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 dshaqileqirahSESLRYVFNfkangldavadfgesvsDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNH 208
Cdd:cd05935 62 -------------ERELEYILN-----------------DSGAKVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 209 TVYNgyEVLNDMLYQPSRLLLFLPLAHCfARYIQY----VAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEKVY 284
Cdd:cd05935 112 NALQ--SAVWTGLTPSDVILACLPLFHV-TGFVGSlntaVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 285 NAAsqkagaGLKGRLFAKafdhfvqwskdemagghhslgariqhsfymqtvgssirsalgpnMKWLACGGAPLNADLAHF 364
Cdd:cd05935 189 ATP------EFKTRDLSS--------------------------------------------LKVLTGGGAPMPPAVAEK 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 365 FNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPGC-ISIRLADDD-----------ELMIKGPNVFLGYYKQPQR 432
Cdd:cd05935 219 LLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FgVDARVIDIEtgrelppnevgEIVVRGPQIFKGYWNRPEE 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 433 TAEALTSDG---WLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIGDGRPFIA----A 505
Cdd:cd05935 299 TEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEVEAKLYKHPAI*EVCVISVPDERVGeevkA 377
|
....*...
gi 489915853 506 LIELDAEM 513
Cdd:cd05935 378 FIVLRPEY 385
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
186-497 |
4.75e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.01 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 186 IVYTSGSTGKPKGVMLSHRNFNHTVyngyevlnDMLYQ-----PSRLLLF-LPLAHCfaryiqyvaigsHGVV-GYI--- 255
Cdd:PRK07787 133 IVYTSGTTGPPKGVVLSRRAIAADL--------DALAEawqwtADDVLVHgLPLFHV------------HGLVlGVLgpl 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 256 -----------PSAKRLLADLRGfKPTYLLGVPRVFEKVynAASQKAGAGLKGrlfakafdhfvqwskdemagghhslgA 324
Cdd:PRK07787 193 rignrfvhtgrPTPEAYAQALSE-GGTLYFGVPTVWSRI--AADPEAARALRG--------------------------A 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 325 RIqhsfymqtvgssirsalgpnmkwLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRP-G 403
Cdd:PRK07787 244 RL-----------------------LVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPlA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 404 CISIRLADDD------------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAG 471
Cdd:PRK07787 301 GVETRLVDEDggpvphdgetvgELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSG 380
|
330 340
....*....|....*....|....*.
gi 489915853 472 GKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK07787 381 GYRIGAGEIETALLGHPGVREAAVVG 406
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-497 |
9.21e-26 |
|
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: 110.60 E-value: 9.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYetdspkqtgdivaevepviAFAGD 128
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLF-------------------ALFGP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DShaqiLEQIRAHSESlryvfnfkanglDAVadfgesVSDEeldkaigrvrADDLFTIVYTSGSTGKPKGVMLSHRnfnh 208
Cdd:cd05971 68 EA----LEYRLSNSGA------------SAL------VTDG----------SDDPALIIYTSGTTGPPKGALHAHR---- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 209 tVYNGYEVLNDMLYQpsrllLFLPLAHCFARYIQYVAIGSHGVVgyipsakrlladlrgFKPTYLLGVPRVFEKvynaaS 288
Cdd:cd05971 112 -VLLGHLPGVQFPFN-----LFPRDGDLYWTPADWAWIGGLLDV---------------LLPSLYFGVPVLAHR-----M 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 289 QKAGAGlkgrlfaKAFDHFVQWSkdemagghhslgarIQHSFYMQTVGSSIRSALGP------NMKWLACGGAPLNADLA 362
Cdd:cd05971 166 TKFDPK-------AALDLMSRYG--------------VTTAFLPPTALKMMRQQGEQlkhaqvKLRAIATGGESLGEELL 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 363 HFFNGFDGITFIQGYGMTETAA---PCLVNFQDANevGSVGR--PGCIsIRLADDD----------ELMIKGPN--VFLG 425
Cdd:cd05971 225 GWAREQFGVEVNEFYGQTECNLvigNCSALFPIKP--GSMGKpiPGHR-VAIVDDNgtplppgevgEIAVELPDpvAFLG 301
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 426 YYKQPQRTAEALTSDgWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05971 302 YWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR-IGPAEIEECLLKHPAVLMAAVVG 371
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
41-521 |
2.20e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 109.54 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 41 DETRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPkqtgdivaeve 120
Cdd:cd05930 8 DGDQSL---TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL-DPSYP----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 121 pviafagDDSHAQILEQIRAhseslRYVFnfkangldavadfgesvsdeeldkaigrVRADDLFTIVYTSGSTGKPKGVM 200
Cdd:cd05930 73 -------AERLAYILEDSGA-----KLVL----------------------------TDPDDLAYVIYTSGSTGKPKGVM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 201 LSHRNFNHTVYNGYEVLNdmLYQPSRLL-------------LFLPLA--HCfaryiqyVAIGSHGVVGyipSAKRLLADL 265
Cdd:cd05930 113 VEHRGLVNLLLWMQEAYP--LTPGDRVLqftsfsfdvsvweIFGALLagAT-------LVVLPEEVRK---DPEALADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 266 RGFKPTYLLGVPRVFEkvynaasqkagaglkgrlfakafdHFVQWSKDEMAgghhslgariqhsfymqtvgssirsalgP 345
Cdd:cd05930 181 AEEGITVLHLTPSLLR------------------------LLLQELELAAL----------------------------P 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 346 NMKWLACGGAPLNADLAH-FFNGFDGITFIQGYGMTE-----TAAPCLVNFQDANEVgSVGRP-GCISIRLADDD----- 413
Cdd:cd05930 209 SLRLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEatvdaTYYRVPPDDEEDGRV-PIGRPiPNTRVYVLDENlrpvp 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 -----ELMIKGPNVFLGYYKQPQRTAEALTSD-----GWLH-TGDLATIDDRG-FVFItGRKKDII-ItaGGKNISPAPM 480
Cdd:cd05930 288 pgvpgELYIGGAGLARGYLNRPELTAERFVPNpfgpgERMYrTGDLVRWLPDGnLEFL-GRIDDQVkI--RGYRIELGEI 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489915853 481 EDVINTCPIVAHAVVI----GDGRPFIAALIELDAEMT------RSWLASQ 521
Cdd:cd05930 365 EAALLAHPGVREAAVVaredGDGEKRLVAYVVPDEGGEldeeelRAHLAER 415
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
61-497 |
4.00e-25 |
|
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: 108.58 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 61 VAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKqtgDIVaevepviafagddshaqileqira 140
Cdd:cd05972 13 AANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPK---DIE------------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 141 hseslryvFNFKANGLDAVadfgesVSDEEldkaigrvradDLFTIVYTSGSTGKPKGVMLSHR-NFNHTVYnGYEVLN- 218
Cdd:cd05972 66 --------YRLEAAGAKAI------VTDAE-----------DPALIYFTSGTTGLPKGVLHTHSyPLGHIPT-AAYWLGl 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 219 ---DMLYQPSR------LL--LFLPLAHcfaryiqyvaiGSHGVVGYIP--SAKRLLADLRGFKPTYLLGVPRVFekvyn 285
Cdd:cd05972 120 rpdDIHWNIADpgwakgAWssFFGPWLL-----------GATVFVYEGPrfDAERILELLERYGVTSFCGPPTAY----- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 286 aasqkagaglkgRLFAKAfdhfvqwskdemaGGHHSlgariqhsfymqtVGSSIRSAlgpnmkwlACGGAPLNADLAHFF 365
Cdd:cd05972 184 ------------RMLIKQ-------------DLSSY-------------KFSHLRLV--------VSAGEPLNPEVIEWW 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 366 NGFDGITFIQGYGMTETAAPClVNFQDAnEV--GSVGRP-GCISIRLADDD----------ELMIKGPNV--FLGYYKQP 430
Cdd:cd05972 218 RAATGLPIRDGYGQTETGLTV-GNFPDM-PVkpGSMGRPtPGYDVAIIDDDgrelppgeegDIAIKLPPPglFLGYVGDP 295
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915853 431 QRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITAgGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05972 296 EKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESALLEHPAVAEAAVVG 360
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
49-497 |
1.74e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 108.01 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLL-GLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAG 127
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 128 DDSHAQiLEQIRAHSESLRYVFNFKaNGLDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFN 207
Cdd:PLN02574 147 PENVEK-LSPLGVPVIGVPENYDFD-SKRIEFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 HTV-------YNGYEV-LNDMLYqpsrlLLFLPLAHCFARYIQYV---AIGSHGVVGYIPSAKRLLADLRGFKPTYLLGV 276
Cdd:PLN02574 225 AMVelfvrfeASQYEYpGSDNVY-----LAALPMFHIYGLSLFVVgllSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 277 PRVFEKVYNAASQKAGAGLKgrlfakafdhfvqwskdemagghhslgariqhsfymqtvgssirsalgpNMKWLACGGAP 356
Cdd:PLN02574 300 PPILMALTKKAKGVCGEVLK-------------------------------------------------SLKQVSCGAAP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 357 LNADLAH-FFNGFDGITFIQGYGMTETAAPCL--VNFQDANEVGSVG--RPGcISIRLAD-----------DDELMIKGP 420
Cdd:PLN02574 331 LSGKFIQdFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGllAPN-MQAKVVDwstgcllppgnCGELWIQGP 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915853 421 NVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PLN02574 410 GVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQ-IAPADLEAVLISHPEIIDAAVTA 485
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
59-497 |
2.39e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 107.37 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 59 REVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVpvyeTDSPKQTGdivAEVEPVIAFAGDD---SHAQIL 135
Cdd:PLN02246 61 RRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT----TANPFYTP---AEIAKQAKASGAKliiTQSCYV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 136 EQIRAHSESLryvfNFKANGLDAVAD----FGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVY 211
Cdd:PLN02246 134 DKLKGLAEDD----GVTVVTIDDPPEgclhFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 212 NGYEVLNDMLY--QPSRLLLFLPLAHCFARyiqyvaigsHGVvgyipsakrLLADLRgfkptyllgvprvfekvynaasq 289
Cdd:PLN02246 210 QQVDGENPNLYfhSDDVILCVLPMFHIYSL---------NSV---------LLCGLR----------------------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 290 kAGAGLkgrLFAKAFD-----HFVQWSKDEMAG---------------GHHSLgariqhsfymqtvgSSIRSALGpnmkw 349
Cdd:PLN02246 249 -VGAAI---LIMPKFEigallELIQRHKVTIAPfvppivlaiakspvvEKYDL--------------SSIRMVLS----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 350 lacGGAPLNADLAHFFNG-FDGITFIQGYGMTEtAAP----CLVNFQDANEVGSvGRPGCI----SIRLADDD------- 413
Cdd:PLN02246 306 ---GAAPLGKELEDAFRAkLPNAVLGQGYGMTE-AGPvlamCLAFAKEPFPVKS-GSCGTVvrnaELKIVDPEtgaslpr 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ----ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPI 489
Cdd:PLN02246 381 nqpgEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQ-VAPAELEALLISHPS 459
|
....*...
gi 489915853 490 VAHAVVIG 497
Cdd:PLN02246 460 IADAAVVP 467
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
52-515 |
2.69e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.53 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAgDDSH 131
Cdd:PRK06018 43 AQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT-DLTF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 132 AQILEQIRAHSESLRY--VFNFKA----NGLDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHR- 204
Cdd:PRK06018 122 VPILEKIADKLPSVERyvVLTDAAhmpqTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRs 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 205 NFNHT-VYNGYEVLNdmLYQPSRLLLFLPLAHCFARYIQYVAIGShGVVGYIPSAKRLLAD----LRGFKPTYLLGVPRV 279
Cdd:PRK06018 202 NVLHAlMANNGDALG--TSAADTMLPVVPLFHANSWGIAFSAPSM-GTKLVMPGAKLDGASvyelLDTEKVTFTAGVPTV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 280 FEKVynaasqkagaglkgrlfakafdhfvqwskdemagghhslgarIQHsfyMQTVGSSIrsalgPNMKWLACGGAPLNA 359
Cdd:PRK06018 279 WLML------------------------------------------LQY---MEKEGLKL-----PHLKMVVCGGSAMPR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 360 DLAHFFNGFDgITFIQGYGMTETA--------APCLVNFQDANEVGSV---GRPG-CISIRLADDD------------EL 415
Cdd:PRK06018 309 SMIKAFEDMG-VEVRHAWGMTEMSplgtlaalKPPFSKLPGDARLDVLqkqGYPPfGVEMKITDDAgkelpwdgktfgRL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 416 MIKGPNVFLGYYKQpqrTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVV 495
Cdd:PRK06018 388 KVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYGYMRITDRSKD-VIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
490 500
....*....|....*....|....*.
gi 489915853 496 IG------DGRPFIAALIELDAEMTR 515
Cdd:PRK06018 464 IGvyhpkwDERPLLIVQLKPGETATR 489
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
50-497 |
6.83e-24 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 106.42 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 50 SAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATC---YEWGvvdFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIaFA 126
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSdlyLEWL---LAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVM-LV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 127 GDDSHAQILEQIRA-HSESLR-YVFNFKANGLDAVADFGESVSDEELDKAIGRVRAD------DLFTIVYTSGSTGKPKG 198
Cdd:PLN02860 110 TDETCSSWYEELQNdRLPSLMwQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDyawapdDAVLICFTSGTTGRPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 199 VMLSHRNFnhTVYN-------GYEvlNDMLYqpsrlLLFLPLAHcfaryiqyvaigshgvVGYIPSAKRLLadlrgfkpt 271
Cdd:PLN02860 190 VTISHSAL--IVQSlakiaivGYG--EDDVY-----LHTAPLCH----------------IGGLSSALAML--------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 272 yLLGVPRVFEKVYNAASqkagaglkgrlfakAFDhfvqwskdemAGGHHSLGARIQHSFYMQTVGSSIRS----ALGPNM 347
Cdd:PLN02860 236 -MVGACHVLLPKFDAKA--------------ALQ----------AIKQHNVTSMITVPAMMADLISLTRKsmtwKVFPSV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 348 KWLACGGAPLNADLAH-FFNGFDGITFIQGYGMTETAA---------PCLVNFQDANEV------GSVGRPG--C----- 404
Cdd:PLN02860 291 RKILNGGGSLSSRLLPdAKKLFPNAKLFSAYGMTEACSsltfmtlhdPTLESPKQTLQTvnqtksSSVHQPQgvCvgkpa 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 405 --ISIRLADDD-----ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISP 477
Cdd:PLN02860 371 phVELKIGLDEssrvgRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYP 449
|
490 500
....*....|....*....|
gi 489915853 478 APMEDVINTCPIVAHAVVIG 497
Cdd:PLN02860 450 EEVEAVLSQHPGVASVVVVG 469
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
47-518 |
1.77e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 104.79 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVE-PVIAF 125
Cdd:PRK07008 38 HRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEdRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 agDDSHAQILEQIRAHSESLR-YVFNFKANGLDAvaDFGESVSDEELDKAigrvrADDLFT-----------IVYTSGST 193
Cdd:PRK07008 118 --DLTFLPLVDALAPQCPNVKgWVAMTDAAHLPA--GSTPLLCYETLVGA-----QDGDYDwprfdenqassLCYTSGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 194 GKPKGVMLSHRNfnhTVYNGY-EVLNDMLYQPSR--LLLFLPLAHCFARYIQYVA--IGSHGVV-GYIPSAKRLLADLRG 267
Cdd:PRK07008 189 GNPKGALYSHRS---TVLHAYgAALPDAMGLSARdaVLPVVPMFHVNAWGLPYSAplTGAKLVLpGPDLDGKSLYELIEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 268 FKPTYLLGVPRVFEKVYNAASQkagAGLKgrlfakaFDHFvqwsKDEMAGGhhslgariqhsfymqtvgssirSALGPNM 347
Cdd:PRK07008 266 ERVTFSAGVPTVWLGLLNHMRE---AGLR-------FSTL----RRTVIGG----------------------SACPPAM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 348 kwlacggaplnadLAHFFNGFdGITFIQGYGMTE-----TAAPcLVNFQDANEVGSV-------GRPGC-ISIRLADDD- 413
Cdd:PRK07008 310 -------------IRTFEDEY-GVEVIHAWGMTEmsplgTLCK-LKWKHSQLPLDEQrkllekqGRVIYgVDMKIVGDDg 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 -----------ELMIKGPNVFLGYYKqpqRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMED 482
Cdd:PRK07008 375 relpwdgkafgDLQVRGPWVIDRYFR---GDASPL-VDGWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIEN 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489915853 483 VINTCPIVAHAVVIG------DGRPFIAALIELDAEMTRSWL 518
Cdd:PRK07008 450 VAVAHPAVAEAACIAcahpkwDERPLLVVVKRPGAEVTREEL 491
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
20-523 |
2.85e-23 |
|
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: 104.11 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 20 YSLLAKRCERDPDDLIAQWQDDETRQwHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAV 99
Cdd:cd05970 20 YDVVDAMAKEYPDKLALVWCDDAGEE-RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 100 SVPVYETDSPKqtgDIV-----AEVEPVIAFAGDDshaqILEQIRAHSESLrYVFNFKANGLDAVADFGESVsDEELDKA 174
Cdd:cd05970 99 AIPATHQLTAK---DIVyriesADIKMIVAIAEDN----IPEEIEKAAPEC-PSKPKLVWVGDPVPEGWIDF-RKLIKNA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 175 IGRVR---------ADDLFTIVYTSGSTGKPKgvMLSHrnfNHTvyngyevlndmlyqpsrlllfLPLAHCF-ARYIQYV 244
Cdd:cd05970 170 SPDFErptansypcGEDILLVYFSSGTTGMPK--MVEH---DFT---------------------YPLGHIVtAKYWQNV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 245 AIGS-HGVVGYIPSAKRlladlrgfkptyllgvprVFEKVYnaASQKAGAGLkgrlFAKAFDHFVQWSKDEMAGGHHSLG 323
Cdd:cd05970 224 REGGlHLTVADTGWGKA------------------VWGKIY--GQWIAGAAV----FVYDYDKFDPKALLEKLSKYGVTT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 324 ARIQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAApCLVNFQDAN-EVGSVGRP 402
Cdd:cd05970 280 FCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWMEpKPGSMGKP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 ---------------------GCISIRLADDDELmikgpNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITG 461
Cdd:cd05970 359 apgyeidlidregrsceageeGEIVIRTSKGKPV-----GLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVG 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 462 RKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIGDGRPFIAALIELDAEMTRSWLASQNL 523
Cdd:cd05970 433 RTDDLIKSSGYR-IGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEEL 493
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
53-508 |
2.92e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 104.32 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdsP------------KQTGDIVAEVE 120
Cdd:PRK09192 54 TLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-----PlpmgfggresyiAQLRGMLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 121 PVIAFAGDDshaqILEQIRAHSESLRYVFNFKANGLDAVadfgesvsdEELDKAIGRVRADDLFTIVYTSGSTGKPKGVM 200
Cdd:PRK09192 129 PAAIITPDE----LLPWVNEATHGNPLLHVLSHAWFKAL---------PEADVALPRPTPDDIAYLQYSSGSTRFPRGVI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 201 LSHR----NFNHTVYNGYEVLNdmlyqPSRLLLFLPLAHcfaryiqyvaigSHGVVGYI--PSAKRLLADLrgfkptyll 274
Cdd:PRK09192 196 ITHRalmaNLRAISHDGLKVRP-----GDRCVSWLPFYH------------DMGLVGFLltPVATQLSVDY--------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 275 gvprvfekvynaasqkagagLKGRLFAKafdHFVQW----SKDEmagghhslgARIQHSfymQTVGSSIrSALGPNMKWL 350
Cdd:PRK09192 250 --------------------LPTRDFAR---RPLQWldliSRNR---------GTISYS---PPFGYEL-CARRVNSKDL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 351 A-----------CGGAPLNADLAHFF------NGFDGITFIQGYGMTE-TAApclVNFQDANE----------------- 395
Cdd:PRK09192 294 AeldlscwrvagIGADMIRPDVLHQFaeafapAGFDDKAFMPSYGLAEaTLA---VSFSPLGSgivveevdrdrleyqgk 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 396 -VGSVGRPG-------C--------ISIRLADDDEL--------MIKGPNVFLGYYKQpQRTAEALTSDGWLHTGDLATI 451
Cdd:PRK09192 371 aVAPGAETRrvrtfvnCgkalpgheIEIRNEAGMPLpervvghiCVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYL 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915853 452 DDrGFVFITGRKKDIIITaGGKNISP------APMEDVINTCPIVAHAVViGDGRPFIAALIE 508
Cdd:PRK09192 450 LD-GYLYITGRAKDLIII-NGRNIWPqdiewiAEQEPELRSGDAAAFSIA-QENGEKIVLLVQ 509
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
174-500 |
4.62e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 105.05 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 174 AIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFnhtVYNGYEVLNDMLYQPSRLLL-FLPLAHCFaryiqyvaigshGVV 252
Cdd:PRK06814 786 YFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNL---LANRAQVAARIDFSPEDKVFnALPVFHSF------------GLT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 253 GYIpsakrLLADLRGFkPTYLLGVPR----VFEKVYNAasqkaGAGLkgrLFakafdhfvqwSKDEMAGGHhslgARIQH 328
Cdd:PRK06814 851 GGL-----VLPLLSGV-KVFLYPSPLhyriIPELIYDT-----NATI---LF----------GTDTFLNGY----ARYAH 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 S--FYmqtvgsSIRsalgpnmkWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGc 404
Cdd:PRK06814 903 PydFR------SLR--------YVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRllPG- 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 405 ISIRL---ADDDE---LMIKGPNVFLGYYK-QPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKK---DIiitaGGKN 474
Cdd:PRK06814 968 IEYRLepvPGIDEggrLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEM 1042
|
330 340
....*....|....*....|....*...
gi 489915853 475 ISPAPMEDVINTC-PIVAHAVV-IGDGR 500
Cdd:PRK06814 1043 ISLAAVEELAAELwPDALHAAVsIPDAR 1070
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
58-541 |
7.88e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 102.66 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 58 VREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYET-DSPKQTGDIVAEVEPVIAFAGDDSHAQILE 136
Cdd:PRK05852 53 VDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPAlPIAEQRVRSQAAGARVVLIDADGPHDRAEP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 137 QIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKAIGRVRADDLFtIVYTSGSTGKPKGVMLSHRNFN---HTVYNG 213
Cdd:PRK05852 133 TTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMVPWTHANIAssvRAIITG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 214 YEvlndmLYQPSRLLLFLPLAHcfaryiqyvaigSHGVVGyipsakRLLADLRGfkptyllgvprvfekvynaasqkAGA 293
Cdd:PRK05852 212 YR-----LSPRDATVAVMPLYH------------GHGLIA------ALLATLAS-----------------------GGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 294 GL---KGRLFAKAFdhfvqWSKDEMAGGHHSLGARIQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDG 370
Cdd:PRK05852 246 VLlpaRGRFSAHTF-----WDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 371 ITFIQGYGMTET---AAPCLVNFQDANE-----VGSVGRPGCISIRLADDD----------ELMIKGPNVFLGYYKQPQR 432
Cdd:PRK05852 321 APVVCAFGMTEAthqVTTTQIEGIGQTEnpvvsTGLVGRSTGAQIRIVGSDglplpagavgEVWLRGTTVVRGYLGDPTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 433 TAEALTsDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVVIGD-----GRPFIAALI 507
Cdd:PRK05852 401 TAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKE-LINRGGEKISPERVEGVLASHPNVMEAAVFGVpdqlyGEAVAAVIV 478
|
490 500 510
....*....|....*....|....*....|....*
gi 489915853 508 ELD-AEMTRSWLASQNLDIDAPMSEIATNDAVRAL 541
Cdd:PRK05852 479 PREsAPPTAEELVQFCRERLAAFEIPASFQEASGL 513
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
182-497 |
9.90e-23 |
|
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: 99.40 E-value: 9.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFNHTVyngyeVLNDMLYQPS---RLLLFLPLAHCFARY--IQYVAIGSHGVVGYIP 256
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESF-----VCNEDLFNISgedAILAPGPLSHSLFLYgaISALYLGGTFIGQRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 257 SAKRLLADLRGFKPTYLLGVPRVFEKVYNaasqkagaglkgrlfakafdhfvqwskdemagghhslgariqhsfyMQTVG 336
Cdd:cd17633 76 NPKSWIRKINQYNATVIYLVPTMLQALAR----------------------------------------------TLEPE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 337 SSIRSALgpnmkwlaCGGAPLNADLAHFF-NGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPGC---ISIRLADD 412
Cdd:cd17633 110 SKIKSIF--------SSGQKLFESTKKKLkNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPnveIEIRNADG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 413 DE---LMIKGPNVFLGYYKqpqrtAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPI 489
Cdd:cd17633 182 GEigkIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLKAIPG 255
|
....*...
gi 489915853 490 VAHAVVIG 497
Cdd:cd17633 256 IEEAIVVG 263
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
18-516 |
1.38e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.01 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDdLIAQWQDDETRQwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:PRK05857 15 TVLDRVFEQARQQPE-AIALRRCDGTSA---LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVyETDSPKQTGDIVAEVEpviafagDDSHAQILEQIRAHSESLRYVFN-FKANGLDAVADFGESVSDEELDKAIG 176
Cdd:PRK05857 91 AIAVMA-DGNLPIAAIERFCQIT-------DPAAALVAPGSKMASSAVPEALHsIPVIAVDIAAVTRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 177 RVR--ADDLFTIVYTSGSTGKPKGVMLSHRNFNhtvyngyeVLNDMLYQPSrlllflplahcfARYIQYVAigshGVVGY 254
Cdd:PRK05857 163 NADqgSEDPLAMIFTSGTTGEPKAVLLANRTFF--------AVPDILQKEG------------LNWVTWVV----GETTY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 255 IPsakrlladlrgFKPTYLLGVPRVFEKVYNAASQkagaglkgrlfakafdhfvqwskdeMAGGHHSLGAR-------IQ 327
Cdd:PRK05857 219 SP-----------LPATHIGGLWWILTCLMHGGLC-------------------------VTGGENTTSLLeilttnaVA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 328 HSFYMQTVGSSIRSALG------PNMKWLACGGAPLNADLAHFFNGfDGITFIQGYGMTETAAPCLVNFQDAN-----EV 396
Cdd:PRK05857 263 TTCLVPTLLSKLVSELKsanatvPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGCTALCLPTDDGsivkiEA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 397 GSVGRP-GCISIRLADDD----------------ELMIKGPNVFLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFI 459
Cdd:PRK05857 342 GAVGRPyPGVDVYLAATDgigptapgagpsasfgTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERREDGFFYI 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 460 TGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIGDGRPFIAALI--------ELDAEMTRS 516
Cdd:PRK05857 421 KGRSSEMIIC-GGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVglavvasaELDESAARA 484
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
50-549 |
3.13e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 100.93 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 50 SAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAgdd 129
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 130 sHAQILEQIRAHSESLRYVFNF-------KANGLDAVA--------DFGESVSDEELDKAiGRVRADDlfTIVYTSGSTG 194
Cdd:PRK12406 90 -HADLLHGLASALPAGVTVLSVptppeiaAAYRISPALltppagaiDWEGWLAQQEPYDG-PPVPQPQ--SMIYTSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 195 KPKGVmlshRNFNHT-----VYNGYEVLNDMLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIP--SAKRLLADLRG 267
Cdd:PRK12406 166 HPKGV----RRAAPTpeqaaAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPrfDPEELLQLIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 268 FKPTYLLGVPRVFEKVynaasqkagagLKgrlfakafdhfvqwskdemagghhsLGARIQHSFYMqtvgSSIRsalgpnm 347
Cdd:PRK12406 242 HRITHMHMVPTMFIRL-----------LK-------------------------LPEEVRAKYDV----SSLR------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 348 kWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDA-NEVGSVGR--PGcISIRLADDD----------E 414
Cdd:PRK12406 275 -HVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDAlSHPGTVGKaaPG-AELRFVDEDgrplpqgeigE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 415 LMIKGP-NVFLGYYKQPQRTAEaLTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHA 493
Cdd:PRK12406 353 IYSRIAgNPDFTYHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIEAVLHAVPGVHDC 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 494 VVIG--D---GRPFIAAL-----IELDAEMTRSWLASQNLDIDAP-----MSEIATND----AVRALVQQYIDKA 549
Cdd:PRK12406 431 AVFGipDaefGEALMAVVepqpgATLDEADIRAQLKARLAGYKVPkhieiMAELPREDsgkiFKRRLRDPYWANA 505
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
49-515 |
1.02e-21 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 98.47 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPK-QTGDIVAEVEPVIAFAg 127
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPL-DASSPAeRIREILDAAKPALLIA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 128 ddshaqileqirahseslryvfnfkangldavadfgesvsDEeldkaigrvraDDLFTIVYTSGSTGKPKGVMLSHRNFn 207
Cdd:cd05945 95 ----------------------------------------DG-----------DDNAYIIFTSGSTGRPKGVQISHDNL- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 HTVYNGyeVLNDMLYQP-SRLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSA-----KRLLADLRGFKPTYLLGVPrvfe 281
Cdd:cd05945 123 VSFTNW--MLSDFPLGPgDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDatadpKQLFRFLAEHGITVWVSTP---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 282 kvynaasqkagaglkgrlfakafdhfvqwSKDEMAGGHHSLGAriqhsfymqtvgssirsALGPNMKW-LACGGAPLNAD 360
Cdd:cd05945 197 -----------------------------SFAAMCLLSPTFTP-----------------ESLPSLRHfLFCGEVLPHKT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 361 LAHFFNGFDGITFIQGYGMTETAAPCLVN-----FQDANEVGSVGR--PGCIsIRLADDD----------ELMIKGPNVF 423
Cdd:cd05945 231 ARALQQRFPDARIYNTYGPTEATVAVTYIevtpeVLDGYDRLPIGYakPGAK-LVILDEDgrpvppgekgELVISGPSVS 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 424 LGYYKQPQRTAEALTSD---GWLHTGDLATIDDRGFVFITGRkKDIIITAGGKNISPAPMEDVINTCPIVAHAVVI---- 496
Cdd:cd05945 310 KGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGR-LDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVpkyk 388
|
490
....*....|....*....
gi 489915853 497 GDGRPFIAALIELDAEMTR 515
Cdd:cd05945 389 GEKVTELIAFVVPKPGAEA 407
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
59-496 |
1.05e-20 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 96.20 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 59 REVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAV----SVPVYETDSPKQtgdivAEVEPVIAFAGDDSHAQI 134
Cdd:PLN02330 66 RRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVfsgaNPTALESEIKKQ-----AEAAGAKLIVTNDTNYGK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 135 -----LEQIRAHSESLRYVFNFKaNGLDAVADFGESVSDEELDKAigrvradDLFTIVYTSGSTGKPKGVMLSHRNFNHT 209
Cdd:PLN02330 141 vkglgLPVIVLGEEKIEGAVNWK-ELLEAADRAGDTSDNEEILQT-------DLCALPFSSGTTGISKGVMLTHRNLVAN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 210 VYNG-YEVLNDMLYQPSRLLLfLPLAHCFaryiqyvaigshGVVGYIpsakrlLADLRgfkptyllgvprvfekvynaas 288
Cdd:PLN02330 213 LCSSlFSVGPEMIGQVVTLGL-IPFFHIY------------GITGIC------CATLR---------------------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 289 QKAGAGLKGRLFAKAFdhfvqwskdemagghhsLGARIQHSFYMQTVGSSIRSALGPN------------MKWLACGGAP 356
Cdd:PLN02330 252 NKGKVVVMSRFELRTF-----------------LNALITQEVSFAPIVPPIILNLVKNpiveefdlsklkLQAIMTAAAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 357 LNADL-AHFFNGFDGITFIQGYGMTETAAPCLVN--------FQDANEVGSVgRPGcISIRLADDD-----------ELM 416
Cdd:PLN02330 315 LAPELlTAFEAKFPGVQVQEAYGLTEHSCITLTHgdpekghgIAKKNSVGFI-LPN-LEVKFIDPDtgrslpkntpgELC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 417 IKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVI 496
Cdd:PLN02330 393 VRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ-VAPAELEAILLTHPSVEDAAVV 471
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
53-501 |
1.32e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 96.24 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAgDDSHA 132
Cdd:PLN03102 44 QTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV-DRSFE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 133 QILEqirahsESLRYVFNFKANGLDAVA-----DFGESVSDEELD---------------KAIGRVRAD-DLFTIVYTSG 191
Cdd:PLN03102 123 PLAR------EVLHLLSSEDSNLNLPVIfiheiDFPKRPSSEELDyecliqrgeptpslvARMFRIQDEhDPISLNYTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 192 STGKPKGVMLSHRNFNHTVYN---GYEVLNDMLYqpsrlLLFLPLAHCFARYIQY--VAIGSHGVVGYIPSAKRLLADLR 266
Cdd:PLN03102 197 TTADPKGVVISHRGAYLSTLSaiiGWEMGTCPVY-----LWTLPMFHCNGWTFTWgtAARGGTSVCMRHVTAPEIYKNIE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 267 GFKPTYLLGVPRVFEKVynaasqkagagLKGrlfakafdhfvqwskDEMAGGHHSlgariqHSFYMQTVGSSIRSALGPN 346
Cdd:PLN03102 272 MHNVTHMCCVPTVFNIL-----------LKG---------------NSLDLSPRS------GPVHVLTGGSPPPAALVKK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 347 MKWLacggaplnadlahffngfdGITFIQGYGMTETAAPCL-VNFQDA-------NEVGSVGRPGCISIRLADDD----- 413
Cdd:PLN03102 320 VQRL-------------------GFQVMHAYGLTEATGPVLfCEWQDEwnrlpenQQMELKARQGVSILGLADVDvknke 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 -------------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPM 480
Cdd:PLN03102 381 tqesvprdgktmgEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEV 458
|
490 500
....*....|....*....|.
gi 489915853 481 EDVINTCPIVAHAVVIGDGRP 501
Cdd:PLN03102 459 ENVLYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
47-499 |
1.46e-20 |
|
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: 95.05 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQ-TGDIVAEVEPVIAF 125
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-DPDYPADrLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AGDDSHAqileqirahseslRYvfnfkANGLDAVADFGESvsDEELDKAIGR-VRADDLFTIVYTSGSTGKPKGVMLSHR 204
Cdd:cd12116 90 TDDALPD-------------RL-----PAGLPVLLLALAA--AAAAPAAPRTpVSPDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 205 NFNHTvyngyevLNDMLYQPS-----RLL-------------LFLPL---AHCfaryiqYVAIGSHgvvgyIPSAKRLLA 263
Cdd:cd12116 150 NLVNF-------LHSMRERLGlgpgdRLLavttyafdislleLLLPLlagARV------VIAPRET-----QRDPEALAR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 264 DLRGFKPTYLLGVPRVFekvynaasqkagaglkgRLFAKAfdhfvQWSKDEmagghhslgariqhsfymqtvgsSIRsal 343
Cdd:cd12116 212 LIEAHSITVMQATPATW-----------------RMLLDA-----GWQGRA-----------------------GLT--- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 344 gpnmkwLACGGAPLNADLAHFFNGFDGiTFIQGYGMTET---AAPCLVnfQDANEVGSVGRP-GCISIRLADDD------ 413
Cdd:cd12116 244 ------ALCGGEALPPDLAARLLSRVG-SLWNLYGPTETtiwSTAARV--TAAAGPIPIGRPlANTQVYVLDAAlrpvpp 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ----ELMIKGPNVFLGYYKQPQRTAEALTSDGWLH-------TGDLATIDDRGFVFITGRkKDIIITAGGKNISPAPMED 482
Cdd:cd12116 315 gvpgELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGR-ADGQVKIRGHRIELGEIEA 393
|
490
....*....|....*..
gi 489915853 483 VINTCPIVAHAVVIGDG 499
Cdd:cd12116 394 ALAAHPGVAQAAVVVRE 410
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
53-507 |
3.14e-20 |
|
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: 94.11 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPkqtgdivaevepviafagddsha 132
Cdd:cd05969 5 QLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGP----------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 133 qileqirahsESLRY-VFNFKANGLdavadfgesVSDEELDKaigRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVY 211
Cdd:cd05969 62 ----------EAIRDrLENSEAKVL---------ITTEELYE---RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 212 NGYEVLN----DMLY---QPSRLL-----LFLPLAHCFARYIQ---------YVAIGSHGV-VGYI-PSAKRLLadlrgf 268
Cdd:cd05969 120 TGKYVLDlhpdDIYWctaDPGWVTgtvygIWAPWLNGVTNVVYegrfdaeswYGIIERVKVtVWYTaPTAIRML------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 269 kptyllgvprvfekvynaasQKAGAGLkgrlfAKAFDHfvqwskdemagghhslgariqhsfymqtvgSSIRsalgpnmk 348
Cdd:cd05969 194 --------------------MKEGDEL-----ARKYDL------------------------------SSLR-------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 349 WLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNF--QDAnEVGSVGRP--GCI---------SIRLADDDEL 415
Cdd:cd05969 211 FIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYpcMPI-KPGSMGKPlpGVKaavvdengnELPPGTKGIL 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 416 MIKG--PNVFLGYYKQPQRTAEALTsDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHA 493
Cdd:cd05969 290 ALKPgwPSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHR-VGPFEVESALMEHPAVAEA 367
|
490
....*....|....
gi 489915853 494 VVIGDGRPFIAALI 507
Cdd:cd05969 368 GVIGKPDPLRGEII 381
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
47-501 |
5.69e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 93.95 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSP--------KQTGDivAE 118
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV----SPlfrehelsYELND--AG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 119 VEPVIAFagdDSHAQILEQIRAHSeSLRYVFNFKA-------------NGLDA-------VADFGESVSDEELDKAIGRV 178
Cdd:PRK06178 131 AEVLLAL---DQLAPVVEQVRAET-SLRHVIVTSLadvlpaeptlplpDSLRAprlaaagAIDLLPALRACTAPVPLPPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 179 RADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVlNDMLYQPSRLLLFLPlahcfaryIQYVAIGSHGVVgyipsa 258
Cdd:PRK06178 207 ALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV-AVVGGEDSVFLSFLP--------EFWIAGENFGLL------ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 259 krlladlrgfKPTYLlGVPRVfekvynaasqkagagLKGRLFAKAFDHFVQWSKDEMAGG----------HHSLGARIQH 328
Cdd:PRK06178 272 ----------FPLFS-GATLV---------------LLARWDAVAFMAAVERYRVTRTVMlvdnavelmdHPRFAEYDLS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 SFYMQTVGSSIRSalgpnmkwlacggapLNADLAHFFNGFDGITFIQG-YGMTET--AAPCLVNFQDANE--------VG 397
Cdd:PRK06178 326 SLRQVRVVSFVKK---------------LNPDYRQRWRALTGSVLAEAaWGMTEThtCDTFTAGFQDDDFdllsqpvfVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 398 sVGRPGCiSIRLADDD-----------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDI 466
Cdd:PRK06178 391 -LPVPGT-EFKICDFEtgellplgaegEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEM 467
|
490 500 510
....*....|....*....|....*....|....*
gi 489915853 467 IITAgGKNISPAPMEDVINTCPIVAHAVVIgdGRP 501
Cdd:PRK06178 468 LKVN-GMSVFPSEVEALLGQHPAVLGSAVV--GRP 499
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
19-516 |
1.43e-19 |
|
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: 92.22 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 19 IYSLLAKRCERDPDDL-IAQWqdDEtrqwhDVSAGQMNDRVREVAKGLLGLGVKPGSMVviyaATCYE---WGVVdfaca 94
Cdd:cd05918 1 VHDLIEERARSQPDAPaVCAW--DG-----SLTYAELDRLSSRLAHHLRSLGVGPGVFV----PLCFEkskWAVV----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 95 SI------GAVSVPVyETDSPKQ-TGDIVAEVEPVIAFAGDDSHAqileqirAhseslrYVfnfkangldavadfgesvs 167
Cdd:cd05918 65 AMlavlkaGGAFVPL-DPSHPLQrLQEILQDTGAKVVLTSSPSDA-------A------YV------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 168 deeldkaigrvraddlftiVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLplAHCFARYIQ--YVA 245
Cdd:cd05918 112 -------------------IFTSGSTGKPKGVVIEHRALSTSALAHGRALG--LTSESRVLQFA--SYTFDVSILeiFTT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 246 IGSHGVVGyIPSAKRLLADLrgfkptyllgvprvfekvynaasqkagaglkgrlfAKAFDHFvqwskdemagghhslgaR 325
Cdd:cd05918 169 LAAGGCLC-IPSEEDRLNDL-----------------------------------AGFINRL-----------------R 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 326 IQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNgfDGITFIQGYGMTETAAPCLVN-FQDANEVGSVGRP-G 403
Cdd:cd05918 196 VTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWA--DRVRLINAYGPAECTIAATVSpVVPSTDPRNIGRPlG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 404 CISIRLADDD-----------ELMIKGPNVFLGYYKQPQRTAEALTSD-GWLH------------TGDLATIDDRG-FVF 458
Cdd:cd05918 274 ATCWVVDPDNhdrlvpigavgELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGsLEY 353
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 459 ItGRKKDII-ItaGGKNISPAPMEDVINTCPIVAHAVVI-------GDGRPFIAALIELDAEMTRS 516
Cdd:cd05918 354 V-GRKDTQVkI--RGQRVELGEIEHHLRQSLPGAKEVVVevvkpkdGSSSPQLVAFVVLDGSSSGS 416
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
18-512 |
1.55e-19 |
|
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: 93.77 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFGDQS------LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVyETDSPKQ-TGDIVAEVEPVIAFAgDDSHAQileqiRAHSESLRYVFnfkangLDAVADFGESVSDEELdkaig 176
Cdd:COG1020 551 AAYVPL-DPAYPAErLAYMLEDAGARLVLT-QSALAA-----RLPELGVPVLA------LDALALAAEPATNPPV----- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 177 RVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLL-------------LFLPLAHcfaryiqy 243
Cdd:COG1020 613 PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG--LGPGDRVLqfaslsfdasvweIFGALLS-------- 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 244 vaiGSHGVV---GYIPSAKRLLADLRGFKPTYLLGVPRVFekvynaasqkagaglkgRLFAkafdhfvqwskDEMAGGHH 320
Cdd:COG1020 683 ---GATLVLappEARRDPAALAELLARHRVTVLNLTPSLL-----------------RALL-----------DAAPEALP 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 321 SLgariqhsfymqtvgssirsalgpnmKWLACGGAPLNADLA-HFFNGFDGITFIQGYGMTETA-----APCLVNFQDAN 394
Cdd:COG1020 732 SL-------------------------RLVLVGGEALPPELVrRWRARLPGARLVNLYGPTETTvdstyYEVTPPDADGG 786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 395 EVgSVGRP-GCISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEA-----LTSDG--WLHTGDLAT------ 450
Cdd:COG1020 787 SV-PIGRPiANTRVYVLDAHlqpvpvgvpgELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARwlpdgn 865
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 451 ------IDD----RGFvfitgRkkdiiitaggknISPAPMEDVINTCPIVAHAVVI----GDGRPFIAALIELDAE 512
Cdd:COG1020 866 leflgrADDqvkiRGF-----R------------IELGEIEAALLQHPGVREAVVVaredAPGDKRLVAYVVPEAG 924
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
188-496 |
3.77e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 91.55 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 188 YTSGSTGKPKGVMLSHR--------NF------NHTVYngyevlndmlyqpsrlLLFLPLAHC----FARYIQYVAiGSH 249
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRgaylnalsNIlawgmpKHPVY----------------LWTLPMFHCngwcFPWTVAARA-GTN 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 250 gVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEKVYNA-ASQKAGaglkgrlfakaFDHFVqwskdemagghhslgariqh 328
Cdd:PRK08162 252 -VCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINApAEWRAG-----------IDHPV-------------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 sfymqtvgssirsalgpnmKWLACGGAPLNADLAHFFN-GFDgITFIqgYGMTETAAPCLVN--------FQDANEVGSV 399
Cdd:PRK08162 300 -------------------HAMVAGAAPPAAVIAKMEEiGFD-LTHV--YGLTETYGPATVCawqpewdaLPLDERAQLK 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 400 GRPGCI-----SIRLADDD-------------ELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITG 461
Cdd:PRK08162 358 ARQGVRyplqeGVTVLDPDtmqpvpadgetigEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKD 436
|
330 340 350
....*....|....*....|....*....|....*
gi 489915853 462 RKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVI 496
Cdd:PRK08162 437 RSKDIIIS-GGENISSIEVEDVLYRHPAVLVAAVV 470
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
57-484 |
4.91e-19 |
|
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: 90.63 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 57 RVREVAKGLLG----LGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdspkqtgdivaevepviAFAGDDSHA 132
Cdd:cd05908 20 HLREEALGYLGalqeLGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV--------------------SIGSNEEHK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 133 QILEQIrahseslryvFNFKANGLdAVADfgesvsDEELDKAigrvrADDLFTIVYTSGSTGKPKGVMLSHRNFnhtVYN 212
Cdd:cd05908 80 LKLNKV----------WNTLKNPY-LITE------EEVLCEL-----ADELAFIQFSSGSTGDPKGVMLTHENL---VHN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 213 GYEVLNDMLYQPS-RLLLFLPLAHCFAryiqyvAIGSHgVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEkvyNAASQKA 291
Cdd:cd05908 135 MFAILNSTEWKTKdRILSWMPLTHDMG------LIAFH-LAPLIAGMNQYLMPTRLFIRRPILWLKKASE---HKATIVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 292 GAGLKGRLFAKAFDHFVQWSKD-----EMAGGHHSLGARIQHSF--YMQTVG---SSIRSALGPNMKWLACGGAPLNADL 361
Cdd:cd05908 205 SPNFGYKYFLKTLKPEKANDWDlssirMILNGAEPIDYELCHEFldHMSKYGlkrNAILPVYGLAEASVGASLPKAQSPF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 362 AHFFNGFDGITFIQGYGMTETAAPclvnfqDANEVGSVGRP-GCISIRLADDDE----------LMIKGPNVFLGYYKQP 430
Cdd:cd05908 285 KTITLGRRHVTHGEPEPEVDKKDS------ECLTFVEVGKPiDETDIRICDEDNkilpdgyighIQIRGKNVTPGYYNNP 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489915853 431 QRTAEALTSDGWLHTGDLATIDDrGFVFITGRKKDIIITaGGKNISPAPMEDVI 484
Cdd:cd05908 359 EATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIA 410
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
23-512 |
8.81e-19 |
|
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: 89.71 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 23 LAKRCERDPDDLIAQWqdDETRqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVP 102
Cdd:cd17651 1 FERQAARTPDAPALVA--EGRR----LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 103 VYETDSPKQTGDIVAEVEPVIAFAgDDSHAQILEQIRAhseslryvfnfkangLDAVADFGESVSDEELDKAIgRVRADD 182
Cdd:cd17651 75 LDPAYPAERLAFMLADAGPVLVLT-HPALAGELAVELV---------------AVTLLDQPGAAAGADAEPDP-ALDADD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 183 LFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSAKRLl 262
Cdd:cd17651 138 LAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS--LGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRT- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 263 adlrgfkptyllgvprvfekvynaasqkagaglkgrlfakAFDHFVQWSKDEmagghhslgaRIQHSF----YMQTVGSS 338
Cdd:cd17651 215 ----------------------------------------DPPALAAWLDEQ----------RISRVFlptvALRALAEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 339 IR--SALGPNMKWLACGGAPL--NADLAHFFNGFDGITFIQGYGMTETA-APCLVNFQD---ANEVGSVGRP-GCISIRL 409
Cdd:cd17651 245 GRplGVRLAALRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTETHvVTALSLPGDpaaWPAPPPIGRPiDNTRVYV 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 410 ADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWL------HTGDLATIDDRGFVFITGRKKDIIITAGGK 473
Cdd:cd17651 325 LDAAlrpvppgvpgELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFR 404
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489915853 474 nISPAPMEDVINTCPIVAHAVVI----GDGRPFIAALIELDAE 512
Cdd:cd17651 405 -IELGEIEAALARHPGVREAVVLaredRPGEKRLVAYVVGDPE 446
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
49-497 |
2.21e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 88.81 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSPKQTGdivaevePVIAFAGD 128
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI----NWHLTA-------AEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQIL----------EQIRAHSE---SLRYVFNFKANGLDAVADFGESVSDEELDkaiGRVRADDLftiVYTSGSTGK 195
Cdd:PRK08276 81 DSGAKVLivsaaladtaAELAAELPagvPLLLVVAGPVPGFRSYEEALAAQPDTPIA---DETAGADM---LYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 196 PKGVM--LSHRNFNhtvyngyEVLNDML---------YQPSRLLLFLPLAHCfA--RYIQYVAIGSHGVVgYIP--SAKR 260
Cdd:PRK08276 155 PKGIKrpLPGLDPD-------EAPGMMLallgfgmygGPDSVYLSPAPLYHT-AplRFGMSALALGGTVV-VMEkfDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 261 LLADLRGFKPTYLLGVPrvfekvynaasqkagaglkgrlfakafDHFVQWSKdemagghhsLGARIQHSFYMqtvgSSIR 340
Cdd:PRK08276 226 ALALIERYRVTHSQLVP---------------------------TMFVRMLK---------LPEEVRARYDV----SSLR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 341 SAlgpnmkwlACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQDANE-VGSVGRPGCISIRLADDD------ 413
Cdd:PRK08276 266 VA--------IHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDWLAhPGSVGKAVLGEVRILDEDgnelpp 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ----ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPI 489
Cdd:PRK08276 338 geigTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYPQEIENLLVTHPK 416
|
....*...
gi 489915853 490 VAHAVVIG 497
Cdd:PRK08276 417 VADVAVFG 424
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
28-497 |
2.40e-18 |
|
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: 88.59 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 28 ERDPDDLIAQWQDDETRQWHDVSAgQMNDRVREVAKGllglGVKPGSMVVIYAATCYEWGVVDFA---CASIGAVSVPVY 104
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSI-ALNRNARAAAAE----GVWIADGVYIYLINSILTVFAAAAawkCGACPAYKSSRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 105 ETDSPKQTGDIVAEVEPVIAFAGDdshaqileqirahseslryvfnfkaNGLDAVADF--GESVSDEELdkaIGRVRADD 182
Cdd:cd05929 77 PRAEACAIIEIKAAALVCGLFTGG-------------------------GALDGLEDYeaAEGGSPETP---IEDEAAGW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 183 LftIVYTSGSTGKPKGVM--LSHRNFNHTVYNGYEvLNDMLYQPSRLLLFLPLAHC--FARYIQYVAIGSHGVVGYIPSA 258
Cdd:cd05929 129 K--MLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAA-LGFGPGADSVYLSPAPLYHAapFRWSMTALFMGGTLVLMEKFDP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 259 KRLLADLRGFKPTYLLGVPrvfekvynaasqkagaglkgrlfakafDHFVQWSKdemagghhsLGARIQHSFYMqtvgSS 338
Cdd:cd05929 206 EEFLRLIERYRVTFAQFVP---------------------------TMFVRLLK---------LPEAVRNAYDL----SS 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 339 IRSAlgpnmkWLAcgGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQD-ANEVGSVGRP--GCISIRLADDDEL 415
Cdd:cd05929 246 LKRV------IHA--AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINGEEwLTHPGSVGRAvlGKVHILDEDGNEV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 416 --------MIKGPNVFLgYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTC 487
Cdd:cd05929 318 ppgeigevYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIIS-GGVNIYPQEIENALIAH 395
|
490
....*....|
gi 489915853 488 PIVAHAVVIG 497
Cdd:cd05929 396 PKVLDAAVVG 405
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
52-481 |
7.24e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 87.36 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYE--------WgvvdFACASIGAVSVPVYETDSP---KQTGDIVAEVE 120
Cdd:PRK07768 33 GEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEiaptaqglW----MRGASLTMLHQPTPRTDLAvwaEDTLRVIGMIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 121 PVIAFAGD--DSHAQILEQirahseslryvfnfKANGLDAVADF--GESVSDEELDkaigrvrADDLFTIVYTSGSTGKP 196
Cdd:PRK07768 109 AKAVVVGEpfLAAAPVLEE--------------KGIRVLTVADLlaADPIDPVETG-------EDDLALMQLTSGSTGSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 197 KGVMLSHRNFnhtVYNGYEVLNDMLYQP--SRLLLFLPLAHcfaryiqyvaigSHGVVGYIPSAKRLLADLRGFKPTYLL 274
Cdd:PRK07768 168 KAVQITHGNL---YANAEAMFVAAEFDVetDVMVSWLPLFH------------DMGMVGFLTVPMYFGAELVKVTPMDFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 275 GVPRVFEKVYN-------AASQKAGAGLKGRLFAKAFDhfvqwskdemagGHHSLgariqhsfymqtvgSSIRSALgpnm 347
Cdd:PRK07768 233 RDPLLWAELISkyrgtmtAAPNFAYALLARRLRRQAKP------------GAFDL--------------SSLRFAL---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 348 kwlaCGGAPLN-ADLAHFFN-----GFDGITFIQGYGMTETA-----APC----LVNFQDANEVGSVGR----------- 401
Cdd:PRK07768 283 ----NGAEPIDpADVEDLLDagarfGLRPEAILPAYGMAEATlavsfSPCgaglVVDEVDADLLAALRRavpatkgntrr 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 402 --------PGCiSIRLADDD----------ELMIKGPNVFLGYyKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRK 463
Cdd:PRK07768 359 latlgpplPGL-EVRVVDEDgqvlpprgvgVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRV 436
|
490
....*....|....*...
gi 489915853 464 KDIIITaGGKNISPAPME 481
Cdd:PRK07768 437 KDVIIM-AGRNIYPTDIE 453
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
49-497 |
8.10e-18 |
|
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: 86.38 E-value: 8.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLG-LGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPviafag 127
Cdd:cd05958 11 WTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARI------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 128 ddSHAQILEQIRAhseslryvfnfkangldavadfgesvsdeeldkaigrvrADDLFTIVYTSGSTGKPKGVMLSHRNFN 207
Cdd:cd05958 85 --TVALCAHALTA---------------------------------------SDDICILAFTSGTTGAPKATMHFHRDPL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 hTVYNGYEVLNDMLYQPSRLLLFLPLAHCFAR---YIQYVAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPrvfeKVY 284
Cdd:cd05958 124 -ASADRYAVNVLRLREDDRFVGSPPLAFTFGLggvLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAP----TAY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 285 NAASQKAGAGlkgrlfakafdhfvqwskdemagghhslgariqhsfymQTVGSSIRSALGpnmkwlacGGAPLNADLAHF 364
Cdd:cd05958 199 RAMLAHPDAA--------------------------------------GPDLSSLRKCVS--------AGEALPAALHRA 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 365 FNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGcISIRLADDD----------ELMIKGPNVFLGYYKQPQR 432
Cdd:cd05958 233 WKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKpvPG-YEAKVVDDEgnpvpdgtigRLAVRGPTGCRYLADKRQR 311
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 433 TaeaLTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05958 312 T---YVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVLLQHPAVAECAVVG 372
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
17-497 |
9.01e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 87.39 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 17 DTIYSLLAKRCERdpddliAQWQDDETRQWHDV-SAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACAS 95
Cdd:PRK06060 4 GNLAGLLAEQASE------AGWYDRPAFYAADVvTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 96 IGAVSV---PVYETDSpkqtgdivaevepvIAFAGDDSHAQILeqirAHSESLRYVFNfKANGLDAVADFGESVSDEELD 172
Cdd:PRK06060 78 RGVMAFlanPELHRDD--------------HALAARNTEPALV----VTSDALRDRFQ-PSRVAEAAELMSEAARVAPGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 173 KAIgrVRADDLFTIVYTSGSTGKPKGVMlsHRNFNHTVYNGYEVLNDMLYQPSRLLLflplahCFAR-YIQY-------- 243
Cdd:PRK06060 139 YEP--MGGDALAYATYTSGTTGPPKAAI--HRHADPLTFVDAMCRKALRLTPEDTGL------CSARmYFAYglgnsvwf 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 244 -VAIGSHGVVGYIPSAKRLLADLRG-FKPTYLLGVPRVFEKVYNAASQkagaglkgrlfakafDHFvqwskdemagghHS 321
Cdd:PRK06060 209 pLATGGSAVINSAPVTPEAAAILSArFGPSVLYGVPNFFARVIDSCSP---------------DSF------------RS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 322 LGARIqhsfymqTVGSSIRSALGPNmkwlacggaplnadLAHFFNGfdgITFIQGYGMTETAAPCLVNFQDANEVGSVGR 401
Cdd:PRK06060 262 LRCVV-------SAGEALELGLAER--------------LMEFFGG---IPILDGIGSTEVGQTFVSNRVDEWRLGTLGR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 402 ---PGCISIRLAD--------DDELMIKGPNVFLGYYKQPQrtaEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITa 470
Cdd:PRK06060 318 vlpPYEIRVVAPDgttagpgvEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI- 393
|
490 500
....*....|....*....|....*..
gi 489915853 471 GGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK06060 394 GGVNVDPREVERLIIEDEAVAEAAVVA 420
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
29-501 |
2.86e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 29 RDPDDL--IAQ--WQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVY 104
Cdd:PRK09274 18 ERPDQLavAVPggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 105 ETDSPKQTGDIVAEVEPViAFAGDdSHAQILEQI-RAHSESLRYVFNF---KANGLDAVADFGESVSDEELDKAigRVRA 180
Cdd:PRK09274 98 PGMGIKNLKQCLAEAQPD-AFIGI-PKAHLARRLfGWGKPSVRRLVTVggrLLWGGTTLATLLRDGAAAPFPMA--DLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNgyeVLNDMLYQP-SRLLLFLPLAHCFAryiqyVAIGSHGVVGYIPSAK 259
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA---LREDYGIEPgEIDLPTFPLFALFG-----PALGMTSVIPDMDPTR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 260 -------RLLADLRGFKPTYLLGVPRVFEKVYNAASQKagaglkgrlfakafdhfvqwskdemagghhslgariQHSFym 332
Cdd:PRK09274 246 patvdpaKLFAAIERYGVTNLFGSPALLERLGRYGEAN------------------------------------GIKL-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 333 qtvgssirsalgPNMKWLACGGAPLNADLAHFFNGF--DGITFIQGYGMTEtAAP--------CLVNFQDANEVGS---V 399
Cdd:PRK09274 288 ------------PSLRRVISAGAPVPIAVIERFRAMlpPDAEILTPYGATE-ALPissiesreILFATRAATDNGAgicV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 400 GRP-GCISI-----------------RLADDD--ELMIKGPNVFLGYYKQPQRTAEALTSDG----WLHTGDLATIDDRG 455
Cdd:PRK09274 355 GRPvDGVEVriiaisdapipewddalRLATGEigEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQG 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 489915853 456 FVFITGRKKDIIITAGGkNISPAPMEDVINTCPIVAHAVVIGDGRP 501
Cdd:PRK09274 435 RLWFCGRKAHRVETAGG-TLYTIPCERIFNTHPGVKRSALVGVGVP 479
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
22-521 |
3.10e-17 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 85.07 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 22 LLAKRCERDPDdLIAQWQDDETrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV 101
Cdd:cd17655 2 LFEEQAEKTPD-HTAVVFEDQT-----LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 102 PVyETDSPKQTgdivaevepvIAFAGDDSHAQIL------EQIRAHSESLRYVFNfkangldavaDFGESVSDEELDKAI 175
Cdd:cd17655 76 PI-DPDYPEER----------IQYILEDSGADILltqshlQPPIAFIGLIDLLDE----------DTIYHEESENLEPVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 176 grvRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVyngyEVLNDMLYQPSRLllflplahcfaRYIQYVAIGSHGVVGYI 255
Cdd:cd17655 135 ---KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLV----EWANKVIYQGEHL-----------RVALFASISFDASVTEI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 256 PSAkrLLADLRgfkptyLLGVPRvfEKVYNAASqkagaglkgrlfakafdhFVQWSKDemagghhslgARIQHSFYMQTV 335
Cdd:cd17655 197 FAS--LLSGNT------LYIVRK--ETVLDGQA------------------LTQYIRQ----------NRITIIDLTPAH 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 336 GSSIRSA---LGPNMKWLACGGAPLNADLA----HFFNgfDGITFIQGYGMTETAAPCLVNFQDANEVGSV----GRP-G 403
Cdd:cd17655 239 LKLLDAAddsEGLSLKHLIVGGEALSTELAkkiiELFG--TNPTITNAYGPTETTVDASIYQYEPETDQQVsvpiGKPlG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 404 CISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWL------HTGDLATIDDRGFVFITGRkKDII 467
Cdd:cd17655 317 NTRIYILDQYgrpqpvgvagELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGR-IDHQ 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489915853 468 ITAGGKNISPAPMEDVINTCPIVAHAVVIG----DGRPFIAALI----ELDAEMTRSWLASQ 521
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIArkdeQGQNYLCAYIvsekELPVAQLREFLARE 457
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-501 |
4.26e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 84.43 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 50 SAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPviafagdd 129
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 130 shaqileqirahseslryvfnfkangldavadfgesvsdeelDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFN-- 207
Cdd:cd05910 76 ------------------------------------------DAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAaq 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 -HTVYNGYEVLndmlyQPSRLLLFLPLAHCFAryiqyVAIGshgVVGYIP----------SAKRLLADLRGFKPTYLLGV 276
Cdd:cd05910 114 iDALRQLYGIR-----PGEVDLATFPLFALFG-----PALG---LTSVIPdmdptrparaDPQKLVGAIRQYGVSIVFGS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 277 PRVFEKVYNAasqkagaglkgrlfakafdhfvqwskdemagghhslGARIQHSFymqtvgssirsalgPNMKWLACGGAP 356
Cdd:cd05910 181 PALLERVARY------------------------------------CAQHGITL--------------PSLRRVLSAGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 357 LNADLAHFFNGF--DGITFIQGYGMTETAAPCLVN----FQDANEVGSVGRPGCISIRLA-----------------DDD 413
Cdd:cd05910 211 VPIALAARLRKMlsDEAEILTPYGATEALPVSSIGsrelLATTTAATSGGAGTCVGRPIPgvrvriieiddepiaewDDT 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ---------ELMIKGPNVFLGYYKQPQRTAEALTSDG----WLHTGDLATIDDRGFVFITGRKKDIIITAGGKNISpAPM 480
Cdd:cd05910 291 lelprgeigEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYT-EPV 369
|
490 500
....*....|....*....|.
gi 489915853 481 EDVINTCPIVAHAVVIGDGRP 501
Cdd:cd05910 370 ERVFNTHPGVRRSALVGVGKP 390
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
48-507 |
4.40e-17 |
|
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: 84.63 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 48 DVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKqtgdivAEVEPVIAfag 127
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV-DIDQPA------ARREAILA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 128 dDSHAQILeqIRAHSESLRYVFNFKANGLDAVADFGEsvsdeeLDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNfn 207
Cdd:cd12114 82 -DAGARLV--LTDGPDAQLDVAVFDVLILDLDALAAP------APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRA-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 htVYNGYEVLNDmLYQPS---RLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSAKRLLAD-----LRGFKPTYLLGVPRV 279
Cdd:cd12114 151 --ALNTILDINR-RFAVGpddRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAhwaelIERHGVTLWNSVPAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 280 FEKVYNAASQKAGAGLKGRLfakafdhfVQWSKDEMAgghHSLGARIQhsfymqtvgssirsALGPNMKWLACGGAplna 359
Cdd:cd12114 228 LEMLLDVLEAAQALLPSLRL--------VLLSGDWIP---LDLPARLR--------------ALAPDARLISLGGA---- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 360 dlahffngfdgitfiqgygmTETAApcLVNFQDANEV----GSV--GRP-GCISIRLADDD----------ELMIKGPNV 422
Cdd:cd12114 279 --------------------TEASI--WSIYHPIDEVppdwRSIpyGRPlANQRYRVLDPRgrdcpdwvpgELWIGGRGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 423 FLGYYKQPQRTAEALTSDG----WLHTGDLATIDDRGFVFITGRkKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGD 498
Cdd:cd12114 337 ALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGR-RDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL 415
|
....*....
gi 489915853 499 GRPFIAALI 507
Cdd:cd12114 416 GDPGGKRLA 424
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
22-519 |
5.68e-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: 84.17 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 22 LLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV 101
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRS------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 102 PVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQileqirahseslryvfnfkANGLDAVADFGESVSDEELDKAIGRVRAD 181
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTDRSLAGR-------------------AGGLEVAVVIDEALDAGPAGNPAVPVSPD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLndmLYQPSRLLLFLPLAHCFARYIQYVAI--GSHGVV---GYIP 256
Cdd:cd12117 137 DLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVT---LGPDDRVLQTSPLAFDASTFEIWGALlnGARLVLapkGTLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 257 SAKRLLADLRGFKPTYLLgvprvfekvynaasqkagaglkgrLFAKAFDHFVQWSKDEMAGGHHSL--GARIQHsfymqt 334
Cdd:cd12117 214 DPDALGALIAEEGVTVLW------------------------LTAALFNQLADEDPECFAGLRELLtgGEVVSP------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 335 vgSSIRSALgpnmkwLACGgaplnadlahffngfdGITFIQGYGMTETA--APCLVNFQDANEVGSV--GRP-GCISIRL 409
Cdd:cd12117 264 --PHVRRVL------AACP----------------GLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPiANTRVYV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 410 ADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWL------HTGDLATID-DRGFVFItGRKKD-IIITag 471
Cdd:cd12117 320 LDEDgrpvppgvpgELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLpDGRLEFL-GRIDDqVKIR-- 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 472 GKNISPAPMEDVINTCPIVAHAVVI------GDGR--PFIAALIELDAEMTRSWLA 519
Cdd:cd12117 397 GFRIELGEIEAALRAHPGVREAVVVvredagGDKRlvAYVVAEGALDAAELRAFLR 452
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
13-521 |
5.95e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 84.35 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 13 TTDLDTIYSLLAKRCErdpDDLIAQWQDDETRQWHDVSAG---------QMNDRVREVAKGLLgLGVKPgsmvviyaatc 83
Cdd:PRK07867 1 TSSAPTVAELLLPLAE---DDDRGLYFEDSFTSWREHIRGsaaraaalrARLDPTRPPHVGVL-LDNTP----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 84 yEWGVVDFACASIGAVSVPVYETDS-PKQTGDIV-AEVEPVIAfagDDSHAQILEQIRAHSESLRYVFNFKANGLDAVAD 161
Cdd:PRK07867 66 -EFSLLLGAAALSGIVPVGLNPTRRgAALARDIAhADCQLVLT---ESAHAELLDGLDPGVRVINVDSPAWADELAAHRD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 162 fgesvsdEELDkaIGRVRADDLFTIVYTSGSTGKPKGVMLSHR-----------NFNHTVyngyevlNDMLYqpsrllLF 230
Cdd:PRK07867 142 -------AEPP--FRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasagvmlaqRFGLGP-------DDVCY------VS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 231 LPLAH---CFARYIQYVAIGSHGVVGYIPSAKRLLADLRGFKPTYLLGVPRVFEKVYnAASQKAGaglkgrlfakafdhf 307
Cdd:PRK07867 200 MPLFHsnaVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVL-ATPERPD--------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 308 vqwSKDemagghhslgariqhsfymqtvgSSIRSALGPNmkwlacgGAPlnADLAHFFNGFdGITFIQGYGMTETAapcl 387
Cdd:PRK07867 264 ---DAD-----------------------NPLRIVYGNE-------GAP--GDIARFARRF-GCVVVDGFGSTEGG---- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 388 VNFQ--DANEVGSVGR-PGCISI------------------RLADDD---ELM-IKGPNVFLGYYKQPQRTAEALtSDGW 442
Cdd:PRK07867 304 VAITrtPDTPPGALGPlPPGVAIvdpdtgtecppaedadgrLLNADEaigELVnTAGPGGFEGYYNDPEADAERM-RGGV 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 443 LHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCP-IVAHAV------VIGDgrPFIAALI-----ELD 510
Cdd:PRK07867 383 YWSGDLAYRDADGYAYFAGRLGD-WMRVDGENLGTAPIERILLRYPdATEVAVyavpdpVVGD--QVMAALVlapgaKFD 459
|
570
....*....|.
gi 489915853 511 AEMTRSWLASQ 521
Cdd:PRK07867 460 PDAFAEFLAAQ 470
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
33-521 |
1.47e-16 |
|
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: 82.80 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 33 DLIAQWQDDETrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQT 112
Cdd:cd17649 2 DAVALVFGDQS-----LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL-DPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 113 gdivaevepvIAFAGDDSHAQILeqIRAHSESLRYVfnfkangldavadfgesvsdeeldkaigrvraddlftiVYTSGS 192
Cdd:cd17649 76 ----------LRYMLEDSGAGLL--LTHHPRQLAYV--------------------------------------IYTSGS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 193 TGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFA--RYIQYVAIGSHGVVGYIP---SAKRLLADLR- 266
Cdd:cd17649 106 TGTPKGVAVSHGPLAAHCQATAERYG--LTPGDRELQFASFNFDGAheQLLPPLICGACVVLRPDElwaSADELAEMVRe 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 267 ------GFKPTYLlgvprvfekvynaasqkagaglkgRLFAKAFDHfvqwskdemagghhsLGARIQHSFYMQTVGSSir 340
Cdd:cd17649 184 lgvtvlDLPPAYL------------------------QQLAEEADR---------------TGDGRPPSLRLYIFGGE-- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 341 sALGPNMKWLACGGAplnadlahffngfdgITFIQGYGMTET-----AAPCLVNFQDANEVGSVGRP-GCISIRLADDD- 413
Cdd:cd17649 223 -ALSPELLRRWLKAP---------------VRLFNAYGPTEAtvtplVWKCEAGAARAGASMPIGRPlGGRSAYILDADl 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ---------ELMIKGPNVFLGYYKQPQRTAEALTSDG-------WLHTGDLATIDDRGFVFITGRkKDIIITAGGKNISP 477
Cdd:cd17649 287 npvpvgvtgELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGR-VDHQVKIRGFRIEL 365
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 478 APMEDVINTCPIVAHAVVI---GDGRPFIAALIEL--------DAEMTRSWLASQ 521
Cdd:cd17649 366 GEIEAALLEHPGVREAAVValdGAGGKQLVAYVVLraaaaqpeLRAQLRTALRAS 420
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
52-517 |
3.48e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.90 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATcYEWGVVD-FACASIGAvSVPVYETDSPKQTGDIVAEVEPVIAFAGDDS 130
Cdd:PRK07788 78 AELDEQSNALARGLLALGVRAGDGVAVLARN-HRGFVLAlYAAGKVGA-RIILLNTGFSGPQLAEVAAREGVKALVYDDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 131 HAQILEQirAHSESLRYvfnfKANGLDAVADFGESVSDEELDKAIGRVRADDLFT-------IVYTSGSTGKPKGVM--- 200
Cdd:PRK07788 156 FTDLLSA--LPPDLGRL----RAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKppkpggiVILTSGTTGTPKGAPrpe 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 201 ----------LSHRNFNHtvyngyevlNDMLYQPSrlllflPLAHC--FARYIQYVAIGSHGVVGYIPSAKRLLADLRGF 268
Cdd:PRK07788 230 psplaplaglLSRVPFRA---------GETTLLPA------PMFHAtgWAHLTLAMALGSTVVLRRRFDPEATLEDIAKH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 269 KPTYLLGVPRVFEKVYNAASQKAGAglkgrlfakaFDhfvqwskdemagghhslgariqhsfymqtvGSSIRSalgpnmk 348
Cdd:PRK07788 295 KATALVVVPVMLSRILDLGPEVLAK----------YD------------------------------TSSLKI------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 349 wLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQD-ANEVGSVGRP--GCiSIRLADDDELMIKGPNV--- 422
Cdd:PRK07788 328 -IFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDlAEAPGTVGRPpkGV-TVKILDENGNEVPRGVVgri 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 423 -------FLGYY--KQPQRTaealtsDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHA 493
Cdd:PRK07788 406 fvgngfpFEGYTdgRDKQII------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVS-GGENVFPAEVEDLLAGHPDVVEA 478
|
490 500 510
....*....|....*....|....*....|....
gi 489915853 494 VVIG-DGRPF---IAALI------ELDAEMTRSW 517
Cdd:PRK07788 479 AVIGvDDEEFgqrLRAFVvkapgaALDEDAIKDY 512
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
52-497 |
4.29e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 81.03 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKqtgdivaevepVIA--FAGDD 129
Cdd:cd05973 4 GELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPK-----------AIEhrLRTSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 130 SHAQILEQIRAHseslryvfnfkangldavadfgesvsdeELDkaigrvraDDLFTIVYTSGSTGKPKGVMLshrnfnht 209
Cdd:cd05973 73 ARLVVTDAANRH----------------------------KLD--------SDPFVMMFTSGTTGLPKGVPV-------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 210 vyngyevlndmlyqPSRLLLflplahCFARYIQYVaigshgvVGYIP-SAKRLLADlrgfkPTYLLGVprvfekvYNAAS 288
Cdd:cd05973 109 --------------PLRALA------AFGAYLRDA-------VDLRPeDSFWNAAD-----PGWAYGL-------YYAIT 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 289 QKAGAGLKGRLFAKAFDHFVQWSKDEMAGGHHSLGARIQHSFYMqTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGF 368
Cdd:cd05973 150 GPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLM-AAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 369 DGITFIQGYGMTETAAPCLVNFQDANEV--GSVGR--PGCISIRLADD-DELmikGPNV---------------FLGYYK 428
Cdd:cd05973 229 LGVPIHDHYGQTELGMVLANHHALEHPVhaGSAGRamPGWRVAVLDDDgDEL---GPGEpgrlaidiansplmwFRGYQL 305
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489915853 429 QPQRTAealtSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05973 306 PDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR-IGPFDVESALIEHPAVAEAAVIG 369
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
47-519 |
8.11e-16 |
|
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: 80.43 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdspkqtgDIVAEVEPVIAFA 126
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPI----------DPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 127 GDDSHAQILeqirahseslryvfnfkangldavadfgesvsdeeldkaigrVRADDLFTIVYTSGSTGKPKGVMLSHRN- 205
Cdd:cd17643 81 ADSGPSLLL------------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANv 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 206 ------------FNHTvyngyevlndmlyqpSRLLLFLPLAHCFARYIQYVAIgSHG----VVGYI----PSAKRLLADL 265
Cdd:cd17643 119 lalfaatqrwfgFNED---------------DVWTLFHSYAFDFSVWEIWGAL-LHGgrlvVVPYEvarsPEDFARLLRD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 266 RGFkpTYLLGVPrvfekvynaasqkagaglkgrlfaKAFDHFVQWSkDEMAGGHHSLgariqhsfymqtvgssirsalgp 345
Cdd:cd17643 183 EGV--TVLNQTP------------------------SAFYQLVEAA-DRDGRDPLAL----------------------- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 346 nmKWLACGGAPLNAD-LAHFFN--GFDGITFIQGYGMTETAApcLVNFQ-------DANEVGSVGRP-GCISIRLADDD- 413
Cdd:cd17643 213 --RYVIFGGEALEAAmLRPWAGrfGLDRPQLVNMYGITETTV--HVTFRpldaadlPAAAASPIGRPlPGLRVYVLDADg 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ---------ELMIKGPNVFLGYYKQPQRTAEALTSDGW-------LHTGDLATIDDRGFVFITGRkKDIIITAGGKNISP 477
Cdd:cd17643 289 rpvppgvvgELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGR-ADEQVKIRGFRIEL 367
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489915853 478 APMEDVINTCPIVAHAVVI----GDGRPFIAALIELDAEMT------RSWLA 519
Cdd:cd17643 368 GEIEAALATHPSVRDAAVIvredEPGDTRLVAYVVADDGAAadiaelRALLK 419
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
181-497 |
9.48e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 79.32 E-value: 9.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFNHTVyngyEVLNDMLYQPSRLLLFLPlAHCFARyIQyVAIGSHgVVGYIPSAKR 260
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASA----DATHDRLGGPGQWLLALP-AHHIAG-LQ-VLVRSV-IAGSEPVELD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 261 LLAdlrGFKPTYL------LGVPRVFekvynaasqkagAGLKGRLFAKAFDHfvqwskdemAGGHHSLgariqhsfymqt 334
Cdd:PRK07824 107 VSA---GFDPTALpravaeLGGGRRY------------TSLVPMQLAKALDD---------PAATAAL------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 335 vgSSIRSALgpnmkwlaCGGAPLNADLAHFFNGFdGITFIQGYGMTETAAPCLVNfqdanevgsvGRP--GcISIRLaDD 412
Cdd:PRK07824 151 --AELDAVL--------VGGGPAPAPVLDAAAAA-GINVVRTYGMSETSGGCVYD----------GVPldG-VRVRV-ED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 413 DELMIKGPNVFLGYYKQPQRTAEAltSDGWLHTGDLATIDDrGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAH 492
Cdd:PRK07824 208 GRIALGGPTLAKGYRNPVDPDPFA--EPGWFRTDDLGALDD-GVLTVLGRADDAIST-GGLTVLPQVVEAALATHPAVAD 283
|
....*
gi 489915853 493 AVVIG 497
Cdd:PRK07824 284 CAVFG 288
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
68-497 |
1.18e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 80.60 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 68 LGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIV--AEVEPVIAfagDDSHAQILEQIRAHSESL 145
Cdd:PRK05620 59 LGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIInhAEDEVIVA---DPRLAEQLGEILKECPCV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 146 RYVFNFKANGLDAVADF---GESVSDEE--LDkaiGR--------VRADDLFTIVYTSGSTGKPKGVMLSHRNF-----N 207
Cdd:PRK05620 136 RAVVFIGPSDADSAAAHmpeGIKVYSYEalLD---GRstvydwpeLDETTAAAICYSTGTTGAPKGVVYSHRSLylqslS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 208 HTVYNGYEVLNDMLYqpsrlLLFLPLAHcfaryiqyvaIGSHGVvgyiPSAkrlladlrgfkpTYLLGVPRVFekvynaa 287
Cdd:PRK05620 213 LRTTDSLAVTHGESF-----LCCVPIYH----------VLSWGV----PLA------------AFMSGTPLVF------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 288 sqkAGAGLKGRLFAkafdHFVQWSKDEMAGGHHSLGARIQhSFYMQTvgSSIRSALgpnmKWLACGGAPLNADLAHFFNG 367
Cdd:PRK05620 255 ---PGPDLSAPTLA----KIIATAMPRVAHGVPTLWIQLM-VHYLKN--PPERMSL----QEIYVGGSAVPPILIKAWEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 368 FDGITFIQGYGMTETAAPCLVNFQDANEVG--------SVGR-PGCISIRLADDDELM-----------IKGPNVFLGYY 427
Cdd:PRK05620 321 RYGVDVVHVWGMTETSPVGTVARPPSGVSGearwayrvSQGRfPASLEYRIVNDGQVMestdrnegeiqVRGNWVTASYY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 428 KQPQRT----------------AEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVA 491
Cdd:PRK05620 401 HSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYIMAAPEVV 479
|
....*.
gi 489915853 492 HAVVIG 497
Cdd:PRK05620 480 ECAVIG 485
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
22-493 |
1.35e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 80.03 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 22 LLAKRCERDPDDLIaqwqdDETRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVsv 101
Cdd:PRK10946 30 ILTRHAASDAIAVI-----CGERQF---SYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 102 PVYETDSPKQT--GDIVAEVEP--VIA------FAGDDshaqILEQIRAHSESLRYVFNFKANGLDAVADFgesVSDEEL 171
Cdd:PRK10946 100 PVNALFSHQRSelNAYASQIEPalLIAdrqhalFSDDD----FLNTLVAEHSSLRVVLLLNDDGEHSLDDA---INHPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 172 DKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFAryiqyvaIGSHGV 251
Cdd:PRK10946 173 DFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICG--FTPQTRYLCALPAAHNYP-------MSSPGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 252 VG--YIPSAKRLLADlrgfkPTYLLGVPRVFEKVYNAASqkagaglkgrLFAKAFDHFVQWSKDemAGGHHSLgariqhs 329
Cdd:PRK10946 244 LGvfLAGGTVVLAPD-----PSATLCFPLIEKHQVNVTA----------LVPPAVSLWLQAIAE--GGSRAQL------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 330 fymqtvgssiRSalgpnMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETaapcLVNF---QDANEV--GSVGRPgc 404
Cdd:PRK10946 300 ----------AS-----LKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEG----LVNYtrlDDSDERifTTQGRP-- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 405 IS----IRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITA 470
Cdd:PRK10946 359 MSpddeVWVADADgnplpqgevgRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-QINR 437
|
490 500
....*....|....*....|...
gi 489915853 471 GGKNISPAPMEDVINTCPIVAHA 493
Cdd:PRK10946 438 GGEKIAAEEIENLLLRHPAVIHA 460
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
377-521 |
1.40e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 79.65 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 377 YGMTETAAPCLVNFQDANEVG--SVGRP---GCISIRLADDDELMIKGPNVFLGYYkqPQrtaeALTSDGWLHTGDLATI 451
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGnnSSGQVlphAQITIPANQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYL 334
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489915853 452 DDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG--D---GRPFIAALI----ELDAEMTRSWLASQ 521
Cdd:PRK07445 335 DAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVLGlpDphwGEVVTAIYVpkdpSISLEELKTAIKDQ 412
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
188-496 |
2.12e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 79.50 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 188 YTSGSTGKPKGVMLSHRNFNHTVYNG---YEVLNDMLYqpsrlLLFLPLAHCFARYIQY--VAIGSHGVVGYIPSAKRLL 262
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAYLMALSNaliWGMNEGAVY-----LWTLPMFHCNGWCFTWtlAALCGTNICLRQVTAKAIY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 263 ADLRGFKPTYLLGVPRVFEKVYNAASQK-------------AGAGLKGRLFAKAfdhfvqwskdemagghHSLGARIQHS 329
Cdd:PLN02479 277 SAIANYGVTHFCAAPVVLNTIVNAPKSEtilplprvvhvmtAGAAPPPSVLFAM----------------SEKGFRVTHT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 330 FYM-QTVGSSIRSALGPNMKWL-ACGGAPLNADLAHFFNGFDGITFIQgygmTETAAPCLVnfqDANEVGsvgrpgcisi 407
Cdd:PLN02479 341 YGLsETYGPSTVCAWKPEWDSLpPEEQARLNARQGVRYIGLEGLDVVD----TKTMKPVPA---DGKTMG---------- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 408 rladddELMIKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTC 487
Cdd:PLN02479 404 ------EIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GGENISSLEVENVVYTH 475
|
....*....
gi 489915853 488 PIVAHAVVI 496
Cdd:PLN02479 476 PAVLEASVV 484
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
22-519 |
5.42e-15 |
|
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: 78.09 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 22 LLAKRCERDPDDLIAQWQDdetrqwHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSV 101
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 102 PVyETDSPkqtgdivaevEPVIAFAGDDSHAQILEQIRAHSESLRyvfnfkanGLDAVADFGESVSDEELDKAIGR-VRA 180
Cdd:cd17646 77 PL-DPGYP----------ADRLAYMLADAGPAVVLTTADLAARLP--------AGGDVALLGDEALAAPPATPPLVpPRP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNfnhtvyngyeVLNDMLYQ--------PSRLL-------------LFLPLAhCFAR 239
Cdd:cd17646 138 DNLAYVIYTSGSTGRPKGVMVTHAG----------IVNRLLWMqdeyplgpGDRVLqktplsfdvsvweLFWPLV-AGAR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 240 YIqyVA-IGSHGVVGYipsakrLLADLRGFKPTYLLGVPRVFekvynaasqkagaglkgrlfakafDHFVQWSKdemAGG 318
Cdd:cd17646 207 LV--VArPGGHRDPAY------LAALIREHGVTTCHFVPSML------------------------RVFLAEPA---AGS 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 319 HHSLgariQHSFymqtvgssirsalgpnmkwlaCGGAPLNADLAHFFNGFDGITFIQGYGMTETA-----APClvnfqDA 393
Cdd:cd17646 252 CASL----RRVF---------------------CSGEALPPELAARFLALPGAELHNLYGPTEAAidvthWPV-----RG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 394 NEVG---SVGRPGC-ISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLH------TGDLATIDD 453
Cdd:cd17646 302 PAETpsvPIGRPVPnTRLYVLDDAlrpvpvgvpgELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRP 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915853 454 RGFVFITGRkKDIIITAGGKNISPAPMEDVINTCPIVAHAVVI----GDGRPFIAALI-------ELDAEMTRSWLA 519
Cdd:cd17646 382 DGALEFLGR-SDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVaraaPAGAARLVGYVvpaagaaGPDTAALRAHLA 457
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
376-497 |
5.75e-15 |
|
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: 76.57 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 376 GYGMTETAAPCLVNFQDANEVGSVGRPGCI-SIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEAlTSDGWLH 444
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLvQVRILDEDgrevpdgevgEIVARGPTVMAGYWNRPEVNARR-TRGGWHH 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 445 TGDLATIDDRG---FVFITGRkkdiIITAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd17636 221 TNDLGRREPDGslsFVGPKTR----MIKSGAENIYPAEVERCLRQHPAVADAAVIG 272
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
53-521 |
9.24e-15 |
|
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: 77.13 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQTgdivaevepvIAFAGDDSHA 132
Cdd:cd17656 18 ELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPI-DPEYPEER----------RIYIMLDSGV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 133 QILEQIRAHSESLRyvFNFKANGLDAvaDFGESVSDEELDKAigrVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYN 212
Cdd:cd17656 87 RVVLTQRHLKSKLS--FNKSTILLED--PSISQEDTSNIDYI---NNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 213 GYEVLNDMLYqpSRLLLFLPLAHCFARYIQYVAIGSHGVVGYIPSAKRL----LADLRGFKPTYLLGVPRVFEKVYnaAS 288
Cdd:cd17656 160 EREKTNINFS--DKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRdveqLFDLVKRHNIEVVFLPVAFLKFI--FS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 289 QKagaGLKGRlFAKAFDHFVqwskdemagghhSLGARIQHSFYMQTVGSSirsalgpnmkwlacggaplnadlahffngf 368
Cdd:cd17656 236 ER---EFINR-FPTCVKHII------------TAGEQLVITNEFKEMLHE------------------------------ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 369 DGITFIQGYGMTET--AAPCLVNFQD-ANEVGSVGRP-GCISIRLADDD----------ELMIKGPNVFLGYYKQPQRTA 434
Cdd:cd17656 270 HNVHLHNHYGPSEThvVTTYTINPEAeIPELPPIGKPiSNTWIYILDQEqqlqpqgivgELYISGASVARGYLNRQELTA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 435 EALTSDGW------LHTGDLATIDDRGFVFITGRkKDIIITAGGKNISPAPMEDVINTCPIVAHAVVIGDGR-------- 500
Cdd:cd17656 350 EKFFPDPFdpnermYRTGDLARYLPDGNIEFLGR-ADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADdkgekylc 428
|
490 500
....*....|....*....|.
gi 489915853 501 PFIAALIELDAEMTRSWLASQ 521
Cdd:cd17656 429 AYFVMEQELNISQLREYLAKQ 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
17-487 |
1.04e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.29 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 17 DTIYSLLAKRCERDPDDLIAQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVkPGSMVVIYAATCYEWGVVDFACASI 96
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 97 GAVSVPVYETDSPKQTG-----DIVAEVEPVIAFAGDDSHA--QILEQIRAHSeslryvfnfkANGLDAVaDFGESVSDE 169
Cdd:PRK05691 88 GVIAVPAYPPESARRHHqerllSIIADAEPRLLLTVADLRDslLQMEELAAAN----------APELLCV-DTLDPALAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 170 ELDKAigRVRADDLFTIVYTSGSTGKPKGVMLSHRNFnhtvyngyeVLNDMLYQ--------PSRLLL-FLPLAHCFAry 240
Cdd:PRK05691 157 AWQEP--ALQPDDIAFLQYTSGSTALPKGVQVSHGNL---------VANEQLIRhgfgidlnPDDVIVsWLPLYHDMG-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 241 iqyvAIGS--HGVVGYIPSAkrLLAdlrgfkPTYLLGVP-RVFEkvynAASQKAGAGLKGRLFAKAFDHfvqwskdemag 317
Cdd:PRK05691 224 ----LIGGllQPIFSGVPCV--LMS------PAYFLERPlRWLE----AISEYGGTISGGPDFAYRLCS----------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 318 ghhslgARIQHSFYMQTVGSSIRSALGpnmkwlacGGAPLNAD-LAHFFN-----GFDGITFIQGYGMTE---------- 381
Cdd:PRK05691 277 ------ERVSESALERLDLSRWRVAYS--------GSEPIRQDsLERFAEkfaacGFDPDSFFASYGLAEatlfvsggrr 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 382 -TAAPCL-VNFQ--DANEV----GSV------GRPGCiSIRLAD-------DD----ELMIKGPNVFLGYYKQPQRTAEA 436
Cdd:PRK05691 343 gQGIPALeLDAEalARNRAepgtGSVlmscgrSQPGH-AVLIVDpqslevlGDnrvgEIWASGPSIAHGYWRNPEASAKT 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489915853 437 LTS-DG--WLHTGDLATIDDrGFVFITGRKKDIIITAgGKNISPAPMEDVINTC 487
Cdd:PRK05691 422 FVEhDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIVR-GHNLYPQDIEKTVERE 473
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
398-497 |
1.31e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 76.74 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 398 SVGRPgC----ISIRLADDDELM--------IKGPNVFLGYyKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKD 465
Cdd:PRK07638 308 SVGRP-FhnvqVRICNEAGEEVQkgeigtvyVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKN 385
|
90 100 110
....*....|....*....|....*....|..
gi 489915853 466 IIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK07638 386 MILF-GGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
16-497 |
1.46e-14 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 76.97 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 16 LDTIYSLLAKRCERDPDDLIA-QWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACA 94
Cdd:cd05967 49 LNTCYNALDRHVEAGRGDQIAlIYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 95 SIGAVSVPVYETDSPKQTGDIVAEVEPVI---AFAGDDSHaQILEQIRAHSESLR---------YVFN---FKANGLDAV 159
Cdd:cd05967 129 RIGAIHSVVFGGFAAKELASRIDDAKPKLivtASCGIEPG-KVVPYKPLLDKALElsghkphhvLVLNrpqVPADLTKPG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 160 ADFGesvSDEELDKAIGR----VRADDLFTIVYTSGSTGKPKGVMlshRNfnhtvYNGYEVlndMLYQPSRLLLFLPLAH 235
Cdd:cd05967 208 RDLD---WSELLAKAEPVdcvpVAATDPLYILYTSGTTGKPKGVV---RD-----NGGHAV---ALNWSMRNIYGIKPGD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 236 CF--ARYIQYVaIGsHGVVGYIPSAKRLLADLRGFKPTyllGVP------RVFEKvYNAASqkagaglkgrLFA--KAFD 305
Cdd:cd05967 274 VWwaASDVGWV-VG-HSYIVYGPLLHGATTVLYEGKPV---GTPdpgafwRVIEK-YQVNA----------LFTapTAIR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 306 HFVQWSKDEMAGGHHSLgariqhsfymqtvgSSIRSAlgpnmkWLAcgGAPLNADLAHFFNGFDGITFIQGYGMTET--- 382
Cdd:cd05967 338 AIRKEDPDGKYIKKYDL--------------SSLRTL------FLA--GERLDPPTLEWAENTLGVPVIDHWWQTETgwp 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 383 -AAPCLVNFQDANEVGSVGRP--GcISIRLADDD----------ELMIKGP---NVFLGYYKQPQRTAEAL--TSDGWLH 444
Cdd:cd05967 396 iTANPVGLEPLPIKAGSPGKPvpG-YQVQVLDEDgepvgpnelgNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYD 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489915853 445 TGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05967 475 TGDAGYKDEDGYLFIMGRTDDVINVAGHR-LSTGEMEESVLSHPAVAECAVVG 526
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
52-467 |
1.48e-14 |
|
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: 76.19 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQTGDIVAEvepviafagdDSH 131
Cdd:cd17653 26 GELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL-DAKLPSARIQAILR----------TSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 132 AQILeqirahseslryVFNfkangldavadfgesvsdeeldkaigrVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVY 211
Cdd:cd17653 95 ATLL------------LTT---------------------------DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 212 NGyevlNDMLY-QP-SRLLLFLPlahcfaryiqyvaigshgvVGYIPSAKRLLADLrGFKPTYLLGvprvfekvynaasq 289
Cdd:cd17653 136 QP----PARLDvGPgSRVAQVLS-------------------IAFDACIGEIFSTL-CNGGTLVLA-------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 290 kagaglkgrlfakafDHFVQWSKDemagghhslgARIQHSFYMQ-TVGSSIRSALGPNMKWLACGGAPLNADLAHFFNGf 368
Cdd:cd17653 178 ---------------DPSDPFAHV----------ARTVDALMSTpSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSP- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 369 dGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPgcI---SIRLADDD----------ELMIKGPNVFLGYYKQPQRTAE 435
Cdd:cd17653 232 -GRRLYNAYGPTECTISSTMTELLPGQPVTIGKP--IpnsTCYILDADlqpvpegvvgEICISGVQVARGYLGNPALTAS 308
|
410 420 430
....*....|....*....|....*....|....*...
gi 489915853 436 ALTSDGWLH------TGDLATIDDRGFVFITGRKKDII 467
Cdd:cd17653 309 KFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQV 346
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
16-497 |
1.52e-14 |
|
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: 77.15 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 16 LDTIYSLLAKRCERDPDDLIAQW--QDDETRQWhdvSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFAC 93
Cdd:cd05968 60 MNIVEQLLDKWLADTRTRPALRWegEDGTSRTL---TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 94 ASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDD--------SHAQILEQIRAHSESLRYVFNFKANGLD-AVADFGE 164
Cdd:cd05968 137 ARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevNLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKGRD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 165 SVSDEELDKA---IGRVRADDLFTIVYTSGSTGKPKGVMLSHRNF----NHTVYNGYEVLN-DMLYQPSRLLLFLPLAHC 236
Cdd:cd05968 217 LSYDEEKETAgdgAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFplkaAQDMYFQFDLKPgDLLTWFTDLGWMMGPWLI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 237 FARYIQYVAIGSH-GVVGYiPSAKRLLADLRGFKPTYLLGVPRVFekvynaasqkagaglkgRLFAKAFDHFVQwskdem 315
Cdd:cd05968 297 FGGLILGATMVLYdGAPDH-PKADRLWRMVEDHEITHLGLSPTLI-----------------RALKPRGDAPVN------ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 316 aggHHSLgariqhsfymqtvgSSIRSalgpnmkwLACGGAPLNADLAHFF---NGFDGITFIQGYGMTETAAPCLVNF-- 390
Cdd:cd05968 353 ---AHDL--------------SSLRV--------LGSTGEPWNPEPWNWLfetVGKGRNPIINYSGGTEISGGILGNVli 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 391 ---QDANEVGSVgrPGCISIRLADD--------DELMIKGPNVFL--GYYKQPQRTAEALTS---DGWLHtGDLATIDDR 454
Cdd:cd05968 408 kpiKPSSFNGPV--PGMKADVLDESgkparpevGELVLLAPWPGMtrGFWRDEDRYLETYWSrfdNVWVH-GDFAYYDEE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489915853 455 GFVFITGRKKDIIITAgGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05968 485 GYFYILGRSDDTINVA-GKRVGPAEIESVLNAHPAVLESAAIG 526
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
39-511 |
2.98e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 75.69 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 39 QDDETRQWhdvsaGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPV---YETDspkqtgdi 115
Cdd:PRK07798 24 CGDRRLTY-----AELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYVED-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 116 vaEVEPVIAFAG------DDSHAQILEQIRAHSESLRYVFNF-----KANGLDAVaDFGESVSDEELDKAIGRVRADDLF 184
Cdd:PRK07798 91 --ELRYLLDDSDavalvyEREFAPRVAEVLPRLPKLRTLVVVedgsgNDLLPGAV-DYEDALAAGSPERDFGERSPDDLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 185 tIVYTSGSTGKPKGVMLSHRNFNHTVYNGY-----EVLNDmLYQ---------PSRLLLFLPLAHCFARYIQYVAIGSHG 250
Cdd:PRK07798 168 -LLYTGGTTGMPKGVMWRQEDIFRVLLGGRdfatgEPIED-EEElakraaagpGMRRFPAPPLMHGAGQWAAFAALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 251 VVgyipsakrLLADLRGFKPTYLL------GVPRVFekvynaasqkagagLKGRLFAKAfdhfvqwskdeMAGGHHSLGa 324
Cdd:PRK07798 246 TV--------VLLPDVRFDADEVWrtiereKVNVIT--------------IVGDAMARP-----------LLDALEARG- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 325 riqhsfymQTVGSSIRSalgpnmkwLACGGAPLNAD-----LAHFFNgfdgITFIQGYGMTETAApCLVNFQDANEVGSV 399
Cdd:PRK07798 292 --------PYDLSSLFA--------IASGGALFSPSvkealLELLPN----VVLTDSIGSSETGF-GGSGTVAKGAVHTG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 400 G-----RPGCISIRlADDDEL--------MI-KGPNVFLGYYKQPQRTAEAL-TSDG--WLHTGDLATIDDRGFVFITGR 462
Cdd:PRK07798 351 GprftiGPRTVVLD-EDGNPVepgsgeigWIaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGR 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489915853 463 KKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIgdGRP------FIAALIELDA 511
Cdd:PRK07798 430 GSVCINTGGEK-VFPEEVEEALKAHPDVADALVV--GVPderwgqEVVAVVQLRE 481
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
53-501 |
3.02e-14 |
|
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: 75.97 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGL-GVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPvyETDSPKQTgDIVAEVEPVIA--FAGDD 129
Cdd:cd05928 46 ELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIP--GTIQLTAK-DILYRLQASKAkcIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 130 SHAQILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNHT 209
Cdd:cd05928 123 ELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 210 VYNGYEVLNDMlyQPSRLLLFLP--------LAHCFARYIQYVAIGSHGVVGYIPsaKRLLADLRGFKPTYLLGVPRVFe 281
Cdd:cd05928 203 LKVNGRYWLDL--TASDIMWNTSdtgwiksaWSSLFEPWIQGACVFVHHLPRFDP--LVILKTLSSYPITTFCGAPTVY- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 282 kvynaasqkagaglkgRLFakafdhfvqwskdemagghhslgarIQHSFymqtvgSSIRSalgPNMKWLACGGAPLNADL 361
Cdd:cd05928 278 ----------------RML-------------------------VQQDL------SSYKF---PSLQHCVTGGEPLNPEV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 362 AHFFNGFDGITFIQGYGMTETAAPCLVNFQDANEVGSVGRPG-CISIRLADDD----------ELMIK-GPN----VFLG 425
Cdd:cd05928 308 LEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASpPYDVQIIDDNgnvlppgtegDIGIRvKPIrpfgLFSG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 426 YYKQPQRTAEALTSDGWLhTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVIGDGRP 501
Cdd:cd05928 388 YVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYR-IGPFEVESALIEHPAVVESAVVSSPDP 461
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
40-519 |
4.81e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 74.91 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 40 DDETRQWHdvsagQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSPKQTGDIVAEV 119
Cdd:PRK09029 25 NDEVLTWQ-----QLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPL----NPQLPQPLLEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 120 EPV--IAFAGDDSHAQILEQIRAHSESLryvfnfkANGLDAVAdfgesvsdeeldkaigrVRADDLFTIVYTSGSTGKPK 197
Cdd:PRK09029 96 LPSltLDFALVLEGENTFSALTSLHLQL-------VEGAHAVA-----------------WQPQRLATMTLTSGSTGLPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 198 GVMLSHRNfnHTVyNGYEVLNDMLYQPS-RLLLFLPLAHcfaryiqyvaIGSHGVV------G---YIPSAKRLLADLRG 267
Cdd:PRK09029 152 AAVHTAQA--HLA-SAEGVLSLMPFTAQdSWLLSLPLFH----------VSGQGIVwrwlyaGatlVVRDKQPLEQALAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 268 FKPTYLlgVPrvfekvynaaSQkagagLKgRLFakafdhfvQWSKDEMAGGHHSLG-ARIQHSFYMQTVGSSIRSalgpn 346
Cdd:PRK09029 219 CTHASL--VP----------TQ-----LW-RLL--------DNRSEPLSLKAVLLGgAAIPVELTEQAEQQGIRC----- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 347 mkWLacggaplnadlahffngfdgitfiqGYGMTETAAP-CLVNFQDANEVGSV--GRpgciSIRLAdDDELMIKGPNVF 423
Cdd:PRK09029 268 --WC-------------------------GYGLTEMASTvCAKRADGLAGVGSPlpGR----EVKLV-DGEIWLRGASLA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 424 LGYYKQPQRTaeALT-SDGWLHTGDLATIDDRGFVfITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVI------ 496
Cdd:PRK09029 316 LGYWRQGQLV--PLVnDEGWFATRDRGEWQNGELT-ILGRLDNLFFS-GGEGIQPEEIERVINQHPLVQQVFVVpvadae 391
|
490 500
....*....|....*....|....
gi 489915853 497 -GDgRPfiAALIELDAEMTRSWLA 519
Cdd:PRK09029 392 fGQ-RP--VAVVESDSEAAVVNLA 412
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
38-497 |
2.45e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 73.01 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 38 WQDDETRQwhDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVA 117
Cdd:PRK04319 65 YLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 118 EVEPVIAFAGDDSHAQIleqIRAHSESLRYVFNFKANG--LDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGK 195
Cdd:PRK04319 143 DSEAKVLITTPALLERK---PADDLPSLKHVLLVGEDVeeGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 196 PKGVMLSHrnfnhtvyngyevlNDML--YQPSRLLL------------------------FLPLAHCFARYIQ------- 242
Cdd:PRK04319 220 PKGVLHVH--------------NAMLqhYQTGKYVLdlheddvywctadpgwvtgtsygiFAPWLNGATNVIDggrfspe 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 243 --YVAIGSHGV-VGYI-PSAKRLLadlrgfkptyllgvprvfekvynaasQKAGAGLkgrlfAKAFDHfvqwskdemagg 318
Cdd:PRK04319 286 rwYRILEDYKVtVWYTaPTAIRML--------------------------MGAGDDL-----VKKYDL------------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 319 hhslgariqhsfymqtvgSSIRSalgpnmkwLACGGAPLNADLAHFfnGFD--GITFIQGYGMTETAAPCLVNFQdANEV 396
Cdd:PRK04319 323 ------------------SSLRH--------ILSVGEPLNPEVVRW--GMKvfGLPIHDNWWMTETGGIMIANYP-AMDI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 397 --GSVGRP--GCISIRLADDD---------ELMIKG--PNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITG 461
Cdd:PRK04319 374 kpGSMGKPlpGIEAAIVDDQGnelppnrmgNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQG 452
|
490 500 510
....*....|....*....|....*....|....*.
gi 489915853 462 RKKDIIITAgGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK04319 453 RVDDVIKTS-GERVGPFEVESKLMEHPAVAEAGVIG 487
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
370-543 |
2.55e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 73.21 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 370 GITFIQGYGMTETAAPCLVNFQDANEVGSVGR--PGcISIRL------ADDDELMIKGPNVFLGYYK--------QPQ-R 432
Cdd:PRK08043 504 GLRILEGYGVTECAPVVSINVPMAAKPGTVGRilPG-MDARLlsvpgiEQGGRLQLKGPNIMNGYLRvekpgvleVPTaE 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 433 TAEALTSDGWLHTGDLATIDDRGFVFITGRKKDIIITAgGKNISPAPMEDVIN-TCPIVAHAVVI-GDGRPFIA-ALIEL 509
Cdd:PRK08043 583 NARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALgVSPDKQHATAIkSDASKGEAlVLFTT 661
|
170 180 190
....*....|....*....|....*....|....
gi 489915853 510 DAEMTRSWLASQNLDIDAPmsEIATNDAVRALVQ 543
Cdd:PRK08043 662 DSELTREKLQQYAREHGVP--ELAVPRDIRYLKQ 693
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
377-497 |
5.14e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 72.03 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 377 YGMTETAAPCLVNFQDANE-VGSVGRPGCISIRLADDD----------ELMIKGPNVFlGYYKQPQRTAEALTSDG-WLH 444
Cdd:PRK13391 307 YAATEGLGFTACDSEEWLAhPGTVGRAMFGDLHILDDDgaelppgepgTIWFEGGRPF-EYLNDPAKTAEARHPDGtWST 385
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489915853 445 TGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK13391 386 VGDIGYVDEDGYLYLTDRAAFMIIS-GGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
178-497 |
6.77e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 71.60 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 178 VRADDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYE----VLNDMLYQPsrlllfLPLAHCFARYIQY-VAIGSHGVV 252
Cdd:PRK13388 147 VDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTErfglTRDDVCYVS------MPLFHSNAVMAGWaPAVASGAAV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 253 GYIP--SAKRLLADLRGFKPTYLLGVprvfekvynaasQKAGAGLkgrlfakafdhfvqwskdeMAGGHHSLGA--RIQH 328
Cdd:PRK13388 221 ALPAkfSASGFLDDVRRYGATYFNYV------------GKPLAYI-------------------LATPERPDDAdnPLRV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 SFYMQtvgSSIRsalgpnmkwlacggaplnaDLAHFFNGFdGITFIQGYGMTETAapCLVNFQDANEVGSVGRPG-CISI 407
Cdd:PRK13388 270 AFGNE---ASPR-------------------DIAEFSRRF-GCQVEDGYGSSEGA--VIVVREPGTPPGSIGRGApGVAI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 408 ------------------RLADDDELM-----IKGPNVFLGYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKK 464
Cdd:PRK13388 325 ynpetltecavarfdahgALLNADEAIgelvnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTA 403
|
330 340 350
....*....|....*....|....*....|...
gi 489915853 465 DiIITAGGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:PRK13388 404 D-WMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-512 |
1.17e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.91 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 19 IYSLLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGA 98
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGG 3132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 99 VSVPVyetdSPKQTGDivaevepVIAFAGDDSHAQILEQirahSESLRYVFNFKANGLDAVADfGESVSDEELDKaigRV 178
Cdd:PRK12316 3133 AYVPL----DPEYPEE-------RLAYMLEDSGAQLLLS----QSHLRLPLAQGVQVLDLDRG-DENYAEANPAI---RT 3193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 179 RADDLFTIVYTSGSTGKPKGVMLSHRNF-NHTVYNGYEVlndMLYQPSRLLLFLPLAHCFARYIQYVAIgshgvvgyIPS 257
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALsNHLCWMQQAY---GLGVGDRVLQFTTFSFDVFVEELFWPL--------MSG 3262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 258 AKRLLADLRgfkptyLLGVPRVFEKVYNAASQKAGAGLKGrlfakafdhfvQWSKDEMAGGHHSLGariqhsfymqtvgs 337
Cdd:PRK12316 3263 ARVVLAGPE------DWRDPALLVELINSEGVDVLHAYPS-----------MLQAFLEEEDAHRCT-------------- 3311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 338 SIRSALgpnmkwlaCGGAPLNADLAHFFNGfdGITFIQGYGMTETAAPCLVNFQDANEVGS--VGRP-GCISIRLADDD- 413
Cdd:PRK12316 3312 SLKRIV--------CGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPiANRACYILDGSl 3381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 414 ---------ELMIKGPNVFLGYYKQPQRTAEALTSDGW------LHTGDLATIDDRGFVFITGRkKDIIITAGGKNISPA 478
Cdd:PRK12316 3382 epvpvgalgELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGR-VDHQVKIRGFRIELG 3460
|
490 500 510
....*....|....*....|....*....|....*
gi 489915853 479 PMEDVINTCPIVAHAVVIG-DGRPFIAALIELDAE 512
Cdd:PRK12316 3461 EIEARLLEHPWVREAVVLAvDGRQLVAYVVPEDEA 3495
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
38-497 |
1.55e-12 |
|
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: 70.74 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 38 WQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVA 117
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 118 EVEPVIAFAGDDSH---------AQILEQIRAHSESLRYVFNFKANGLDAVA-------DFGESVSDEELDKAIGRVRAD 181
Cdd:TIGR02188 158 DAGAKLVITADEGLrggkviplkAIVDEALEKCPVSVEHVLVVRRTGNPVVPwvegrdvWWHDLMAKASAYCEPEPMDSE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMlshrnfnHTVyNGYevlndmlyqpsrlLLFLPLAH-------------CFA--------RY 240
Cdd:TIGR02188 238 DPLFILYTSGSTGKPKGVL-------HTT-GGY-------------LLYAAMTMkyvfdikdgdifwCTAdvgwitghSY 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 241 IQY--VAIGS-----HGVVGYiPSAKRLLADLRGFKPTYLLGVPRVFekvynaasqkagaglkgRLFAKAFDHFVQwskd 313
Cdd:TIGR02188 297 IVYgpLANGAttvmfEGVPTY-PDPGRFWEIIEKHKVTIFYTAPTAI-----------------RALMRLGDEWVK---- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 314 emaggHHSLgariqhsfymqtvgSSIRSalgpnmkwLACGGAPLNADLAHFFN---GFDGITFIQGYGMTETAAPCLVNF 390
Cdd:TIGR02188 355 -----KHDL--------------SSLRL--------LGSVGEPINPEAWMWYYkvvGKERCPIVDTWWQTETGGIMITPL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 391 QDANEV--GSVGRP--GcISIRLADDDELMIKGPNV-------------FLGYYKQPQRTAEALTSD--GWLHTGDLATI 451
Cdd:TIGR02188 408 PGATPTkpGSATLPffG-IEPAVVDEEGNPVEGPGEggylvikqpwpgmLRTIYGDHERFVDTYFSPfpGYYFTGDGARR 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 489915853 452 DDRGFVFITGRKKDIIITAgGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:TIGR02188 487 DKDGYIWITGRVDDVINVS-GHRLGTAEIESALVSHPAVAEAAVVG 531
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
49-547 |
2.10e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 70.04 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAE--VEPVIAFA 126
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDsgARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 127 GDDShaqILEQIRAHSEsLRYVFNFKANGL----DAVADFGESVSDEeldkAIGRVraddlftIVYTSGSTGKPKGVM-- 200
Cdd:PRK13390 105 ALDG---LAAKVGADLP-LRLSFGGEIDGFgsfeAALAGAGPRLTEQ----PCGAV-------MLYSSGTTGFPKGIQpd 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 201 LSHRNFNH------TVYNGYEVL--NDMLYQPSRLLLFLPLAHCFARYiqyvAIGSHGVVGYIPSAKRLLADLRGFKPTY 272
Cdd:PRK13390 170 LPGRDVDApgdpivAIARAFYDIseSDIYYSSAPIYHAAPLRWCSMVH----ALGGTVVLAKRFDAQATLGHVERYRITV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 273 LLGVPRVFEKVynaasqkagagLKgrlfakafdhfvqwskdemagghhsLGARIQHSFYMQTVGSSIRSAlgpnmkwlac 352
Cdd:PRK13390 246 TQMVPTMFVRL-----------LK-------------------------LDADVRTRYDVSSLRAVIHAA---------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 353 ggAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLVNFQD-ANEVGSVGRPGCISIRLADDDELMIKGPNVFLGYYKQ-- 429
Cdd:PRK13390 280 --APCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDwLAHPGSVGRSVLGDLHICDDDGNELPAGRIGTVYFERdr 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 430 --------PQRTAEAL--TSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIGDG 499
Cdd:PRK13390 358 lpfrylndPEKTAAAQhpAHPFWTTVGDLGSVDEDGYLYLADRKSFMIIS-GGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489915853 500 RP----FIAALIELDAEMTRSWLASQNLdIDAPMSEIATNDAVRALvqQYID 547
Cdd:PRK13390 437 DPemgeQVKAVIQLVEGIRGSDELAREL-IDYTRSRIAHYKAPRSV--EFVD 485
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-510 |
3.54e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 68.56 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 180 ADDLFtIVYTSGSTGKPKGVMLSHRNFNHTVYNGY------EVLNDMLYQ------PSRLLLFLPLAHCFARYIQYVAIG 247
Cdd:cd05924 3 ADDLY-ILYTGGTTGMPKGVMWRQEDIFRMLMGGAdfgtgeFTPSEDAHKaaaaaaGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 248 SHGVVgyipsakrLLADLRgFKPTYLLgvpRVFEKvynaasQKAG-AGLKGRLFAK----AFDhfvqwskdemAGGHHSL 322
Cdd:cd05924 82 GGQTV--------VLPDDR-FDPEEVW---RTIEK------HKVTsMTIVGDAMARplidALR----------DAGPYDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 323 gariqhsfymqtvgSSIRSalgpnmkwLACGGAPLNAD-----LAHFFNgfdgITFIQGYGMTETAAPCL-VNFQDANEV 396
Cdd:cd05924 134 --------------SSLFA--------ISSGGALLSPEvkqglLELVPN----ITLVDAFGSSETGFTGSgHSAGSGPET 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 397 GSVGRPGCISIRLADDDELMIKGP----------NVFLGYYKQPQRTAEAL-TSDG--WLHTGDLATIDDRGFVFITGRk 463
Cdd:cd05924 188 GPFTRANPDTVVLDDDGRVVPPGSggvgwiarrgHIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGR- 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489915853 464 KDIIITAGGKNISPAPMEDVINTCPIVAHAVVIgdGRP------FIAALIELD 510
Cdd:cd05924 267 GSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV--GRPderwgqEVVAVVQLR 317
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
345-544 |
1.33e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 67.33 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 345 PNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETAAPCLV---NFQDANEvgSVGRP--GCiSIRLADDDELMIkG 419
Cdd:PRK13383 292 PQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALAtpaDLRDAPE--TVGKPvaGC-PVRILDRNNRPV-G 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 420 PNV----FLGYYKQPQRTAEA---LTSDGWLHTGDLATIDDRGFVFITGRKKDIIITaGGKNISPAPMEDVINTCPIVAH 492
Cdd:PRK13383 368 PRVtgriFVGGELAGTRYTDGggkAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAHPAVAD 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915853 493 AVVIG--DGR--PFIAALI------ELDAEMTRSWLASQNLDIDAP-----MSEIATNDAVRALVQQ 544
Cdd:PRK13383 447 NAVIGvpDERfgHRLAAFVvlhpgsGVDAAQLRDYLKDRVSRFEQPrdiniVSSIPRNPTGKVLRKE 513
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
49-462 |
4.48e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.72 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQTgdivaevepvIAFAGD 128
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL-DPEYPQDR----------LAYMLD 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQILeqiRAHSESLRYV---FNFKANGLDAVADFGESVSDEELDKAIGrvrADDLFTIVYTSGSTGKPKGVMLSHRN 205
Cdd:PRK12467 607 DSGVRLL---LTQSHLLAQLpvpAGLRSLCLDEPADLLCGYSGHNPEVALD---PDNLAYVIYTSGSTGQPKGVAISHGA 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 206 FNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFARYIQYVAIGSHGVVgyipsakrLLADlrgfkptyllgvprvFEKVYN 285
Cdd:PRK12467 681 LANYVCVIAERLQ--LAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLP---------------PDCARD 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 286 AASqkagaglkgrlfakafdhFVQWSKDemagghHSLGARIQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADL-AHF 364
Cdd:PRK12467 736 AEA------------------FAALMAD------QGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLlARV 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 365 FNGFDGITFIQGYGMTETAA-----PCLVNFQDANEVgSVGRP-GCISIRLADDD----------ELMIKGPNVFLGYYK 428
Cdd:PRK12467 792 RALGPGARLINHYGPTETTVgvstyELSDEERDFGNV-PIGQPlANLGLYILDHYlnpvpvgvvgELYIGGAGLARGYHR 870
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489915853 429 QPQRTAEALTSD------GWLH-TGDLATIDDRGFVFITGR 462
Cdd:PRK12467 871 RPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGR 911
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-513 |
7.41e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.13 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 19 IYSLLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGA 98
Cdd:PRK12316 4553 VHQLVAERARMTPDAVAVVFDEEK------LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 99 VSVPVyETDSPKQTgdivaevepvIAFAGDDSHAQILEQIRAHSESLRYVFNFKANGLDAVADF-GESVSDEELdkaigR 177
Cdd:PRK12316 4627 AYVPL-DPEYPRER----------LAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWeGFPAHDPAV-----R 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 178 VRADDLFTIVYTSGSTGKPKGVMLSHRNF-NHTVYNG--YEVLNDmlyqpSRLLLFLPLAhcFAryiqyvaiGSHgvvgy 254
Cdd:PRK12316 4691 LHPDNLAYVIYTSGSTGRPKGVAVSHGSLvNHLHATGerYELTPD-----DRVLQFMSFS--FD--------GSH----- 4750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 255 ipsakrlladlRGFKPTYLLGVPRVFekvynaasQKAGAGLKGRLFAKAFDHFVqwskdemagghhSLGARIQHSFYMQT 334
Cdd:PRK12316 4751 -----------EGLYHPLINGASVVI--------RDDSLWDPERLYAEIHEHRV------------TVLVFPPVYLQQLA 4799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 335 VGSSIRSALGPNMKWLACGGAPLNADLAHFFNGFDGITFIQGYGMTETA-APCLVNFQDANEVGS----VGRP-GCISIR 408
Cdd:PRK12316 4800 EHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTvTVLLWKARDGDACGAaympIGTPlGNRSGY 4879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 409 LADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSD------GWLH-TGDLATIDDRGFVFITGRkKDIIITAG 471
Cdd:PRK12316 4880 VLDGQlnplpvgvagELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGR-VDHQVKIR 4958
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 489915853 472 GKNISPAPMEDVINTCPIVAHAVVIGD----GRPFIAALIELDAEM 513
Cdd:PRK12316 4959 GFRIELGEIEARLREHPAVREAVVIAQegavGKQLVGYVVPQDPAL 5004
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-528 |
8.56e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 8.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 19 IYSLLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGA 98
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQH------LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 99 VSVPVyETDSPKQTgdivaevepvIAFAGDDSHAQILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDkaigRV 178
Cdd:PRK12316 2079 AYVPL-DPNYPAER----------LAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAEWADYPDTAPAV----QL 2143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 179 RADDLFTIVYTSGSTGKPKGVMLSHRnfnhtvyngyevlndmlyqpsrlllflPLA-HCFARYIQYVAIGSHGVVGYIPS 257
Cdd:PRK12316 2144 AGENLAYVIYTSGSTGLPKGVAVSHG---------------------------ALVaHCQAAGERYELSPADCELQFMSF 2196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 258 AkrlladLRGFkptyllgVPRVFEKVYNAAsqkagaglkgRLFAKAFDHfvqWSKDEMAGGHHSLGARIQH---SFYMQT 334
Cdd:PRK12316 2197 S------FDGA-------HEQWFHPLLNGA----------RVLIRDDEL---WDPEQLYDEMERHGVTILDfppVYLQQL 2250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 335 VGSSIRSALGPNMKWLACGGAPLNADLAH-FFNGFDGITFIQGYGMTETAAPCLV---NFQDANEVGSV--GRP-GCISI 407
Cdd:PRK12316 2251 AEHAERDGRPPAVRVYCFGGEAVPAASLRlAWEALRPVYLFNGYGPTEAVVTPLLwkcRPQDPCGAAYVpiGRAlGNRRA 2330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 408 RLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLH-------TGDLATIDDRGFVFITGRkKDIIITA 470
Cdd:PRK12316 2331 YILDADlnllapgmagELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGR-IDHQVKI 2409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915853 471 GGKNISPAPMEDVINTCPIVAHAVVIG----DGRPFIAALI-----ELDAEMTRSWLASQNLDIDAP 528
Cdd:PRK12316 2410 RGFRIELGEIEARLQAHPAVREAVVVAqdgaSGKQLVAYVVpddaaEDLLAELRAWLAARLPAYMVP 2476
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
20-497 |
1.27e-10 |
|
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: 64.50 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 20 YSLLAKRCERDPDDLIAQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAV 99
Cdd:cd05966 56 YNCLDRHLKERGDKVAIIWEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 100 -SVpVYETDSPKQTGDIVAEVEPVIAFAGDDS--------HAQILEQIRAHSESLRYVFNFKANGLDAVADFGESV-SDE 169
Cdd:cd05966 136 hSV-VFAGFSAESLADRINDAQCKLVITADGGyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEGRDLwWHD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 170 ELDKAIGRVRA------DDLFtIVYTSGSTGKPKGVMlshrnfnHTVyNGYevlndMLYQpsrlllflplahcfARYIQY 243
Cdd:cd05966 215 LMAKQSPECEPewmdseDPLF-ILYTSGSTGKPKGVV-------HTT-GGY-----LLYA--------------ATTFKY 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 244 V-------------AIG---SHGVVGYIPsakrLLADLrgfkpTYLL--GVP------RVFE-----KVynaaSQKAGAG 294
Cdd:cd05966 267 VfdyhpddiywctaDIGwitGHSYIVYGP----LANGA-----TTVMfeGTPtypdpgRYWDivekhKV----TIFYTAP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 295 LKGRLFAKAFDHFVQwskdemaggHHSLgariqhsfymqtvgSSIRSalgpnmkwLACGGAPLNADLAHFFNGFDG---I 371
Cdd:cd05966 334 TAIRALMKFGDEWVK---------KHDL--------------SSLRV--------LGSVGEPINPEAWMWYYEVIGkerC 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 372 TFIQGYGMTETAAPCLVNFQDANEV--GSVGRP--GcISIRLADDDELMIKG------------PNVFLGYYKQPQRTAE 435
Cdd:cd05966 383 PIVDTWWQTETGGIMITPLPGATPLkpGSATRPffG-IEPAILDEEGNEVEGevegylvikrpwPGMARTIYGDHERYED 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915853 436 ALTSD--GWLHTGDLATIDDRGFVFITGRKKDIIITAgGKNISPAPMEDVINTCPIVAHAVVIG 497
Cdd:cd05966 462 TYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVS-GHRLGTAEVESALVAHPAVAEAAVVG 524
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
47-512 |
1.82e-10 |
|
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: 63.49 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdspkqtgdivaevepviafa 126
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPL----------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 127 gDDSHAQileqirahsESLRYVFnfkangldavadfgesvsdEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNf 206
Cdd:cd12115 80 -DPAYPP---------ERLRFIL-------------------EDAQARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHRN- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 207 nhtvyngyevlndmlyqpsrlllflplAHCFaryIQYVAigshgvvgyipsakrlladlRGFKPTYLLGVP--------- 277
Cdd:cd12115 130 ---------------------------AAAF---LQWAA--------------------AAFSAEELAGVLastsicfdl 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 278 RVFEKVYNAAsqkagAGLKGRLFAKAFDHFvqwskdemagghhSLGARIQHSFyMQTVGSSIRS-----ALGPNMKWLAC 352
Cdd:cd12115 160 SVFELFGPLA-----TGGKVVLADNVLALP-------------DLPAAAEVTL-INTVPSAAAEllrhdALPASVRVVNL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 353 GGAPLNADLAHFFNGFDGITFIQG-YGMTET---AAPCLVNFQDANEVgSVGRP-GCISIRLADDD----------ELMI 417
Cdd:cd12115 221 AGEPLPRDLVQRLYARLQVERVVNlYGPSEDttySTVAPVPPGASGEV-SIGRPlANTQAYVLDRAlqpvplgvpgELYI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 418 KGPNVFLGYYKQPQRTAEALTSDGWL------HTGDLATIDDRGFVFITGRkKDIIITAGGKNISPAPMEDVINTCPIVA 491
Cdd:cd12115 300 GGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGR-ADNQVKVRGFRIELGEIEAALRSIPGVR 378
|
490 500
....*....|....*....|....*
gi 489915853 492 HAVV--IGDG--RPFIAALIELDAE 512
Cdd:cd12115 379 EAVVvaIGDAagERRLVAYIVAEPG 403
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
18-567 |
3.77e-10 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 62.85 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPD--DLIaqwqdDE--TRQWHdvsagQMNDRVREVAKGLLGLGVKPGSMVVIYAATcyEWGVVDFAC 93
Cdd:PRK13382 44 GPTSGFAIAAQRCPDrpGLI-----DElgTLTWR-----ELDERSDALAAALQALPIGEPRVVGIMCRN--HRGFVEALL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 94 AS--IGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQILEQIRAHSESLRYVfnfkanglDAVADFGESVSDEEL 171
Cdd:PRK13382 112 AAnrIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQATRIV--------AWTDEDHDLTVEVLI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 172 DKAIG-----RVRADDlfTIVYTSGSTGKPKGVmlshrnfNHTVYNGYEVLNDMLYQ-PSR----LLLFLPLAHC--FAR 239
Cdd:PRK13382 184 AAHAGqrpepTGRKGR--VILLTSGTTGTPKGA-------RRSGPGGIGTLKAILDRtPWRaeepTVIVAPMFHAwgFSQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 240 yIQYVAIGSHGVV---GYIPSAKRLLADlrGFKPTYLLGVPRVFEKVynaasqkagaglkgrlfakafdhfvqwskdema 316
Cdd:PRK13382 255 -LVLAASLACTIVtrrRFDPEATLDLID--RHRATGLAVVPVMFDRI--------------------------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 317 gghhslgariqhsfyMQTVGSSIRSALGPNMKWLACGGAPLNADLA-HFFNGFdGITFIQGYGMTE-----TAAPclVNF 390
Cdd:PRK13382 299 ---------------MDLPAEVRNRYSGRSLRFAAASGSRMRPDVViAFMDQF-GDVIYNNYNATEagmiaTATP--ADL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 391 QDANEvgSVGRP-GCISIRLADDD----------ELMIKGPNVFLGYykQPQRTAEalTSDGWLHTGDLATIDDRGFVFI 459
Cdd:PRK13382 361 RAAPD--TAGRPaEGTEIRILDQDfrevptgevgTIFVRNDTQFDGY--TSGSTKD--FHDGFMASGDVGYLDENGRLFV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 460 TGRKKDIIITaGGKNISPAPMEDVINTCPIVAHAVVIG-DGRPF---IAALIELDAEMTrswlasqnldidapmseiATN 535
Cdd:PRK13382 435 VGRDDEMIVS-GGENVYPIEVEKTLATHPDVAEAAVIGvDDEQYgqrLAAFVVLKPGAS------------------ATP 495
|
570 580 590
....*....|....*....|....*....|..
gi 489915853 536 DAVRALVQQyidkangNVSRAESVRKFVILDE 567
Cdd:PRK13382 496 ETLKQHVRD-------NLANYKVPRDIVVLDE 520
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
32-203 |
4.56e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 62.89 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 32 DDLIAQWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEwGVVDF-ACASIGAV-SV--PVYETD 107
Cdd:PRK03584 98 DDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPE-TVVAMlATASLGAIwSScsPDFGVQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 108 SpkqtgdiVAE----VEPVIAFAGDDSH--------AQILEQIRAHSESLR------YVFNFKANGLDAVA----DFGES 165
Cdd:PRK03584 177 G-------VLDrfgqIEPKVLIAVDGYRyggkafdrRAKVAELRAALPSLEhvvvvpYLGPAAAAAALPGAllweDFLAP 249
|
170 180 190
....*....|....*....|....*....|....*...
gi 489915853 166 VSDEELDKAigRVRADDLFTIVYTSGSTGKPKGVMLSH 203
Cdd:PRK03584 250 AEAAELEFE--PVPFDHPLWILYSSGTTGLPKCIVHGH 285
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
19-462 |
5.23e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.26 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 19 IYSLLAKRCERDPDDLIAQWQDDEtrqwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGA 98
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGDQQ------LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGG 3170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 99 VSVPVyETDSPKqtgdivaevEPVIAFAGDD------SHAQILEQIRAHSESLRYVfnfkangLDAVADFGESvsDEELD 172
Cdd:PRK12467 3171 AYVPL-DPEYPR---------ERLAYMIEDSgvklllTQAHLLEQLPAPAGDTALT-------LDRLDLNGYS--ENNPS 3231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 173 KaigRVRADDLFTIVYTSGSTGKPKGVMLSH---RNFNHTVYNGYEvlndmLYQPSRLLLFLPLAhcfaryiqyvaigsh 249
Cdd:PRK12467 3232 T---RVMGENLAYVIYTSGSTGKPKGVGVRHgalANHLCWIAEAYE-----LDANDRVLLFMSFS--------------- 3288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 250 gvvgYIPSAKRLLadlrgfkPTYLLGvprvfekvynaasqkagaglkGRLFAKAFDHfvqWSKDEMAGGHHSLGARIQH- 328
Cdd:PRK12467 3289 ----FDGAQERFL-------WTLICG---------------------GCLVVRDNDL---WDPEELWQAIHAHRISIACf 3333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 -SFYMQTVGSSIRSALGPNMKWLACGGAPLNAD-LAHFFNGFDGITFIQGYGMTETAA-----PCLVNFQDANEVGSVGR 401
Cdd:PRK12467 3334 pPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAaFEQVKRKLKPRGLTNGYGPTEAVVtvtlwKCGGDAVCEAPYAPIGR 3413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489915853 402 P-GCISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSD------GWLH-TGDLATIDDRGFVFITGR 462
Cdd:PRK12467 3414 PvAGRSIYVLDGQlnpvpvgvagELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGR 3492
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
29-203 |
5.39e-10 |
|
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: 62.67 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 29 RDPDDLIAQWQD-DETRQwhDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetd 107
Cdd:cd05943 80 ADADDPAAIYAAeDGERT--EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSC---- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 108 SPkQTG-----DIVAEVEPVIAFAGDD--------SHAQILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKA 174
Cdd:cd05943 154 SP-DFGvpgvlDRFGQIEPKVLFAVDAytyngkrhDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDF 232
|
170 180 190
....*....|....*....|....*....|....*....
gi 489915853 175 IG----------RVRADDLFTIVYTSGSTGKPKGVMLSH 203
Cdd:cd05943 233 LAtgaagelefePLPFDHPLYILYSSGTTGLPKCIVHGA 271
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
53-205 |
6.76e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 53 QMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSPKQTGDIVAevepviaFAGDDSHA 132
Cdd:PRK12316 541 ELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL----DPEYPAERLA-------YMLEDSGV 609
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915853 133 QILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKaigRVRADDLFTIVYTSGSTGKPKGVMLSHRN 205
Cdd:PRK12316 610 QLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGT---ELNPENLAYVIYTSGSTGKPKGAGNRHRA 679
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
46-501 |
7.25e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 62.06 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 46 WHdvsagQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAF 125
Cdd:cd05915 27 YA-----EVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AgdDShaqilEQIRAHSESLRYVFNFKAN-----GLDAVADFgESVSDEELdKAIGRVRADDLFTIVYTSGSTGKPKGVM 200
Cdd:cd05915 102 F--DP-----NLLPLVEAIRGELKTVQHFvvmdeKAPEGYLA-YEEALGEE-ADPVRVPERAACGMAYTTGTTGLPKGVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 201 LSHRN--FNHTVYNgyeVLNDMLYQPSRLLL-FLPLAHCFARYIQYVAIGSHGVV---GYIPSAKRLLADLRGFKPTYLL 274
Cdd:cd05915 173 YSHRAlvLHSLAAS---LVDGTALSEKDVVLpVVPMFHVNAWCLPYAATLVGAKQvlpGPRLDPASLVELFDGEGVTFTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 275 GVPRVFEKVYNAASQkagaglkgrlFAKAFdhfvQWSKDEMAGGHHS----LGARIQHSF-YMQTVGSSIRSALGPNMKW 349
Cdd:cd05915 250 GVPTVWLALADYLES----------TGHRL----KTLRRLVVGGSAAprslIARFERMGVeVRQGYGLTETSPVVVQNFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 350 LAcggaplnadlahffngfDGITFIQGYGMTETAAPCLVNFQDANEV-----GSVGRPGcISIRLadddeLMIKGPNVFL 424
Cdd:cd05915 316 KS-----------------HLESLSEEEKLTLKAKTGLPIPLVRLRVadeegRPVPKDG-KALGE-----VQLKGPWITG 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915853 425 GYYKQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHAVVIgdGRP 501
Cdd:cd05915 373 GYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDLENALMGHPKVKEAAVV--AIP 446
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
41-228 |
2.15e-09 |
|
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: 60.17 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 41 DETRQwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQTgdivaeve 120
Cdd:cd17650 8 DATRQ---LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPI-DPDYPAER-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 121 pvIAFAGDDSHAQILeqirahseslryvfnfkangldavadfgesvsdeeldkaigRVRADDLFTIVYTSGSTGKPKGVM 200
Cdd:cd17650 76 --LQYMLEDSGAKLL-----------------------------------------LTQPEDLAYVIYTSGTTGKPKGVM 112
|
170 180
....*....|....*....|....*...
gi 489915853 201 LSHRNFNHTVYnGYEVLNDMLYQPSRLL 228
Cdd:cd17650 113 VEHRNVAHAAH-AWRREYELDSFPVRLL 139
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
181-507 |
4.11e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 59.37 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFARYIQYVAIGSHG---VVGYIPS 257
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLN--LKNGDRTYTCMPLYHGTAAFLGACNCLMSGgtlALSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 258 AKRLLADLRGFKPT----------YLLGVP-RVFEKVYNAasQKA-GAGLKGRLFAKAFDHFvqwskdemagghhslGAR 325
Cdd:cd05937 165 ASQFWKDVRDSGATiiqyvgelcrYLLSTPpSPYDRDHKV--RVAwGNGLRPDIWERFRERF---------------NVP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 326 IQHSFYMQT--VGSSIRSALGPnmkWLAcGGAPLNADLAHFFngFDGITFIQGYGmTETAAPCLVNFQDANEVGSVGRPG 403
Cdd:cd05937 228 EIGEFYAATegVFALTNHNVGD---FGA-GAIGHHGLIRRWK--FENQVVLVKMD-PETDDPIRDPKTGFCVRAPVGEPG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 404 CISIRLADDDElmikgpNVFLGYYKQPQRTAEALTS------DGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISP 477
Cdd:cd05937 301 EMLGRVPFKNR------EAFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGD-TFRWKSENVST 373
|
330 340 350
....*....|....*....|....*....|....*.
gi 489915853 478 APMEDVINTCPIVAHAVVIG------DGRPFIAALI 507
Cdd:cd05937 374 TEVADVLGAHPDIAEANVYGvkvpghDGRAGCAAIT 409
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
354-496 |
5.85e-09 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 58.73 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 354 GAPLNADLAHFFNGFDGITFIQGYGMTETAapCLVNFQDANEV--GSVGRP-GCISIRLADDDELMIKGPNVFL------ 424
Cdd:cd05974 209 GEPLNPEVIEQVRRAWGLTIRDGYGQTETT--ALVGNSPGQPVkaGSMGRPlPGYRVALLDPDGAPATEGEVALdlgdtr 286
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489915853 425 ------GYYKQPQRTAEALtSDGWLHTGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVI 496
Cdd:cd05974 287 pvglmkGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEAAVV 362
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
52-496 |
6.24e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 58.75 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQ-TGDIVAEVEPVIAFAGDDS 130
Cdd:PRK04813 31 GQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV-DVSSPAErIEMIIEVAKPSLIIATEEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 131 hAQILEQIRAHSeslryvfnfkangLDAVADFGESVSDEELDKAigrVRADDLFTIVYTSGSTGKPKGVMLSHRNFNhtv 210
Cdd:PRK04813 110 -PLEILGIPVIT-------------LDELKDIFATGNPYDFDHA---VKGDDNYYIIFTSGTTGKPKGVQISHDNLV--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 211 yngyEVLNDMLYQpsrlllflplahcFAryiqyvaigshgvvgyIPSAKRLLA------DLRGFK--PTYLLG-----VP 277
Cdd:PRK04813 170 ----SFTNWMLED-------------FA----------------LPEGPQFLNqapysfDLSVMDlyPTLASGgtlvaLP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 278 RvfEKVYNaasqkagaglkgrlFAKAFDHFVQ-----W----SKDEMAgghhslgariqhsfymqtvgssirsALGPNMK 348
Cdd:PRK04813 217 K--DMTAN--------------FKQLFETLPQlpinvWvstpSFADMC-------------------------LLDPSFN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 349 wlacggAPLNADLAHFFngFDG-----------------ITFIQGYGMTE-TAA-------PCLVNFQDANEVGSVgRPG 403
Cdd:PRK04813 256 ------EEHLPNLTHFL--FCGeelphktakkllerfpsATIYNTYGPTEaTVAvtsieitDEMLDQYKRLPIGYA-KPD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 404 C-ISI------RLAD--DDELMIKGPNVFLGYYKQPQRTAEAL-TSDGW--LHTGDLATIDDrGFVFITGRkKDIIITAG 471
Cdd:PRK04813 327 SpLLIideegtKLPDgeQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLED-GLLFYQGR-IDFQIKLN 404
|
490 500
....*....|....*....|....*...
gi 489915853 472 GKNISpapMEDV---INTCPIVAHAVVI 496
Cdd:PRK04813 405 GYRIE---LEEIeqnLRQSSYVESAVVV 429
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
47-481 |
8.23e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 58.59 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 47 HDVSAGQMNDRVREVAKGLLGLGvKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGD---IVAEVEPVI 123
Cdd:PRK07769 54 RDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRlhaVLDDCTPSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 124 AFAGDDSHAQILEQIRAHSESLRYvfnfKANGLDAVAD-FGESVSDEELDKaigrvraDDLFTIVYTSGSTGKPKGVMLS 202
Cdd:PRK07769 133 ILTTTDSAEGVRKFFRARPAKERP----RVIAVDAVPDeVGATWVPPEANE-------DTIAYLQYTSGSTRIPAGVQIT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 203 HRNFNHTVYNGYEVLNdmLYQPSRLLLFLPLAHCFAR-YIQYVAIGSHGVVGYIPSAkrlladlrgFkptyllgVPRVFE 281
Cdd:PRK07769 202 HLNLPTNVLQVIDALE--GQEGDRGVSWLPFFHDMGLiTVLLPALLGHYITFMSPAA---------F-------VRRPGR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 282 KVYNAASQKAGAglkGRLFAK----AFDHFVQ--WSKDemagGHHSLGARiqhsfymqtvgssirsalgpNMKWLACGGA 355
Cdd:PRK07769 264 WIRELARKPGGT---GGTFSAapnfAFEHAAArgLPKD----GEPPLDLS--------------------NVKGLLNGSE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 356 PLNADLAHFFN------GFDGITFIQGYGMTET----------AAPCLV-------NFQDANEV-------------GSV 399
Cdd:PRK07769 317 PVSPASMRKFNeafapyGLPPTAIKPSYGMAEAtlfvsttpmdEEPTVIyvdrdelNAGRFVEVpadapnavaqvsaGKV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 400 GRP--GCI-----SIRLADDD--ELMIKGPNVFLGYYKQPQRTAEA----LTS-------------DGWLHTGDLATIDD 453
Cdd:PRK07769 397 GVSewAVIvdpetASELPDGQigEIWLHGNNIGTGYWGKPEETAATfqniLKSrlseshaegapddALWVRTGDYGVYFD 476
|
490 500
....*....|....*....|....*...
gi 489915853 454 rGFVFITGRKKDIIITaGGKNISPAPME 481
Cdd:PRK07769 477 -GELYITGRVKDLVII-DGRNHYPQDLE 502
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
49-521 |
9.64e-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: 58.03 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 49 VSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPkqtgdivaevEPVIAFAGD 128
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPL-DPAYP----------AERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQILeqiRAHSESLRYVfnfkangldavadfgesvsdeeldkaigrvraddlftiVYTSGSTGKPKGVMLSHRNFNH 208
Cdd:cd17652 82 DARPALL---LTTPDNLAYV--------------------------------------IYTSGSTGRPKGVVVTHRGLAN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 209 TVYNGYEVLNdmlYQP-SRLLlflplahcfaryiQYVAIGSHGVVGYIPSAkrLLADLRgfkptyLLGVPRvfekvynaA 287
Cdd:cd17652 121 LAAAQIAAFD---VGPgSRVL-------------QFASPSFDASVWELLMA--LLAGAT------LVLAPA--------E 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 288 SQKAGAGLKGRLFAKafdhfvqwskdemagghhslgaRIQHSFYMQTVGSSIRSALGPNMKWLACGGAPLNADLAHFFNg 367
Cdd:cd17652 169 ELLPGEPLADLLREH----------------------RITHVTLPPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA- 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 368 fDGITFIQGYGMTE-----TAAPCLVnfqDANEVgSVGRPgcIS---IRLADDD----------ELMIKGPNVFLGYYKQ 429
Cdd:cd17652 226 -PGRRMINAYGPTEttvcaTMAGPLP---GGGVP-PIGRP--VPgtrVYVLDARlrpvppgvpgELYIAGAGLARGYLNR 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 430 PQRTAEALTSD------GWLH-TGDLATIDDRGFVFITGRKKDIIITAGGKnISPAPMEDVINTCPIVAHAVVI-GDGRP 501
Cdd:cd17652 299 PGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFR-IELGEVEAALTEHPGVAEAVVVvRDDRP 377
|
490 500
....*....|....*....|....*....
gi 489915853 502 FIAALI---------ELDAEMTRSWLASQ 521
Cdd:cd17652 378 GDKRLVayvvpapgaAPTAAELRAHLAER 406
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
18-204 |
1.07e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 58.52 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDdliAQWQDDETRQwhdVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIG 97
Cdd:PRK10252 459 TLSALVAQQAAKTPD---APALADARYQ---FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAG 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 98 AVSVPVyETDSPKQTGD-IVAEVEPVIAFAGDD-----SHAQILEqirahseSLRYvfnfkaNGLDAVADfgesvsdeel 171
Cdd:PRK10252 533 AAWLPL-DTGYPDDRLKmMLEDARPSLLITTADqlprfADVPDLT-------SLCY------NAPLAPQG---------- 588
|
170 180 190
....*....|....*....|....*....|...
gi 489915853 172 DKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHR 204
Cdd:PRK10252 589 AAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQT 621
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
18-486 |
4.15e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 56.49 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 18 TIYSLLAKRCERDPDDLIAQWQDDETRqWHDVSA----GQMNDRVREVAKGLLGLGVkPGSMVVIYAATCYEWgVVDFAC 93
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIDYEQD-PAGVAEtltwSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEY-IVAFLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 94 A-SIGAVSVPVyetdSPKQTGdivAEVEPVIAFAGDDSHAQILEQIRAHSESLRYVfnfKANGLDAVADFGEsVSDEELD 172
Cdd:PRK05850 79 AlQAGLIAVPL----SVPQGG---AHDERVSAVLRDTSPSVVLTTSAVVDDVTEYV---APQPGQSAPPVIE-VDLLDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 173 KAIG-RVRADDLFTIVY---TSGSTGKPKGVMLSHRN----FNHTVYNGYEVLNDMLYQPSRLLLFLPLAH--------C 236
Cdd:PRK05850 148 SPRGsDARPRDLPSTAYlqyTSGSTRTPAGVMVSHRNvianFEQLMSDYFGDTGGVPPPDTTVVSWLPFYHdmglvlgvC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 237 F--------------------ARYIQYVAIGSH----------------------------GVVGYIPSAKRL-LADLRG 267
Cdd:PRK05850 228 ApilggcpavltspvaflqrpARWMQLLASNPHafsaapnfafelavrktsdddmagldlgGVLGIISGSERVhPATLKR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 268 F--------------KPTYLLGVPRVFekvynAASQKAGAGLKgrlfAKAFDHfvqwskDEMAGGHhslgARiqhsfymq 333
Cdd:PRK05850 308 FadrfapfnlretaiRPSYGLAEATVY-----VATREPGQPPE----SVRFDY------EKLSAGH----AK-------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 334 tvgssiRSALGpnmkwlacGGAPLnadlahffngfdgitfiQGYGMTETAAPCLVNFQDANEV--GSVGrpgcisirlad 411
Cdd:PRK05850 361 ------RCETG--------GGTPL-----------------VSYGSPRSPTVRIVDPDTCIECpaGTVG----------- 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 412 ddELMIKGPNVFLGYYKQPQRTAE----------ALTSDG-WLHTGDLATIDDrGFVFITGRKKDIIITAgGKNISPapm 480
Cdd:PRK05850 399 --EIWVHGDNVAAGYWQKPEETERtfgatlvdpsPGTPEGpWLRTGDLGFISE-GELFIVGRIKDLLIVD-GRNHYP--- 471
|
....*.
gi 489915853 481 EDVINT 486
Cdd:PRK05850 472 DDIEAT 477
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
20-225 |
6.54e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 55.67 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 20 YSLLAKRCERDPDDLIA-QWQDDETRQWHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGA 98
Cdd:PLN02654 91 YNCLDRNVEAGNGDKIAiYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 99 VSVPVYETDSPKQTGDIVAEVEPVIA-------------FAGDDSHAQILE----------------QIRAHSESLRYVF 149
Cdd:PLN02654 171 VHSVVFAGFSAESLAQRIVDCKPKVVitcnavkrgpktiNLKDIVDAALDEsakngvsvgicltyenQLAMKREDTKWQE 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 150 NFKANGLDAVADFGESVSDEELDkaigrvrADDLFTIVYTSGSTGKPKGVMlsHRNFNHTVYNGYEVLNDMLYQPS 225
Cdd:PLN02654 251 GRDVWWQDVVPNYPTKCEVEWVD-------AEDPLFLLYTSGSTGKPKGVL--HTTGGYMVYTATTFKYAFDYKPT 317
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
52-216 |
6.76e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 55.92 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAV-SVpVYETDSPKqtgdivaevepviAFAG--D 128
Cdd:PRK00174 102 RELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhSV-VFGGFSAE-------------ALADriI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 129 DSHAQIL----EQIR---------------AHSESLRYVFNFKANGLDaVA----------DFGESVSD----EELDkai 175
Cdd:PRK00174 168 DAGAKLVitadEGVRggkpiplkanvdealANCPSVEKVIVVRRTGGD-VDwvegrdlwwhELVAGASDecepEPMD--- 243
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489915853 176 grvrADD-LFtIVYTSGSTGKPKGVMlshrnfnHTVyNGYEV 216
Cdd:PRK00174 244 ----AEDpLF-ILYTSGSTGKPKGVL-------HTT-GGYLV 272
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-205 |
8.79e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 55.94 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 50 SAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyETDSPKQTgdivaevepvIAFAGDD 129
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPL-DPEYPRER----------LAYMIED 1669
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489915853 130 SHAQILEQIRAHSESLRYVFNFKANGLDAVADFGESVSDEELDKAIGrvrADDLFTIVYTSGSTGKPKGVMLSHRN 205
Cdd:PRK12467 1670 SGIELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLA---PQNLAYVIYTSGSTGRPKGAGNRHGA 1742
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
20-518 |
1.03e-07 |
|
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: 54.87 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 20 YSLLAKRCERDPDDLIAQWQDdetrqwHDVSAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAV 99
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRG------QSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 100 SVPVyETDSPKQTgdivaevepvIAFAGDDSHAQILeqirahseslryvfnfkangldavadfgesVSDeeldkaigrvr 179
Cdd:cd17645 75 YVPI-DPDYPGER----------IAYMLADSSAKIL------------------------------LTN----------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 180 ADDLFTIVYTSGSTGKPKGVMLSHRN-----------FNHTVYNGYEVLNDMLYQPSRLLLFlplahcfaryiQYVAIGS 248
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNlvnlcewhrpyFGVTPADKSLVYASFSFDASAWEIF-----------PHLTAGA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 249 hgVVGYIPSAKRLlaDLRGFKptyllgvpRVFEkvynaasqkagaglkgrlfakafDHFVQWSkdemagghhSLGARIQH 328
Cdd:cd17645 172 --ALHVVPSERRL--DLDALN--------DYFN-----------------------QEGITIS---------FLPTGAAE 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 329 SFyMQTVGSSIRSALgpnmkwlaCGGAPLNADLAhffngfDGITFIQGYGMTE-----TAAPclVNFQDANEvgSVGRP- 402
Cdd:cd17645 208 QF-MQLDNQSLRVLL--------TGGDKLKKIER------KGYKLVNNYGPTEntvvaTSFE--IDKPYANI--PIGKPi 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 GCISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWL------HTGDLATIDDRGFVFITGRkKDI 466
Cdd:cd17645 269 DNTRVYILDEAlqlqpigvagELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGR-LDQ 347
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 467 IITAGGKNISPAPMEDVINTCPIVAHAVVI----GDGRPFIAALI----ELDAEMTRSWL 518
Cdd:cd17645 348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLakedADGRKYLVAYVtapeEIPHEELREWL 407
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
50-235 |
1.74e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.50 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 50 SAGQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVyetdSPKQTGDIVA----EVEPVIAF 125
Cdd:PRK08279 64 SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALL----NTQQRGAVLAhslnLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 126 AGDD-SHAqiLEQIRAH------SESLRYVFNFKANGLDAVADFGESVSDEELDKAiGRVRADDLFTIVYTSGSTGKPKG 198
Cdd:PRK08279 140 VGEElVEA--FEEARADlarpprLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASR-SGVTAKDTAFYIYTSGTTGLPKA 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 489915853 199 VMLSHRNFnHTVYNGYEVLNDMlyQPS-RLLLFLPLAH 235
Cdd:PRK08279 217 AVMSHMRW-LKAMGGFGGLLRL--TPDdVLYCCLPLYH 251
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
41-507 |
2.14e-07 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 53.90 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 41 DETRQWHDVSAgqMNDRVrevAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSvpvyetdspkqtgdivaeve 120
Cdd:cd05940 1 DEALTYAELDA--MANRY---ARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVA-------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 121 pviafagddshAQILEQIRAhsESLRYVFNfkangldavadfgesVSDEELdkaigrVRADDLFTIvYTSGSTGKPKGVM 200
Cdd:cd05940 56 -----------ALINYNLRG--ESLAHCLN---------------VSSAKH------LVVDAALYI-YTSGTTGLPKAAI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 201 LSHrnfnHTVYNGYEVLNDM--LYQPSRLLLFLPLAHCFARYIQYVAIGSHG---VVGYIPSAKRLLADLRGFKPT---- 271
Cdd:cd05940 101 ISH----RRAWRGGAFFAGSggALPSDVLYTCLPLYHSTALIVGWSACLASGatlVIRKKFSASNFWDDIRKYQATifqy 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 272 ------YLLGVPRVFEKVYNAASQKAGAGLKGRLFAKAFDHFVQwskdemagghhslgARIQHsFYMQTVG--SSIRSAL 343
Cdd:cd05940 177 igelcrYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGV--------------PRIAE-FYAATEGnsGFINFFG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 344 GPNmkwlACGGAPlnADLAHFFNgfdgITFIQgYGMtETAAPclvnFQDAN----EVGsVGRPG-CISirladddelMIK 418
Cdd:cd05940 242 KPG----AIGRNP--SLLRKVAP----LALVK-YDL-ESGEP----IRDAEgrciKVP-RGEPGlLIS---------RIN 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 419 GPNVFLGYYKQPQRTAEALTS-----DGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTCPIVAHA 493
Cdd:cd05940 296 PLEPFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGD-TFRWKGENVSTTEVAAVLGAFPGVEEA 374
|
490 500
....*....|....*....|
gi 489915853 494 VVIG------DGRPFIAALI 507
Cdd:cd05940 375 NVYGvqvpgtDGRAGMAAIV 394
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
52-280 |
3.71e-07 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 53.71 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 52 GQMNDRVREVAKGLLGLGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTgdIVAEVEPVIAFAGDDSH 131
Cdd:PTZ00297 461 GTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPLVGKGSTMRT--LIDEHKIKVVFADRNSV 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 132 AQILEQIRAHSESLRYVFNFKANGLDAVA-DFGESVSDEELDKAIGRVR---------ADDLFTIVY---TSGSTGKPKG 198
Cdd:PTZ00297 539 AAILTCRSRKLETVVYTHSFYDEDDHAVArDLNITLIPYEFVEQKGRLCpvplkehvtTDTVFTYVVdntTSASGDGLAV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 199 VMLSHrnfnhtvyngyevlNDMLYQPSRLLL---------------FLPLAHCFARyIQYVAIGSHG-VVGYIPSAKRLL 262
Cdd:PTZ00297 619 VRVTH--------------ADVLRDISTLVMtgvlpssfkkhlmvhFTPFAMLFNR-VFVLGLFAHGsAVATVDAAHLQR 683
|
250
....*....|....*...
gi 489915853 263 ADLRgFKPTYLLGVPRVF 280
Cdd:PTZ00297 684 AFVK-FQPTILVAAPSLF 700
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
181-496 |
8.15e-07 |
|
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: 52.05 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHR---NFNHTVYNGYEVLNDMlyqpsRLLLFLPLahCF---ARYIQYVAIGSHGVV-- 252
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQslvNLSHGLIKEYGITSSD-----RVLQFASI--AFdvaAEEIYVTLLSGATLVlr 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 253 --GYIPSAKRLLADLRGFKPTYLLGVPRVFEKVYNAASQkagaglkgrlfakafdhfvqwskdEMAGGHHSL------GA 324
Cdd:cd17644 179 peEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLL------------------------STIDLPSSLrlvivgGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 325 RIQHSFYMQtvgssIRSALGPNmkwlacggaplnadlahffngfdgITFIQGYGMTE---TAAPCLVNFQDANEVGSV-- 399
Cdd:cd17644 235 AVQPELVRQ-----WQKNVGNF------------------------IQLINVYGPTEatiAATVCRLTQLTERNITSVpi 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 400 GRP-GCISIRLADDD----------ELMIKGPNVFLGYYKQPQRTAEALTSDGWLH--------TGDLATIDDRGFVFIT 460
Cdd:cd17644 286 GRPiANTQVYILDENlqpvpvgvpgELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYL 365
|
330 340 350
....*....|....*....|....*....|....*.
gi 489915853 461 GRkKDIIITAGGKNISPAPMEDVINTCPIVAHAVVI 496
Cdd:cd17644 366 GR-IDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVI 400
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
182-496 |
5.29e-06 |
|
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: 49.32 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 182 DLFTIVYTSGSTGKPKGVMLSHRNFNHTVyNGYEVLNDMLYQPSRLLLFLPlAHCFARYIQYVA---IGSHGVVGYIPSA 258
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSVVNLR-TSLSERYFGRDNGDEAVLFFS-NYVFDFFVEQMTlalLNGQKLVVPPDEM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 259 K----RLLADLRGFKPTYLLGVPRVFEkvynaasqkagaglkgrlfakafdhfvqwskdemaggHHSLGARiqhsfymqt 334
Cdd:cd17648 173 RfdpdRFYAYINREKVTYLSGTPSVLQ-------------------------------------QYDLARL--------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 335 vgssirsalgPNMKWLACGGAPLNAdlAHF---FNGFDGItFIQGYGMTETAAPCLVNFQDANEV--GSVGRP-GCISIR 408
Cdd:cd17648 207 ----------PHLKRVDAAGEEFTA--PVFeklRSRFAGL-IINAYGPTETTVTNHKRFFPGDQRfdKSLGRPvRNTKCY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 409 LADDD----------ELMIKGPNVFLGYYKQPQRTAE-------------ALTSDGWLH-TGDLATIDDRGFVFITGRkK 464
Cdd:cd17648 274 VLNDAmkrvpvgavgELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGR-N 352
|
330 340 350
....*....|....*....|....*....|..
gi 489915853 465 DIIITAGGKNISPAPMEDVINTCPIVAHAVVI 496
Cdd:cd17648 353 DFQVKIRGQRIEPGEVEAALASYPGVRECAVV 384
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
353-499 |
1.08e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 353 GGAPLNAD--------LAHFfnGFDGITFIQGYGMTEtaAPCLVN---------FQDANEVGSVGR----------PGcI 405
Cdd:PRK05851 280 GGEPVDCDgferfataMAPF--GFDAGAAAPSYGLAE--STCAVTvpvpgiglrVDEVTTDDGSGArrhavlgnpiPG-M 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 406 SIRLADDD-----------ELMIKGPNVFLGYYKQPqrtaeALTSDGWLHTGDLATIDDRGFVfITGRKKDIIITAgGKN 474
Cdd:PRK05851 355 EVRISPGDgaagvagreigEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVA-GRN 427
|
170 180
....*....|....*....|....*
gi 489915853 475 ISPAPMEDVINTCPIVAHAVVIGDG 499
Cdd:PRK05851 428 IFPTEIERVAAQVRGVREGAVVAVG 452
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
181-484 |
8.93e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.58 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 181 DDLFTIVYTSGSTGKPKGVMLSHRNFnhtVYNGYEVLNdmLYQPSR---LLLFLPLAH-----CFARYIqyVAIGSHGVV 252
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANL---LANQRACLK--FFSPKEddvMMSFLPPFHaygfnSCTLFP--LLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 253 GYIP-SAKRLLADLRGFKPTYLLGVPRVFEKVYNAAsQKAGAGLKGRLFAkafdhfvqwskdeMAGGHhslgaRIQHSFY 331
Cdd:PRK06334 256 AYNPlYPKKIVEMIDEAKVTFLGSTPVFFDYILKTA-KKQESCLPSLRFV-------------VIGGD-----AFKDSLY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 332 MQTVGSsirsalgpnmkwlacggaplnadlahffngFDGITFIQGYGMTETAAPCLVNFQDANEVGSvgrpgCISIRLAD 411
Cdd:PRK06334 317 QEALKT------------------------------FPHIQLRQGYGTTECSPVITINTVNSPKHES-----CVGMPIRG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 412 DDEL------------------MIKGPNVFLGYY-KQPQRTAEALTSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGG 472
Cdd:PRK06334 362 MDVLivseetkvpvssgetglvLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGA 440
|
330
....*....|..
gi 489915853 473 KNISPAPMEDVI 484
Cdd:PRK06334 441 EMVSLEALESIL 452
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
364-507 |
2.67e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.20 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 364 FFNGFDGITFIQGYGMTEtAAPCLVNFqdANEVGSVGRPGCIS--------IR--------LADDDELMIKGP------- 420
Cdd:cd05938 276 FLRRFGPIRIREFYGSTE-GNIGFFNY--TGKIGAVGRVSYLYkllfpfelIKfdvekeepVRDAQGFCIPVAkgepgll 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 421 -------NVFLGYYKQPQRTAEAL------TSDGWLHTGDLATIDDRGFVFITGRKKDiIITAGGKNISPAPMEDVINTC 487
Cdd:cd05938 353 vakitqqSPFLGYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQDQQNFLYFHDRVGD-TFRWKGENVATTEVADVLGLL 431
|
170 180
....*....|....*....|....*.
gi 489915853 488 PIVAHAVVIG------DGRPFIAALI 507
Cdd:cd05938 432 DFLQEVNVYGvtvpghEGRIGMAAVK 457
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
57-208 |
3.27e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 43.88 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 57 RVREVAKGLLG-LGVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTGDIVAEVEPVIAFAGDDSHAQIL 135
Cdd:cd05905 23 RAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVEACLKGLP 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915853 136 EQIRAHSESlryVFNFKANG----LDAVADFGESVSDEELDKAIGRVRADDLFTIVYTSGSTGKPKGVMLSHRNFNH 208
Cdd:cd05905 103 KKLLKSKTA---AEIAKKKGwpkiLDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLA 176
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
41-205 |
9.34e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 42.42 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 41 DETRQWHDVSAGQMNDRVREVAKGLLGLgVKPGSMVVIYAATCYEWGVVDFACASIGAVSVPVYETDSPKQTG--DIV-A 117
Cdd:PRK12476 61 SAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAErlDTAlR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 118 EVEPVIAFAGDDSHAQILEQIRAHSESLRYvfnfKANGLDAVAD-FGESVSDEELDkaigrvrADDLFTIVYTSGSTGKP 196
Cdd:PRK12476 140 DAEPTVVLTTTAAAEAVEGFLRNLPRLRRP----RVIAIDAIPDsAGESFVPVELD-------TDDVSHLQYTSGSTRPP 208
|
....*....
gi 489915853 197 KGVMLSHRN 205
Cdd:PRK12476 209 VGVEITHRA 217
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
180-204 |
1.97e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 1.97e-03
10 20
....*....|....*....|....*
gi 489915853 180 ADDLFTIVYTSGSTGKPKGVMLSHR 204
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQR 3892
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
403-557 |
2.54e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 40.79 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 403 GCISI--RLADDDELMIKGPNVFLGYYKQPQRTAEAL--TSDGWLHTGDLATIDDRGFVFITGRKKDIIITAgGKNISPA 478
Cdd:PRK08308 249 GCVSIcpDMKSHLDLGNPLPHVSVSAGSDENAPEEIVvkMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVS-GLNVYPI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915853 479 PMEDVINTCPIVAHAVVIGDGRPF----IAALI----ELDAEMTRSWLASQNLDIDAPMseiatnDAVRalVQQYIDKAN 550
Cdd:PRK08308 328 EVEDVMLRLPGVQEAVVYRGKDPVagerVKAKVisheEIDPVQLREWCIQHLAPYQVPH------EIES--VTEIPKNAN 399
|
....*..
gi 489915853 551 GNVSRAE 557
Cdd:PRK08308 400 GKVSRKL 406
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
186-203 |
3.98e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 3.98e-03
|
| |
