|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
13-614 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 573.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 13 ATTTIPALLIERVKNDADANAFFQRRAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICS 92
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 93 GAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQL-RVMKAADTSSRLLKIVVLDPDWKRSPDetgmNVVSLAEF---- 167
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLdKLLEVRDELPSLRHIVVLDPRGLRDDP----RLLSLDELlalg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 168 ASHFDGDEVAYLREQselARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPaiLSEPQRMVIHLPLSHTVAR 247
Cdd:COG1022 165 REVADPAELEARRAA---VKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP--LGPGDRTLSFLPLAHVFER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 248 IqATTLPLIAKTVPYFVDVSADFAKCIQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALGIAREVLADRQD 327
Cdd:COG1022 240 T-VSYYALAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 328 AGTGDPFKEQLYAICRERVFKPLLARIGfDDLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSRP 407
Cdd:COG1022 319 GKSPSLLLRLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 408 GNSGVPLddPAWETRVLPDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGK 486
Cdd:COG1022 398 GTVGPPL--PGVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 487 SISPVQIENELRQSPYITEALVIGEGRKYLTALIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLIREEVEKANARLA 566
Cdd:COG1022 476 NVAPQPIENALKASPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYTSYAELAQDPEVRALIQEEVDRANAGLS 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 981242995 567 RAEQIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLYDDA 614
Cdd:COG1022 556 RAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
40-599 |
3.27e-127 |
|
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: 382.71 E-value: 3.27e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 40 GAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATL 119
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 120 AFAGsaeqlrvmkaadtssrllkivvlDPDwkrspdetgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSG 199
Cdd:cd05907 81 LFVE-----------------------DPD----------------------------------------DLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 200 TTGAPKGAMLTHVSMLAGAFTWPTFCPAilSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFVDVSADFAKCIQEVRP 279
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLPA--TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 280 TSYMAPPRFYQKFATQIinHVNGSSEAERRNYTLALGiarevladrqdagtgdpfkeqlyaicrervfkpllarigfDDL 359
Cdd:cd05907 176 TVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAVG----------------------------------------GRL 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 360 RYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLDDPawETRVLPDGEMIVRGPGLFIG 439
Cdd:cd05907 214 RFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGV--EVRIADDGEILVRGPNVMLG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 440 YWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIENELRQSPYITEALVIGEGRKYLTA 518
Cdd:cd05907 292 YYKNPEATAEALdADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 519 LIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLIREEVEKANARLARAEQIKAFRIFPEELTPENGVMTATRKKRRKA 598
Cdd:cd05907 372 LIVPDPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPV 451
|
.
gi 981242995 599 L 599
Cdd:cd05907 452 I 452
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
36-603 |
3.71e-122 |
|
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: 373.68 E-value: 3.71e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 36 QRRAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDS 115
Cdd:cd17641 3 EKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 116 GATLAFAGSAEQL-RVMKAADTSSRLLKIVVLDPDWKRSPDETGMNVVS--LAEFASHFDGDEVAYLREQSElARPTDLV 192
Cdd:cd17641 83 GARVVIAEDEEQVdKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEdvVALGRALDRRDPGLYEREVAA-GKGEDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 193 SLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPaiLSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFVDVSADFAK 272
Cdd:cd17641 162 VLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADP--LGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPETMME 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 273 CIQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALGIAREVLADRQDAGTGDPFKEQLYAICRERVFKPLLA 352
Cdd:cd17641 240 DLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 353 RIGFDDLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLDDPawETRVLPDGEMIVR 432
Cdd:cd17641 320 RLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGT--EVRIDEVGEILVR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 433 GPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIENELRQSPYITEALVIGE 511
Cdd:cd17641 398 SPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 512 GRKYLTALIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLIREEVEKANARLARAEQIKAFRIFPEELTPENGVMTAT 591
Cdd:cd17641 478 GRPYLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELTRT 557
|
570
....*....|..
gi 981242995 592 RKKRRKALMARY 603
Cdd:cd17641 558 RKVRRGVIAEKY 569
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
40-611 |
1.48e-75 |
|
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: 251.37 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 40 GAWVPTTWKGYANAVCSVSAALGAAGV--ARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGa 117
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 118 tlafagsaeqlrvmkaadtssrlLKIVVLDPDWKrspdetgmnVVSLAEFASHFDGDEVAYlreqsELARPTDLVSLGYT 197
Cdd:cd05927 80 -----------------------ISIVFCDAGVK---------VYSLEEFEKLGKKNKVPP-----PPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 198 SGTTGAPKGAMLTH---VSMLAGAFTWPTFCPAILSEpQRMVIHLPLSHTVAR-IQATTLPLIAKtVPYFvdvSADFAKC 273
Cdd:cd05927 123 SGTTGNPKGVMLTHgniVSNVAGVFKILEILNKINPT-DVYISYLPLAHIFERvVEALFLYHGAK-IGFY---SGDIRLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 274 ---IQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALgiAREVLADRQDAGTGDPFKEQLyaicrerVFKPL 350
Cdd:cd05927 198 lddIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFAL--NYKLAELRSGVVRASPFWDKL-------VFNKI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 351 LARIGfDDLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVL----- 424
Cdd:cd05927 269 KQALG-GNVRLMLTGSAPLSPEVLEFLRvALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPL--PCAEVKLVdvpem 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 425 --------PDGEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIEN 495
Cdd:cd05927 346 nydakdpnPRGEVCIRGPNVFSGYYKDPEKTAEALDeDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIEN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 496 ELRQSPYITEALVIGEGRK-YLTALIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLIREEVEKA--NARLARAEQIK 572
Cdd:cd05927 426 IYARSPFVAQIFVYGDSLKsFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLVRLgkENGLKGFEQVK 505
|
570 580 590
....*....|....*....|....*....|....*....
gi 981242995 573 AFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLY 611
Cdd:cd05927 506 AIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
37-611 |
1.47e-74 |
|
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: 249.97 E-value: 1.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 37 RRAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSG 116
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 117 ATLAFAGSAEQLRVMKAADTSSRLLKIVVldpDWKRSPDETGMNVVSLAEFASHFDGDEVAYLREQSELARPTDLVSLGY 196
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAII---QYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGAMLTHVSMlagafTWPT---------FCPAILSEpqRMVIHLPLSHTVARIQATTLPLIAKTVPYFVDVS 267
Cdd:cd05933 158 TSGTTGMPKGVMLSHDNI-----TWTAkaasqhmdlRPATVGQE--SVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 268 A---DFAKCIQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALGIAREVLADRQDAGTGDPFKeqlYAICRE 344
Cdd:cd05933 231 AlkgTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLF---YRLAKK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 345 RVFKPLLARIGFDDLRYPYTASAPVPPEVVTLFqlWGVNLK--ENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETR 422
Cdd:cd05933 308 LVFKKVRKALGLDRCQKFFTGAAPISRETLEFF--LSLNIPimELYGMSETSGPHTISNPQAYRLLSCGKAL--PGCKTK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 423 VL-PD----GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIENE 496
Cdd:cd05933 384 IHnPDadgiGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 497 LRQS-PYITEALVIGEGRKYLTALI----EVDGTL----------AMDWARTHDPSVTQYADLASS--PPVIDLIREEVE 559
Cdd:cd05933 464 VKKElPIISNAMLIGDKRKFLSMLLtlkcEVNPETgepldelteeAIEFCRKLGSQATRVSEIAGGkdPKVYEAIEEGIK 543
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 981242995 560 KANAR-LARAEQIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLY 611
Cdd:cd05933 544 RVNKKaISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
40-603 |
3.33e-66 |
|
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: 225.43 E-value: 3.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 40 GAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATL 119
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 120 AFAGSAEQLRVMKAAdTSSRLLKIVVLDPDWKRSPDEtgmnvvslaefashFDGDEVAYLREQSELAR-PTDLVSLGYTS 198
Cdd:cd05932 82 LFVGKLDDWKAMAPG-VPEGLISISLPPPSAANCQYQ--------------WDDLIAQHPPLEERPTRfPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 199 GTTGAPKGAMLTHvsmlaGAFTWPtfCPAI-----LSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFVDVSADFAKC 273
Cdd:cd05932 147 GTTGQPKGVMLTF-----GSFAWA--AQAGiehigTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 274 IQEVRPTSYMAPPRFYQKFATQIINHVngssEAERRNYTLALgiarevladrqdagtgdPFKEQLyaicrerVFKPLLAR 353
Cdd:cd05932 220 VQRARPTLFFSVPRLWTKFQQGVQDKI----PQQKLNLLLKI-----------------PVVNSL-------VKRKVLKG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 354 IGFDDLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPDGEMIVRG 433
Cdd:cd05932 272 LGLDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAG--PGVEVRISEDGEILVRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 434 PGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIENELRQSPYITEALVIGEG 512
Cdd:cd05932 350 PALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 513 RKYLTALI---EVDGTLAMDWARThdpsvtqyaDLASSppvidlIREEVEKANARLARAEQIKAFRIFPEELTPENGVMT 589
Cdd:cd05932 430 LPAPLALVvlsEEARLRADAFARA---------ELEAS------LRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILT 494
|
570
....*....|....
gi 981242995 590 ATRKKRRKALMARY 603
Cdd:cd05932 495 PTLKIKRNVLEKAY 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
17-510 |
3.68e-64 |
|
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: 218.53 E-value: 3.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 17 IPALLIERVKNDADANAF-FQRRAgawvpTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAV 95
Cdd:COG0318 1 LADLLRRAAARHPDRPALvFGGRR-----LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 96 TVGVYFTASVEEVRYYLEDSGATLAFagsaeqlrvmkaadtssrllkivvldpdwkrspdetgmnvvslaefashfdgde 175
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALV------------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 176 VAYLreqselarptdlvslGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPaiLSEPQRMVIHLPLSHTVARIQATTLPL 255
Cdd:COG0318 102 TALI---------------LYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 256 I--AKTV--PYFVDvsADFAKCIQEVRPTSYMAPPRFYQkfatQIINHvngsseaerrnytlalgiarevladrqdagtg 331
Cdd:COG0318 165 LagATLVllPRFDP--ERVLELIERERVTVLFGVPTMLA----RLLRH-------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 332 dpfkeqlyaicrervfkPLLARIGFDDLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMVGGNLAQVTD--WSRPG 408
Cdd:COG0318 207 -----------------PEFARYDLSSLRLVVSGGAPLPPELLERFEeRFGVRIVEGYGLTETSPVVTVNPEDpgERRPG 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 409 NSGVPLddPAWETRVLPD----------GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKE 478
Cdd:COG0318 270 SVGRPL--PGVEVRIVDEdgrelppgevGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKD 347
|
490 500 510
....*....|....*....|....*....|..
gi 981242995 479 LINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:COG0318 348 MIIS-GGENVYPAEVEEVLAAHPGVAEAAVVG 378
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
21-483 |
1.81e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 215.64 E-value: 1.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 21 LIERVKNDADANAFfqrRAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVY 100
Cdd:pfam00501 1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 101 FTASVEEVRYYLEDSGATLAFAGSAEQL-RVMKAADTSSRLLKIVVLDPDWKRSPDEtgmnvvslaefaSHFDGDEVAYL 179
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLeELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 180 REQSELARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPA--ILSEPQRMVIHLPLSHTVARIQATTLPLI- 256
Cdd:pfam00501 146 PPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLa 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 257 -AKTVPYFVDVSAD---FAKCIQEVRPTSYMAPPRFYQkfatQIINHvngsseaerrnytlalgiarevladrqdagtgd 332
Cdd:pfam00501 226 gATVVLPPGFPALDpaaLLELIERYKVTVLYGVPTLLN----MLLEA--------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 333 pfkeqlyaicrervfkPLLARIGFDDLRYPYTASAPVPPEVVT-LFQLWGVNLKENYGQTEMVGG---NLAQVTDWSRPG 408
Cdd:pfam00501 269 ----------------GAPKRALLSSLRLVLSGGAPLPPELARrFRELFGGALVNGYGLTETTGVvttPLPLDEDLRSLG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 409 NSGVP--------LDDPawETRVLPD---GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRK 476
Cdd:pfam00501 333 SVGRPlpgtevkiVDDE--TGEPVPPgepGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRK 410
|
....*..
gi 981242995 477 KELINTA 483
Cdd:pfam00501 411 KDQIKLG 417
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
46-612 |
1.04e-54 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 197.24 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAvCSVSAALGAA----GVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLedSGATLAF 121
Cdd:PLN02736 77 KWMTYGEA-GTARTAIGSGlvqhGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIV--NHAEVAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 122 AG-SAEQLRVMKAADT---SSRLLKIVVLDPDWKRS-PDETGMNVVSLAEFASHFDGDEVAYLReqselARPTDLVSLGY 196
Cdd:PLN02736 154 IFcVPQTLNTLLSCLSeipSVRLIVVVGGADEPLPSlPSGTGVEIVTYSKLLAQGRSSPQPFRP-----PKPEDVATICY 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGAMLTH---VSMLAGAFTWPTFCPAilsepQRMVIHLPLSHTVARIQATTLPLIAKTVPYFvdvSADFAKC 273
Cdd:PLN02736 229 TSGTTGTPKGVVLTHgnlIANVAGSSLSTKFYPS-----DVHISYLPLAHIYERVNQIVMLHYGVAVGFY---QGDNLKL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 274 ---IQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALGIAREVLADRQDAGtgdPFKEQLyaicrerVFKPL 350
Cdd:PLN02736 301 mddLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNPS---PMWDRL-------VFNKI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 351 LARIGfDDLRYPYTASAPVPPEVVTLFQL-WGVNLKENYGQTEM--------VGGNLAqvtdwsrpGNSGVPldDPAWET 421
Cdd:PLN02736 371 KAKLG-GRVRFMSSGASPLSPDVMEFLRIcFGGRVLEGYGMTETscvisgmdEGDNLS--------GHVGSP--NPACEV 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 422 RVL--------------PDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGK 486
Cdd:PLN02736 440 KLVdvpemnytsedqpyPRGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGE 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 487 SISPVQIENELRQSPYITEALVIGEG-RKYLTALIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLIREEVEK--ANA 563
Cdd:PLN02736 520 YIAPEKIENVYAKCKFVAQCFVYGDSlNSSLVAVVVVDPEVLKAWAASEGIKYEDLKQLCNDPRVRAAVLADMDAvgREA 599
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 981242995 564 RLARAEQIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLYD 612
Cdd:PLN02736 600 QLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
46-596 |
6.43e-54 |
|
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: 191.42 E-value: 6.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATlafagsa 125
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 eqlrvmkaadtssrllkIVVLDPDwkrspdetgmnvvslaefashfdgdevaylreqselarPTDLVSLGYTSGTTGAPK 205
Cdd:cd17640 80 -----------------ALVVEND--------------------------------------SDDLATIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 206 GAMLTHVSMLAGAFTWPTFCPAilsEP-QRMVIHLPLSHTVARIQATTLplIAK-------TVPYFVDvsaDFAKCiqev 277
Cdd:cd17640 105 GVMLTHANLLHQIRSLSDIVPP---QPgDRFLSILPIWHSYERSAEYFI--FACgcsqaytSIRTLKD---DLKRV---- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 278 RPTSYMAPPRFYQKFATQIINHVNGSSeaerrnytlalgiarevladrqdagtgdPFKEQLyaicrervFKPLLArIGfd 357
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGIQKQVSKSS----------------------------PIKQFL--------FLFFLS-GG-- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 358 DLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLDDPAWETR------VLP---DGE 428
Cdd:cd17640 214 IFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVdpegnvVLPpgeKGI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 429 MIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIENELRQSPYITEAL 507
Cdd:cd17640 294 VWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIM 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 508 VIGEGRKYLTALIEVDGTLAMDWARTHDPSV-TQYADLASSPPVIDLIREEVEK--ANARLARA-EQIKAFRIFPEELTp 583
Cdd:cd17640 374 VVGQDQKRLGALIVPNFEELEKWAKESGVKLaNDRSQLLASKKVLKLYKNEIKDeiSNRPGFKSfEQIAPFALLEEPFI- 452
|
570
....*....|...
gi 981242995 584 ENGVMTATRKKRR 596
Cdd:cd17640 453 ENGEMTQTMKIKR 465
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
44-599 |
3.29e-52 |
|
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: 187.42 E-value: 3.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 44 PTTWKGYANA---VCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATla 120
Cdd:cd17639 2 EYKYMSYAEVwerVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 121 fagsaeqlrvmkaadtssrllkIVVLDPdwkrspdetgmnvvslaefashfdgdevaylreqselaRPTDLVSLGYTSGT 200
Cdd:cd17639 80 ----------------------AIFTDG--------------------------------------KPDDLACIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 201 TGAPKGAMLTHVSMLAGAFTWPTFCPAILSEPQRMVIHLPLSHTV------------ARIQ-ATTLPLIAKTvpyfvdvs 267
Cdd:cd17639 100 TGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDRYLAYLPLAHIFelaaenvclyrgGTIGyGSPRTLTDKS-------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 268 adFAKC---IQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALGIAREvladRQDAGTGDPFkeqlyaiCRE 344
Cdd:cd17639 172 --KRGCkgdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLK----ALKEGPGTPL-------LDE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 345 RVFKPLLARIGfDDLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMV-GGNLAQVTDWSrPGNSGVPLddPAWETRV 423
Cdd:cd17639 239 LVFKKVRAALG-GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCaGGTVQDPGDLE-TGRVGPPL--PCCEIKL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 424 L-------------PDGEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSIS 489
Cdd:cd17639 315 VdweeggystdkppPRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIA 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 490 PVQIENELRQSPYITEALVIGEGRK-YLTALIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLIREEVEKA--NARLA 566
Cdd:cd17639 395 LEKLESIYRSNPLVNNICVYADPDKsYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETarAAGLE 474
|
570 580 590
....*....|....*....|....*....|...
gi 981242995 567 RAEQIKAFRIFPEELTPENGVMTATRKKRRKAL 599
Cdd:cd17639 475 KFEIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
49-515 |
1.16e-50 |
|
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: 182.38 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 49 GYANAVCsvsAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQL 128
Cdd:cd05936 32 ALAEAFA---AGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 129 RVMKAADTSSRllkiVVLDPDwkrspdetgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSGTTGAPKGAM 208
Cdd:cd05936 109 LLAAGAPLGER----VALTPE----------------------------------------DVAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 209 LTHVSMLAGAFTWPTFCPAILSEPQRMVIHLPLSHTVARIQATTLPLIAKT----VPYFVDvsADFAKCIQEVRPTSYMA 284
Cdd:cd05936 145 LTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGAtivlIPRFRP--IGVLKEIRKHRVTIFPG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 285 PPRFYqkfaTQIINHvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyaicrervfkPLLARIGFDDLRYPYT 364
Cdd:cd05936 223 VPTMY----IALLNA-------------------------------------------------PEFKKRDFSSLRLCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 365 ASAPVPPEVVTLF-QLWGVNLKENYGQTEM---VGGNlaQVTDWSRPGNSGVPLDDPAW-----ETRVLPD---GEMIVR 432
Cdd:cd05936 250 GGAPLPVEVAERFeELTGVPIVEGYGLTETspvVAVN--PLDGPRKPGSIGIPLPGTEVkivddDGEELPPgevGELWVR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 433 GPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINtAAGKSISPVQIENELRQSPYITEALVIGEG 512
Cdd:cd05936 328 GPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVEEVLYEHPAVAEAAVVGVP 406
|
...
gi 981242995 513 RKY 515
Cdd:cd05936 407 DPY 409
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
43-596 |
2.13e-49 |
|
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: 178.79 E-value: 2.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 43 VPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFA 122
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 123 GsaeqlrvmkaadtssrllkivvlDPDwkrspdetgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSGTTG 202
Cdd:cd05914 86 S-----------------------DED----------------------------------------DVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 203 APKGAMLTHVSMLAGAftwpTFCPAI--LSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFVD-VSADFAKCIQEVRP 279
Cdd:cd05914 103 NSKGVMLTYRNIVSNV----DGVKEVvlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDkIPSAKIIALAFAQV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 280 TSYMAPPRFYQ---KFATQIINHVNGSSeaerrnytlalgiarevladrqdagtgdpFKEQLYAIC-----RERVFKPLL 351
Cdd:cd05914 179 TPTLGVPVPLViekIFKMDIIPKLTLKK-----------------------------FKFKLAKKInnrkiRKLAFKKVH 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 352 ARIGfDDLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMvgGNLAQVTDWSRP--GNSGVPLD-------DPAWETR 422
Cdd:cd05914 230 EAFG-GNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTET--APIISYSPPNRIrlGSAGKVIDgvevridSPDPATG 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 423 vlpDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIENELRQSP 501
Cdd:cd05914 307 ---EGEIIVRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMP 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 502 YITEALVI-GEGRKYLTALIevdgtlamdwarthdpsvtqYADLASS-----PPVIDLIREEV-EKANARLARAEQIKAF 574
Cdd:cd05914 384 FVLESLVVvQEKKLVALAYI--------------------DPDFLDVkalkqRNIIDAIKWEVrDKVNQKVPNYKKISKV 443
|
570 580
....*....|....*....|..
gi 981242995 575 RIFPEELTPengvmTATRKKRR 596
Cdd:cd05914 444 KIVKEEFEK-----TPKGKIKR 460
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
43-510 |
8.05e-48 |
|
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: 173.57 E-value: 8.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 43 VPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATlafa 122
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAK---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 123 gsaeqlrvmkaadtssrllkiVVLDpdwkrspdetgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSGTTG 202
Cdd:cd17631 95 ---------------------VLFD------------------------------------------DLALLMYTSGTTG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 203 APKGAMLTHVSMLAGAFTWPTFCPaiLSEPQRMVIHLPLSHTVArIQATTLPLIAK-----TVPYF-VDVSADFakcIQE 276
Cdd:cd17631 112 RPKGAMLTHRNLLWNAVNALAALD--LGPDDVLLVVAPLFHIGG-LGVFTLPTLLRggtvvILRKFdPETVLDL---IER 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 277 VRPTSYMAPPRFYQKfatqIINHVNgsseaerrnytlalgiarevlADRQDagtgdpfkeqlyaicrervfkpllarigF 356
Cdd:cd17631 186 HRVTSFFLVPTMIQA----LLQHPR---------------------FATTD----------------------------L 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 357 DDLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTD--WSRPGNSGVPLddPAWETRVL-PD------- 426
Cdd:cd17631 213 SSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEdhRRKLGSAGRPV--FFVEVRIVdPDgrevppg 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 --GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYIT 504
Cdd:cd17631 291 evGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVLYEHPAVA 369
|
....*.
gi 981242995 505 EALVIG 510
Cdd:cd17631 370 EVAVIG 375
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2-541 |
9.82e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 176.34 E-value: 9.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 2 SAAPWTSGN-QFATTTIPALLIERVKNDADANA--FFQRRagawvpTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDV 78
Cdd:PRK05605 18 SYAPWTPHDlDYGDTTLVDLYDNAVARFGDRPAldFFGAT------TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 79 SREWLIADMATICSGAVTV--GVYFTAsvEEVRYYLEDSGATLAF-----AGSAEQLR------------VMKAADTSSR 139
Cdd:PRK05605 92 CPQHIVAFYAVLRLGAVVVehNPLYTA--HELEHPFEDHGARVAIvwdkvAPTVERLRrttpletivsvnMIAAMPLLQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 L-LKIVVldPDWKRSPDE-TGM--NVVSLAEFASHFDGDEVAylREQSELARPTDLVSLGYTSGTTGAPKGAMLTHVSML 215
Cdd:PRK05605 170 LaLRLPI--PALRKARAAlTGPapGTVPWETLVDAAIGGDGS--DVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 216 AGAFTWPTFCPAILSEPQRMVIHLPLSHTVA-RIQATTLPLIAKTVPYFVDVSADFAKCIQEVRPTSYM-APPRFYQKFA 293
Cdd:PRK05605 246 ANAAQGKAWVPGLGDGPERVLAALPMFHAYGlTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLpGVPPLYEKIA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 294 tqiinhvngsSEAERRNYTLAlGIarevladrqdagtgdpfkeqlyaicrervfkpllarigfddlRYPYTASAPVPPEV 373
Cdd:PRK05605 326 ----------EAAEERGVDLS-GV------------------------------------------RNAFSGAMALPVST 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 374 VTLFQ-LWGVNLKENYGQTE---MVGGNlaQVTDWSRPGNSGVPLD-------DPAWETRVLPD---GEMIVRGPGLFIG 439
Cdd:PRK05605 353 VELWEkLTGGLLVEGYGLTEtspIIVGN--PMSDDRRPGYVGVPFPdtevrivDPEDPDETMPDgeeGELLVRGPQVFKG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 440 YWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG----EGRKY 515
Cdd:PRK05605 431 YWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLREHPGVEDAAVVGlpreDGSEE 509
|
570 580 590
....*....|....*....|....*....|..
gi 981242995 516 LTALIEVDGTLAMD------WARTHdpsVTQY 541
Cdd:PRK05605 510 VVAAVVLEPGAALDpeglraYCREH---LTRY 538
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
38-616 |
1.71e-47 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 177.34 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 38 RAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGA 117
Cdd:PLN02861 71 KVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 118 TLAFAGSAEQLRVMKAADTSSRLLKIVV----LDPDWKRSPDETGMNVVSLAEFAShfdgdeVAYLREQSELARPTDLVS 193
Cdd:PLN02861 151 SIAFVQESKISSILSCLPKCSSNLKTIVsfgdVSSEQKEEAEELGVSCFSWEEFSL------MGSLDCELPPKQKTDICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 194 LGYTSGTTGAPKGAMLTHVSMLAGAFTwptfCPAILSEPQRMVI-------HLPLSHTVARIQATTLPLIAKTVPYFVDV 266
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVLS----TDHLLKVTDRVATeedsyfsYLPLAHVYDQVIETYCISKGASIGFWQGD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 267 SADFAKCIQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERR----NYTLALGIAREVLADRQDAgtgdpfkeqlyaic 342
Cdd:PLN02861 301 IRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKlfdfAYNYKLGNLRKGLKQEEAS-------------- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 343 rervfkPLLARIGFDDL--------RYPYTASAPVPPEVVTLFQLWGV-NLKENYGQTEMVGGNLAQVTD-WSRPGNSGV 412
Cdd:PLN02861 367 ------PRLDRLVFDKIkeglggrvRLLLSGAAPLPRHVEEFLRVTSCsVLSQGYGLTESCGGCFTSIANvFSMVGTVGV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 413 PLddPAWETRV-------------LPDGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKEL 479
Cdd:PLN02861 441 PM--TTIEARLesvpemgydalsdVPRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 480 INTAAGKSISPVQIENELRQSPYITEALVIGEG-RKYLTALIEVDGTLAMDWARTHDpSVTQYADLASSPPVIDLIREEV 558
Cdd:PLN02861 519 FKLSQGEYVAVENLENTYSRCPLIASIWVYGNSfESFLVAVVVPDRQALEDWAANNN-KTGDFKSLCKNLKARKYILDEL 597
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 559 EKANAR--LARAEQIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLYDDAEE 616
Cdd:PLN02861 598 NSTGKKlqLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
38-622 |
4.20e-47 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 176.36 E-value: 4.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 38 RAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGA 117
Cdd:PLN02614 73 KPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 118 TLAFAGSAEQLRVMKAADTSSRLLKIVV----LDPDWKRSPDETGMNVVSLAEFASHFDGdevaylrEQSEL--ARPTDL 191
Cdd:PLN02614 153 SIVFVEEKKISELFKTCPNSTEYMKTVVsfggVSREQKEEAETFGLVIYAWDEFLKLGEG-------KQYDLpiKKKSDI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 192 VSLGYTSGTTGAPKGAMLTH---VSMLAGAFTWPTFCPAILSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFVDVSA 268
Cdd:PLN02614 226 CTIMYTSGTTGDPKGVMISNesiVTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 269 DFAKCIQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALGIAREVLADRQDAGTGDPFkeqlyaiCRERVFK 348
Cdd:PLN02614 306 LLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQSHVEASPL-------CDKLVFN 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 349 PLLARIGfDDLRYPYTASAPVPPEVVTLFQLWGV-NLKENYGQTEMVGGNLAQVTD-WSRPGNSGVPLDD--------PA 418
Cdd:PLN02614 379 KVKQGLG-GNVRIILSGAAPLASHVESFLRVVACcHVLQGYGLTESCAGTFVSLPDeLDMLGTVGPPVPNvdirlesvPE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 419 WETRVL---PDGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIEN 495
Cdd:PLN02614 458 MEYDALastPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIEN 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 496 ELRQSPYITEALVIGEG-RKYLTALIEVDGTLAMDWARTHDPSvTQYADLASSPPVIDLIREEVEKA--NARLARAEQIK 572
Cdd:PLN02614 538 IYGEVQAVDSVWVYGNSfESFLVAIANPNQQILERWAAENGVS-GDYNALCQNEKAKEFILGELVKMakEKKMKGFEIIK 616
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 981242995 573 AFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLYDDAEERLIKEQ 622
Cdd:PLN02614 617 AIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTNEKLASRG 666
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
16-534 |
6.31e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 170.09 E-value: 6.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIE--RVKNDADANAFFQRRagawvpTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSG 93
Cdd:PRK07656 6 TLPELLARaaRRFGDKEAYVFGDQR------LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 94 AVTVGV--YFTAsvEEVRYYLEDSGATLAFAgSAEQLRVMKAADTSSRLLKIVVLDPDwkRSPDETGMNVVSLAEFASHF 171
Cdd:PRK07656 80 AVVVPLntRYTA--DEAAYILARGDAKALFV-LGLFLGVDYSATTRLPALEHVVICET--EEDDPHTEKMKTFTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 172 DGDEVAylreqSELaRPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFcpAILSEPQRMVIHLPLSHT------- 244
Cdd:PRK07656 155 DPAERA-----PEV-DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEY--LGLTEGDRYLAANPFFHVfgykagv 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 245 VARIQ--ATTLPliaktVPYFvDVSADFAKcIQEVRPTSYMAPPRFYQkfatQIINHVNGSSEAerrnytlalgiarevl 322
Cdd:PRK07656 227 NAPLMrgATILP-----LPVF-DPDEVFRL-IETERITVLPGPPTMYN----SLLQHPDRSAED---------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 323 adrqdagtgdpfkeqlyaicrervfkpllarigFDDLRYPYTASAPVPPEVVTLFQ-LWGVN-LKENYGQTEMVGgnlaq 400
Cdd:PRK07656 280 ---------------------------------LSSLRLAVTGAASMPVALLERFEsELGVDiVLTGYGLSEASG----- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 401 VTDWSR--------PGNSGVPLDD--------PAWETRVLPDGEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDIVD 463
Cdd:PRK07656 322 VTTFNRldddrktvAGTIGTAIAGvenkivneLGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDaDGWLHTGDLGR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 464 VGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG--------EGRKYLTAL--IEVDGTLAMDWART 533
Cdd:PRK07656 402 LDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVIGvpderlgeVGKAYVVLKpgAELTEEELIAYCRE 480
|
.
gi 981242995 534 H 534
Cdd:PRK07656 481 H 481
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
190-510 |
1.14e-43 |
|
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: 159.37 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 190 DLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWptFCPAILSEPQRMVIHLPLSHTVARIQATTlPLI--AKTVPYFVDVS 267
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAAL--AASGGLTEGDVFLSTLPLFHIGGLFGLLG-ALLagGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 268 ADFAKCIQEVRPTSYMAPPRFYQKFATQiinhvngsseAERRNYTLAlgiarevladrqdagtgdpfkeqlyaicrervf 347
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKA----------PESAGYDLS--------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 348 kpllarigfdDLRYPYTASAPVPPEVVTLF-QLWGVNLKENYGQTEmVGGNLAQVT---DWSRPGNSGVPLDDPAW---- 419
Cdd:cd04433 115 ----------SLRALVSGGAPLPPELLERFeEAPGIKLVNGYGLTE-TGGTVATGPpddDARKPGSVGRPVPGVEVrivd 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 420 -ETRVLPD---GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIEN 495
Cdd:cd04433 184 pDGGELPPgeiGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEA 262
|
330
....*....|....*
gi 981242995 496 ELRQSPYITEALVIG 510
Cdd:cd04433 263 VLLGHPGVAEAAVVG 277
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
16-511 |
7.25e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 161.89 E-value: 7.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIERVKNDADANAFFQRRAGawvpTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAV 95
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRR----TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 96 TVGVYFTASVEEVRYYLEDSGATLAFAGS--AEQLRVMKAADTSSRllKIVVLDPDWKRSPDETGMNVVS-LAEFASHFD 172
Cdd:PRK06187 83 LHPINIRLKPEEIAYILNDAEDRVVLVDSefVPLLAAILPQLPTVR--TVIVEGDGPAAPLAPEVGEYEElLAAASDTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 173 GDEVaylreqselaRPTDLVSLGYTSGTTGAPKGAMLTH---VSMLAGAFTWPTFCPAILSepqrMVIhLPLSHtvarIQ 249
Cdd:PRK06187 161 FPDI----------DENDAAAMLYTSGTTGHPKGVVLSHrnlFLHSLAVCAWLKLSRDDVY----LVI-VPMFH----VH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 250 ATTLPLI-----AKTV-PYFVDVSAdFAKCIQEVRPT-SYMAPprfyqkfatQIINhvngsseaerrnytlalGIAREVL 322
Cdd:PRK06187 222 AWGLPYLalmagAKQViPRRFDPEN-LLDLIETERVTfFFAVP---------TIWQ-----------------MLLKAPR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 323 ADRQDagtgdpfkeqlyaicrervfkpllarigFDDLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEM---VGGNL 398
Cdd:PRK06187 275 AYFVD----------------------------FSSLRLVIYGGAALPPALLREFKeKFGIDLVQGYGMTETspvVSVLP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 399 --AQVTD-WSRPGNSGVPLddPAWETRVL--------PD----GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVD 463
Cdd:PRK06187 327 peDQLPGqWTKRRSAGRPL--PGVEARIVdddgdelpPDggevGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGY 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 981242995 464 VGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIGE 511
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIIS-GGENIYPRELEDALYGHPAVAEVAVIGV 451
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-510 |
1.30e-42 |
|
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: 160.46 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSA 125
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 EQLRVMKAADTSSRLLKIVVLDPdwkrSPDEtgmnVVSLAEFASHFDGDEVAYLREQSELArPTDLVSLGYTSGTTGAPK 205
Cdd:cd05911 92 GLEKVKEAAKELGPKDKIIVLDD----KPDG----VLSIEDLLSPTLGEEDEDLPPPLKDG-KDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 206 GAMLTHVSMLAGA-FTWPTFCPAILSEPqRMVIHLPLSHTVARIQATTLPLIAKTV---PYFVdvSADFAKCIQEVRPTS 281
Cdd:cd05911 163 GVCLSHRNLIANLsQVQTFLYGNDGSND-VILGFLPLYHIYGLFTTLASLLNGATViimPKFD--SELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 282 -YMAPPrfyqkfatqiinhvngsseaerrnytLALGIAREVLADRQDAGTgdpfkeqlyaicrervfkpllarigfddLR 360
Cdd:cd05911 240 lYLVPP--------------------------IAAALAKSPLLDKYDLSS----------------------------LR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 361 YPYTASAPVPPEVVTLFQ--LWGVNLKENYGQTEMvGGNLAQVTDWS-RPGNSGVPLddPAWETRVLPD----------- 426
Cdd:cd05911 266 VILSGGAPLSKELQELLAkrFPNATIKQGYGMTET-GGILTVNPDGDdKPGSVGRLL--PNVEAKIVDDdgkdslgpnep 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELI--NtaaGKSISPVQIENELRQSPYI 503
Cdd:cd05911 343 GEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIkyK---GFQVAPAELEAVLLEHPGV 419
|
....*..
gi 981242995 504 TEALVIG 510
Cdd:cd05911 420 ADAAVIG 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
52-510 |
2.84e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 160.10 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 52 NAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAeqlrVM 131
Cdd:PRK08316 44 AAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA----LA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 132 KAADTSSRLLKivVLDPDWKRSPDETGMnVVSLAEFASHFDGDEVAylrEQSELARPTDLVSLGYTSGTTGAPKGAMLTH 211
Cdd:PRK08316 120 PTAEAALALLP--VDTLILSLVLGGREA-PGGWLDFADWAEAGSVA---EPDVELADDDLAQILYTSGTESLPKGAMLTH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 212 VSMLAgaftwpTFCPAI----LSEPQRMVIHLPLSHTVAR---------IQATTLPLIAKTVPYFVDVsadfakcIQEVR 278
Cdd:PRK08316 194 RALIA------EYVSCIvagdMSADDIPLHALPLYHCAQLdvflgpylyVGATNVILDAPDPELILRT-------IEAER 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 279 PTSYMAPPrfyqkfatqiinhvngsseaerrnyTLALGIAREVLADRQDAGTgdpfkeqlyaicrervfkpllarigfdd 358
Cdd:PRK08316 261 ITSFFAPP-------------------------TVWISLLRHPDFDTRDLSS---------------------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 359 LRYPYTASAPVPPEVVTLFQ--LWGVNLKENYGQTEMvgGNLAQV----TDWSRPGNSGVPLDDPawETRV-------LP 425
Cdd:PRK08316 288 LRKGYYGASIMPVEVLKELRerLPGLRFYNCYGQTEI--APLATVlgpeEHLRRPGSAGRPVLNV--ETRVvdddgndVA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 426 DGEM--IV-RGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPY 502
Cdd:PRK08316 364 PGEVgeIVhRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASREVEEALYTHPA 442
|
....*...
gi 981242995 503 ITEALVIG 510
Cdd:PRK08316 443 VAEVAVIG 450
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
47-611 |
7.18e-42 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 161.44 E-value: 7.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 47 WKGYANA---VCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAG 123
Cdd:PLN02387 106 WITYGQVferVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 124 SaEQLRvmKAADTSSRL--LKIVV-LDPDWKRSP----DETGMNVVSLAEFASHFDGDEVaylreQSELARPTDLVSLGY 196
Cdd:PLN02387 186 S-KQLK--KLIDISSQLetVKRVIyMDDEGVDSDsslsGSSNWTVSSFSEVEKLGKENPV-----DPDLPSPNDIAVIMY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGAMLTHVSMLAGAFTWPTFCPAiLSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPY-----FVDVSADFA 271
Cdd:PLN02387 258 TSGSTGLPKGVMMTHGNIVATVAGVMTVVPK-LGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYgspltLTDTSNKIK 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 272 KCIQ----EVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLALgiarevlADRQDAGTGDPFKeqlyAICRER-- 345
Cdd:PLN02387 337 KGTKgdasALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAY-------KRRLAAIEGSWFG----AWGLEKll 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 346 ----VFKPLLARIGfDDLRYPYTASAPVPPEVVTLFQL-WGVNLKENYGQTEMVGGnlAQVTDWSRP--GNSGVPL---- 414
Cdd:PLN02387 406 wdalVFKKIRAVLG-GRIRFMLSGGAPLSGDTQRFINIcLGAPIGQGYGLTETCAG--ATFSEWDDTsvGRVGPPLpccy 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 415 --------------DDPawetrvLPDGEMIVRGPGLFIGYWNKEAETKAALRDG-----WLYTGDIVDVGADGSYKLIDR 475
Cdd:PLN02387 483 vklvsweeggylisDKP------MPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDR 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 476 KKELINTAAGKSISPVQIENELRQSPYITEALVIGEG-RKYLTALIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLI 554
Cdd:PLN02387 557 KKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPfHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCEKEEAVKEV 636
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 981242995 555 REEVEKA--NARLARAEQIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLY 611
Cdd:PLN02387 637 QQSLSKAakAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
44-617 |
3.19e-39 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 153.43 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 44 PTTWKGYANA---VCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLA 120
Cdd:PLN02430 73 PYMWKTYKEVyeeVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 121 FAGSAEQLRVMKAADTSSRLLKIVV----LDPDWKRSPDETGMNVVSLAEFASHfdGDEVAylrEQSELARPTDLVSLGY 196
Cdd:PLN02430 153 FVQDKKIKELLEPDCKSAKRLKAIVsftsVTEEESDKASQIGVKTYSWIDFLHM--GKENP---SETNPPKPLDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGAMLTHVSMLAGAFTWPTFCPAI---LSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFV-DVSAdFAK 272
Cdd:PLN02430 228 TSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFedkMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHgDLNA-LRD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 273 CIQEVRPTSYMAPPRFYQKFATQIINHVNGSSEAERR------NYTLA---LGIAREvladrqdagTGDPFKEQLyaicr 343
Cdd:PLN02430 307 DLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLifnalyKYKLAwmnRGYSHK---------KASPMADFL----- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 344 erVFKPLLARIGfDDLRYPYTASAPVPPEVVTLFQLWGVN-LKENYGQTEMVGG-NLAQVTDWSRPGNSGV--------- 412
Cdd:PLN02430 373 --AFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLRVTSCAfVVQGYGLTETLGPtTLGFPDEMCMLGTVGApavynelrl 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 413 ---------PLDDPawetrvlPDGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTA 483
Cdd:PLN02430 450 eevpemgydPLGEP-------PRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 484 AGKSISPVQIENELRQSPYITEALVIGEG-RKYLTALIEVDGTLAMDWARTHDpSVTQYADLASSPPVIDLIREEVEKAN 562
Cdd:PLN02430 523 QGEYVALEYLENVYGQNPIVEDIWVYGDSfKSMLVAVVVPNEENTNKWAKDNG-FTGSFEELCSLPELKEHILSELKSTA 601
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 981242995 563 AR--LARAEQIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLYDDAEER 617
Cdd:PLN02430 602 EKnkLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKLAEK 658
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
52-613 |
2.31e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 145.12 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 52 NAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYL-EDSGATLAFAGS--AEQL 128
Cdd:PTZ00216 129 ERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALrETECKAIVCNGKnvPNLL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 129 RVMKAADTSSrlLKIVVLD--PDwkrSPDETGMNVVSLAEFAShfDGDEVAylrEQSELARPT---DLVSLGYTSGTTGA 203
Cdd:PTZ00216 209 RLMKSGGMPN--TTIIYLDslPA---SVDTEGCRLVAWTDVVA--KGHSAG---SHHPLNIPEnndDLALIMYTSGTTGD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 204 PKGAMLTHVSMLAGAFT---WPTFCPAILSEPQRMVIHLPLSH----TVARIQATTLPLIAKTVPY-FVDVSA----DFA 271
Cdd:PTZ00216 279 PKGVMHTHGSLTAGILAledRLNDLIGPPEEDETYCSYLPLAHimefGVTNIFLARGALIGFGSPRtLTDTFArphgDLT 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 272 kciqEVRPTSYMAPPRFYqkfatqiinhvngssEAERRNYTLAL----GIAREVL----ADRQDA---GTGDPFkeqlya 340
Cdd:PTZ00216 359 ----EFRPVFLIGVPRIF---------------DTIKKAVEAKLppvgSLKRRVFdhayQSRLRAlkeGKDTPY------ 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 341 iCRERVFKPLLARIGfDDLRYPYTASAPVPPE------VV--TLFQLWGVnlkenygqTEMVGGNLAQVTDWSRPGNSGV 412
Cdd:PTZ00216 414 -WNEKVFSAPRAVLG-GRVRAMLSGGGPLSAAtqefvnVVfgMVIQGWGL--------TETVCCGGIQRTGDLEPNAVGQ 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 413 PLddPAWETRVL------------PDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKEL 479
Cdd:PTZ00216 484 LL--KGVEMKLLdteeykhtdtpePRGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKAL 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 480 INTAAGKSISPVQIEnelrqSPYITEALVIGEG--------RKYLTALIEVDGTLAMDWARTHDPSVTqYADLASSPpvi 551
Cdd:PTZ00216 562 AKNCLGEYIALEALE-----ALYGQNELVVPNGvcvlvhpaRSYICALVLTDEAKAMAFAKEHGIEGE-YPAILKDP--- 632
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981242995 552 dLIREEVEKANARLARAEQIKAF------RIFPEELTPENGVMTATRKKRRKALMARYAHIIAGLYDD 613
Cdd:PTZ00216 633 -EFQKKATESLQETARAAGRKSFeivrhvRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
29-510 |
1.29e-34 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 137.44 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 29 ADANAFFQRRAGAWVptTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEV 108
Cdd:cd05926 1 PDAPALVVPGSTPAL--TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 109 RYYLEDSGATLAFAGSAEQLRVMKAADTssrlLKIVVLDPDWkrsPDETGMNVVSLAEFASHFDGDEVAYLREqseLARP 188
Cdd:cd05926 79 EFYLADLGSKLVLTPKGELGPASRAASK----LGLAILELAL---DVGVLIRAPSAESLSNLLADKKNAKSEG---VPLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 189 TDLVSLGYTSGTTGAPKGAMLTHVSMLAGAftwptfcPAI-----LSEPQRMVIHLPLSHTVARIQATTLPLIAK---TV 260
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHRNLAASA-------TNItntykLTPDDRTLVVMPLFHVHGLVASLLSTLAAGgsvVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 261 PYFVDVSAdFAKCIQEVRPTSYMAPPRFYQkfatqiinhvngsseaerrnytlalgiareVLADRQDAGTGDPFKEqlya 340
Cdd:cd05926 222 PPRFSAST-FWPDVRDYNATWYTAVPTIHQ------------------------------ILLNRPEPNPESPPPK---- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 341 icrervfkpllarigfddLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMVggnlAQVT------DWSRPGNSGVP 413
Cdd:cd05926 267 ------------------LRFIRSCSASLPPAVLEALEaTFGAPVLEAYGMTEAA----HQMTsnplppGPRKPGSVGKP 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 414 LddpAWETRVLPD----------GEMIVRGPGLFIGYWNKEAETKA-ALRDGWLYTGDIVDVGADGSYKLIDRKKELINT 482
Cdd:cd05926 325 V---GVEVRILDEdgeilppgvvGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR 401
|
490 500
....*....|....*....|....*...
gi 981242995 483 aAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05926 402 -GGEKISPLEVDGVLLSHPAVLEAVAFG 428
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
45-511 |
4.21e-34 |
|
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: 135.11 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 45 TTWKGYANAVCSVSAALGAAG-VARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLafag 123
Cdd:cd05941 12 ITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 124 saeqlrvmkaadtssrllkivVLDPdwkrspdetGMNVvslaefashfdgdevaylreqselarptdlvslgYTSGTTGA 203
Cdd:cd05941 88 ---------------------VLDP---------ALIL----------------------------------YTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 204 PKGAMLTH------VSMLAGAFTWptfcpailSEPQRMVIHLPLSHTVARIQATTLPLIAK-TVPYFVDVSADFAKCIQE 276
Cdd:cd05941 104 PKGVVLTHanlaanVRALVDAWRW--------TEDDVLLHVLPLHHVHGLVNALLCPLFAGaSVEFLPKFDPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 277 VRP-TSYMAPPRFYQKfatqiinhvngsseaerrnytlalgiarevLADRQDAGTGDPfkEQLYAICRERvfkpllarig 355
Cdd:cd05941 176 MPSiTVFMGVPTIYTR------------------------------LLQYYEAHFTDP--QFARAAAAER---------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 356 fddLRYPYTASAPVPPEVVTLF-QLWGVNLKENYGQTEmVGGNLAQVTDWSR-PGNSGVPLddPAWETRVLPD------- 426
Cdd:cd05941 214 ---LRLMVSGSAALPVPTLEEWeAITGHTLLERYGMTE-IGMALSNPLDGERrPGTVGMPL--PGVQARIVDEetgeplp 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 ----GEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKSISPVQIENELRQSP 501
Cdd:cd05941 288 rgevGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHP 367
|
490
....*....|
gi 981242995 502 YITEALVIGE 511
Cdd:cd05941 368 GVSECAVIGV 377
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
53-511 |
4.38e-33 |
|
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: 133.26 E-value: 4.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 53 AVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAgSAEQLRVMK 132
Cdd:cd05959 38 EARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV-SGELAPVLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 133 AADTSSRLLKIVVLDPDWKRSPDETGmnvvSLAEFashfdgdeVAYLREQSELAR--PTDLVSLGYTSGTTGAPKGAMLT 210
Cdd:cd05959 117 AALTKSEHTLVVLIVSGGAGPEAGAL----LLAEL--------VAAEAEQLKPAAthADDPAFWLYSSGSTGRPKGVVHL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 211 HVSMLAGAFTWPTFCPAI------LSEPQRMVIH-------LPLShtvarIQATTLPLIAKTVPyfvdvsADFAKCIQEV 277
Cdd:cd05959 185 HADIYWTAELYARNVLGIreddvcFSAAKLFFAYglgnsltFPLS-----VGATTVLMPERPTP------AAVFKRIRRY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 278 RPTSYMAPPRFYqkfatqiinhvngsseaerrnytlALGIAREVLADRqdagtgdpfkeqlyaicrervfkpllariGFD 357
Cdd:cd05959 254 RPTVFFGVPTLY------------------------AAMLAAPNLPSR-----------------------------DLS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 358 DLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPD---------- 426
Cdd:cd05959 281 SLRLCVSAGEALPAEVGERWKaRFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPV--PGYEVELRDEdggdvadgep 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINtAAGKSISPVQIENELRQSPYITEA 506
Cdd:cd05959 359 GELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEA 437
|
....*
gi 981242995 507 LVIGE 511
Cdd:cd05959 438 AVVGV 442
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
63-534 |
1.22e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 132.39 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 63 AAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSaEQLRVMKAADTSSRLLK 142
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS-ELAPKVAPAVGNLRLRH 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 143 IVVLD-------------PDWKRS----PDETGMNVVSLAEFAShfdgdevAYLREQSELARPTDLVSLGYTSGTTGAPK 205
Cdd:PRK08314 134 VIVAQysdylpaepeiavPAWLRAepplQALAPGGVVAWKEALA-------AGLAPPPHTAGPDDLAVLPYTSGTTGVPK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 206 GAMLTHVSMLA---GAFTWPTfcpaiLSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFV-----DVSADfakCIQEV 277
Cdd:PRK08314 207 GCMHTHRTVMAnavGSVLWSN-----STPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMprwdrEAAAR---LIERY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 278 RPTSYMAPPrfyqkfaTQIInhvngsseaerrnytlalgiarEVLADrqdagtgdpfkeqlyaicrervfkPLLARIGFD 357
Cdd:PRK08314 279 RVTHWTNIP-------TMVV----------------------DFLAS------------------------PGLAERDLS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 358 DLRYPYTASAPVPPEVVT-LFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPL---D----DPawET-RVLPD-- 426
Cdd:PRK08314 306 SLRYIGGGGAAMPEAVAErLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTfgvDarviDP--ETlEELPPge 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 -GEMIVRGPGLFIGYWNKEAETKAAL--RDG--WLYTGDIVDVGADGSYKLIDRKKELINtAAGKSISPVQIENELRQSP 501
Cdd:PRK08314 384 vGEIVVHGPQVFKGYWNRPEATAEAFieIDGkrFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHP 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 981242995 502 YITEALVI-------GEGRKYLTAL-IEVDGTLA----MDWARTH 534
Cdd:PRK08314 463 AIQEACVIatpdprrGETVKAVVVLrPEARGKTTeeeiIAWAREH 507
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
15-510 |
1.36e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.95 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 15 TTIPALLIERVKNDADANAFFqrragaWVPTTWKG--YANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICS 92
Cdd:PRK06188 12 ATYGHLLVSALKRYPDRPALV------LGDTRLTYgqLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 93 GAVTVGVYFTASVEEVRYYLEDSGA-TLAFAGSAEQLRVMKAADTSSRLLKIVVLDPdwkrspdetgmnVVSLAEFASHF 171
Cdd:PRK06188 86 GLRRTALHPLGSLDDHAYVLEDAGIsTLIVDPAPFVERALALLARVPSLKHVLTLGP------------VPDGVDLLAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 172 DGDEVAYLREQselARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGA------FTWPtfcpailsEPQRMVIHLPLSHTV 245
Cdd:PRK06188 154 AKFGPAPLVAA---ALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAqiqlaeWEWP--------ADPRFLMCTPLSHAG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 246 AriqATTLPLIAKTVPYFVDVS---ADFAKCIQEVRPTSYMAPPrfyqkfaTQIinhvngsseaerrnYtlalgiareVL 322
Cdd:PRK06188 223 G---AFFLPTLLRGGTVIVLAKfdpAEVLRAIEEQRITATFLVP-------TMI--------------Y---------AL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 323 ADRQDAGTGD-PFKEQLYaicrervfkpllarigfddlrypYTASAPVPPEVVTLFQLWGVNLKENYGQTE--MVGGNLA 399
Cdd:PRK06188 270 LDHPDLRTRDlSSLETVY-----------------------YGASPMSPVRLAEAIERFGPIFAQYYGQTEapMVITYLR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 400 QV----TDWSRPGNSGVPLddPAWETRVLPD----------GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVG 465
Cdd:PRK06188 327 KRdhdpDDPKRLTSCGRPT--PGLRVALLDEdgrevaqgevGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVARED 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 981242995 466 ADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK06188 405 EDGFYYIVDRKKDMIVT-GGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
46-510 |
2.76e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 127.67 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAAL-GAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAgS 124
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFV-E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 125 AEQlrvmkAADTSSRLLKIVVLDPDWkrspdetgmnVVSLAEFASHfdgdEVAYLREQSElarpTDLVSLGYTSGTTGAP 204
Cdd:PRK06839 108 KTF-----QNMALSMQKVSYVQRVIS----------ITSLKEIEDR----KIDNFVEKNE----SASFIICYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSMLAGAFTwPTFCPAILSEpQRMVIHLPLSHtVARIQATTLPLIaktvpyfvdvsadFAKCIQEVrptsyma 284
Cdd:PRK06839 165 KGAVLTQENMFWNALN-NTFAIDLTMH-DRSIVLLPLFH-IGGIGLFAFPTL-------------FAGGVIIV------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 285 PPRFYQKFATQIInhvngsseaERRNYTLALGIArevladrqdagtgdpfkeqlyAICRERVFKPLLARIGFDDLRYPYT 364
Cdd:PRK06839 222 PRKFEPTKALSMI---------EKHKVTVVMGVP---------------------TIHQALINCSKFETTNLQSVRWFYN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 365 ASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSR--PGNSGVPLddPAWETRVLPD----------GEMIVR 432
Cdd:PRK06839 272 GGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPV--LFCDYELIDEnknkvevgevGELLIR 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981242995 433 GPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK06839 350 GPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
46-510 |
6.82e-31 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 127.54 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVgVYFTA-SVEEVRYYLEDSGATLAFAgS 124
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS-PVFPGfGAEALADRIEDAEAKVLIT-A 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 125 AEQLRVMKAADTSSRLLKIVVLDPD------WKRSPDETGM-NVVSLAEFASHFDGDEVAylreqsELARPTDLVSLGYT 197
Cdd:COG0365 119 DGGLRGGKVIDLKEKVDEALEELPSlehvivVGRTGADVPMeGDLDWDELLAAASAEFEP------EPTDADDPLFILYT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 198 SGTTGAPKGAMLTHVSMLAGAFTWPT-----------FCPA-----------ILSepqrmvihlPLSHtvariQATTlpL 255
Cdd:COG0365 193 SGTTGKPKGVVHTHGGYLVHAATTAKyvldlkpgdvfWCTAdigwatghsyiVYG---------PLLN-----GATV--V 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 256 IAKTVPYFVDVSAdFAKCIQEVRPTSYMAPPRFYQKFatqiinhvngsseaerrnytLALGIArevladrqdagtgdpfk 335
Cdd:COG0365 257 LYEGRPDFPDPGR-LWELIEKYGVTVFFTAPTAIRAL--------------------MKAGDE----------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 336 eqlyaicrervfkpLLARIGFDDLRYPYTASAPVPPEVVT-LFQLWGVNLKENYGQTEMVG--GNLAQVTDwSRPGNSGV 412
Cdd:COG0365 299 --------------PLKKYDLSSLRLLGSAGEPLNPEVWEwWYEAVGVPIVDGWGQTETGGifISNLPGLP-VKPGSMGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 413 PLddPAWETRVLPD----------GEMIVRG--PGLFIGYWNKEAETKAALRD---GWLYTGDIVDVGADGSYKLIDRKK 477
Cdd:COG0365 364 PV--PGYDVAVVDEdgnpvppgeeGELVIKGpwPGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSD 441
|
490 500 510
....*....|....*....|....*....|...
gi 981242995 478 ELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:COG0365 442 DVINV-SGHRIGTAEIESALVSHPAVAEAAVVG 473
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1-510 |
2.53e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 125.66 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 1 MSAAPWTSGNQ---FATTTIPALLIERVKNDADANAFFQRRAGawVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGD 77
Cdd:PRK12583 1 MPQPSYYQGGGdkpLLTQTIGDAFDATVARFPDREALVVRHQA--LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 78 VSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFagsaeqlrVMKAADTSSRLLKIVVLDPDWKRSPDET 157
Cdd:PRK12583 79 NCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVI--------CADAFKTSDYHAMLQELLPGLAEGQPGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 158 GM--------NVVSLA-----------EFASHFDGDEVAYLREQSELARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGA 218
Cdd:PRK12583 151 LAcerlpelrGVVSLApapppgflawhELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 219 ftWPTFCPAILSEPQRMVIHLPLSHTVARIQATtlpLIAKTVpyfvdvsadfAKCIqeVRPTSYMAPprfyqkfatqiin 298
Cdd:PRK12583 231 --YFVAESLGLTEHDRLCVPVPLYHCFGMVLAN---LGCMTV----------GACL--VYPNEAFDP------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 299 hvngsseaerrnytlaLGIAREVLADRQDAGTGDP--FKEQLYaicrervfKPLLARIGFDDLRYPYTASAPVPPEVV-- 374
Cdd:PRK12583 281 ----------------LATLQAVEEERCTALYGVPtmFIAELD--------HPQRGNFDLSSLRTGIMAGAPCPIEVMrr 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 375 TLFQLWGVNLKENYGQTEM-------------------VGGNLAQVTdwsrpgnsgVPLDDPAWETrVLPD--GEMIVRG 433
Cdd:PRK12583 337 VMDEMHMAEVQIAYGMTETspvslqttaaddlerrvetVGRTQPHLE---------VKVVDPDGAT-VPRGeiGELCTRG 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981242995 434 PGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK12583 407 YSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
65-510 |
4.06e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 125.15 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 65 GVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADTSSRLLKIV 144
Cdd:PRK06710 70 GVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 145 VLDPDWKRSPDETGMNVVS--LAEFASHFDGDEVAYLREQSELARPT----------DLVSLGYTSGTTGAPKGAMLTHV 212
Cdd:PRK06710 150 TRIADFLPFPKNLLYPFVQkkQSNLVVKVSESETIHLWNSVEKEVNTgvevpcdpenDLALLQYTGGTTGFPKGVMLTHK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 213 SMLAGAFT---WPTFCpailSEPQRMVIH-LPLSHTVARIQATTLPLIAK----TVPYFvDVSADFaKCIQEVRPTSYMA 284
Cdd:PRK06710 230 NLVSNTLMgvqWLYNC----KEGEEVVLGvLPFFHVYGMTAVMNLSIMQGykmvLIPKF-DMKMVF-EAIKKHKVTLFPG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 285 PPRFYqkfatqiinhvngsseaerrnytLALgiarevladrqdagtgdpfkeqlyaicrerVFKPLLARIGFDDLRYPYT 364
Cdd:PRK06710 304 APTIY-----------------------IAL------------------------------LNSPLLKEYDISSIRACIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 365 ASAPVPPEVVTLFQ-LWGVNLKENYGQTEMvggnlAQVTD----WSR--PGNSGVPLDDP-----AWET-RVLPDGEM-- 429
Cdd:PRK06710 331 GSAPLPVEVQEKFEtVTGGKLVEGYGLTES-----SPVTHsnflWEKrvPGSIGVPWPDTeamimSLETgEALPPGEIge 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 430 -IVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALV 508
Cdd:PRK06710 406 iVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYEHEKVQEVVT 484
|
..
gi 981242995 509 IG 510
Cdd:PRK06710 485 IG 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-510 |
5.03e-30 |
|
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: 122.79 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 59 AALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFagsaeqlrvmkaadtss 138
Cdd:cd05934 18 AALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 139 rllkivvldpdwkrspdetgmnvvslaefashfdgdevaylreqselarpTDLVSLGYTSGTTGAPKGAMLTHVSMLAGA 218
Cdd:cd05934 81 --------------------------------------------------VDPASILYTSGTTGPPKGVVITHANLTFAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 219 FTWPTFCPaiLSEPQRMVIHLPLSHTVAriQATTlpliaktvpyfvdvsadfakciqevrptsymapprFYQKFatqiin 298
Cdd:cd05934 111 YYSARRFG--LGEDDVYLTVLPLFHINA--QAVS-----------------------------------VLAAL------ 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 299 hVNGSSEAERRNYTlalgiAREVLADRQDAGTgdpfkeqLYAICRERVFKPLLAR-IGFDDLRYPY--TASAPVPPEVVT 375
Cdd:cd05934 146 -SVGATLVLLPRFS-----ASRFWSDVRRYGA-------TVTNYLGAMLSYLLAQpPSPDDRAHRLraAYGAPNPPELHE 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 376 LF-QLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLDDpaWETRV-------LPD---GEMIVR---GPGLFIGYW 441
Cdd:cd05934 213 EFeERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPG--YEVRIvdddgqeLPAgepGELVIRglrGWGFFKGYY 290
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981242995 442 NKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05934 291 NMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRR-RGENISSAEVERAILRHPAVREAAVVA 358
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
52-510 |
2.44e-29 |
|
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: 121.96 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 52 NAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEqlrvm 131
Cdd:cd05904 40 RRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAEL----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 132 kAADTSSRLLKIVVLDpdwkrSPDetgmnVVSLAEFASHFDGDEVAYLREQselARPTDLVSLGYTSGTTGAPKGAMLTH 211
Cdd:cd05904 115 -AEKLASLALPVVLLD-----SAE-----FDSLSFSDLLFEADEAEPPVVV---IKQDDVAALLYSSGTTGRSKGVMLTH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 212 ---VSMLAG--AFTWPTFCPailsePQRMVIHLPLSHT--VARIQATTLPLIAKTV--PYFvdVSADFAKCIQEVRPTS- 281
Cdd:cd05904 181 rnlIAMVAQfvAGEGSNSDS-----EDVFLCVLPMFHIygLSSFALGLLRLGATVVvmPRF--DLEELLAAIERYKVTHl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 282 YMAPPrfyqkfatqiinhvngsseaerrnytLALGIAREVLADRQDagtgdpfkeqlyaicrervfkpLLArigfddLRY 361
Cdd:cd05904 254 PVVPP--------------------------IVLALVKSPIVDKYD----------------------LSS------LRQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 362 PYTASAPVPPEVVTLF--QLWGVNLKENYGQTEMVGG---NLAQVTDWSRPGNSGVPLddPAWETRV--------LP--- 425
Cdd:cd05904 280 IMSGAAPLGKELIEAFraKFPNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLV--PNVEAKIvdpetgesLPpnq 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 426 DGEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYIT 504
Cdd:cd05904 358 TGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEIL 436
|
....*.
gi 981242995 505 EALVIG 510
Cdd:cd05904 437 DAAVIP 442
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
47-590 |
1.08e-28 |
|
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: 121.02 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 47 WKGYANAVCSVSAAlgAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLaFAGSAE 126
Cdd:cd17632 73 LWERVGAVAAAHDP--EQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRL-LAVSAE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 127 QLRVMKAADTSSRLL-KIVVLDpdwKRSPDETGMNVVS-----LAEFASHFDGDEVAYLREQSELARPTD--------LV 192
Cdd:cd17632 150 HLDLAVEAVLEGGTPpRLVVFD---HRPEVDAHRAALEsarerLAAVGIPVTTLTLIAVRGRDLPPAPLFrpepdddpLA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 193 SLGYTSGTTGAPKGAMLTHvSMLAGAFTWPTFCPAIlSEPQRMVIH-LPLSHTVARIqattlPLIAKT----VPYFV--- 264
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTE-RLVATFWLKVSSIQDI-RPPASITLNfMPMSHIAGRI-----SLYGTLarggTAYFAaas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 265 DVSA---DFAkciqEVRPTSYMAPPR----FYQKFatqiinhvngSSEAERRnytlalgiarevLADRQDAGTgdpFKEQ 337
Cdd:cd17632 300 DMSTlfdDLA----LVRPTELFLVPRvcdmLFQRY----------QAELDRR------------SVAGADAET---LAER 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 338 LYAICRERVF-KPLLARIgfddlrypyTASAPVPPEVVTLF-QLWGVNLKENYGQTE----MVGGNLA--QVTDWSRpgn 409
Cdd:cd17632 351 VKAELRERVLgGRLLAAV---------CGSAPLSAEMKAFMeSLLDLDLHDGYGSTEagavILDGVIVrpPVLDYKL--- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 410 SGVP------LDDPAwetrvlPDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIV-DVGADgSYKLIDRKKELIN 481
Cdd:cd17632 419 VDVPelgyfrTDRPH------PRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVMaELGPD-RLVYVDRRNNVLK 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 482 TAAGKSISPVQIENELRQSPYITEALVIGEG-RKYLTALIevdgtlamdwARTHDPsvtqyadLASSPPviDLIREEVEK 560
Cdd:cd17632 492 LSQGEFVTVARLEAVFAASPLVRQIFVYGNSeRAYLLAVV----------VPTQDA-------LAGEDT--ARLRAALAE 552
|
570 580 590
....*....|....*....|....*....|....*.
gi 981242995 561 ANARLARAEQIKA------FRIFPEELTPENGVMTA 590
Cdd:cd17632 553 SLQRIAREAGLQSyeiprdFLIETEPFTIANGLLSG 588
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
46-510 |
2.67e-28 |
|
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: 118.25 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAgsa 125
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 eqlrvmkaadtssrllkivvldpdwkrsPDEtgmnvvslaefashfdgdevayLREQSELARPTDLVSLGYTSGTTGAPK 205
Cdd:cd05903 80 ----------------------------PER----------------------FRQFDPAAMPDAVALLLFTSGTTGEPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 206 GAMLTHVSMLAGAftwptfCPAI----LSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFVDV--SADFAKCIQEVRP 279
Cdd:cd05903 110 GVMHSHNTLSASI------RQYAerlgLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwdPDKALALMREHGV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 280 TSYMAPPrfyqKFATQIINHVngsseaerrnytlalgiarevlaDRQDAgtgdpfkeqlyAICRERVFkpllarigfddl 359
Cdd:cd05903 184 TFMMGAT----PFLTDLLNAV-----------------------EEAGE-----------PLSRLRTF------------ 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 360 rypYTASAPVPPEVVT-LFQLWGVNLKENYGQTEMVG--GNLAQVTDWSRPGNSGVPLddPAWETRVLPD---------- 426
Cdd:cd05903 214 ---VCGGATVPRSLARrAAELLGAKVCSAYGSTECPGavTSITPAPEDRRLYTDGRPL--PGVEIKVVDDtgatlapgve 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEA 506
Cdd:cd05903 289 GELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLLLGHPGVIEA 367
|
....
gi 981242995 507 LVIG 510
Cdd:cd05903 368 AVVA 371
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
65-573 |
5.40e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 115.54 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 65 GVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLA-----FAGSAEQLrVMKAA----- 134
Cdd:PRK08974 70 GLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIvivsnFAHTLEKV-VFKTPvkhvi 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 135 -----DTSSR----LLKIVV-----LDPDWKRsPDETGM-NVVSLaefashfdGDEVAYLREQSElarPTDLVSLGYTSG 199
Cdd:PRK08974 149 ltrmgDQLSTakgtLVNFVVkyikrLVPKYHL-PDAISFrSALHK--------GRRMQYVKPELV---PEDLAFLQYTGG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 200 TTGAPKGAMLTHVSMLAGAF--TWpTFCPAILSEPQRMVIHLPLSHTVArIQATTLPLIAK-------TVPyfvdvsADF 270
Cdd:PRK08974 217 TTGVAKGAMLTHRNMLANLEqaKA-AYGPLLHPGKELVVTALPLYHIFA-LTVNCLLFIELggqnlliTNP------RDI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 271 AKCIQEVRPTSYMApprfyqkfatqiINHVNgsseaerrnyTLAlgiarEVLADRQDagtgdpFKEqlyaicrervfkpl 350
Cdd:PRK08974 289 PGFVKELKKYPFTA------------ITGVN----------TLF-----NALLNNEE------FQE-------------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 351 larIGFDDLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTE---MVGGNLAQVTDWSrpGNSGVPLddPAWETRVLPD 426
Cdd:PRK08974 322 ---LDFSSLKLSVGGGMAVQQAVAERWVkLTGQYLLEGYGLTEcspLVSVNPYDLDYYS--GSIGLPV--PSTEIKLVDD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 ----------GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENE 496
Cdd:PRK08974 395 dgnevppgepGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 497 LRQSPYITEALVIGEGRKYLTALIEV-----DGTLAMDWARTHdpsVTQYADLASSPPVIDLiREEVEKANA-----RLA 566
Cdd:PRK08974 474 VMLHPKVLEVAAVGVPSEVSGEAVKIfvvkkDPSLTEEELITH---CRRHLTGYKVPKLVEF-RDELPKSNVgkilrREL 549
|
....*..
gi 981242995 567 RAEQIKA 573
Cdd:PRK08974 550 RDEARAK 556
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
53-510 |
6.37e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 112.15 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 53 AVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQ----- 127
Cdd:PRK06087 58 AASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKqtrpv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 128 LRVMKAADTSSRLLKIVVLDPDWKRSPDETGMNVVSLAEFASHF---DGDEVAylreqselarptdlvSLGYTSGTTGAP 204
Cdd:PRK06087 138 DLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEPLTTAittHGDELA---------------AVLFTSGTEGLP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSMLagaFTWPTFCPAI-LSEPQRMVIHLPLSHTVARIQATTLPLI--AKTVpyfvdvsadfakcIQEvrpts 281
Cdd:PRK06087 203 KGVMLTHNNIL---ASERAYCARLnLTWQDVFMMPAPLGHATGFLHGVTAPFLigARSV-------------LLD----- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 282 ymappRFYQKFATQIINhvngsseaeRRNYTLALGiarevladrqdagtGDPFKEQLYAICRErvfkpllARIGFDDLRY 361
Cdd:PRK06087 262 -----IFTPDACLALLE---------QQRCTCMLG--------------ATPFIYDLLNLLEK-------QPADLSALRF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 362 PYTASAPVPPEVVTLFQLWGVNLKENYGQTE-----MVggNLAQVTDWSRpGNSGVPLddPAWETRVLPD---------- 426
Cdd:PRK06087 307 FLCGGTTIPKKVARECQQRGIKLLSVYGSTEssphaVV--NLDDPLSRFM-HTDGYAA--AGVEIKVVDEarktlppgce 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITE 505
Cdd:PRK06087 382 GEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHD 460
|
....*
gi 981242995 506 ALVIG 510
Cdd:PRK06087 461 ACVVA 465
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
16-509 |
1.96e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 110.84 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIERVKNDADANAFFQRRAGAWVptTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAV 95
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAVTGKAV--TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 96 TVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVmkaadtSSRLLKIVVLDpdwkRSPDETGMNVVSLAEfASHFDGDE 175
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKV------KGLGLPVIVLG----EEKIEGAVNWKELLE-AADRAGDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 176 VAYlreqsELARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAgaftwpTFCPAILSEPQRMVIhlplshtvariQATTLPL 255
Cdd:PLN02330 176 SDN-----EEILQTDLCALPFSSGTTGISKGVMLTHRNLVA------NLCSSLFSVGPEMIG-----------QVVTLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 256 IaktvPYFvDVSADFAKCIQEVR-PTSYMAPPRFyqkfatqiinhvngsseaERRNYTLALgIAREVladrqdagtgdPF 334
Cdd:PLN02330 234 I----PFF-HIYGITGICCATLRnKGKVVVMSRF------------------ELRTFLNAL-ITQEV-----------SF 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 335 KEQLYAICRERVFKPLLARigFD----DLRYPYTASAPVPPEVVTLFQ--LWGVNLKENYGQTE-----MVGGNLAQVTD 403
Cdd:PLN02330 279 APIVPPIILNLVKNPIVEE--FDlsklKLQAIMTAAAPLAPELLTAFEakFPGVQVQEAYGLTEhscitLTHGDPEKGHG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 404 WSRPGNSGVPLddPAWETRVL-PD----------GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYK 471
Cdd:PLN02330 357 IAKKNSVGFIL--PNLEVKFIdPDtgrslpkntpGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIF 434
|
490 500 510
....*....|....*....|....*....|....*...
gi 981242995 472 LIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI 509
Cdd:PLN02330 435 IVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAVV 471
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
45-510 |
1.22e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 108.33 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 45 TTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGS 124
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 125 AEQlRVMKAADTSSRLLKIVVldpdwkrspdetgmnVVSLAEFASHFDGDEVayLREQSELARPTDL-----VSLGYTSG 199
Cdd:PRK07786 123 ALA-PVATAVRDIVPLLSTVV---------------VAGGSSDDSVLGYEDL--LAEAGPAHAPVDIpndspALIMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 200 TTGAPKGAMLTHVSMLAGAFTWpTFCPAILSEPQRMVIHLPLSHtVARI--QATTLPLIAKTVPYfvdvsadfakciqev 277
Cdd:PRK07786 185 TTGRPKGAVLTHANLTGQAMTC-LRTNGADINSDVGFVGVPLFH-IAGIgsMLPGLLLGAPTVIY--------------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 278 rPTSYMAPprfyqkfaTQIINHVngssEAERRNyTLALGIArevladrqdagtgdpfkeQLYAICRERVFKPL-LArigf 356
Cdd:PRK07786 248 -PLGAFDP--------GQLLDVL----EAEKVT-GIFLVPA------------------QWQAVCAEQQARPRdLA---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 357 ddLRYPYTASAPVPPEVvtLFQLW----GVNLKENYGQTEMvggnlAQVT------DWSRP-GNSGVPLddPAWETRVLP 425
Cdd:PRK07786 292 --LRVLSWGAAPASDTL--LRQMAatfpEAQILAAFGQTEM-----SPVTcmllgeDAIRKlGSVGKVI--PTVAARVVD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 426 D----------GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIEN 495
Cdd:PRK07786 361 EnmndvpvgevGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVEN 439
|
490
....*....|....*
gi 981242995 496 ELRQSPYITEALVIG 510
Cdd:PRK07786 440 VLASHPDIVEVAVIG 454
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
57-601 |
1.50e-24 |
|
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: 106.65 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 57 VSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGAtlafagsaeqlrvmkaadt 136
Cdd:cd05972 13 AANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 137 ssrllKIVVLDPDwkrspdetgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSGTTGAPKGAMLTHVSMLA 216
Cdd:cd05972 74 -----KAIVTDAE----------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 217 gafTWPTFCPAILSEPQRmvIHLPLSHTvARIQATTLPLIAKT---VPYFVDVSADFA-----KCIQEVRPTSYMAPPRF 288
Cdd:cd05972 109 ---HIPTAAYWLGLRPDD--IHWNIADP-GWAKGAWSSFFGPWllgATVFVYEGPRFDaerilELLERYGVTSFCGPPTA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 289 YQKFAtqiinhvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyaicrervfKPLLARIGFDDLRYPYTASAP 368
Cdd:cd05972 183 YRMLI------------------------------------------------------KQDLSSYKFSHLRLVVSAGEP 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 369 VPPEVVTLFQ-LWGVNLKENYGQTE---MVGGNLAQVTdwsRPGNSGVP--------LDDPAWETRVLPDGEMIVR--GP 434
Cdd:cd05972 209 LNPEVIEWWRaATGLPIRDGYGQTEtglTVGNFPDMPV---KPGSMGRPtpgydvaiIDDDGRELPPGEEGDIAIKlpPP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 435 GLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIGEGRk 514
Cdd:cd05972 286 GLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKS-SGYRIGPFEVESALLEHPAVAEAAVVGSPD- 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 515 yltaliEVDGTLamdwarthdpsVTQYADLASS-PPVIDLIREEVEKANARLARAeqiKAFRI--FPEELtPEngvmTAT 591
Cdd:cd05972 364 ------PVRGEV-----------VKAFVVLTSGyEPSEELAEELQGHVKKVLAPY---KYPREieFVEEL-PK----TIS 418
|
570
....*....|
gi 981242995 592 RKKRRKALMA 601
Cdd:cd05972 419 GKIRRVELRD 428
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
46-510 |
1.63e-24 |
|
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: 107.56 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAgSA 125
Cdd:TIGR03098 27 TYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVT-SS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 EQLRVMKAADTSSRLL-KIVVLDPDWKRSPDETGMNVVSLAEFASHfdGDEVAYLReqselARPTDLVSLGYTSGTTGAP 204
Cdd:TIGR03098 106 ERLDLLHPALPGCHDLrTLIIVGDPAHASEGHPGEEPASWPKLLAL--GDADPPHP-----VIDSDMAAILYTSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSMLAGAFTWPTFCPaiLSEPQRMVIHLPLSHTVARIQATTLPLI-AKTVPYFVDVSADFAKCIQEVRPTSYM 283
Cdd:TIGR03098 179 KGVVLSHRNLVAGAQSVATYLE--NRPDDRLLAVLPLSFDYGFNQLTTAFYVgATVVLHDYLLPRDVLKALEKHGITGLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 284 A-PPRFYQKFATQIinhvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyaicrervfkPLLArigFDDLRYP 362
Cdd:TIGR03098 257 AvPPLWAQLAQLDW----------------------------------------------------PESA---APSLRYL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 363 YTASAPVPPEVVT----------LFQLWGvnLKENYGQT----EMVGgnlaqvtdwSRPGNSGVPLddPAWETRVLPD-- 426
Cdd:TIGR03098 282 TNSGGAMPRATLSrlrsflpnarLFLMYG--LTEAFRSTylppEEVD---------RRPDSIGKAI--PNAEVLVLREdg 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 --------GEMIVRGPGLFIGYWNKEAETKAALR------------DGWLYTGDIVDVGADGSYKLIDRKKELINTaAGK 486
Cdd:TIGR03098 349 secapgeeGELVHRGALVAMGYWNDPEKTAERFRplppfpgelhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKT-SGY 427
|
490 500
....*....|....*....|....
gi 981242995 487 SISPVQIENELRQSPYITEALVIG 510
Cdd:TIGR03098 428 RVSPTEVEEVAYATGLVAEAVAFG 451
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-510 |
5.75e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 105.73 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVtvgvYF---TASVE-EVRYYLEDSGATLAF 121
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAV----FLplnTAYTLaELDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 122 AGSAEQLRVMKAADTSSrLLKIVVLDPDwkrspdETGmnvvSLAEFASHFDGDEVAYLREqselarPTDLVSLGYTSGTT 201
Cdd:PRK07514 106 CDPANFAWLSKIAAAAG-APHVETLDAD------GTG----SLLEAAAAAPDDFETVPRG------ADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 202 GAPKGAMLTHVSMLAGAFTwptfcpaiLSE-----PQRMVIH-LPLSHTVARIQATTLPLIAKT----VPYFvdvsaDFA 271
Cdd:PRK07514 169 GRSKGAMLSHGNLLSNALT--------LVDywrftPDDVLIHaLPIFHTHGLFVATNVALLAGAsmifLPKF-----DPD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 272 KCIQEV-RPTSYMAPPRFYQKfatqiinhvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyaicrervfkpL 350
Cdd:PRK07514 236 AVLALMpRATVMMGVPTFYTR----------------------------------------------------------L 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 351 LARIGFDD-----LRYPYTASAPVPPEVvtlFQLW----GVNLKENYGQTE--MVGGNLAQvtDWSRPGNSGVPL----- 414
Cdd:PRK07514 258 LQEPRLTReaaahMRLFISGSAPLLAET---HREFqertGHAILERYGMTEtnMNTSNPYD--GERRAGTVGFPLpgvsl 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 415 --DDPAwETRVLPDGE--MI-VRGPGLFIGYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSI 488
Cdd:PRK07514 333 rvTDPE-TGAELPPGEigMIeVKGPNVFKGYWRMPEKTAEEFRaDGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNV 410
|
490 500
....*....|....*....|..
gi 981242995 489 SPVQIENELRQSPYITEALVIG 510
Cdd:PRK07514 411 YPKEVEGEIDELPGVVESAVIG 432
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-510 |
7.12e-24 |
|
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: 103.51 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 188 PTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTwpTFCPAILSEPQRMVIHLPLSH----------TVARIQATTLPlia 257
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYF--IGERLGLTEQDRLCIPVPLFHcfgsvlgvlaCLTHGATMVFP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 258 ktVPYFvDVSADFAKcIQEVRPTS-YMAPPRFyqkfaTQIINHvngsseaerrnytlalgiarevladrqdagtgdpfke 336
Cdd:cd05917 76 --SPSF-DPLAVLEA-IEKEKCTAlHGVPTMF-----IAELEH------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 337 qlyaicrervfkPLLARIGFDDLRYPYTASAPVPPEVVT-LFQLwgVNLKE---NYGQTEMVGGNLAQVTDWS---RPGN 409
Cdd:cd05917 110 ------------PDFDKFDLSSLRTGIMAGAPCPPELMKrVIEV--MNMKDvtiAYGMTETSPVSTQTRTDDSiekRVNT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 410 SGVPLD-------DPawETRVLPD----GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKK 477
Cdd:cd05917 176 VGRIMPhteakivDP--EGGIVPPvgvpGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRIK 253
|
330 340 350
....*....|....*....|....*....|...
gi 981242995 478 ELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05917 254 DMI-IRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
22-510 |
7.85e-24 |
|
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: 105.69 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 22 IERVKNDADANAFFQRRAGawVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYF 101
Cdd:cd17642 24 MKRYASVPGTIAFTDAHTG--VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 102 TASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADTSSRLLKIVVLDPDwkrspdETGMNVVSLAEF-ASHFDGDEVAYLR 180
Cdd:cd17642 102 IYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSK------EDYKGYQCLYTFiTQNLPPGFNEYDF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 181 EQSELARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAgAFTW---PTFCPAILSEPQRMVIhLPLSHTVARIQATTLPLIA 257
Cdd:cd17642 176 KPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVA-RFSHardPIFGNQIIPDTAILTV-IPFHHGFGMFTTLGYLICG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 258 KTVPYFVDVSAD-FAKCIQEVRPTS-YMAPPRFYQKFATQIINHVNGSSEAErrnytLALG---IAREVladrqdagtGD 332
Cdd:cd17642 254 FRVVLMYKFEEElFLRSLQDYKVQSaLLVPTLFAFFAKSTLVDKYDLSNLHE-----IASGgapLSKEV---------GE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 333 PFKEQlyaicrervfkpllarigfddlrypytasapvppevvtlFQLWGVnlKENYGQTEMVGGNLAQVTDWSRPGNSGV 412
Cdd:cd17642 320 AVAKR---------------------------------------FKLPGI--RQGYGLTETTSAILITPEGDDKPGAVGK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 413 PLddPAWETRVL-PD----------GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELI 480
Cdd:cd17642 359 VV--PFFYAKVVdLDtgktlgpnerGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLI 436
|
490 500 510
....*....|....*....|....*....|
gi 981242995 481 NTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd17642 437 KY-KGYQVPPAELESILLQHPKIFDAGVAG 465
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
51-511 |
1.74e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 104.27 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 51 ANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAF-AGSAEQLR 129
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLItDDDFEAKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 130 VMKAADTSSRLLKIVVLDPDWKrspdetgmnvvslaefaSHFDGDEVAylreqselarptdlvSLGYTSGTTGAPKGAML 209
Cdd:PRK03640 114 IPGISVKFAELMNGPKEEAEIQ-----------------EEFDLDEVA---------------TIMYTSGTTGKPKGVIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 210 T---HvsmlagaftwptFCPAILSepqrmVIHLPLshtvariQATTLPLIAktVPYFvdvsadfakciqevrptsymapp 286
Cdd:PRK03640 162 TygnH------------WWSAVGS-----ALNLGL-------TEDDCWLAA--VPIF----------------------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 287 rfyqkfatqiinHVNGSSEAERrnyTLALGIaREVLADRQDAgtgdpfKEQLYAICRERV---------FKPLLARIGfd 357
Cdd:PRK03640 193 ------------HISGLSILMR---SVIYGM-RVVLVEKFDA------EKINKLLQTGGVtiisvvstmLQRLLERLG-- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 358 DLRYPYTASA------PVPPEVVTLFQLWGVNLKENYGQTEMVggnlAQVTDWS------RPGNSGVPL-------DDPA 418
Cdd:PRK03640 249 EGTYPSSFRCmllgggPAPKPLLEQCKEKGIPVYQSYGMTETA----SQIVTLSpedaltKLGSAGKPLfpcelkiEKDG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 419 WETRVLPDGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELR 498
Cdd:PRK03640 325 VVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLL 403
|
490
....*....|...
gi 981242995 499 QSPYITEALVIGE 511
Cdd:PRK03640 404 SHPGVAEAGVVGV 416
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-510 |
2.43e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 103.29 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 52 NAVCSVSAALGAAGVARGDRIAIMGDVSRE--WLIAD--MATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFagsaeq 127
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTyiELSFAvaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 128 lrVMKAADTSSRLLKIVVLDPDwkrspdetgmnVVSLAEFASHfDGDevayLREQSELARPtDLVSLGYTSGTTGAPKGA 207
Cdd:cd05922 75 --ADAGAADRLRDALPASPDPG-----------TVLDADGIRA-ARA----SAPAHEVSHE-DLALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 208 MLTHVSMLAGAftwptfcPAI-----LSEPQRMVIHLPLSHTVARIQATTLPLI-AKTV--PYFVdVSADFAKCIQEVRP 279
Cdd:cd05922 136 RLSHQNLLANA-------RSIaeylgITADDRALTVLPLSYDYGLSVLNTHLLRgATLVltNDGV-LDDAFWEDLREHGA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 280 TSYMAPPRFYQkfatqiinhvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyaicrervfkpLLARIGFDD- 358
Cdd:cd05922 208 TGLAGVPSTYA-----------------------------------------------------------MLTRLGFDPa 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 359 ----LRYPYTASAPVPPEVVT----LFQLWGVNLKenYGQTE----MVGGNLAQVTDwsRPGNSGVP--------LDDPA 418
Cdd:cd05922 229 klpsLRYLTQAGGRLPQETIArlreLLPGAQVYVM--YGQTEatrrMTYLPPERILE--KPGSIGLAipggefeiLDDDG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 419 WETRVLPDGEMIVRGPGLFIGYWNKEA-ETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTAaGKSISPVQIENEL 497
Cdd:cd05922 305 TPTPPGEPGEIVHRGPNVMKGYWNDPPyRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAA 383
|
490
....*....|...
gi 981242995 498 RQSPYITEALVIG 510
Cdd:cd05922 384 RSIGLIIEAAAVG 396
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
45-510 |
9.47e-23 |
|
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: 101.38 E-value: 9.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 45 TTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGvyftASVEevryyledsgatlafagS 124
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVV----INPL-----------------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 125 AEQLRVMKAADTSSRLLKIvvldpdwkrspdetgmnvvslaefashfDGDEVAYLReqselarptdlvslgYTSGTTGAP 204
Cdd:cd05919 70 HPDDYAYIARDCEARLVVT----------------------------SADDIAYLL---------------YSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSMLAGAFTWPTFCPAILSEPQ-----RMVIHLPLSHTVariqatTLPLI----AKTVPYFVDVSADFAKcIQ 275
Cdd:cd05919 107 KGVMHAHRDPLLFADAMAREALGLTPGDRvfssaKMFFGYGLGNSL------WFPLAvgasAVLNPGWPTAERVLAT-LA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 276 EVRPTSYMAPPRFYQKfatqIINHVNGSSEAERrnytlalgiarevladrqdagtgdpfkeqlyaicrervfkpllarig 355
Cdd:cd05919 180 RFRPTVLYGVPTFYAN----LLDSCAGSPDALR----------------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 356 fdDLRYPYTASAPVPPEvvtLFQLW----GVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVL------- 424
Cdd:cd05919 209 --SLRLCVSAGEALPRG---LGERWmehfGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPV--PGYEIRLVdeeghti 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 425 PDGE---MIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSP 501
Cdd:cd05919 282 PPGEegdLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQHP 360
|
....*....
gi 981242995 502 YITEALVIG 510
Cdd:cd05919 361 AVAEAAVVA 369
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
46-510 |
1.16e-22 |
|
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: 101.61 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSA 125
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 EQLR-VMKAADTssrllkivvlDPDWKRSPDETgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSGTTGAP 204
Cdd:cd12118 111 FEYEdLLAEGDP----------DFEWIPPADEW--------------------------------DPIALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTH----VSMLAGAFTWptfcpailsEPQRMVIHLplshtvariqaTTLPLI---AKTVPYFVDVSADFAKCIQEV 277
Cdd:cd12118 149 KGVVYHHrgayLNALANILEW---------EMKQHPVYL-----------WTLPMFhcnGWCFPWTVAAVGGTNVCLRKV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 278 RPtsymapPRFYQKFATQIINHVNGsseaerrnytlalgiAREVLAdrqdagtgdpfkeqLYAICRERVFKPLLARIGFD 357
Cdd:cd12118 209 DA------KAIYDLIEKHKVTHFCG---------------APTVLN--------------MLANAPPSDARPLPHRVHVM 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 358 dlrypyTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGgnLAQVTDWSRPGNS-------------GV------PLD--D 416
Cdd:cd12118 254 ------TAGAPPPAAVLAKMEELGFDVTHVYGLTETYG--PATVCAWKPEWDElpteerarlkarqGVryvgleEVDvlD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 417 PAWETRVLPDGEMI----VRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQ 492
Cdd:cd12118 326 PETMKPVPRDGKTIgeivFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVE 404
|
490
....*....|....*...
gi 981242995 493 IENELRQSPYITEALVIG 510
Cdd:cd12118 405 VEGVLYKHPAVLEAAVVA 422
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
51-511 |
1.22e-22 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 101.84 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 51 ANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAgSAEQLRV 130
Cdd:TIGR02262 37 EAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFV-SGALLPV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 131 MKAADTSSRLLKIVVLDPDwKRSPDetgmnvVSLAEF-ASHFDGDEVAylreqseLARPTDLVSLGYTSGTTGAPKGAML 209
Cdd:TIGR02262 116 IKAALGKSPHLEHRVVVGR-PEAGE------VQLAELlATESEQFKPA-------ATQADDPAFWLYSSGSTGMPKGVVH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 210 THVSMLAGAFTWptfcpailsepQRMVIHLPLSHTV---ARI-------QATTLPLI--AKTVPYFVDVSADFA-KCIQE 276
Cdd:TIGR02262 182 THSNPYWTAELY-----------ARNTLGIREDDVCfsaAKLffayglgNALTFPMSvgATTVLMGERPTPDAVfDRLRR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 277 VRPTSYMAPPRFYqkfaTQIINHVNGSSEAERRnytlalgiarevladrqdagtgdpfkeqlyaicrervfkpllarigf 356
Cdd:TIGR02262 251 HQPTIFYGVPTLY----AAMLADPNLPSEDQVR----------------------------------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 357 ddLRYPYTASAPVPPEVVTLFQL-WGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPD--------- 426
Cdd:TIGR02262 280 --LRLCTSAGEALPAEVGQRWQArFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPV--PGYRLRLVGDggqdvadge 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 -GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITE 505
Cdd:TIGR02262 356 pGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKV-SGIYVSPFEIESALIQHPAVLE 434
|
....*.
gi 981242995 506 ALVIGE 511
Cdd:TIGR02262 435 AAVVGV 440
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
58-510 |
1.41e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 101.50 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 58 SAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGsaEQLRVMKAADTs 137
Cdd:PRK06145 41 AGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVD--EEFDAIVALET- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 138 srllKIVVLDPDWKRSPDETGMNVVSLAEFAShfdgdevaylreqselARPTDLVSLGYTSGTTGAPKGAMLTHvsmlaG 217
Cdd:PRK06145 118 ----PKIVIDAAAQADSRRLAQGGLEIPPQAA----------------VAPTDLVRLMYTSGTTDRPKGVMHSY-----G 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 218 AFTWPTFCPAI---LSEPQRMVIHLPLSHtvarIQATTLPLIAktvpyfVDVSADFAKCIQEVRPTSYMApprfyqkfat 294
Cdd:PRK06145 173 NLHWKSIDHVIalgLTASERLLVVGPLYH----VGAFDLPGIA------VLWVGGTLRIHREFDPEAVLA---------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 295 qiinhvngsseaerrnytlalGIARevlaDRQDAGTGDPFKEQLYAICRERvfkpllARIGFDDLRYPYTASAPVPPEVV 374
Cdd:PRK06145 233 ---------------------AIER----HRLTCAWMAPVMLSRVLTVPDR------DRFDLDSLAWCIGGGEKTPESRI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 375 TLFQLWGVNLK--ENYGQTEMVGGN--LAQVTDWSRPGNSG-----VPLDDPAWETRVLP---DGEMIVRGPGLFIGYWN 442
Cdd:PRK06145 282 RDFTRVFTRARyiDAYGLTETCSGDtlMEAGREIEKIGSTGralahVEIRIADGAGRWLPpnmKGEICMRGPKVTKGYWK 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981242995 443 KEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK06145 362 DPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
53-534 |
1.69e-22 |
|
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: 100.63 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 53 AVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAeqlrvmk 132
Cdd:cd05935 10 VVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 133 aadtssrllkivvLDpdwkrspdetgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSGTTGAPKGAMLTHV 212
Cdd:cd05935 83 -------------LD------------------------------------------DLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 213 SMLAGAFTwpTFCPAILSEPQRMVIHLPLSHTVARIQATTLPLIAKTvpyfvdvsadfakciqevrptSYMAPPRFYQKF 292
Cdd:cd05935 108 SAAANALQ--SAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGG---------------------TYVLMARWDRET 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 293 ATQIInhvngsseaERRNYTLALGIAREVLAdrqdagtgdpfkeqlyaicrervfkpLLARIGFDD-----LRYPYTASA 367
Cdd:cd05935 165 ALELI---------EKYKVTFWTNIPTMLVD--------------------------LLATPEFKTrdlssLKVLTGGGA 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 368 PVPPEVVT-LFQLWGVNLKENYGQTEmvggNLAQVTDwSRPGNS-----GVPLDD------PAWETRVLPD---GEMIVR 432
Cdd:cd05935 210 PMPPAVAEkLLKLTGLRFVEGYGLTE----TMSQTHT-NPPLRPklqclGIP*FGvdarviDIETGRELPPnevGEIVVR 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 433 GPGLFIGYWNKEAET-KAALRDG---WLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALV 508
Cdd:cd05935 285 GPQIFKGYWNRPEETeESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINV-SGFKVWPAEVEAKLYKHPAI*EVCV 363
|
490 500 510
....*....|....*....|....*....|....*...
gi 981242995 509 I-------GEGRKYLTAL-----IEVDGTLAMDWARTH 534
Cdd:cd05935 364 IsvpdervGEEVKAFIVLrpeyrGKVTEEDIIEWAREQ 401
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
16-509 |
2.34e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 101.37 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIERVKNDADANAFfqrRAGawvpTTWKGYA---NAVCSVSAALGAAGVARGDRIAIMGDVSREWLiaDMATICS 92
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLL---VFG----GTRWTYAeaaRAAAAAAHALAAAGVKRGDRVALMCGNRIEFL--DVFLGCA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 93 --GAVTVGVYFTASVEEVRYYLEDSGATL--AFAGSAEQLRVMKAADTSSRLLKIVVLDPDWKRspdETGMNVVSLAEFA 168
Cdd:PRK06155 93 wlGAIAVPINTALRGPQLEHILRNSGARLlvVEAALLAALEAADPGDLPLPAVWLLDAPASVSV---PAGWSTAPLPPLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 169 SHFDGDEVaylreqselaRPTDLVSLGYTSGTTGAPKGAMLTHVSMlagaFTWPTFCPAILSEPQRMVIH--LPLSHTVA 246
Cdd:PRK06155 170 APAPAAAV----------QPGDTAAILYTSGTTGPSKGVCCPHAQF----YWWGRNSAEDLEIGADDVLYttLPLFHTNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 247 riQATTLPLIaktvpyfvdvsadfakciqeVRPTSYMAPPRFyqkfatqiinHVNGSSEAERRN---YTLALGIAREVLa 323
Cdd:PRK06155 236 --LNAFFQAL--------------------LAGATYVLEPRF----------SASGFWPAVRRHgatVTYLLGAMVSIL- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 324 DRQDAGTGDpfKEQlyaicRERVfkpllarigfddlrypytASAP-VPPEVVTLF-QLWGVNLKENYGQTEMvggNLAQV 401
Cdd:PRK06155 283 LSQPARESD--RAH-----RVRV------------------ALGPgVPAALHAAFrERFGVDLLDGYGSTET---NFVIA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 402 TDWS--RPGNSGVPLddPAWETRV-------LPD---GEMIVRG--PGLFI-GYWNKEAETKAALRDGWLYTGDIVDVGA 466
Cdd:PRK06155 335 VTHGsqRPGSMGRLA--PGFEARVvdehdqeLPDgepGELLLRAdePFAFAtGYFGMPEKTVEAWRNLWFHTGDRVVRDA 412
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 981242995 467 DGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI 509
Cdd:PRK06155 413 DGWFRFVDRIKDAIRR-RGENISSFEVEQVLLSHPAVAAAAVF 454
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
46-510 |
3.66e-22 |
|
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: 99.45 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSA 125
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 EQLRVMKAadtssrllkiVVLDPDWKRSPDETgmnvvslaEFASHFDGDevaylreqselarptDLVSLGYTSGTTGAPK 205
Cdd:TIGR01923 81 LEEKDFQA----------DSLDRIEAAGRYET--------SLSASFNMD---------------QIATLMFTSGTTGKPK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 206 GAMLTHVSMLAGAFTWPTFCPAilSEPQRMVIHLPLSHtVARIQATTLPLIAKTVPYFVDVSADFAKCIqevrptsymap 285
Cdd:TIGR01923 128 AVPHTFRNHYASAVGSKENLGF--TEDDNWLLSLPLYH-ISGLSILFRWLIEGATLRIVDKFNQLLEMI----------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 286 prfyqkfATQIINHVNgsseaerrnytlalgiarevladrqdagtgdPFKEQLYAICRERVFKPLLARIgfddlrypYTA 365
Cdd:TIGR01923 194 -------ANERVTHIS-------------------------------LVPTQLNRLLDEGGHNENLRKI--------LLG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 366 SAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSR-PGNSGVPLddPAWETRVLPD-----GEMIVRGPGLFIG 439
Cdd:TIGR01923 228 GSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEMLHaRPDVGRPL--AGREIKIKVDnkeghGEIMVKGANLMKG 305
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981242995 440 YWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:TIGR01923 306 YLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVVP 375
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
45-510 |
7.61e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 99.24 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 45 TTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAV--TVGVYFtaSVEEVRYYLEDSGATLAFA 122
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlhTINPRL--FPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 123 GSAEQLRVMKAADTSSRLLKIVVLDPDWKRsPDETGMNVVSLAEFASHFDGDEVAYlrEQSElarpTDLVSLGYTSGTTG 202
Cdd:cd12119 104 DRDFLPLLEAIAPRLPTVEHVVVMTDDAAM-PEPAGVGVLAYEELLAAESPEYDWP--DFDE----NTAAAICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 203 APKGAMLTHvsmlagaftwptfcpailsepqRMVIHlplsHTVARIQATTLPLIAKTVpyfvdvsadfakciqevrptsY 282
Cdd:cd12119 177 NPKGVVYSH----------------------RSLVL----HAMAALLTDGLGLSESDV---------------------V 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 283 MaP--PRFyqkfatqiinHVNGSSEAerrnYTLALGIAREVLADRQDAGtgdpfKEQLYAICRERV------------FK 348
Cdd:cd12119 210 L-PvvPMF----------HVNAWGLP----YAAAMVGAKLVLPGPYLDP-----ASLAELIEREGVtfaagvptvwqgLL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 349 PLLARIGFDD--LRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEM--VG---------GNLAQVTDWSRPGNSGVPL- 414
Cdd:cd12119 270 DHLEANGRDLssLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETspLGtvarppsehSNLSEDEQLALRAKQGRPVp 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 415 -------DDpawETRVLP-D----GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINT 482
Cdd:cd12119 350 gvelrivDD---DGRELPwDgkavGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKS 426
|
490 500
....*....|....*....|....*...
gi 981242995 483 aAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd12119 427 -GGEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
61-562 |
7.85e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 99.57 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 61 LGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLA-----FAGSAEQLrvmkAAD 135
Cdd:PRK08751 68 LGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvidnFGTTVQQV----IAD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 136 TSSRLLKIVVLDpDWKRSPDETGMNVV--SLAEFASHFDGDEVAYLREQSELAR----------PTDLVSLGYTSGTTGA 203
Cdd:PRK08751 144 TPVKQVITTGLG-DMLGFPKAALVNFVvkYVKKLVPEYRINGAIRFREALALGRkhsmptlqiePDDIAFLQYTGGTTGV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 204 PKGAMLTHVSMLAG---AFTWPTFCPAILSEPQRMVIHLPLSHTVArIQATTLpliaktvpyfvdVSADFAKCiqevrpT 280
Cdd:PRK08751 223 AKGAMLTHRNLVANmqqAHQWLAGTGKLEEGCEVVITALPLYHIFA-LTANGL------------VFMKIGGC------N 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 281 SYMAPPRFYQKFAtqiinhvngsSEAERRNYTLALGIarevladrqdagtgdpfkeqlyaicrERVFKPLLARIGFDD-- 358
Cdd:PRK08751 284 HLISNPRDMPGFV----------KELKKTRFTAFTGV--------------------------NTLFNGLLNTPGFDQid 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 359 ---LRYPYTASAPVPPEVVTLF-QLWGVNLKENYGQTEMVGG---NLAQVTDWSrpGNSGVPL--------DDpawETRV 423
Cdd:PRK08751 328 fssLKMTLGGGMAVQRSVAERWkQVTGLTLVEAYGLTETSPAaciNPLTLKEYN--GSIGLPIpstdacikDD---AGTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 424 LPDGEM---IVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQ 499
Cdd:PRK08751 403 LAIGEIgelCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAM 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981242995 500 SPYITEALVIG-----EGRKYLTALIEVDGTLAMDWARTH-DPSVTQYadlaSSPPVIDLiREEVEKAN 562
Cdd:PRK08751 482 MPGVLEVAAVGvpdekSGEIVKVVIVKKDPALTAEDVKAHaRANLTGY----KQPRIIEF-RKELPKTN 545
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
65-510 |
2.34e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 97.83 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 65 GVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATL-----AFAGSAEQLRvmkaADTSSR 139
Cdd:PRK08008 58 GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLlvtsaQFYPMYRQIQ----QEDATP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 LLKIVVLDPDwkrSPDETGmnvvslaefASHFD---GDEVAYLREQSELArPTDLVSLGYTSGTTGAPKGAMLTHVSML- 215
Cdd:PRK08008 134 LRHICLTRVA---LPADDG---------VSSFTqlkAQQPATLCYAPPLS-TDDTAEILFTSGTTSRPKGVVITHYNLRf 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 216 AGAFT-WPTfcpaILSEPQRMVIHLPLSH-----TVARIQAT---TLPLIAKtvpYfvdvSAD-FAKCIQEVRPTSYMAP 285
Cdd:PRK08008 201 AGYYSaWQC----ALRDDDVYLTVMPAFHidcqcTAAMAAFSagaTFVLLEK---Y----SARaFWGQVCKYRATITECI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 286 PRFYQKFATQiinhvngSSEAERRNYTLalgiaREV-----LADRQDagtgDPFKEQlyaicrervfkpllarigfddlr 360
Cdd:PRK08008 270 PMMIRTLMVQ-------PPSANDRQHCL-----REVmfylnLSDQEK----DAFEER----------------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 361 ypytasapvppevvtlfqlWGVNLKENYGQTEMVGGNL----AQVTDW---SRPG---------NSGVPLddPAWETrvl 424
Cdd:PRK08008 311 -------------------FGVRLLTSYGMTETIVGIIgdrpGDKRRWpsiGRPGfcyeaeirdDHNRPL--PAGEI--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 425 pdGEMIVRG-PG--LFIGYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQS 500
Cdd:PRK08008 367 --GEICIKGvPGktIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKR-GGENVSCVELENIIATH 443
|
490
....*....|
gi 981242995 501 PYITEALVIG 510
Cdd:PRK08008 444 PKIQDIVVVG 453
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
49-510 |
2.75e-21 |
|
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: 97.16 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 49 GYANAVCSVsaALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFagsaeql 128
Cdd:cd05958 18 ALANRIANV--LVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 129 rvmkaadtssrllkivvldpdwkrspdetgmnvvsLAEFASHFDgdevaylreqselarptDLVSLGYTSGTTGAPKGAM 208
Cdd:cd05958 89 -----------------------------------CAHALTASD-----------------DICILAFTSGTTGAPKATM 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 209 LTHVSMLAGAFTWPtfcPAIL--SEPQRMVIHLPLSHTVARIQATTLPLI--AKTVPYFVDVSADFAKCIQEVRPTSYMA 284
Cdd:cd05958 117 HFHRDPLASADRYA---VNVLrlREDDRFVGSPPLAFTFGLGGVLLFPFGvgASGVLLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 285 PPRFYqkfatqiinhvngsseaerrnytlalgiaREVLADRQDAGtgdpfkeqlyaicrervfkPLLArigfdDLRYPYT 364
Cdd:cd05958 194 APTAY-----------------------------RAMLAHPDAAG-------------------PDLS-----SLRKCVS 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 365 ASAPVPPEvvtLFQLW----GVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRV-------LPDGEM---I 430
Cdd:cd05958 221 AGEALPAA---LHRAWkeatGIPIIDGIGSTEMFHIFISARPGDARPGATGKPV--PGYEAKVvddegnpVPDGTIgrlA 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 431 VRGPglfIGYW-NKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVI 509
Cdd:cd05958 296 VRGP---TGCRyLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMI-VSGGYNIAPPEVEDVLLQHPAVAECAVV 371
|
.
gi 981242995 510 G 510
Cdd:cd05958 372 G 372
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
190-510 |
5.44e-21 |
|
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: 94.49 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 190 DLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFcpAILSEPQRMVIHLPLSHTVARIQATTLPLI--AKTVPYFV-DV 266
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADC--ADLTEDDRYLIINPFFHTFGYKAGIVACLLtgATVVPVAVfDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 267 SAdFAKCIQEVRPTSYMAPPRFYQkfatQIINHvngsseAERRNYTLAlgiarevladrqdagtgdpfkeqlyaicrerv 346
Cdd:cd17638 79 DA-ILEAIERERITVLPGPPTLFQ----SLLDH------PGRKKFDLS-------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 347 fkpllarigfdDLRYPYTASAPVPPEVVTLFQ--LWGVNLKENYGQTEMVGGNLaqvtdwSRPGNSGVPLDD------PA 418
Cdd:cd17638 116 -----------SLRAAVTGAATVPVELVRRMRseLGFETVLTAYGLTEAGVATM------CRPGDDAETVATtcgracPG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 419 WETRVLPDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENEL 497
Cdd:cd17638 179 FEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGAL 257
|
330
....*....|...
gi 981242995 498 RQSPYITEALVIG 510
Cdd:cd17638 258 AEHPGVAQVAVIG 270
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
16-510 |
5.85e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 97.05 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIERVKNDADANAFFQRRAGAWVPT--TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSG 93
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAVRLGTGAPRrfTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 94 AVTVGVYFTASVEEVRYYLEDSGATLA----------FAGSAEQLRVMKAAdtssrLLKIVVLD-------------PDW 150
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLvvpktfrgfdHAAMARRLRPELPA-----LRHVVVVGgdgadsfeallitPAW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 151 KRSPDETGMnvvslaeFASHFDGdevaylreqselarPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGaftwptfcpaILS 230
Cdd:PRK13295 180 EQEPDAPAI-------LARLRPG--------------PDDVTQLIYTSGTTGEPKGVMHTANTLMAN----------IVP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 231 EPQRM------VIHL--PLSHTVARIQATTLPLIAKTVPYFVDV--SADFAKCIQEVRPTSYMAPPRFyqkfatqiinhv 300
Cdd:PRK13295 229 YAERLglgaddVILMasPMAHQTGFMYGLMMPVMLGATAVLQDIwdPARAAELIRTEGVTFTMASTPF------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 301 ngsseaerrnytlALGIAREVLADRQDAGTGDPFkeqlyaICrervfkpllarigfddlrypytASAPVPPEVV-TLFQL 379
Cdd:PRK13295 297 -------------LTDLTRAVKESGRPVSSLRTF------LC----------------------AGAPIPGALVeRARAA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 380 WGVNLKENYGQTE---MVGGNLAQVTDwsRPGNS-GVPLddPAWETRV-------LPDGE---MIVRGPGLFIGYWnKEA 445
Cdd:PRK13295 336 LGAKIVSAWGMTEngaVTLTKLDDPDE--RASTTdGCPL--PGVEVRVvdadgapLPAGQigrLQVRGCSNFGGYL-KRP 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 446 ETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK13295 411 QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVA 474
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
16-510 |
6.96e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 96.80 E-value: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIERVKNDADANAFFQRRAGA-WvptTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGA 94
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYRDQGLrW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 95 VTVGV---YFTAsveEVRYYLEDSGA-TLAFAGS-------------AEQLRVMKA-ADTSSRL--LKIVV-LDPDWKRs 153
Cdd:PRK08315 94 ILVTInpaYRLS---ELEYALNQSGCkALIAADGfkdsdyvamlyelAPELATCEPgQLQSARLpeLRRVIfLGDEKHP- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 154 pdetGM-NVVSLAEFASHFDGDEVAylREQSELaRPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFtWPTFCPAiLSEP 232
Cdd:PRK08315 170 ----GMlNFDELLALGRAVDDAELA--ARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNNGY-FIGEAMK-LTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 233 QRMVIHLPLSH-----------------TVARIQA----TTLPLIAK---TVPYFVdvsadfakciqevrPTSYMApprf 288
Cdd:PRK08315 241 DRLCIPVPLYHcfgmvlgnlacvthgatMVYPGEGfdplATLAAVEEercTALYGV--------------PTMFIA---- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 289 yqkfatqIINHvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyaicrervfkPLLARIGFDDLRYPYTASAP 368
Cdd:PRK08315 303 -------ELDH-------------------------------------------------PDFARFDLSSLRTGIMAGSP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 369 VPPE----VVTLFqlwgvNLKE---NYGQTEmvggnlaqvtdwSRPGNSGVPLDDPA---WET--RVLPD---------- 426
Cdd:PRK08315 327 CPIEvmkrVIDKM-----HMSEvtiAYGMTE------------TSPVSTQTRTDDPLekrVTTvgRALPHlevkivdpet 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 ---------GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENE 496
Cdd:PRK08315 390 getvprgeqGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF 468
|
570
....*....|....
gi 981242995 497 LRQSPYITEALVIG 510
Cdd:PRK08315 469 LYTHPKIQDVQVVG 482
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
190-524 |
2.22e-20 |
|
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: 92.39 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 190 DLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPaiLSEPQRMVIHLPLSHtVARIQATTLPLIAKTVPYFVDVSAD 269
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG--FGGGDSWLLSLPLYH-VGGLAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 270 FAKCIQEVRPTSYMAPPrfyqkfaTQIinhvngsseaerrnytlalgiaREVLADRQDAGTGDPFKEQLyaicrervfkp 349
Cdd:cd17630 78 LAEDLAPPGVTHVSLVP-------TQL----------------------QRLLDSGQGPAALKSLRAVL----------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 350 llarIGfddlrypytaSAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPDGEM 429
Cdd:cd17630 118 ----LG----------GAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLL--PGRELRIVEDGEI 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 430 IVRGPGLFIGYWNKEaETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI 509
Cdd:cd17630 182 WVGGASLAMGYLRGQ-LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAHPAVRDAFVV 259
|
330
....*....|....*....
gi 981242995 510 GEG-RKY---LTALIEVDG 524
Cdd:cd17630 260 GVPdEELgqrPVAVIVGRG 278
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
59-510 |
2.48e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 95.11 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 59 AALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATL-----AFAGSAEQLR---- 129
Cdd:PRK06178 73 ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVllaldQLAPVVEQVRaets 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 130 -----VMKAADTSSRLLKIVVldPDWKRSPDETgmnVVSLAEFASHFDGDEVAYLREQSELarpTDLVSLGYTSGTTGAP 204
Cdd:PRK06178 153 lrhviVTSLADVLPAEPTLPL--PDSLRAPRLA---AAGAIDLLPALRACTAPVPLPPPAL---DALAALNYTGGTTGMP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSMLagaFTWPTFCPA--ILSEPQRMVIHLP--------LSHTVARIQATTLPLIAKTvpyfvDVSAdFAKCI 274
Cdd:PRK06178 225 KGCEHTQRDMV---YTAAAAYAVavVGGEDSVFLSFLPefwiagenFGLLFPLFSGATLVLLARW-----DAVA-FMAAV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 275 QEVRPTS----------YMAPPRFYQkFATQIINHVNGSS-------EAERRNYTLALGIAREVLADRQDAGTGDPFKEq 337
Cdd:PRK06178 296 ERYRVTRtvmlvdnaveLMDHPRFAE-YDLSSLRQVRVVSfvkklnpDYRQRWRALTGSVLAEAAWGMTETHTCDTFTA- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 338 lyaicrervfkpllariGFD----DLRY-PYTASAPVPpevvtlfqlwGVNLKenygqtemvggnlaqVTDWsrpgNSGV 412
Cdd:PRK06178 374 -----------------GFQdddfDLLSqPVFVGLPVP----------GTEFK---------------ICDF----ETGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 413 PLddPAWETrvlpdGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQ 492
Cdd:PRK06178 408 LL--PLGAE-----GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSE 479
|
490
....*....|....*...
gi 981242995 493 IENELRQSPYITEALVIG 510
Cdd:PRK06178 480 VEALLGQHPAVLGSAVVG 497
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
15-510 |
5.93e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 93.65 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 15 TTIPALLIERVKNDADANAFFQRRagawVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGA 94
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALIDED----RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 95 VTVGVYFTASVEEVRYYLEDSGAT-LAFAGSAEQL---RVMKAADTSS--RLLKIVVLDPDWKRSPDETGMNVVSLAEFA 168
Cdd:PRK06164 86 TVIAVNTRYRSHEVAHILGRGRARwLVVWPGFKGIdfaAILAAVPPDAlpPLRAIAVVDDAADATPAPAPGARVQLFALP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 169 shfDGDEVAYLREqsELARPTDLVSLGYTSGTTGAPK------GAMLTHVSMLAGAFTwptfcpaiLSEPQRMVIHLPLS 242
Cdd:PRK06164 166 ---DPAPPAAAGE--RAADPDAGALLFTTSGTTSGPKlvlhrqATLLRHARAIARAYG--------YDPGAVLLAALPFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 243 HTVAriQATTLPLIAKTVPYFVDVSADFAKCIQEVRptsymapprfyqkfaTQIINHVNGSSEAERRnytlalgIAREvl 322
Cdd:PRK06164 233 GVFG--FSTLLGALAGGAPLVCEPVFDAARTARALR---------------RHRVTHTFGNDEMLRR-------ILDT-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 323 adrqdAGTGDPFkeqlyaicrervfkPLLARIGFDDLrypytasAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNLAQ-- 400
Cdd:PRK06164 287 -----AGERADF--------------PSARLFGFASF-------APALGELAALARARGVPLTGLYGSSEVQALVALQpa 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 401 VTDWSRPGNSGVPLDDPAWETRV--------LPD---GEMIVRGPGLFIGYW-NKEAETKAALRDGWLYTGDIVDVGADG 468
Cdd:PRK06164 341 TDPVSVRIEGGGRPASPEARVRArdpqdgalLPDgesGEIEIRAPSLMRGYLdNPDATARALTDDGYFRTGDLGYTRGDG 420
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 981242995 469 SYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK06164 421 QFVYQTRMGDSLRL-GGFLVNPAEIEHALEALPGVAAAQVVG 461
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
43-497 |
1.13e-19 |
|
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: 92.39 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 43 VPTTWKGYANAVCSVSAALgAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFA 122
Cdd:cd05909 6 TSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 123 GSA--EQLRVMKAADTSSRLlKIVVLDpDWKrspdetgmNVVSLAE----FASHFDGDEVAYLREQSELARPTDLVSLGY 196
Cdd:cd05909 85 SKQfiEKLKLHHLFDVEYDA-RIVYLE-DLR--------AKISKADkckaFLAGKFPPKWLLRIFGVAPVQPDDPAVILF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGAMLTHVSMLAGAFTWPTFCPAilSEPQRMVIHLPLSH----TVARIQATTL---------PLIAKTVPYF 263
Cdd:cd05909 155 TSGSEGLPKGVVLSHKNLLANVEQITAIFDP--NPEDVVFGALPFFHsfglTGCLWLPLLSgikvvfhpnPLDYKKIPEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 264 VDvsadfakciqEVRPTSYMAPPRFYqkfaTQIINHVNgsseaerrnytlalgiarevladrqdagtgdpfKEQLYAicr 343
Cdd:cd05909 233 IY----------DKKATILLGTPTFL----RGYARAAH---------------------------------PEDFSS--- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 344 ervfkpllarigfddLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEM---VGGNLAQVTdwSRPGNSGVPLddPAW 419
Cdd:cd05909 263 ---------------LRLVVAGAEKLKDTLRQEFQeKFGIRILEGYGTTECspvISVNTPQSP--NKEGTVGRPL--PGM 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 420 ETRVLP-----------DGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSI 488
Cdd:cd05909 324 EVKIVSvetheevpigeGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKI-AGEMV 402
|
....*....
gi 981242995 489 SPVQIENEL 497
Cdd:cd05909 403 SLEAIEDIL 411
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
53-510 |
2.66e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 91.41 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 53 AVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAeqlrvMK 132
Cdd:PRK09088 31 LVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA-----VA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 133 AAdtssrllkivvldpdwkrspdetGMNVVSLAEFASHFDGDEVAYLReqselARPTDLVSL-GYTSGTTGAPKGAMLTH 211
Cdd:PRK09088 106 AG-----------------------RTDVEDLAAFIASADALEPADTP-----SIPPERVSLiLFTSGTSGQPKGVMLSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 212 VSMLAGAFTWPTFcpAILSEPQRMVIHLPLSHTVAriqattlpliaktvpyfvdvsadfakCIQEVRPTsymapprFYQK 291
Cdd:PRK09088 158 RNLQQTAHNFGVL--GRVDAHSSFLCDAPMFHIIG--------------------------LITSVRPV-------LAVG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 292 FATQIINhvngSSEAERRNYTLalgiarevladrqdagtGDPFKEQLYAICRERVFKPLLARIGFD-----DLRYPYTAS 366
Cdd:PRK09088 203 GSILVSN----GFEPKRTLGRL-----------------GDPALGITHYFCVPQMAQAFRAQPGFDaaalrHLTALFTGG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 367 APVPPEVVTLFQLWGVNLKENYGQTEmVGGNLAQVTDW----SRPGNSGVPLddPAWETRVLPD----------GEMIVR 432
Cdd:PRK09088 262 APHAAEDILGWLDDGIPMVDGFGMSE-AGTVFGMSVDCdvirAKAGAAGIPT--PTVQTRVVDDqgndcpagvpGELLLR 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 981242995 433 GPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK09088 339 GPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
46-510 |
2.99e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 91.26 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGAT--LAFAG 123
Cdd:PRK07470 34 TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARamICHAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 124 SAEQLRVMKAAdtssrllkivvldpdwkrSPDETGMNVVSLAEFASHFDgdevAYLREQSELARPTDLVS------LGYT 197
Cdd:PRK07470 114 FPEHAAAVRAA------------------SPDLTHVVAIGGARAGLDYE----ALVARHLGARVANAAVDhddpcwFFFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 198 SGTTGAPKGAMLTHVSM-------LAGAFtwptfcPAiLSEPQRMVIHLPLSH--------TVARIQATTLPLIAKTVPy 262
Cdd:PRK07470 172 SGTTGRPKAAVLTHGQMafvitnhLADLM------PG-TTEQDASLVVAPLSHgagihqlcQVARGAATVLLPSERFDP- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 263 fvdvsADFAKCIQEVRPTSYMAPPrfyqkfatqiinhvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyAIC 342
Cdd:PRK07470 244 -----AEVWALVERHRVTNLFTVP-----------------------------------------------------TIL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 343 RERVFKPLLARIGFDDLRYPYTASAPVPPE--VVTLFQLwGVNLKENYGQTEmVGGNLAQVT---------DWSRPGNSG 411
Cdd:PRK07470 266 KMLVEHPAVDRYDHSSLRYVIYAGAPMYRAdqKRALAKL-GKVLVQYFGLGE-VTGNITVLPpalhdaedgPDARIGTCG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 412 VP--------LDD-----PAWETrvlpdGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKE 478
Cdd:PRK07470 344 FErtgmevqiQDDegrelPPGET-----GEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASD 418
|
490 500 510
....*....|....*....|....*....|..
gi 981242995 479 LInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK07470 419 MY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
56-510 |
3.51e-19 |
|
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: 90.64 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 56 SVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGAtlafagsaeqlrvmkaad 135
Cdd:cd05969 12 RFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEA------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 136 tssrllKIVVLDPDWKRSPDetgmnvvslaefashfdgdevaylreqselarPTDLVSLGYTSGTTGAPKGAMLTHVSML 215
Cdd:cd05969 74 ------KVLITTEELYERTD--------------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 216 AGAFT-------------WPTFCPAILSepqrmvihlplsHTVARIQATTLpliaKTVPYFVDvSADFAkciqevrptsy 282
Cdd:cd05969 116 FYYFTgkyvldlhpddiyWCTADPGWVT------------GTVYGIWAPWL----NGVTNVVY-EGRFD----------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 283 maPPRFYqkfatqiinhvnGSSEAERRN--YTLALGIarevladRQDAGTGDPfkeqlyaicrervfkpLLARIGFDDLR 360
Cdd:cd05969 168 --AESWY------------GIIERVKVTvwYTAPTAI-------RMLMKEGDE----------------LARKYDLSSLR 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 361 YPYTASAPVPPEVVTlfqlWGVN-----LKENYGQTEMVGGNLAQ-VTDWSRPGNSGVPLddPAWETRV-------LPDG 427
Cdd:cd05969 211 FIHSVGEPLNPEAIR----WGMEvfgvpIHDTWWQTETGSIMIANyPCMPIKPGSMGKPL--PGVKAAVvdengneLPPG 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 428 EM----IVRG-PGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPY 502
Cdd:cd05969 285 TKgilaLKPGwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPA 363
|
....*...
gi 981242995 503 ITEALVIG 510
Cdd:cd05969 364 VAEAGVIG 371
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
388-510 |
3.64e-19 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 89.25 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 388 YGQTEMVG-GNLAQVTDwsRPGNSGVPL--------DDPAWETRVLPDGEMIVRGPGLFIGYWNKEAETKAALRDGWLYT 458
Cdd:cd17637 143 YGQTETSGlVTLSPYRE--RPGSAGRPGplvrvrivDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHT 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 981242995 459 GDIVDVGADGSYKLIDRK--KELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVEKVILEHPAIAEVCVIG 273
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
61-510 |
4.81e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 90.73 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 61 LGAAGVARGDRIAIMGDVSrewliADMATICSGAVTVGVYFTA-----SVEEVRYYLEDSGATlAFAGSAEQLRVMKAAd 135
Cdd:PRK08276 28 LRALGLREGDVVAILLENN-----PEFFEVYWAARRSGLYYTPinwhlTAAEIAYIVDDSGAK-VLIVSAALADTAAEL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 136 tssrllkivvldpdwkrsPDETGMNVVSLAEFASHFDGDE--VAYLREQSelARPTDLVSLG----YTSGTTGAPKGAM- 208
Cdd:PRK08276 101 ------------------AAELPAGVPLLLVVAGPVPGFRsyEEALAAQP--DTPIADETAGadmlYSSGTTGRPKGIKr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 209 -LTHV-------SMLAGAFTWPTFCPAilsepqrmVIHL---PLSHTvariqattlpliaktvpyfvdvsadfakciqev 277
Cdd:PRK08276 161 pLPGLdpdeapgMMLALLGFGMYGGPD--------SVYLspaPLYHT--------------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 278 rptsymAPPRFYQKfatqiinhvngsseaerrnyTLALGIaREVLADRQDAgtgdpfKEQLYAICRERV---------FK 348
Cdd:PRK08276 200 ------APLRFGMS--------------------ALALGG-TVVVMEKFDA------EEALALIERYRVthsqlvptmFV 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 349 PLLA-----RIGFD--DLRYPYTASAPVPPEV-VTLFQLWGVNLKENYGQTEMVGGNLAQVTDW-SRPGNSGVPLDDpaw 419
Cdd:PRK08276 247 RMLKlpeevRARYDvsSLRVAIHAAAPCPVEVkRAMIDWWGPIIHEYYASSEGGGVTVITSEDWlAHPGSVGKAVLG--- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 420 ETRVLPD----------GEMIVRGPGLFIGYWNKEAETKAALRD-GWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSI 488
Cdd:PRK08276 324 EVRILDEdgnelppgeiGTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVNI 402
|
490 500
....*....|....*....|..
gi 981242995 489 SPVQIENELRQSPYITEALVIG 510
Cdd:PRK08276 403 YPQEIENLLVTHPKVADVAVFG 424
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
188-511 |
2.34e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 89.39 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 188 PTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFtwPTFCPAILSE--PQRMVIHLPLSHTVARIQA-------TTLPLIAK 258
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVV--PLCKHSIFKKynPKTHLSYLPISHIYERVIAylsfmlgGTINIWSK 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 259 TVPYFvdvSADFAKCIQEVrptsyMAP-PRFYQKFATQIINHVNGSSEAERRnytlalgIAREVLADRQ--DAGTGDPFK 335
Cdd:PTZ00342 381 DINYF---SKDIYNSKGNI-----LAGvPKVFNRIYTNIMTEINNLPPLKRF-------LVKKILSLRKsnNNGGFSKFL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 336 EQLYAIC---RERVfKPLLARIgfddlrypYTASAPVPPEVVT-LFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSG 411
Cdd:PTZ00342 446 EGITHISskiKDKV-NPNLEVI--------LNGGGKLSPKIAEeLSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIG 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 412 VPLDdP-------AWETR----VLPDGEMIVRGPGLFIGYW-NKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKEL 479
Cdd:PTZ00342 517 GPIS-PntkykvrTWETYkatdTLPKGELLIKSDSIFSGYFlEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGL 595
|
330 340 350
....*....|....*....|....*....|..
gi 981242995 480 INTAAGKSISPVQIENELRQSPYITEALVIGE 511
Cdd:PTZ00342 596 VKLSQGEYIETDMLNNLYSQISFINFCVVYGD 627
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
45-601 |
4.07e-18 |
|
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: 87.10 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 45 TTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATlafags 124
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 125 aeqlrvmkaadtssrllkIVVLDpdwkrspdetgmnvvslaefashfDGDEVAYLReqselarptdlvslgYTSGTTGAP 204
Cdd:cd05971 81 ------------------ALVTD------------------------GSDDPALII---------------YTSGTTGPP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSMLAgaftwptfcpailsepqrmviHLP---LSHTVARIQATTlpliaktvpYFVdvSADFA---KCIQEVR 278
Cdd:cd05971 104 KGALHAHRVLLG---------------------HLPgvqFPFNLFPRDGDL---------YWT--PADWAwigGLLDVLL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 279 PTSYMAPP-------RFYQKFATQIInhvngsseaERRNYTL------ALGIAREVLADRQDAGT--------GDPFKEQ 337
Cdd:cd05971 152 PSLYFGVPvlahrmtKFDPKAALDLM---------SRYGVTTaflpptALKMMRQQGEQLKHAQVklraiatgGESLGEE 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 338 LYAICRERvfkpllarigfddlrypytasapvppevvtlfqlWGVNLKENYGQTE--MVGGNLAQVTDwSRPGNSGVP-- 413
Cdd:cd05971 223 LLGWAREQ----------------------------------FGVEVNEFYGQTEcnLVIGNCSALFP-IKPGSMGKPip 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 414 ------LDDPAweTRVLPD--GEMIVRGPG--LFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTa 483
Cdd:cd05971 268 ghrvaiVDDNG--TPLPPGevGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS- 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 484 AGKSISPVQIENELRQSPYITEALVIGegrkyltalievdgtlAMDWARTHdpSVTQYADLASSPPVIDLIREEV-EKAN 562
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVG----------------IPDPIRGE--IVKAFVVLNPGETPSDALAREIqELVK 406
|
570 580 590
....*....|....*....|....*....|....*....
gi 981242995 563 ARLARAEQIKAFrIFPEELTpengvMTATRKKRRKALMA 601
Cdd:cd05971 407 TRLAAHEYPREI-EFVNELP-----RTATGKIRRRELRA 439
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
63-508 |
1.54e-17 |
|
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: 85.01 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 63 AAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAAdtssrlLK 142
Cdd:TIGR01733 19 AGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLV------LP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 143 IVVLDPDWkrSPDETGMNVVSLAEFASHfdGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSMLagAFTWP 222
Cdd:TIGR01733 93 VILLDPLE--LAALDDAPAPPPPDAPSG--PDDLAYVI---------------YTSGSTGRPKGVVVTHRSLV--NLLAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 223 TFCPAILSEPQRMVIHLPLSHTVARIQ-ATTLPLIAKTVPYFVDVSADFAKCIQEV---RPTSYM-APPRFYQKFAtqii 297
Cdd:TIGR01733 152 LARRYGLDPDDRVLQFASLSFDASVEEiFGALLAGATLVVPPEDEERDDAALLAALiaeHPVTVLnLTPSLLALLA---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 298 nhvngsSEAERRNYTLalgiaREVLAdrqdagTGDPFKEQLYAICRERVfkpllarigfddlrypytasapvppEVVTLF 377
Cdd:TIGR01733 228 ------AALPPALASL-----RLVIL------GGEALTPALVDRWRARG-------------------------PGARLI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 378 QLwgvnlkenYGQTE---MVGGNL--AQVTDWSRPGNSGVPLDD-PAW----ETRVLPD---GEMIVRGPGLFIGYWNKE 444
Cdd:TIGR01733 266 NL--------YGPTEttvWSTATLvdPDDAPRESPVPIGRPLANtRLYvlddDLRPVPVgvvGELYIGGPGVARGYLNRP 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981242995 445 AETK--------AALRDGWLY-TGDIVDVGADGSYKLIDRK----KelINtaaGKSISPVQIENELRQSPYITEALV 508
Cdd:TIGR01733 338 ELTAerfvpdpfAGGDGARLYrTGDLVRYLPDGNLEFLGRIddqvK--IR---GYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
46-529 |
3.15e-17 |
|
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: 84.50 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLafagsa 125
Cdd:cd05930 14 TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 eqlrvmkaadtssrllkivVLDpdwkrspdetgmnvvslaefashfDGDEVAYLReqselarptdlvslgYTSGTTGAPK 205
Cdd:cd05930 88 -------------------VLT------------------------DPDDLAYVI---------------YTSGSTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 206 GAMLTH---VSMLAGA-FTWPtfcpaiLSEPQRMVIHLPLSHTVArIQATTLPLIA-KTVpYFVDVSADFAkciqevrpt 280
Cdd:cd05930 110 GVMVEHrglVNLLLWMqEAYP------LTPGDRVLQFTSFSFDVS-VWEIFGALLAgATL-VVLPEEVRKD--------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 281 symaPPRFYQKFATQIINHVNGsseaerrnyTLALgiAREVLADRQDAGtgdpfkeqlyaicrervfkpllarigFDDLR 360
Cdd:cd05930 173 ----PEALADLLAEEGITVLHL---------TPSL--LRLLLQELELAA--------------------------LPSLR 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 361 YPYTASAPVPPEVVTLFQLWGVNLK-EN-YGQTEMVGGNLAQVTDWSRPGNSGVPLDDPAWETRV---------LPD--- 426
Cdd:cd05930 212 LVLVGGEALPPDLVRRWRELLPGARlVNlYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVyvldenlrpVPPgvp 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAALRD------GWLY-TGDIVDVGADGSYKLIDRK----KelINtaaGKSISPVQIEN 495
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERFVPnpfgpgERMYrTGDLVRWLPDGNLEFLGRIddqvK--IR---GYRIELGEIEA 366
|
490 500 510
....*....|....*....|....*....|....*...
gi 981242995 496 ELRQSPYITEALVI----GEGRKYLTALIEVDGTLAMD 529
Cdd:cd05930 367 ALLAHPGVREAAVVaredGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
187-534 |
2.03e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 82.70 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 187 RPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFcpaILSEPQRMVIH-LPLSHTVARIQATTLPLI--AKTV--- 260
Cdd:PRK07529 211 GPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALL---LGLGPGDTVFCgLPLFHVNALLVTGLAPLArgAHVVlat 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 261 ------PYFVDvsaDFAKCIQEVRPTSYMAPPRFYQKFATQIINHVNGSSeaerrnytlalgiarevladrqdagtgdpf 334
Cdd:PRK07529 288 pqgyrgPGVIA---NFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISS------------------------------ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 335 keqlyaicrervfkpllarigfddLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMV-GGNLAQVTDWSRPGNSGV 412
Cdd:PRK07529 335 ------------------------LRYALCGAAPLPVEVFRRFEaATGVRIVEGYGLTEATcVSSVNPPDGERRIGSVGL 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 413 PL-----------DDPAWETRVLPD--GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKEL 479
Cdd:PRK07529 391 RLpyqrvrvvildDAGRYLRDCAVDevGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDL 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 480 InTAAGKSISPVQIENELRQSPYITEALVIGEGRKYL----TALIE-VDGTLA-----MDWARTH 534
Cdd:PRK07529 471 I-IRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAgelpVAYVQlKPGASAteaelLAFARDH 534
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
63-511 |
2.07e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 82.35 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 63 AAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLafagsaeqlrVMKAADTSSRLLK 142
Cdd:PRK07787 39 AERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQA----------WLGPAPDDPAGLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 143 IVVLDPD---WKRSPDEtgmnvvslaefashfDGDEVAylreqselarptdLVSlgYTSGTTGAPKGAMLTH------VS 213
Cdd:PRK07787 109 HVPVRLHarsWHRYPEP---------------DPDAPA-------------LIV--YTSGTTGPPKGVVLSRraiaadLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 214 MLAGAFTWptfcpailsEPQRMVIH-LPLSHTVARIQATTLPL-IAKTVPYFVDVSADFAKCIQEVRPTSYMAPPRFYQK 291
Cdd:PRK07787 159 ALAEAWQW---------TADDVLVHgLPLFHVHGLVLGVLGPLrIGNRFVHTGRPTPEAYAQALSEGGTLYFGVPTVWSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 292 FAtqiinhvnGSSEAERrnytlALGIARevladrqdagtgdpfkeqlyaicrervfkpLLArigfddlrypyTASAPVP- 370
Cdd:PRK07787 230 IA--------ADPEAAR-----ALRGAR------------------------------LLV-----------SGSAALPv 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 371 PEVVTLFQLWGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPD------------GEMIVRGPGLFI 438
Cdd:PRK07787 256 PVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPL--AGVETRLVDEdggpvphdgetvGELQVRGPTLFD 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 439 GYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKK-ELINTaAGKSISPVQIENELRQSPYITEALVIGE 511
Cdd:PRK07787 334 GYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGREStDLIKS-GGYRIGAGEIETALLGHPGVREAAVVGV 407
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
56-510 |
2.86e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 82.38 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 56 SVSAALGA----AGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLA-----FAGSAE 126
Cdd:PRK07059 56 ELSRALAAwlqsRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIvvlenFATTVQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 127 QLrvmkAADTSSR----------------LLKIVV-----LDPDWKrSPDETGMNVVsLAEFAShfdgdevayLREQSEL 185
Cdd:PRK07059 136 QV----LAKTAVKhvvvasmgdllgfkghIVNFVVrrvkkMVPAWS-LPGHVRFNDA-LAEGAR---------QTFKPVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 186 ARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAF---TWptFCPAILSEPQ----RMVIHLPLSHtvariqattlpLIAK 258
Cdd:PRK07059 201 LGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeAW--LQPAFEKKPRpdqlNFVCALPLYH-----------IFAL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 259 TVPYFVDVSA-----------DFAKCIQEVrptsymapprfyQKFATQIINHVNgsseaerrnyTLALGiarevLADRQD 327
Cdd:PRK07059 268 TVCGLLGMRTggrnilipnprDIPGFIKEL------------KKYQVHIFPAVN----------TLYNA-----LLNNPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 328 AGTGDpfkeqlyaicrervFKPLLARIGfddlrypyTASAPVPPEVVTLFQLWGVNLKENYGQTE---MVGGNLAQVTDW 404
Cdd:PRK07059 321 FDKLD--------------FSKLIVANG--------GGMAVQRPVAERWLEMTGCPITEGYGLSEtspVATCNPVDATEF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 405 SrpGNSGVPL--------DDPAWETRVLPDGEMIVRGPGLFIGYWNKEAET-KAALRDGWLYTGDIVDVGADGSYKLIDR 475
Cdd:PRK07059 379 S--GTIGLPLpstevsirDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETaKVMTADGFFRTGDVGVMDERGYTKIVDR 456
|
490 500 510
....*....|....*....|....*....|....*
gi 981242995 476 KKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK07059 457 KKDMI-LVSGFNVYPNEIEEVVASHPGVLEVAAVG 490
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
51-510 |
3.61e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 81.67 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 51 ANAVCSVSAALGAAGVARGDRIAIM--GDVSreWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATL--AFAGSAE 126
Cdd:PRK12406 18 AQRAARAAGGLAALGVRPGDCVALLmrNDFA--FFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVliAHADLLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 127 QLR-------VMKAADTSSRLLKIVVLDPDWKRSPdetgmnvvslaEFASHFDG---DEVAYlrEQSELARPTDLVslgY 196
Cdd:PRK12406 96 GLAsalpagvTVLSVPTPPEIAAAYRISPALLTPP-----------AGAIDWEGwlaQQEPY--DGPPVPQPQSMI---Y 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGA---------MLTHVSMLAGAFTwptfcpaiLSEPQRMVIHLPLSHTVAR---IQATTLPLIAKTVPYFV 264
Cdd:PRK12406 160 TSGTTGHPKGVrraaptpeqAAAAEQMRALIYG--------LKPGIRALLTGPLYHSAPNaygLRAGRLGGVLVLQPRFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 265 dvSADFAKCIQEVRPTS-YMAPPRFYqkfatqiinhvngsseaerrnytlalgiarevladrqdagtgdpfkeqlyaicr 343
Cdd:PRK12406 232 --PEELLQLIERHRITHmHMVPTMFI------------------------------------------------------ 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 344 eRVFK-PLLARIGFD--DLRYPYTASAPVPPEVV-TLFQLWGVNLKENYGQTEMVGGNLAQVTDW-SRPGNSGVP----- 413
Cdd:PRK12406 256 -RLLKlPEEVRAKYDvsSLRHVIHAAAPCPADVKrAMIEWWGPVIYEYYGSTESGAVTFATSEDAlSHPGTVGKAapgae 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 414 ---LDDpawETRVLPD---GEMIVRGPG--LFIgYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAG 485
Cdd:PRK12406 335 lrfVDE---DGRPLPQgeiGEIYSRIAGnpDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGG 409
|
490 500
....*....|....*....|....*
gi 981242995 486 KSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK12406 410 VNIYPAEIEAVLHAVPGVHDCAVFG 434
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
359-510 |
5.33e-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: 80.64 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 359 LRYPYTASAPVPPEVVTLFQL-WGVNLKENYGQTE--MVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPD-------GE 428
Cdd:cd05973 207 LRRVSSAGEPLTPEVIRWFDAaLGVPIHDHYGQTElgMVLANHHALEHPVHAGSAGRAM--PGWRVAVLDDdgdelgpGE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 429 M------IVRGPGL-FIGYWNKEaetKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSP 501
Cdd:cd05973 285 PgrlaidIANSPLMwFRGYQLPD---TPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVI-TMSGYRIGPFDVESALIEHP 360
|
....*....
gi 981242995 502 YITEALVIG 510
Cdd:cd05973 361 AVAEAAVIG 369
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
367-511 |
6.95e-16 |
|
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: 80.08 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 367 APVPPEVVTLFQLWGVNLKENYGQTEmvggNLAQVTDWS------RPGNSGVPL----------DDPAWEtrvlpDGEMI 430
Cdd:cd05912 199 GPAPKPLLEQCKEKGIPVYQSYGMTE----TCSQIVTLSpedalnKIGSAGKPLfpvelkieddGQPPYE-----VGEIL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 431 VRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05912 270 LKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGVVG 348
|
.
gi 981242995 511 E 511
Cdd:cd05912 349 I 349
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
46-509 |
9.38e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 80.38 E-value: 9.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWK-GYANAvCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGS 124
Cdd:PRK08162 45 TWAeTYARC-RRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 125 aEQLRVMKAADTSSRLLKIVVLDPDwkrSPDETGmnvvslAEFASHFDGDE-VAYLREQSELARPTD---LVSLGYTSGT 200
Cdd:PRK08162 124 -EFAEVAREALALLPGPKPLVIDVD---DPEYPG------GRFIGALDYEAfLASGDPDFAWTLPADewdAIALNYTSGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 201 TGAPKGAMLTH----VSMLAGAFTWptfcpailSEPQRMVI--HLPLSH--------TVARIQATTLpliaktvpyfvdv 266
Cdd:PRK08162 194 TGNPKGVVYHHrgayLNALSNILAW--------GMPKHPVYlwTLPMFHcngwcfpwTVAARAGTNV------------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 267 sadfakCIQEVRPTSymapprFYQKFATQIINHVNGSSeaerrnytlalgIAREVLADRQDAgtgdpfkeqlyaicrerv 346
Cdd:PRK08162 253 ------CLRKVDPKL------IFDLIREHGVTHYCGAP------------IVLSALINAPAE------------------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 347 fkpllARIGFDDLRYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGnlAQVTDWsRPGNSGVPLDDPAW------- 419
Cdd:PRK08162 291 -----WRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETYGP--ATVCAW-QPEWDALPLDERAQlkarqgv 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 420 ------ETRVL-PD------------GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELI 480
Cdd:PRK08162 363 ryplqeGVTVLdPDtmqpvpadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDII 442
|
490 500
....*....|....*....|....*....
gi 981242995 481 nTAAGKSISPVQIENELRQSPYITEALVI 509
Cdd:PRK08162 443 -ISGGENISSIEVEDVLYRHPAVLVAAVV 470
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
16-613 |
1.24e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 80.48 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIERVKNDADANAFFQRRA--GAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREwliadMATICSG 93
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIE-----HALMTLA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 94 AVTVGV--------YFTASVE--EVRYYLEDSGATLAFAGSAEQ----LRVMKAADTSsrllkIVVLDPDwkrspdETGM 159
Cdd:PRK12582 125 AMQAGVpaapvspaYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPfaraLAALDLLDVT-----VVHVTGP------GEGI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 160 NVVSLAEFASHFDGDEVAYLREQselARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAG-AFTWPTFCPAILSEPQRMVIH 238
Cdd:PRK12582 194 ASIAFADLAATPPTAAVAAAIAA---ITPDTVAKYLFTSGSTGMPKAVINTQRMMCANiAMQEQLRPREPDPPPPVSLDW 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 239 LPLSHTVARIQATTLPLIAKTVPYFVD---VSADFAKCIQ---EVRPTSYMAPPrfyqkfatqiinhvngsseaerrnyt 312
Cdd:PRK12582 271 MPWNHTMGGNANFNGLLWGGGTLYIDDgkpLPGMFEETIRnlrEISPTVYGNVP-------------------------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 313 lalgIAREVLADRQDAgtgDPfkeqlyAICReRVFKpllarigfdDLRYPYTASAPVPPEVVTLFQLWGVN-------LK 385
Cdd:PRK12582 325 ----AGYAMLAEAMEK---DD------ALRR-SFFK---------NLRLMAYGGATLSDDLYERMQALAVRttghripFY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 386 ENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPDG---EMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGD- 460
Cdd:PRK12582 382 TGYGATETAPTTTGTHWDTERVGLIGLPL--PGVELKLAPVGdkyEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDa 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 461 --IVDvGADGSYKLI--DRKKELINTAAGK--SISPVQIENELRQSPYITEALVIGEGRKYLTAL----IEVDGTLAMDw 530
Cdd:PRK12582 460 arFVD-PDDPEKGLIfdGRVAEDFKLSTGTwvSVGTLRPDAVAACSPVIHDAVVAGQDRAFIGLLawpnPAACRQLAGD- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 531 artHDPSvtqYADLASSPPVIDLIREEVEKANARLARAE-QIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIAG 609
Cdd:PRK12582 538 ---PDAA---PEDVVKHPAVLAILREGLSAHNAEAGGSSsRIARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVER 611
|
....
gi 981242995 610 LYDD 613
Cdd:PRK12582 612 LYAE 615
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
60-510 |
1.94e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 79.55 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVtVGVYFTASVEE-VRYYLEDSGATlAFAGSAEQLRVMKAADTSS 138
Cdd:PRK04319 89 VLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAI-VGPLFEAFMEEaVRDRLEDSEAK-VLITTPALLERKPADDLPS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 139 rLLKIVVLDPDwkRSPDETGMNVVSLAEFAS-HFDgdevaylreqSELARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAG 217
Cdd:PRK04319 167 -LKHVLLVGED--VEEGPGTLDFNALMEQASdEFD----------IEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQH 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 218 AFT-------------WPTFCPAILSepqrmvihlplshtvariqATTLPLIAktvPYFVDVSadfaKCIQEVRptsyMA 284
Cdd:PRK04319 234 YQTgkyvldlheddvyWCTADPGWVT-------------------GTSYGIFA---PWLNGAT----NVIDGGR----FS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 285 PPRFYQkfatqIInhvngssEAERRN--YTLALGIarevladRQDAGTGDPfkeqlyaicrervfkpLLARIGFDDLRYP 362
Cdd:PRK04319 284 PERWYR-----IL-------EDYKVTvwYTAPTAI-------RMLMGAGDD----------------LVKKYDLSSLRHI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 363 YTASAPVPPEVVTlfqlWGVN-----LKENYGQTEmVGGNL-----AQVTdwsRPGNSGVPL--------DDpawETRVL 424
Cdd:PRK04319 329 LSVGEPLNPEVVR----WGMKvfglpIHDNWWMTE-TGGIMianypAMDI---KPGSMGKPLpgieaaivDD---QGNEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 425 PDGEM----IVRG-PGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQ 499
Cdd:PRK04319 398 PPNRMgnlaIKKGwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKT-SGERVGPFEVESKLME 476
|
490
....*....|.
gi 981242995 500 SPYITEALVIG 510
Cdd:PRK04319 477 HPAVAEAGVIG 487
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
28-510 |
3.49e-15 |
|
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: 78.82 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 28 DADANAFFQRRAGAWVPTTWKGYANAVCSVSAALGAAGvARGDRIAIMGDVSREWLIADMATICSGAVTVGVYF---TAS 104
Cdd:cd05931 8 DRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPptpGRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 105 VEEVRYYLEDSGATLAF--AGSAEQLRVMKAADTSSRLLKIVVLDpdwkrSPDETGMNVVSLAEFAShfdgDEVAYLreQ 182
Cdd:cd05931 87 AERLAAILADAGPRVVLttAAALAAVRAFAASRPAAGTPRLLVVD-----LLPDTSAADWPPPSPDP----DDIAYL--Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 183 selarptdlvslgYTSGTTGAPKGAMLTH------VSMLAGAFtwptfcpaILSEPQRMVIHLPLSHTVARIQATTLPLi 256
Cdd:cd05931 156 -------------YTSGSTGTPKGVVVTHrnllanVRQIRRAY--------GLDPGDVVVSWLPLYHDMGLIGGLLTPL- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 257 aktvpyFVDVSADFakciqevrptsyMAPPRFYQKFATQIinhvngsseaerrnytlalgiarEVLADRQDAGTGDP-FK 335
Cdd:cd05931 214 ------YSGGPSVL------------MSPAAFLRRPLRWL-----------------------RLISRYRATISAAPnFA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 336 eqlYAICRERVFKPLLARIGFDDLRYPYTASAPVPPEVVTLFQ--LWGVNLKEN-----YGQTE---MVGG--------- 396
Cdd:cd05931 253 ---YDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAeaFAPFGFRPEafrpsYGLAEatlFVSGgppgtgpvv 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 397 -------NLAQVTDWSRPGNSGVPL-----DDPAWETRV--------LPD---GEMIVRGPGLFIGYWNKEAETKAALR- 452
Cdd:cd05931 330 lrvdrdaLAGRAVAVAADDPAARELvscgrPLPDQEVRIvdpetgreLPDgevGEIWVRGPSVASGYWGRPEATAETFGa 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981242995 453 ------DGWLYTGDIvdvG--ADGSYKLIDRKKELInTAAGKSISPVQIENELRQSpyiTEALVIG 510
Cdd:cd05931 410 laatdeGGWLRTGDL---GflHDGELYITGRLKDLI-IVRGRNHYPQDIEATAEEA---HPALRPG 468
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
188-510 |
5.69e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 78.27 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 188 PTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPAILSEPQRMVIH-LPLSHtvarIQATTLPLIAKTV----PY 262
Cdd:PRK05677 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIApLPLYH----IYAFTFHCMAMMLignhNI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 263 FVDVSADFAKCIQEVRPtsymapprfyQKFATQI-INhvngsseaerrnyTLalgiarevladrqdagtgdpfkeqLYAI 341
Cdd:PRK05677 282 LISNPRDLPAMVKELGK----------WKFSGFVgLN-------------TL------------------------FVAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 342 CRERVFKPLlariGFDDLRYpyTASAPVPPEVVTLfQLW----GVNLKENYGQTE---MVGGNLAQVTdwsRPGNSGVPL 414
Cdd:PRK05677 315 CNNEAFRKL----DFSALKL--TLSGGMALQLATA-ERWkevtGCAICEGYGMTEtspVVSVNPSQAI---QVGTIGIPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 415 --------DDPAWETRVLPDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELInTAAG 485
Cdd:PRK05677 385 pstlckviDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSG 463
|
330 340
....*....|....*....|....*
gi 981242995 486 KSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK05677 464 FNVYPNELEDVLAALPGVLQCAAIG 488
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
18-518 |
5.86e-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: 77.70 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 18 PALLIERVKNDADANAFfqrrAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTV 97
Cdd:cd17646 1 HALVAEQAARTPDAPAV----VDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 98 GVYFTASVEEVRYYLEDSGATLAFAGSAEQLRvmkaadtssrllkivvldpdwkrSPDETGMNVVSLAEFASHFDGDEva 177
Cdd:cd17646 77 PLDPGYPADRLAYMLADAGPAVVLTTADLAAR-----------------------LPAGGDVALLGDEALAAPPATPP-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 178 ylreqSELARPTDLVSLGYTSGTTGAPKGAMLTHVSmLAGAFTWptfcpailsepqrMVIHLPLSHTVARIQATtlplia 257
Cdd:cd17646 132 -----LVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLW-------------MQDEYPLGPGDRVLQKT------ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 258 ktvPYFVDVSAdfakciqevrptsymapprfYQKFAtqiinhvngsseaerrnyTLALGiAREVLAdRQDaGTGDPfkEQ 337
Cdd:cd17646 187 ---PLSFDVSV--------------------WELFW------------------PLVAG-ARLVVA-RPG-GHRDP--AY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 338 LYAICRE-------------RVFKPLLARIGFDDLRYPYTASAPVPPEVVTLF-QLWGVNLKENYGQTEMVGGnlaqVTD 403
Cdd:cd17646 221 LAALIREhgvttchfvpsmlRVFLAEPAAGSCASLRRVFCSGEALPPELAARFlALPGAELHNLYGPTEAAID----VTH 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 404 W---SRPGNSGVPLDDPAWETR--VLPD----------GEMIVRGPGLFIGYWNKEAETKAALRDGW------LY-TGDI 461
Cdd:cd17646 297 WpvrGPAETPSVPIGRPVPNTRlyVLDDalrpvpvgvpGELYLGGVQLARGYLGRPALTAERFVPDPfgpgsrMYrTGDL 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981242995 462 VDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI----GEGRKYLTA 518
Cdd:cd17646 377 ARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVVaraaPAGAARLVG 436
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-536 |
6.35e-15 |
|
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: 76.75 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 188 PTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAftWPTFCPAILSEPQRMVIHLPLSHTVARIQATTLPLI--AKTV----- 260
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNA--WMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLAsgAHVVlagpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 261 ----PYFVDvsaDFAKCIQEVRPTSYMAPPRFYqkfatqiinhvngsseaerrnytlALGIAREVLADrqdagtgdpfke 336
Cdd:cd05944 79 gyrnPGLFD---NFWKLVERYRITSLSTVPTVY------------------------AALLQVPVNAD------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 337 qlyaicrervfkpllarigFDDLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMV-GGNLAQVTDWSRPGNSGVPL 414
Cdd:cd05944 120 -------------------ISSLRFAMSGAAPLPVELRARFEdATGLPVVEGYGLTEATcLVAVNPPDGPKRPGSVGLRL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 415 ddPAWETRVL-------------PD--GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKEL 479
Cdd:cd05944 181 --PYARVRIKvldgvgrllrdcaPDevGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDL 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981242995 480 InTAAGKSISPVQIENELRQSPYITEALVIGEGRKYLTAL----------IEVDGTLAMDWARTHDP 536
Cdd:cd05944 259 I-IRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELpvayvqlkpgAVVEEEELLAWARDHVP 324
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
57-532 |
7.98e-15 |
|
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: 77.33 E-value: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 57 VSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGAtlafagsaeqlrvmkaadt 136
Cdd:cd12116 25 LAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEP------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 137 ssrllKIVVLDPDWKRSPDETGMnVVSLAEFASHFDGDEVaylreqSELARPTDLVSLGYTSGTTGAPKGAMLTH---VS 213
Cdd:cd12116 86 -----ALVLTDDALPDRLPAGLP-VLLLALAAAAAAPAAP------RTPVSPDDLAYVIYTSGSTGRPKGVVVSHrnlVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 214 MLAG--------------AFTWPTFCPAILSepqrmvIHLPLSH----TVARIQATTLPliaktvpyfvdvsADFAKCIQ 275
Cdd:cd12116 154 FLHSmrerlglgpgdrllAVTTYAFDISLLE------LLLPLLAgarvVIAPRETQRDP-------------EALARLIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 276 EVRPTSYMAPPRFYQKFATqiinhvngSSEAERRNYTLALGiarevladrqdagtGDPFKEQLYAicrervfkPLLARIG 355
Cdd:cd12116 215 AHSITVMQATPATWRMLLD--------AGWQGRAGLTALCG--------------GEALPPDLAA--------RLLSRVG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 356 fddlrypytasapvppevvtlfQLWGVnlkenYGQTEmvggnlaqVTDWS-----RPGNSGVPLDDPAWETR--VLPD-- 426
Cdd:cd12116 265 ----------------------SLWNL-----YGPTE--------TTIWStaarvTAAAGPIPIGRPLANTQvyVLDAal 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 --------GEMIVRGPGLFIGYWNKEAETKAALRD-------GWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISP 490
Cdd:cd12116 310 rpvppgvpGELYIGGDGVAQGYLGRPALTAERFVPdpfagpgSRLYrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIEL 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 981242995 491 VQIENELRQSPYITEALVI---GEGRKYLTALIEVDGTLAMDWAR 532
Cdd:cd12116 389 GEIEAALAAHPGVAQAAVVvreDGGDRRLVAYVVLKAGAAPDAAA 433
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
190-510 |
9.07e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 77.55 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 190 DLVSLGYTSGTTGAPKGAMLTHVSMLAG--------AFTWPTFCPAILSEPQRMVIHLPLSHTVArIQATTLPLIaktvp 261
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraclSQLGPDGQPLMKEGQEVMIAPLPLYHIYA-FTANCMCMM----- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 262 yfvdVSADFAKCIQEvrptsymapPRFYQKFAtqiinhvngsSEAERRNYTLALGIarevladrqdagtgdpfkeqlyai 341
Cdd:PRK12492 282 ----VSGNHNVLITN---------PRDIPGFI----------KELGKWRFSALLGL------------------------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 342 crERVFKPLLARIGFDDLRYPYT------ASAPVPPEVVTLFQLWGVNLKENYGQTEMVG-------GNLAqvtdwsRPG 408
Cdd:PRK12492 315 --NTLFVALMDHPGFKDLDFSALkltnsgGTALVKATAERWEQLTGCTIVEGYGLTETSPvastnpyGELA------RLG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 409 NSGVP--------LDDPAWETRVLPDGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKEL 479
Cdd:PRK12492 387 TVGIPvpgtalkvIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDL 466
|
330 340 350
....*....|....*....|....*....|.
gi 981242995 480 InTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK12492 467 I-IVSGFNVYPNEIEDVVMAHPKVANCAAIG 496
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
351-510 |
9.71e-15 |
|
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: 77.15 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 351 LARIGFDDLRYPYTASAPVPPEVVTLF-QLWGVNLKENYGQTEMVggnlAQVTDWS----RPGNSGVPLddPAWETRVL- 424
Cdd:cd05970 295 LSRYDLSSLRYCTTAGEALNPEVFNTFkEKTGIKLMEGFGQTETT----LTIATFPwmepKPGSMGKPA--PGYEIDLId 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 425 ---------PDGEMIVRGP-----GLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISP 490
Cdd:cd05970 369 regrsceagEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKS-SGYRIGP 447
|
170 180
....*....|....*....|
gi 981242995 491 VQIENELRQSPYITEALVIG 510
Cdd:cd05970 448 FEVESALIQHPAVLECAVTG 467
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
388-510 |
1.12e-14 |
|
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: 75.42 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 388 YGQTEMVGgnLAQVTDWSRPGNSGVPLDDPAWETRVL-------PDG---EMIVRGPGLFIGYWNKEAETKAALRDGWLY 457
Cdd:cd17636 143 YGQTEVMG--LATFAALGGGAIGGAGRPSPLVQVRILdedgrevPDGevgEIVARGPTVMAGYWNRPEVNARRTRGGWHH 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 981242995 458 TGDIVDVGADGSYKLIDRKKELINTAAgKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMIKSGA-ENIYPAEVERCLRQHPAVADAAVIG 272
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
60-520 |
2.08e-14 |
|
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: 76.21 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADtssr 139
Cdd:cd17655 38 TLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIAFIGL---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 llkIVVLDPDWKRSPDETGMNVVSlaefashfdgdevaylreqselaRPTDLVSLGYTSGTTGAPKGAMLTHvsmlagaf 219
Cdd:cd17655 114 ---IDLLDEDTIYHEESENLEPVS-----------------------KSDDLAYVIYTSGSTGKPKGVMIEH-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 220 twptfcpailsepqRMVIHLPLSHTVARIQATTLPlIAKTVPYFVDVSAD--FAK-------CIqeVRPTSYMAPPRFYQ 290
Cdd:cd17655 160 --------------RGVVNLVEWANKVIYQGEHLR-VALFASISFDASVTeiFASllsgntlYI--VRKETVLDGQALTQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 291 KFATQIINHVNGSSeaerrnytlalgiAREVLADRQDAGTGDPFKEQLyaicrervfkpllarIGFDDLrypytasapvP 370
Cdd:cd17655 223 YIRQNRITIIDLTP-------------AHLKLLDAADDSEGLSLKHLI---------------VGGEAL----------S 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 371 PEVVT----LFQLwGVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLDDPAWETRV-LPD-----------GEMIVRGP 434
Cdd:cd17655 265 TELAKkiieLFGT-NPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIyILDqygrpqpvgvaGELYIGGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 435 GLFIGYWNKEAETKAALRD------GWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEAL 507
Cdd:cd17655 344 GVARGYLNRPELTAEKFVDdpfvpgERMYrTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEAV 422
|
490
....*....|....*..
gi 981242995 508 VIG----EGRKYLTALI 520
Cdd:cd17655 423 VIArkdeQGQNYLCAYI 439
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
46-510 |
4.96e-14 |
|
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: 74.85 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSA 125
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 EQlrVMKA-ADTSSRLLKIVVLDPDwkRSPDETGmnvvSLAEFAShfdgdevaylreqselARPTDLVSLGYTSGTTGAP 204
Cdd:cd05923 110 AQ--VMDAiFQSGVRVLALSDLVGL--GEPESAG----PLIEDPP----------------REPEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSMLAGAFTWPTFCPAILSEPQRMVIHLPLSHTVARIQATTLPLIAKTVPYFV--DVSADFAKCIQEVRPTSY 282
Cdd:cd05923 166 KGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVeeFDPADALKLIEQERVTSL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 283 MAPPRFYQKFATqiinHVNGSSEaeRRNYTLALGIAREVLADrqdagtgdpfkeqlyaicrervfkPLLARIgfddlryp 362
Cdd:cd05923 246 FATPTHLDALAA----AAEFAGL--KLSSLRHVTFAGATMPD------------------------AVLERV-------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 363 ytaSAPVPPEVVTLfqlwgvnlkenYGQTEMVGGNLAQVtdwSRPGNSGVP-----------LDDPAWETRVLPDGEMIV 431
Cdd:cd05923 288 ---NQHLPGEKVNI-----------YGTTEAMNSLYMRD---ARTGTEMRPgffsevrivriGGSPDEALANGEEGELIV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 432 RGPG--LFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI 509
Cdd:cd05923 351 AAAAdaAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRHPGVTEVVVI 429
|
.
gi 981242995 510 G 510
Cdd:cd05923 430 G 430
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
57-510 |
7.48e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 74.34 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 57 VSAALGAAGVARGDRIAIMGDVSrewliADMATICSGAVTVGVYFTA-----SVEEVRYYLEDSGATLAFaGSAEQLRVM 131
Cdd:PRK13391 37 LAHLFRSLGLKRGDHVAIFMENN-----LRYLEVCWAAERSGLYYTCvnshlTPAEAAYIVDDSGARALI-TSAAKLDVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 132 KAA-DTSSRLLKIVVLDPDWKRSPdetgmnvvslaefashFDGDEVAyLREQSelARPTDLVSLG----YTSGTTGAPKG 206
Cdd:PRK13391 111 RALlKQCPGVRHRLVLDGDGELEG----------------FVGYAEA-VAGLP--ATPIADESLGtdmlYSSGTTGRPKG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 207 amlthvsmlagaftwptfcpailsepqrmvIHLPLSHtvariqattlPLIAKTVPYFvdvsADFAKCIQEVRPTSYMAPP 286
Cdd:PRK13391 172 ------------------------------IKRPLPE----------QPPDTPLPLT----AFLQRLWGFRSDMVYLSPA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 287 RFYQ---KFATQIINHVNGSSeaerrnytlalgiareVLADRQDAgtgdpfkEQ-LYAICRERV---------FKPLL-- 351
Cdd:PRK13391 208 PLYHsapQRAVMLVIRLGGTV----------------IVMEHFDA-------EQyLALIEEYGVthtqlvptmFSRMLkl 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 352 ---ARIGFD--DLRYPYTASAPVPPEVVT-LFQLWGVNLKENYGQTEMVGGNLAQVTDW-SRPGNSGVP-------LDDp 417
Cdd:PRK13391 265 peeVRDKYDlsSLEVAIHAAAPCPPQVKEqMIDWWGPIIHEYYAATEGLGFTACDSEEWlAHPGTVGRAmfgdlhiLDD- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 418 awETRVLPDGE--MIVRGPGLFIGYWNKEAETKAAlRD---GWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQ 492
Cdd:PRK13391 344 --DGAELPPGEpgTIWFEGGRPFEYLNDPAKTAEA-RHpdgTWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQE 419
|
490
....*....|....*...
gi 981242995 493 IENELRQSPYITEALVIG 510
Cdd:PRK13391 420 AENLLITHPKVADAAVFG 437
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
46-509 |
1.10e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.90 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 46 TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSA 125
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 126 ------EQLRVMKAADTSSRLLKIVVLDPDWKRSPDETGMNVVSLAEFASHFDGDEVAYLREQSElarpTDLVSLGYTSG 199
Cdd:PLN03102 121 feplarEVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEELDYECLIQRGEPTPSLVARMFRIQDE----HDPISLNYTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 200 TTGAPKGAMLTH----VSMLAGAFTWPT-FCPAILSEpqrmvihLPLSHTVARiqattlpliakTVPYFVDVSADFAKCI 274
Cdd:PLN03102 197 TTADPKGVVISHrgayLSTLSAIIGWEMgTCPVYLWT-------LPMFHCNGW-----------TFTWGTAARGGTSVCM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 275 QEVrptsymAPPRFYQKFATQIINHVNgsseaerrnytlalgiarevladrqdagtgdpfkeqlyaiCRERVFKPLL--A 352
Cdd:PLN03102 259 RHV------TAPEIYKNIEMHNVTHMC----------------------------------------CVPTVFNILLkgN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 353 RIGFDDLRYP---YTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNL--AQVTDWSR-PGNSGVPL------------ 414
Cdd:PLN03102 293 SLDLSPRSGPvhvLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLfcEWQDEWNRlPENQQMELkarqgvsilgla 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 415 DDPAWETRVLPD--------GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGK 486
Cdd:PLN03102 373 DVDVKNKETQESvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGE 451
|
490 500
....*....|....*....|...
gi 981242995 487 SISPVQIENELRQSPYITEALVI 509
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVV 474
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
26-509 |
1.72e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 73.34 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 26 KNDADANA----FFQRRAGAWVPT-----------TWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATI 90
Cdd:PLN02479 12 KNAANYTAltplWFLERAAVVHPTrksvvhgsvryTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 91 CSGAVTVGVYFTASVEEVRYYLEDSGATLA------FAGSAEQLRVMKAADTSS--RLLKIVVLDP--DWKRSPDETGMN 160
Cdd:PLN02479 92 MAGAVVNCVNIRLNAPTIAFLLEHSKSEVVmvdqefFTLAEEALKILAEKKKSSfkPPLLIVIGDPtcDPKSLQYALGKG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 161 VVSLAEFAShfDGD-EVAYLREQSELarptDLVSLGYTSGTTGAPKGAMLTHvsmlAGAFTWPTFCPAILSEPQRMVI-- 237
Cdd:PLN02479 172 AIEYEKFLE--TGDpEFAWKPPADEW----QSIALGYTSGTTASPKGVVLHH----RGAYLMALSNALIWGMNEGAVYlw 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 238 HLPLSHTVARIQATTLPLIAKTvpyfvdvsadfAKCIQEVRPTSymapprFYQKFATQIINHVNGsseaerrnytlalgi 317
Cdd:PLN02479 242 TLPMFHCNGWCFTWTLAALCGT-----------NICLRQVTAKA------IYSAIANYGVTHFCA--------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 318 AREVLADRQDAGtgdpfkeqlyaicRERVFKPLLARIgfddlrYPYTASAPVPPEVVTLFQLWGVNLKENYGQTEMVGGN 397
Cdd:PLN02479 290 APVVLNTIVNAP-------------KSETILPLPRVV------HVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYGPS 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 398 L--AQVTDW-SRP----------------GNSGVPLDDPAWETRVLPD----GEMIVRGPGLFIGYWNKEAETKAALRDG 454
Cdd:PLN02479 351 TvcAWKPEWdSLPpeeqarlnarqgvryiGLEGLDVVDTKTMKPVPADgktmGEIVMRGNMVMKGYLKNPKANEEAFANG 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 455 WLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVI 509
Cdd:PLN02479 431 WFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLEVENVVYTHPAVLEASVV 484
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
54-510 |
3.46e-13 |
|
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: 72.52 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 54 VCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFA--GSAEQLRVM 131
Cdd:cd05968 101 VKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITadGFTRRGREV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 132 -------KAADTSSRLLKIVVLDPDWKRSPDETGMNVVSLAEFASHFDGDEvaylREQSElarptDLVSLGYTSGTTGAP 204
Cdd:cd05968 181 nlkeeadKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAE----RTESE-----DPLMIIYTSGTTGKP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 205 KGAMLTHVSM-LAGAFTwpTFCPAILSEPQRMVIHLPLSHTVAR-IQATTLPLIAKTVPYfvDVSADFAKC------IQE 276
Cdd:cd05968 252 KGTVHVHAGFpLKAAQD--MYFQFDLKPGDLLTWFTDLGWMMGPwLIFGGLILGATMVLY--DGAPDHPKAdrlwrmVED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 277 VRPTSYMAPPRFYQKFATQIINHVNGSSEAERRnytlALGiarevladrqdaGTGDPFKEQLYAICRERVFK---PLLar 353
Cdd:cd05968 328 HEITHLGLSPTLIRALKPRGDAPVNAHDLSSLR----VLG------------STGEPWNPEPWNWLFETVGKgrnPII-- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 354 igfddlrypytasapvppevvtlfqlwgvnlkeNY-GQTEMVGGNLAQVT---------DWSRPGNSGVPLDDPAweTRV 423
Cdd:cd05968 390 ---------------------------------NYsGGTEISGGILGNVLikpikpssfNGPVPGMKADVLDESG--KPA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 424 LPD-GEMIVRGP--GLFIGYWNKEA---ETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENEL 497
Cdd:cd05968 435 RPEvGELVLLAPwpGMTRGFWRDEDrylETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINV-AGKRVGPAEIESVL 513
|
490
....*....|...
gi 981242995 498 RQSPYITEALVIG 510
Cdd:cd05968 514 NAHPAVLESAAIG 526
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
62-510 |
5.13e-13 |
|
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: 71.73 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 62 GAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMK-AADTSSRL 140
Cdd:cd05928 60 GACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSvASECPSLK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 141 LKIVVLDPDWkrspdETGMNVVSLAEFAShfdgDEVAYLREQSElarptDLVSLGYTSGTTGAPKGAMLTHVSMLAGAft 220
Cdd:cd05928 140 TKLLVSEKSR-----DGWLNFKELLNEAS----TEHHCVETGSQ-----EPMAIYFTSGTTGSPKMAEHSHSSLGLGL-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 221 wpTFCPAILSEPQRMVIHLPLSHT---VARIQATTLPLIAKtvpyfvdvSADFAKCIQEVRPTSymapprFYQKFATQII 297
Cdd:cd05928 204 --KVNGRYWLDLTASDIMWNTSDTgwiKSAWSSLFEPWIQG--------ACVFVHHLPRFDPLV------ILKTLSSYPI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 298 NHVNGSSEAERrnytlalgiarevLADRQDagtgdpfkeqlyaicrervfkplLARIGFDDLRYPYTASAPVPPEVVtlf 377
Cdd:cd05928 268 TTFCGAPTVYR-------------MLVQQD-----------------------LSSYKFPSLQHCVTGGEPLNPEVL--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 378 QLW----GVNLKENYGQTEMVggnLAQVTDWS---RPGNSGVPLddPAWETR-------VLP---DGEMIVR-GP----G 435
Cdd:cd05928 309 EKWkaqtGLDIYEGYGQTETG---LICANFKGmkiKPGSMGKAS--PPYDVQiiddngnVLPpgtEGDIGIRvKPirpfG 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 436 LFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINtAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05928 384 LFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVIN-SSGYRIGPFEVESALIEHPAVVESAVVS 457
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
54-514 |
2.02e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 69.87 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 54 VCSVSAAL-GAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAgsaeqlrvmk 132
Cdd:PLN02574 76 VKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT---------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 133 AADTSSRLLKIvvldpdwkrspdetGMNVVSLAEfASHFDGDEVAY------LREQSE-LARPT----DLVSLGYTSGTT 201
Cdd:PLN02574 146 SPENVEKLSPL--------------GVPVIGVPE-NYDFDSKRIEFpkfyelIKEDFDfVPKPVikqdDVAAIMYSSGTT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 202 GAPKGAMLTHVSMLAGAFTWPTFCPAILSEPQRMVIHL---PLSHTVA-RIQATTLPLIAKTVPYF--VDVSaDFAKCIQ 275
Cdd:PLN02574 211 GASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLaalPMFHIYGlSLFVVGLLSLGSTIVVMrrFDAS-DMVKVID 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 276 EVRPTSY-MAPPRFYQKFATqiinhvngsseaerrnytlALGIAREVLADRQDAGTGDpfkeqlyAICRERVFKPLLARI 354
Cdd:PLN02574 290 RFKVTHFpVVPPILMALTKK-------------------AKGVCGEVLKSLKQVSCGA-------APLSGKFIQDFVQTL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 355 GFDDL--RYPYTASAPVPPEvvtlfqlwGVNLKE--NYGQTEMVGGNL-AQVTDWSR-----PGNSGvplddpawetrvl 424
Cdd:PLN02574 344 PHVDFiqGYGMTESTAVGTR--------GFNTEKlsKYSSVGLLAPNMqAKVVDWSTgcllpPGNCG------------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 425 pdgEMIVRGPGLFIGYWN-KEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYI 503
Cdd:PLN02574 403 ---ELWIQGPGVMKGYLNnPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAVLISHPEI 478
|
490
....*....|.
gi 981242995 504 TEALVIGEGRK 514
Cdd:PLN02574 479 IDAAVTAVPDK 489
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
57-510 |
2.91e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 69.24 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 57 VSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAV--TVGVYFTASveEVRYYLEDSGATLAFAGSA--EQLRVMK 132
Cdd:PLN02246 63 VAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVttTANPFYTPA--EIAKQAKASGAKLIITQSCyvDKLKGLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 133 AADTssrlLKIVVLDPDwkrspdetgmnvvslAEFASHFDGDEVAylrEQSELA----RPTDLVSLGYTSGTTGAPKGAM 208
Cdd:PLN02246 141 EDDG----VTVVTIDDP---------------PEGCLHFSELTQA---DENELPeveiSPDDVVALPYSSGTTGLPKGVM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 209 LTHVSMLAGAFTW-----PTFcpaILSEPQRMVIHLPLSHTVA---------RIQATTLpliakTVPYFvDVSAdFAKCI 274
Cdd:PLN02246 199 LTHKGLVTSVAQQvdgenPNL---YFHSDDVILCVLPMFHIYSlnsvllcglRVGAAIL-----IMPKF-EIGA-LLELI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 275 QEVRPT-SYMAPPrfyqkfatqiinhvngsseaerrnytLALGIAREVLADRQDagtgdpfkeqlyaicrervfkplLAR 353
Cdd:PLN02246 269 QRHKVTiAPFVPP--------------------------IVLAIAKSPVVEKYD-----------------------LSS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 354 IgfddlRYPYTASAPVPPEVVTLF--QLWGVNLKENYGQTEmVGGNLAQVTDWS------RPG-------NSGVPLDDPa 418
Cdd:PLN02246 300 I-----RMVLSGAAPLGKELEDAFraKLPNAVLGQGYGMTE-AGPVLAMCLAFAkepfpvKSGscgtvvrNAELKIVDP- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 419 wET-----RVLPdGEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQ 492
Cdd:PLN02246 373 -ETgaslpRNQP-GEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAE 449
|
490
....*....|....*...
gi 981242995 493 IENELRQSPYITEALVIG 510
Cdd:PLN02246 450 LEALLISHPSIADAAVVP 467
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
359-509 |
3.05e-12 |
|
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: 69.13 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 359 LRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTE---MVGGNLAQVTdwsRPGNSGVPLddPAWETRVL-PDGEMIVRG 433
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVRrAWGLTIRDGYGQTEttaLVGNSPGQPV---KAGSMGRPL--PGYRVALLdPDGAPATEG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 434 P-----------GLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTAAGKsISPVQIENELRQSPY 502
Cdd:cd05974 277 EvaldlgdtrpvGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPA 355
|
....*..
gi 981242995 503 ITEALVI 509
Cdd:cd05974 356 VAEAAVV 362
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
51-534 |
4.18e-12 |
|
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: 68.77 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 51 ANAVcsvSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRV 130
Cdd:cd12117 32 ANRL---ARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 131 mkaadtsSRLLKIVVLDPDWKRSPDEtgmnvvslaEFASHFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLT 210
Cdd:cd12117 109 -------GGLEVAVVIDEALDAGPAG---------NPAVPVSPDDLAYVM---------------YTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 211 HVSMLAGAFTwPTFcpAILSEPQRMVIHLPLShtvariqattlpliaktvpyFvDVSAdfakciqevrptsymapprfYQ 290
Cdd:cd12117 158 HRGVVRLVKN-TNY--VTLGPDDRVLQTSPLA--------------------F-DAST--------------------FE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 291 KFATQIinhvNGsseaerrnytlalgiAREVLADRQDAGTGDPFKEqlyAICRERV---------FKpLLARIG---FDD 358
Cdd:cd12117 194 IWGALL----NG---------------ARLVLAPKGTLLDPDALGA---LIAEEGVtvlwltaalFN-QLADEDpecFAG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 359 LRYPYTASAPVPPE-VVTLFQLW-GVNLKENYGQTEMVGGNLAQVTDWSRPGNSGVPLDDPAWETRVLP-D--------- 426
Cdd:cd12117 251 LRELLTGGEVVSPPhVRRVLAACpGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRVYVlDedgrpvppg 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 --GEMIVRGPGLFIGYWNKEAETKA------ALRDGWLY-TGDIVDVGADGSYKLIDR-----KkelINtaaGKSISPVQ 492
Cdd:cd12117 331 vpGELYVGGDGLALGYLNRPALTAErfvadpFGPGERLYrTGDLARWLPDGRLEFLGRiddqvK---IR---GFRIELGE 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 981242995 493 IENELRQSPYITEALVI----GEGRKYLTALIEVDGTLAMDWARTH 534
Cdd:cd12117 405 IEAALRAHPGVREAVVVvredAGGDKRLVAYVVAEGALDAAELRAF 450
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
28-510 |
1.25e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 67.60 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 28 DADANAFFQRRagawVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEE 107
Cdd:PRK05852 31 EAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 108 VRYYLEDSGATLAFAGSaeqLRVMKAADTSSRLLKIVVldpdwkrspDETGMNVVSLAEFASHFDGDEVAYLREQSELA- 186
Cdd:PRK05852 107 QRVRSQAAGARVVLIDA---DGPHDRAEPTTRWWPLTV---------NVGGDSGPSGGTLSVHLDAATEPTPATSTPEGl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 187 RPTDLVSLgYTSGTTGAPKGAMLTHVSMlagAFTWPTFCPAI-LSEPQRMVIHLPLSH---TVARIQATTLPLIAKTVPY 262
Cdd:PRK05852 175 RPDDAMIM-FTGGTTGLPKMVPWTHANI---ASSVRAIITGYrLSPRDATVAVMPLYHghgLIAALLATLASGGAVLLPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 263 FVDVSA-DFAKCIQEVRPTSYMAPPRFYQKFATQiinhvngSSEAERRNYTLALGIAREVLAdrqdagtgdPFKEQLYAI 341
Cdd:PRK05852 251 RGRFSAhTFWDDIKAVGATWYTAVPTIHQILLER-------AATEPSGRKPAALRFIRSCSA---------PLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 342 CRERVFKPLLARIGFDDLRYPytasapvppevVTLFQLWGVNLKENYGQTE-MVGGNLAqvTDWSRPGNSGVPLddPAWE 420
Cdd:PRK05852 315 LQTEFAAPVVCAFGMTEATHQ-----------VTTTQIEGIGQTENPVVSTgLVGRSTG--AQIRIVGSDGLPL--PAGA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 421 TrvlpdGEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQS 500
Cdd:PRK05852 380 V-----GEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINR-GGEKISPERVEGVLASH 453
|
490
....*....|
gi 981242995 501 PYITEALVIG 510
Cdd:PRK05852 454 PNVMEAAVFG 463
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
34-614 |
1.52e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 67.21 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 34 FFQRR--AGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSrewliADMATICSGAVTVGVYFtASV------ 105
Cdd:PRK08180 57 FLAERgaDGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNS-----IEHALLALAAMYAGVPY-APVspaysl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 106 -----EEVRYYLEDSGATLAFAGSAEQLRVMKAADTSSRLLKIVVLDPDWkrspdetGMNVVSLAEFASHFDGDEVAYLR 180
Cdd:PRK08180 131 vsqdfGKLRHVLELLTPGLVFADDGAAFARALAAVVPADVEVVAVRGAVP-------GRAATPFAALLATPPTAAVDAAH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 181 EQselARPTDLVSLGYTSGTTGAPKGAMLTHvSMLAG-----AFTWPTFcpaiLSEPQRMVIHLPLSHT---------VA 246
Cdd:PRK08180 204 AA---VGPDTIAKFLFTSGSTGLPKAVINTH-RMLCAnqqmlAQTFPFL----AEEPPVLVDWLPWNHTfggnhnlgiVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 247 RIQAT--------TLPLIAKTVpyfvdvsadfaKCIQEVRPTSYMAPPRFYqkfatqiinhvngsseaerrnytlalgia 318
Cdd:PRK08180 276 YNGGTlyiddgkpTPGGFDETL-----------RNLREISPTVYFNVPKGW----------------------------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 319 rEVLAD--RQDAGtgdpfkeqlyaicrervfkplLARIGFDDLRYPYTASAPVPPEVvtlfqlWG-------------VN 383
Cdd:PRK08180 316 -EMLVPalERDAA---------------------LRRRFFSRLKLLFYAGAALSQDV------WDrldrvaeatcgerIR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 384 LKENYGQTEMvgGNLAQVTDW--SRPGNSGVPLddPAWETRVLPDG---EMIVRGPGLFIGYWNKEAETKAAL-RDGWLY 457
Cdd:PRK08180 368 MMTGLGMTET--APSATFTTGplSRAGNIGLPA--PGCEVKLVPVGgklEVRVKGPNVTPGYWRAPELTAEAFdEEGYYR 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 458 TGDIVdvgadgsyKLID------------RKKELINTAAGK--SISPVQIENELRQSPYITEALVIGEGRKYLTALIEVD 523
Cdd:PRK08180 444 SGDAV--------RFVDpadperglmfdgRIAEDFKLSSGTwvSVGPLRARAVSAGAPLVQDVVITGHDRDEIGLLVFPN 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 524 gtlaMDWARTH--DPSVTQYADLASSPPVIDLIREEVEKANA-------RLARAeqikafRIFPEELTPENGVMTATRKK 594
Cdd:PRK08180 516 ----LDACRRLagLLADASLAEVLAHPAVRAAFRERLARLNAqatgsstRVARA------LLLDEPPSLDAGEITDKGYI 585
|
650 660
....*....|....*....|
gi 981242995 595 RRKALMARYAHIIAGLYDDA 614
Cdd:PRK08180 586 NQRAVLARRAALVEALYADE 605
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2-510 |
2.42e-11 |
|
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: 66.45 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 2 SAAPWTSGNQFATTTIPALLIER-VKNDADANAFFQRRAGAWVPTTWKgYA---NAVCSVSAALGAAGVARGDRIAIMGD 77
Cdd:cd17634 39 PGAPSIKWFEDATLNLAANALDRhLRENGDRTAIIYEGDDTSQSRTIS-YRelhREVCRFAGTLLDLGVKKGDRVAIYMP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 78 VSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGAtlafagsaeqlRVMKAADTSSRLLKIVVLDPDWKRSPDET 157
Cdd:cd17634 118 MIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSS-----------RLLITADGGVRAGRSVPLKKNVDDALNPN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 158 GM---NVVSLAEFASHFDGDEVAYL-----------REQSELARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPT 223
Cdd:cd17634 187 VTsveHVIVLKRTGSDIDWQEGRDLwwrdliakaspEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 224 FCPAI--------LSEPQRMVIHLPLSHTvariqattlPLIAKTVPYFVDVSADfakciqevrptsYMAPPRFYQKFATQ 295
Cdd:cd17634 267 YVFDYgpgdiywcTADVGWVTGHSYLLYG---------PLACGATTLLYEGVPN------------WPTPARMWQVVDKH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 296 IINHVNGSSEAERrnytlALGIAREVLADRQD-------AGTGDPFKEQLYAICRERVFK---PLLARIGFDDlrypyTA 365
Cdd:cd17634 326 GVNILYTAPTAIR-----ALMAAGDDAIEGTDrsslrilGSVGEPINPEAYEWYWKKIGKekcPVVDTWWQTE-----TG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 366 SAPVPPevvtlfqLWGVNLKENYGQTEMVGGNLAQVTDwsrpgNSGVPLdDPAWEtrvlpdGEMIVRG--PGLFIGYW-- 441
Cdd:cd17634 396 GFMITP-------LPGAIELKAGSATRPVFGVQPAVVD-----NEGHPQ-PGGTE------GNLVITDpwPGQTRTLFgd 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 442 -NKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd17634 457 hERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINV-AGHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
158-614 |
2.57e-11 |
|
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: 66.30 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 158 GMNVVSLAEFASHFDGDEVAYLREQselARPTDLVSLGYTSGTTGAPKGAMLTHvSMLAG-----AFTWPTFCPailsEP 232
Cdd:cd05921 137 GRGAISFAELAATPPTAAVDAAFAA---VGPDTVAKFLFTSGSTGLPKAVINTQ-RMLCAnqamlEQTYPFFGE----EP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 233 QRMVIHLPLSHTVARIQATTLPLIAKTVPYFVD---VSADFAKCI---QEVRPTSYMAPPRFYQKFATqiinhvngssea 306
Cdd:cd05921 209 PVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDgkpMPGGFEETLrnlREISPTVYFNVPAGWEMLVA------------ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 307 errnytlalgiarevlADRQDAGtgdpfkeqlyaicrervfkplLARIGFDDLRYPYTASAPVPPEVVTLFQLWGVN--- 383
Cdd:cd05921 277 ----------------ALEKDEA---------------------LRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVAtvg 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 384 ----LKENYGQTEMVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPDG---EMIVRGPGLFIGYWNKEAETKAAL-RDGW 455
Cdd:cd05921 320 eripMMAGLGATETAPTATFTHWPTERSGLIGLPA--PGTELKLVPSGgkyEVRVKGPNVTPGYWRQPELTAQAFdEEGF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 456 LYTGDIVD--VGADGSYKLI--DRKKELINTAAGK--SISPVQIENELRQSPYITEALVIGEGRKYLTALIEVDGTLAMD 529
Cdd:cd05921 398 YCLGDAAKlaDPDDPAKGLVfdGRVAEDFKLASGTwvSVGPLRARAVAACAPLVHDAVVAGEDRAEVGALVFPDLLACRR 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 530 WARTHDPSVtqyADLASSPPVIDLIREEVEKANARLA-RAEQIKAFRIFPEELTPENGVMTATRKKRRKALMARYAHIIA 608
Cdd:cd05921 478 LVGLQEASD---AEVLRHAKVRAAFRDRLAALNGEATgSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVE 554
|
....*.
gi 981242995 609 GLYDDA 614
Cdd:cd05921 555 RLYADT 560
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
45-510 |
3.36e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 65.98 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 45 TTWKGYANAVCSVSAALGAAGVARGDRIAIMG---DVSREWLiadMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAF 121
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAAlnsDLYLEWL---LAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 122 AGSAEQLRVMKAADTSSRLLKIVVLdpdwkrspdeTGMNVVSLAEFASHFDGDEVAYLREQSELA-----RPTDLVSLGY 196
Cdd:PLN02860 110 TDETCSSWYEELQNDRLPSLMWQVF----------LESPSSSVFIFLNSFLTTEMLKQRALGTTEldyawAPDDAVLICF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGAMLTHVSMLAGAFTWPtfcpAILSEPQRMV-IHL-PLSHtVARIQATTLPLIAKTVPYFVdvsadfakci 274
Cdd:PLN02860 180 TSGTTGRPKGVTISHSALIVQSLAKI----AIVGYGEDDVyLHTaPLCH-IGGLSSALAMLMVGACHVLL---------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 275 qevrptsymapPRFYQKFATQIINHVNGSSeaerrnYTLALGIAREVLADRQDAGTGDpfkeqlyaiCRERVFKPLLARI 354
Cdd:PLN02860 245 -----------PKFDAKAALQAIKQHNVTS------MITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 355 GFddlrypytaSAPVPPEVVTLFQlwGVNLKENYGQTE-------------------MVGGNLAQVTDWSRPGNSGVPLD 415
Cdd:PLN02860 299 SL---------SSRLLPDAKKLFP--NAKLFSAYGMTEacssltfmtlhdptlespkQTLQTVNQTKSSSVHQPQGVCVG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 416 DPA--WETRVLPD-----GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKS 487
Cdd:PLN02860 368 KPAphVELKIGLDessrvGRILTRGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGEN 446
|
490 500
....*....|....*....|...
gi 981242995 488 ISPVQIENELRQSPYITEALVIG 510
Cdd:PLN02860 447 VYPEEVEAVLSQHPGVASVVVVG 469
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-475 |
3.60e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 66.49 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 187 RPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAftwptfcpailsEPQRMVIH----------LPLSHTVARIQATTLPLI 256
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNI------------EQISDVFNlrnddvilssLPFFHSFGLTVTLWLPLL 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 257 AKtvpyfvdvsadfAKCIQEVRPTSymapprfyqkfATQIinhvngSSEAERRNYTLALGiarevladrqdagTGDPFke 336
Cdd:PRK08633 848 EG------------IKVVYHPDPTD-----------ALGI------AKLVAKHRATILLG-------------TPTFL-- 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 337 QLYAicRERVFKPLLarigFDDLRYPYTASAPVPPEVVTLFQL-WGVNLKENYGQTEM------------VGGNLAQVTd 403
Cdd:PRK08633 884 RLYL--RNKKLHPLM----FASLRLVVAGAEKLKPEVADAFEEkFGIRILEGYGATETspvasvnlpdvlAADFKRQTG- 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 404 wSRPGNSGVPLD-------DPawET-RVLPDGE--MI-VRGPGLFIGYWNKEAETKAALRD----GWLYTGDIVDVGADG 468
Cdd:PRK08633 957 -SKEGSVGMPLPgvavrivDP--ETfEELPPGEdgLIlIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDG 1033
|
....*..
gi 981242995 469 SYKLIDR 475
Cdd:PRK08633 1034 FLTITDR 1040
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
175-510 |
4.13e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 66.21 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 175 EVAYLREQSELARPTDLVSLG--------YTSGTTGAPKGAMLTHVSMLAgaFTWPTFCPAILSEPQ-------RMVIHL 239
Cdd:PRK06060 123 EAAELMSEAARVAPGGYEPMGgdalayatYTSGTTGPPKAAIHRHADPLT--FVDAMCRKALRLTPEdtglcsaRMYFAY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 240 PLSHTVARIQATTLPLIAKTVPYFVDVSADFAKciqEVRPTSYMAPPRFYqkfatqiinhvngsseaerrnytlalgiAR 319
Cdd:PRK06060 201 GLGNSVWFPLATGGSAVINSAPVTPEAAAILSA---RFGPSVLYGVPNFF----------------------------AR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 320 EVladrqDAGTGDPFKEQLYAICRERVFKPLLArigfddlrypytasapvppEVVTLFqLWGVNLKENYGQTEmVGGNLA 399
Cdd:PRK06060 250 VI-----DSCSPDSFRSLRCVVSAGEALELGLA-------------------ERLMEF-FGGIPILDGIGSTE-VGQTFV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 400 Q--VTDWsRPGNSGVPLddPAWETRVL-PDG---------EMIVRGPGLFIGYWNKeaeTKAALRD-GWLYTGDIVDVGA 466
Cdd:PRK06060 304 SnrVDEW-RLGTLGRVL--PPYEIRVVaPDGttagpgvegDLWVRGPAIAKGYWNR---PDSPVANeGWLDTRDRVCIDS 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 981242995 467 DG--SYKLIDRKKELIntaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK06060 378 DGwvTYRCRADDTEVI---GGVNVDPREVERLIIEDEAVAEAAVVA 420
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
58-510 |
6.70e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 65.03 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 58 SAALGA----AGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKA 133
Cdd:PRK13390 34 SAALARvlydAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 134 -ADTSSRLlkivvldpdwkrspdETGMNVVSLAEFASHFDGDEvAYLREQselarPTDLVSLgYTSGTTGAPKGAMlthv 212
Cdd:PRK13390 114 gADLPLRL---------------SFGGEIDGFGSFEAALAGAG-PRLTEQ-----PCGAVML-YSSGTTGFPKGIQ---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 213 smlagaftwptfcPAIlsePQRMVihlplshtvariQATTLPLIAKTVPYFVDVSADFakcIQEVRPTSYMAPPRFyqkf 292
Cdd:PRK13390 168 -------------PDL---PGRDV------------DAPGDPIVAIARAFYDISESDI---YYSSAPIYHAAPLRW---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 293 aTQIINHVNGSSeaerrnytlalgiareVLADRQDAGTGDPFKEQLYAICRERV---FKPLL-------ARIGFDDLRYP 362
Cdd:PRK13390 213 -CSMVHALGGTV----------------VLAKRFDAQATLGHVERYRITVTQMVptmFVRLLkldadvrTRYDVSSLRAV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 363 YTASAPVPPEVVTLFQLW-GVNLKENYGQTEMVGGNLAQVTDW-SRPGNSGVPL-------DDPAWEtrvLPDGEMIV-- 431
Cdd:PRK13390 276 IHAAAPCPVDVKHAMIDWlGPIVYEYYSSTEAHGMTFIDSPDWlAHPGSVGRSVlgdlhicDDDGNE---LPAGRIGTvy 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 432 ----RGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEAL 507
Cdd:PRK13390 353 ferdRLPFRYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVA 431
|
...
gi 981242995 508 VIG 510
Cdd:PRK13390 432 VIG 434
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
197-510 |
6.78e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 64.30 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 197 TSGTTGAPKGAMLTHVSMLAGAFTWPTFcpaiLSEPQRMVIHLPLSHtVARIQATTLPLIAKTVPYFVDVSADFAkcIQE 276
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDR----LGGPGQWLLALPAHH-IAGLQVLVRSVIAGSEPVELDVSAGFD--PTA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 277 -VRPTSYMAPPRFYQKF-ATQIINHVnGSSEAerrnyTLALgiarevladrqdagtgdpfkeqlyaicreRVFKPLLarI 354
Cdd:PRK07824 116 lPRAVAELGGGRRYTSLvPMQLAKAL-DDPAA-----TAAL-----------------------------AELDAVL--V 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 355 GfddlrypytaSAPVPPEVVTLFQLWGVNLKENYGQTEMVGGNlaqVTDwsrpgnsGVPLDDpaweTRV-LPDGEMIVRG 433
Cdd:PRK07824 159 G----------GGPAPAPVLDAAAAAGINVVRTYGMSETSGGC---VYD-------GVPLDG----VRVrVEDGRIALGG 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981242995 434 PGLFIGYWNKEaETKAALRDGWLYTGDIVDVGaDGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK07824 215 PTLAKGYRNPV-DPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAIST-GGLTVLPQVVEAALATHPAVADCAVFG 288
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
187-568 |
1.07e-10 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 64.10 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 187 RPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAftwPTFCPAILSEPQRMVIHLpLSHTvariqattlpliaktvpyFvDV 266
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSA---LAHGRALGLTSESRVLQF-ASYT------------------F-DV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 267 SadfakcIQEVrptsymapprfyqkFATQIinhVNGS----SEAERRNytlalGIARevladrqdagtgdpfkeqlyAIC 342
Cdd:cd05918 161 S------ILEI--------------FTTLA---AGGClcipSEEDRLN-----DLAG--------------------FIN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 343 RERV----FKPLLARI----GFDDLRYPYTASAPVPPEVVtlfQLW--GVNLKENYGQTEM-VGGNLAQVTDWSRPGNSG 411
Cdd:cd05918 193 RLRVtwafLTPSVARLldpeDVPSLRTLVLGGEALTQSDV---DTWadRVRLINAYGPAECtIAATVSPVVPSTDPRNIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 412 VPLD------DPAWETRVLPD---GEMIVRGPGLFIGYWNKEAETKAA-------------LRDGWLY-TGDIVDVGADG 468
Cdd:cd05918 270 RPLGatcwvvDPDNHDRLVPIgavGELLIEGPILARGYLNDPEKTAAAfiedpawlkqegsGRGRRLYrTGDLVRYNPDG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 469 SYKLIDRK----KelINtaaGKSISPVQIENELRQS-PYITEALVI------GEGRKYLTALIEVDGTlamdwarthdpS 537
Cdd:cd05918 350 SLEYVGRKdtqvK--IR---GQRVELGEIEHHLRQSlPGAKEVVVEvvkpkdGSSSPQLVAFVVLDGS-----------S 413
|
410 420 430
....*....|....*....|....*....|.
gi 981242995 538 VTQYADLASSPPVIDLIREEVEKANARLARA 568
Cdd:cd05918 414 SGSGDGDSLFLEPSDEFRALVAELRSKLRQR 444
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
13-510 |
1.13e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 64.32 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 13 ATTTIPALLIERVKNDADANAFFQRRagawvpTTWKGYANAvcsvSAALGAAGVARGDR-----IAIMGDVSREWLIADM 87
Cdd:PRK07867 3 SAPTVAELLLPLAEDDDRGLYFEDSF------TSWREHIRG----SAARAAALRARLDPtrpphVGVLLDNTPEFSLLLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 88 ATICSGAVTVGVYFTASveevryyledsGATLAfagsaeqlRVMKAADTssrllKIVVLDPDWKRSPDETGMNVVSLAEF 167
Cdd:PRK07867 73 AAALSGIVPVGLNPTRR-----------GAALA--------RDIAHADC-----QLVLTESAHAELLDGLDPGVRVINVD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 168 ASHFDGDEVAYLREQSEL--ARPTDLVSLGYTSGTTGAPKGAMLTHV------SMLAGAFTwptfcpaiLSEPQRMVIHL 239
Cdd:PRK07867 129 SPAWADELAAHRDAEPPFrvADPDDLFMLIFTSGTSGDPKAVRCTHRkvasagVMLAQRFG--------LGPDDVCYVSM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 240 PLSHTVARIQAttlpliaktvpYFVDVSADFAkciqevrptsyMAPPRfyqKF-ATQIINHVngsseaeRR------NYT 312
Cdd:PRK07867 201 PLFHSNAVMAG-----------WAVALAAGAS-----------IALRR---KFsASGFLPDV-------RRygatyaNYV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 313 ---LALGIAREVLADRQDagtgdpfkeqlyaicrervfKPLlaRIGFddlrypytASAPVPPEVVTLFQLWGVNLKENYG 389
Cdd:PRK07867 249 gkpLSYVLATPERPDDAD--------------------NPL--RIVY--------GNEGAPGDIARFARRFGCVVVDGFG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 390 QTEmvGGNLAQVTDWSRPGNSGVPLD-----DPAWETRVLPD--------------GEMI-VRGPGLFIGYWNKEAETKA 449
Cdd:PRK07867 299 STE--GGVAITRTPDTPPGALGPLPPgvaivDPDTGTECPPAedadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAE 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981242995 450 ALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK07867 377 RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA 436
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
45-510 |
1.33e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 64.42 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 45 TTWKGYANAVCSVS------AALGAA-----GVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLE 113
Cdd:PRK05620 29 TTWGGAEQEQTTFAaigaraAALAHAlhdelGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 114 DSGATLAFAGS--AEQLRVMKAADTSSRllKIVVLDPDWKRSPDETGMNVVSLAEFASHFDGDEVAY-LREQSElarpTD 190
Cdd:PRK05620 109 HAEDEVIVADPrlAEQLGEILKECPCVR--AVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYdWPELDE----TT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 191 LVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPAILSEPQRMVIHLPLSHtvariqattlpLIAKTVPYfvdvsADF 270
Cdd:PRK05620 183 AAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGESFLCCVPIYH-----------VLSWGVPL-----AAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 271 AKCIQEVRPTSYMAPPRFYQKFATQIINHVNGSSeaerrnytlALGIAREVLADRQDAgtgdpfkeqlyaicrERVfkpl 350
Cdd:PRK05620 247 MSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVP---------TLWIQLMVHYLKNPP---------------ERM---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 351 larigfdDLRYPYTASAPVPPEVVTLF-QLWGVNLKENYGQTEMVggnlaQVTDWSRP--GNSGVPLDD--------PA- 418
Cdd:PRK05620 299 -------SLQEIYVGGSAVPPILIKAWeERYGVDVVHVWGMTETS-----PVGTVARPpsGVSGEARWAyrvsqgrfPAs 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 419 WETRVLPD-----------GEMIVRGPGLFIGYWNKEAETKAALR-----------------DGWLYTGDIVDVGADGSY 470
Cdd:PRK05620 367 LEYRIVNDgqvmestdrneGEIQVRGNWVTASYYHSPTEEGGGAAstfrgedvedandrftaDGWLRTGDVGSVTRDGFL 446
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 981242995 471 KLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK05620 447 TIHDRARDVIRS-GGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
193-510 |
1.44e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 63.96 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 193 SLGYTSGTTGAPKGAMLTHVSMLAGAFTwptfcpAILsePQRMVIHlplshtvARiqATTLPLI------AKTVPYfvdv 266
Cdd:PRK07008 180 SLCYTSGTTGNPKGALYSHRSTVLHAYG------AAL--PDAMGLS-------AR--DAVLPVVpmfhvnAWGLPY---- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 267 SADFAKCiQEVRPTSYMAPPRFYQKFatqiinhvngssEAERrnYTLALGIAREVLadrqdagtgdpfkeQLYAICRErv 346
Cdd:PRK07008 239 SAPLTGA-KLVLPGPDLDGKSLYELI------------EAER--VTFSAGVPTVWL--------------GLLNHMRE-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 347 fkpllARIGFDDLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMVG-GNLAQVTdW---SRPGNS----------- 410
Cdd:PRK07008 288 -----AGLRFSTLRRTVIGGSACPPAMIRTFEdEYGVEVIHAWGMTEMSPlGTLCKLK-WkhsQLPLDEqrkllekqgrv 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 411 --GVPLDDPAWETRVLP-DG----EMIVRGPGLFIGYWNKEAetkAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTa 483
Cdd:PRK07008 362 iyGVDMKIVGDDGRELPwDGkafgDLQVRGPWVIDRYFRGDA---SPLVDGWFPTGDVATIDADGFMQITDRSKDVIKS- 437
|
330 340
....*....|....*....|....*..
gi 981242995 484 AGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK07008 438 GGEWISSIDIENVAVAHPAVAEAACIA 464
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
427-510 |
1.62e-10 |
|
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: 64.01 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITE 505
Cdd:COG1021 381 GELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIAAEEVENLLLAHPAVHD 459
|
....*
gi 981242995 506 ALVIG 510
Cdd:COG1021 460 AAVVA 464
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
44-521 |
2.17e-10 |
|
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: 63.03 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 44 PTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAg 123
Cdd:cd05945 16 TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIA- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 124 saeqlrvmkaadtssrllkivvldpdwkrspdetgmnvvslaefashfDGDEVAYLReqselarptdlvslgYTSGTTGA 203
Cdd:cd05945 95 ------------------------------------------------DGDDNAYII---------------FTSGSTGR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 204 PKGAMLTHvSMLAGAFTWptfcpailsepqrMVIHLPLshtvariqaTTLPLIAKTVPYFVDVS--------ADFAKCIQ 275
Cdd:cd05945 112 PKGVQISH-DNLVSFTNW-------------MLSDFPL---------GPGDVFLNQAPFSFDLSvmdlypalASGATLVP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 276 eVRPTSYMAPPRFYQKFATQIINHVNGSSEAERRNYTLAlGIAREVLAD-RQDAGTGDPFKEQLYAICRERVfkPLlARI 354
Cdd:cd05945 169 -VPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSP-TFTPESLPSlRHFLFCGEVLPHKTARALQQRF--PD-ARI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 355 gfddlrypytasapvppevvtlfqlwgVNLkenYGQTE-MVGGNLAQVTDWSRPGNSGVP------------LDDPAWET 421
Cdd:cd05945 244 ---------------------------YNT---YGPTEaTVAVTYIEVTPEVLDGYDRLPigyakpgaklviLDEDGRPV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 422 RVLPDGEMIVRGPGLFIGYWNKEAETKAALRD----GWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENEL 497
Cdd:cd05945 294 PPGEKGELVISGPSVSKGYLNNPEKTAAAFFPdegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAAL 372
|
490 500
....*....|....*....|....*...
gi 981242995 498 RQSPYITEALVI----GEGRKYLTALIE 521
Cdd:cd05945 373 RQVPGVKEAVVVpkykGEKVTELIAFVV 400
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
427-508 |
3.97e-10 |
|
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: 61.89 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINtAAGKSISPVQIENELRQSPYITEA 506
Cdd:cd17635 197 GTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESIN-CGGVKIAPDEVERIAEGVSGVQEC 275
|
..
gi 981242995 507 LV 508
Cdd:cd17635 276 AC 277
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
57-510 |
7.23e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 61.82 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 57 VSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADT 136
Cdd:PRK07798 41 LAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 137 SSRLLKIVVLDPDwkrSPDETGMNVVSLAEFASHFDGdevaylrEQSELARPTDLVSLGYTSGTTGAPKGAMLTHVSMLA 216
Cdd:PRK07798 121 LPKLRTLVVVEDG---SGNDLLPGAVDYEDALAAGSP-------ERDFGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 217 GAFTWPTFcpailsepqrmvihlplshtvariqattlpliaKTVPYFVDVSADFAKCIQEVRPTSYMAPPRFYQkfATQ- 295
Cdd:PRK07798 191 VLLGGRDF---------------------------------ATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHG--AGQw 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 296 --IINHVNGSSEAERRNYTLAlgiAREVL--ADRQDAG----TGDPFKeqlyaicrervfKPLLARIgfdDLRYPYTAS- 366
Cdd:PRK07798 236 aaFAALFSGQTVVLLPDVRFD---ADEVWrtIEREKVNvitiVGDAMA------------RPLLDAL---EARGPYDLSs 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 367 --------APVPPEVVTLFQ--LWGVNLKENYGQTEmvGGNLAQVTDWSRPGNSGVPLDDPAWETRVL-PDGE------- 428
Cdd:PRK07798 298 lfaiasggALFSPSVKEALLelLPNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPRFTIGPRTVVLdEDGNpvepgsg 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 429 ---MIVRGPGLFIGYWNKEAETKAALR--DG--WLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSP 501
Cdd:PRK07798 376 eigWIARRGHIPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINT-GGEKVFPEEVEEALKAHP 454
|
....*....
gi 981242995 502 YITEALVIG 510
Cdd:PRK07798 455 DVADALVVG 463
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
427-510 |
1.30e-09 |
|
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: 60.80 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITE 505
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINR-GGEKIAAEEVENLLLRHPAVHD 414
|
....*
gi 981242995 506 ALVIG 510
Cdd:cd05920 415 AAVVA 419
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
61-501 |
1.94e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.40 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 61 LGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTAS-------VEEVRYYLEDSGATLAFAGsAEQLRVMKA 133
Cdd:PRK09192 66 LLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQPAAIITP-DELLPWVNE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 134 ADTSSRLLKivVLDPDWKRSPDETGMnvvslaefashfdgdevaylreqsELARPT--DLVSLGYTSGTTGAPKGAMLTH 211
Cdd:PRK09192 145 ATHGNPLLH--VLSHAWFKALPEADV------------------------ALPRPTpdDIAYLQYSSGSTRFPRGVIITH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 212 VSMLAGaftwptfCPAI------LSEPQRMVIHLPLSHTVARIQATTLPLIAK-TVPYFVdvSADFA-------KCIQEV 277
Cdd:PRK09192 199 RALMAN-------LRAIshdglkVRPGDRCVSWLPFYHDMGLVGFLLTPVATQlSVDYLP--TRDFArrplqwlDLISRN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 278 RPTSYMAPPRFYQKFATQiinhVNGSSEAErrnytLALGIAREvladrqdAGTG-DPFK-EQLyaicreRVFKPLLARIG 355
Cdd:PRK09192 270 RGTISYSPPFGYELCARR----VNSKDLAE-----LDLSCWRV-------AGIGaDMIRpDVL------HQFAEAFAPAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 356 FDDlrYPYTAS------------APVPPEVVTLfqLWGVNLKENYGQTEMVGGNLAQVTDWSrpgNSGVPLDDPAWETR- 422
Cdd:PRK09192 328 FDD--KAFMPSyglaeatlavsfSPLGSGIVVE--EVDRDRLEYQGKAVAPGAETRRVRTFV---NCGKALPGHEIEIRn 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 423 ----VLPD---GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIvdvG--ADGSYKLIDRKKELI--NtaaGKSISPV 491
Cdd:PRK09192 401 eagmPLPErvvGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDL---GylLDGYLYITGRAKDLIiiN---GRNIWPQ 474
|
490
....*....|
gi 981242995 492 QIENELRQSP 501
Cdd:PRK09192 475 DIEWIAEQEP 484
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
365-510 |
2.12e-09 |
|
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: 60.08 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 365 ASAPVPPEV-VTLFQLWGVNLKENYGQTEMVGGNLAQVTDW-SRPGNSGVP-------LDDPAWETRVLPDGEMIVRGPG 435
Cdd:cd05929 252 AAAPCPPWVkEQWIDWGGPIIWEYYGGTEGQGLTIINGEEWlTHPGSVGRAvlgkvhiLDEDGNEVPPGEIGEVYFANGP 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 436 LFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05929 332 GFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVG 405
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
383-524 |
4.17e-09 |
|
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: 58.57 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 383 NLKENYGQTEM--VGGNLAQvtDWSRPGNSGVPLddPAWETRVLPD-----GEMIVRGPGLFIGYWNKEAETKaalrDGW 455
Cdd:cd17633 138 NLIEFYGTSELsfITYNFNQ--ESRPPNSVGRPF--PNVEIEIRNAdggeiGKIFVKSEMVFSGYVRGGFSNP----DGW 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981242995 456 LYTGDIVDVGADGSYKLIDRKKELINTAaGKSISPVQIENELRQSPYITEALVIGEGRKY----LTALIEVDG 524
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIG-GINIFPTEIESVLKAIPGIEEAIVVGIPDARfgeiAVALYSGDK 281
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
170-531 |
5.13e-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: 59.02 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 170 HFDGDEVAYLREQSE----LARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWptfcpailsepqRMVIHLPlSHTV 245
Cdd:cd17650 70 DYPAERLQYMLEDSGakllLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW------------RREYELD-SFPV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 246 ARIQATTLPliaktvpyfVDVSA-DFAK----------CIQEVRptsyMAPPRFYqkfatQIINhvngSSEAERRNYTLA 314
Cdd:cd17650 137 RLLQMASFS---------FDVFAgDFARsllnggtlviCPDEVK----LDPAALY-----DLIL----KSRITLMESTPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 315 LgiAREVLADRQDAGTGDPFKEQLYA---ICRERVFKPLLARIGfddlrypytasapvppevvtlfqlWGVNLKENYGQT 391
Cdd:cd17650 195 L--IRPVMAYVYRNGLDLSAMRLLIVgsdGCKAQDFKTLAARFG------------------------QGMRIINSYGVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 392 EM-VGGNLAQVTDWSRPGNSGVPLDDPAWETR--VLPD----------GEMIVRGPGLFIGYWNKEAETKAALRD----- 453
Cdd:cd17650 249 EAtIDSTYYEEGRDPLGDSANVPIGRPLPNTAmyVLDErlqpqpvgvaGELYIGGAGVARGYLNRPELTAERFVEnpfap 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 454 -GWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIGE----GRKYLTALIEVDGTLa 527
Cdd:cd17650 329 gERMYrTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVAVRedkgGEARLCAYVVAAATL- 406
|
....
gi 981242995 528 mDWA 531
Cdd:cd17650 407 -NTA 409
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
51-211 |
6.28e-09 |
|
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: 58.82 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 51 ANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAfagsaeqlrv 130
Cdd:cd12114 19 AERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 131 mkaadtssrllkiVVLDPDWKrsPDETGMNVVSLAEFASHFDGDEVAYLREqselarPTDLVSLGYTSGTTGAPKGAMLT 210
Cdd:cd12114 89 -------------LTDGPDAQ--LDVAVFDVLILDLDALAAPAPPPPVDVA------PDDLAYVIFTSGSTGTPKGVMIS 147
|
.
gi 981242995 211 H 211
Cdd:cd12114 148 H 148
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
65-215 |
2.13e-08 |
|
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: 57.10 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 65 GVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGAtlafagsaeqlrvmkaadtssrllKIV 144
Cdd:cd17656 34 GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGV------------------------RVV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981242995 145 VLDPDWKRSPDETGMNVVSLAEFASHFDGDEVAYLREQSelarptDLVSLGYTSGTTGAPKGAMLTHVSML 215
Cdd:cd17656 90 LTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSD------DLLYIIYTSGTTGKPKGVQLEHKNMV 154
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
51-523 |
3.34e-08 |
|
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: 56.20 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 51 ANAVcsvSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLafagsaeqlrV 130
Cdd:cd17651 30 ANRL---AHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVL----------V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 131 MKAADTSSRLLKIVVLDPDWKRSPDETGmnvvSLAEFASHFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLT 210
Cdd:cd17651 97 LTHPALAGELAVELVAVTLLDQPGAAAG----ADAEPDPALDADDLAYVI---------------YTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 211 HVSmLAGAFTWptFCPAILSEPQRMVIHL-PLSHTVArIQATTLPLIAktvpyfvdvsadfAKCIQEVRPTSYMAPPRFY 289
Cdd:cd17651 158 HRS-LANLVAW--QARASSLGPGARTLQFaGLGFDVS-VQEIFSTLCA-------------GATLVLPPEEVRTDPPALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 290 QKFATQIINHVngsseaerrnyTLALGIAREVLADRQDAGTGDPfkeqlyaicrervfkpllarigfdDLRYPYTASAPV 369
Cdd:cd17651 221 AWLDEQRISRV-----------FLPTVALRALAEHGRPLGVRLA------------------------ALRYLLTGGEQL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 370 P--PEVVTLF-QLWGVNLKENYGQTEMvggnlAQVTDWSRPGNSG-----VPLDDPAWETRV---------LPD---GEM 429
Cdd:cd17651 266 VltEDLREFCaGLPGLRLHNHYGPTET-----HVVTALSLPGDPAawpapPPIGRPIDNTRVyvldaalrpVPPgvpGEL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 430 IVRGPGLFIGYWNKEAETKA------ALRDGWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPY 502
Cdd:cd17651 341 YIGGAGLARGYLNRPELTAErfvpdpFVPGARMYrTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALARHPG 419
|
490 500
....*....|....*....|....*
gi 981242995 503 ITEALVI----GEGRKYLTALIEVD 523
Cdd:cd17651 420 VREAVVLaredRPGEKRLVAYVVGD 444
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
55-534 |
3.47e-08 |
|
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: 56.22 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 55 CSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLafagsaeqlrvmkaa 134
Cdd:cd17649 23 NRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGL--------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 135 dtssrLLkivvldpdwkrspdetgmnvvslaefaSHfDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHvsm 214
Cdd:cd17649 88 -----LL---------------------------TH-HPRQLAYVI---------------YTSGSTGTPKGVAVSH--- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 215 laGAFTwpTFCPAILS----EPQRMVIH-LPLSHTVArIQATTLPLIAktvpyfvdvsadfAKCIQeVRPTSYMAPPRFY 289
Cdd:cd17649 117 --GPLA--AHCQATAEryglTPGDRELQfASFNFDGA-HEQLLPPLIC-------------GACVV-LRPDELWASADEL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 290 qkfATQIINHvnGSSEAErrnytLALGIAREVLADRQDAGTGDPFKEQLYAICRERVfkpllarigfddlrypytasapv 369
Cdd:cd17649 178 ---AEMVREL--GVTVLD-----LPPAYLQQLAEEADRTGDGRPPSLRLYIFGGEAL----------------------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 370 PPEVVTLFQLWGVNLKENYGQTEMVGGNLAQV--TDWSRPGNS---GVPL-------DDPAweTRVLPD---GEMIVRGP 434
Cdd:cd17649 225 SPELLRRWLKAPVRLFNAYGPTEATVTPLVWKceAGAARAGASmpiGRPLggrsayiLDAD--LNPVPVgvtGELYIGGE 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 435 GLFIGYWNKEAETKAA-LRD------GWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEA 506
Cdd:cd17649 303 GLARGYLGRPELTAERfVPDpfgapgSRLYrTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAALLEHPGVREA 381
|
490 500 510
....*....|....*....|....*....|....*
gi 981242995 507 LVI---GEGRKYLTALI--EVDGTLAMDWA--RTH 534
Cdd:cd17649 382 AVValdGAGGKQLVAYVvlRAAAAQPELRAqlRTA 416
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
187-496 |
1.02e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 55.36 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 187 RPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPAilsEPQRMVIH-LPLSHTVARIQATTLPLIAKtVPYFVD 265
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDF---SPEDKVFNaLPVFHSFGLTGGLVLPLLSG-VKVFLY 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 266 VSadfakciqevrPTSYMAPPRF-YQKFATQIInhvnGSSeaerrnyTLALGIARevladrqdagTGDPFKeqlyaicre 344
Cdd:PRK06814 867 PS-----------PLHYRIIPELiYDTNATILF----GTD-------TFLNGYAR----------YAHPYD--------- 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 345 rvfkpllarigFDDLRYPYTASAPVPPEVvtlFQLW----GVNLKENYGQTEmVGGNLAQVTD-WSRPGNSGVPLddPAW 419
Cdd:PRK06814 906 -----------FRSLRYVFAGAEKVKEET---RQTWmekfGIRILEGYGVTE-TAPVIALNTPmHNKAGTVGRLL--PGI 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 420 ETRVLP------DGEMIVRGPGLFIGYWnkEAETKAALR---DGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISP 490
Cdd:PRK06814 969 EYRLEPvpgideGGRLFVRGPNVMLGYL--RAENPGVLEppaDGWYDTGDIVTIDEEGFITIKGRAKRFAKI-AGEMISL 1045
|
....*.
gi 981242995 491 VQIENE 496
Cdd:PRK06814 1046 AAVEEL 1051
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
43-494 |
1.46e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 54.62 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 43 VPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMAT-ICSGAVTVGVYFTASVEEVRyYLEDSGATLAF 121
Cdd:PRK07768 28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLwMRGASLTMLHQPTPRTDLAV-WAEDTLRVIGM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 122 AGSaeqlrvmkaadtssrllKIVVL-DPDWKRSP--DETGMNVVSLAEFASHFDGDEVaylreqseLARPTDLVSLGYTS 198
Cdd:PRK07768 107 IGA-----------------KAVVVgEPFLAAAPvlEEKGIRVLTVADLLAADPIDPV--------ETGEDDLALMQLTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 199 GTTGAPKGAMLTH---VSMLAGAFTWPTFCPailsEPQRMVIHLPLSHTVARIQATTLPLiaktvpYFvdvSADFAKciq 275
Cdd:PRK07768 162 GSTGSPKAVQITHgnlYANAEAMFVAAEFDV----ETDVMVSWLPLFHDMGMVGFLTVPM------YF---GAELVK--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 276 eVRPTSYMAPPRFYQKFATQiinhvngsseaERRNYTLALGIAREVLADRQDAGTGDpfkeqlyaicrervfkpllARIG 355
Cdd:PRK07768 226 -VTPMDFLRDPLLWAELISK-----------YRGTMTAAPNFAYALLARRLRRQAKP-------------------GAFD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 356 FDDLRYPYTASAPVPPEVVTLFQLWGV--NLKEN-----YGQTE------MVGGNLAQVTDW--------------SRPG 408
Cdd:PRK07768 275 LSSLRFALNGAEPIDPADVEDLLDAGArfGLRPEailpaYGMAEatlavsFSPCGAGLVVDEvdadllaalrravpATKG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 409 NS------GVPLDDpaWETRV-------LPD---GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKL 472
Cdd:PRK07768 355 NTrrlatlGPPLPG--LEVRVvdedgqvLPPrgvGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVV 432
|
490 500
....*....|....*....|..
gi 981242995 473 IDRKKELInTAAGKSISPVQIE 494
Cdd:PRK07768 433 CGRVKDVI-IMAGRNIYPTDIE 453
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
59-568 |
3.29e-07 |
|
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: 53.71 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 59 AALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGAtlafagsaeqlrvmkaadtss 138
Cdd:COG1020 516 HHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGA--------------------- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 139 rllKIVVLDPDWKRSPDETGMNVVSLaefashfdgDEVAYLREQSEL----ARPTDLVSLGYTSGTTGAPKGAMLTH--- 211
Cdd:COG1020 575 ---RLVLTQSALAARLPELGVPVLAL---------DALALAAEPATNppvpVTPDDLAYVIYTSGSTGRPKGVMVEHral 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 212 VSMLAGAFTWPTFCPAilsepqrmvihlplshtvARI-QATTLpliaktvpyfvdvSADFAkcIQEVrptsymapprfyq 290
Cdd:COG1020 643 VNLLAWMQRRYGLGPG------------------DRVlQFASL-------------SFDAS--VWEI------------- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 291 kFAtqiinhvngsseaerrnyTLALGiAREVLADRQDAGTGDPFKEqlyAICRERV---------FKPLLARI--GFDDL 359
Cdd:COG1020 677 -FG------------------ALLSG-ATLVLAPPEARRDPAALAE---LLARHRVtvlnltpslLRALLDAApeALPSL 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 360 RYPYTASAPVPPEVVT-LFQLWG----VNLkenYGQTE-MVGGNLAQVTDWSRPGNS---GVPLDDpaweTRV------- 423
Cdd:COG1020 734 RLVLVGGEALPPELVRrWRARLPgarlVNL---YGPTEtTVDSTYYEVTPPDADGGSvpiGRPIAN----TRVyvldahl 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 424 --LPD---GEMIVRGPGLFIGYWNKEAETKAA-LRDGW------LY-TGDIVDVGADGSYKLIDRK----KelINtaaGK 486
Cdd:COG1020 807 qpVPVgvpGELYIGGAGLARGYLNRPELTAERfVADPFgfpgarLYrTGDLARWLPDGNLEFLGRAddqvK--IR---GF 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 487 SISPVQIENELRQSPYITEALVI----GEGRKYLTALIEVDGTLAMDWARTHDPSVTQYADLASSPPVIDLIREEVEKAN 562
Cdd:COG1020 882 RIELGEIEAALLQHPGVREAVVVaredAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNG 961
|
....*.
gi 981242995 563 ARLARA 568
Cdd:COG1020 962 KLDRLA 967
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-510 |
3.37e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.77 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 196 YTSGTTGAPKGAMLTHV---SMLAGA--FTWPTFCP-------AILSEPQRMVIHLPLSHTVARIQATTLPLIAKTVpYF 263
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEdifRMLMGGadFGTGEFTPsedahkaAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV-VL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 264 VDVSADFAKCIQEVrptsymapprfyqkfatqiinhvngssEAERRNYTLALG--IAREVLADRQDAGTGDpfKEQLYAI 341
Cdd:cd05924 89 PDDRFDPEEVWRTI---------------------------EKHKVTSMTIVGdaMARPLIDALRDAGPYD--LSSLFAI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 342 CrervfkpllarigfddlrypyTASAPVPPEV----------VTLFQLWGVNlKENYGQTEMVGGNLAQVTDWSRPGNSG 411
Cdd:cd05924 140 S---------------------SGGALLSPEVkqgllelvpnITLVDAFGSS-ETGFTGSGHSAGSGPETGPFTRANPDT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 412 VPLDDpawETRVLPDGEMIV-----RG--PglfIGYWNKEAETKAALR--DG--WLYTGDIVDVGADGSYKLIDRKKELI 480
Cdd:cd05924 198 VVLDD---DGRVVPPGSGGVgwiarRGhiP---LGYYGDEAKTAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCI 271
|
330 340 350
....*....|....*....|....*....|
gi 981242995 481 NTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05924 272 NT-GGEKVFPEEVEEALKSHPAVYDVLVVG 300
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-532 |
3.55e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADTSSr 139
Cdd:PRK12316 4592 ALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLAS- 4670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 llkiVVLDP--DWKRSPDETGmnvvslaefASHFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSMLAG 217
Cdd:PRK12316 4671 ----LALDRdeDWEGFPAHDP---------AVRLHPDNLAYVI---------------YTSGSTGRPKGVAVSHGSLVNH 4722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 218 AFTWPTFCPaiLSEPQRMVIHLPLSHTVARIQaTTLPLIAktvpyfvdvsadfAKCIQeVRPTSYMAPPRFYQKFATQII 297
Cdd:PRK12316 4723 LHATGERYE--LTPDDRVLQFMSFSFDGSHEG-LYHPLIN-------------GASVV-IRDDSLWDPERLYAEIHEHRV 4785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 298 NHVNGSSEAErrnYTLALGIAREvladrqdagtGDPFKEQLYaICRERVFKPLLARIGFDDLRYPYTASAPVPPEVVTLF 377
Cdd:PRK12316 4786 TVLVFPPVYL---QQLAEHAERD----------GEPPSLRVY-CFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTV 4851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 378 QLWGVNLKENYGQTEM-VGGNLaqvtdwsrPGNSGVPLDDPAWETRVLPDGEMIVRGPGLFIGYWNKEAETKAAL----- 451
Cdd:PRK12316 4852 LLWKARDGDACGAAYMpIGTPL--------GNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpf 4923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 452 --RDGWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI---GEGRKYLTA-LIEVDG 524
Cdd:PRK12316 4924 gaPGGRLYrTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVIaqeGAVGKQLVGyVVPQDP 5002
|
....*...
gi 981242995 525 TLAMDWAR 532
Cdd:PRK12316 5003 ALADADEA 5010
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
61-215 |
4.14e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 53.63 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 61 LGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSaEQLRVMKAADtSSRL 140
Cdd:PRK12467 554 LIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS-HLLAQLPVPA-GLRS 631
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 141 LKIVVLDPDWKRSPDETgmnvVSLAefashFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSML 215
Cdd:PRK12467 632 LCLDEPADLLCGYSGHN----PEVA-----LDPDNLAYVI---------------YTSGSTGQPKGVAISHGALA 682
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
427-510 |
4.27e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 52.83 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAAlrDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEA 506
Cdd:PRK06018 385 GRLKVRGPAVAAAYYRVDGEILDD--DGFFDTGDVATIDAYGYMRITDRSKDVIKS-GGEWISSIDLENLAVGHPKVAEA 461
|
....
gi 981242995 507 LVIG 510
Cdd:PRK06018 462 AVIG 465
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
185-513 |
4.47e-07 |
|
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: 52.82 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 185 LARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFcpAILSEPQRMVIHLPLSHTVARIQATTLPLI-AKTVPYF 263
Cdd:cd05937 83 IVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHD--LNLKNGDRTYTCMPLYHGTAAFLGACNCLMsGGTLALS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 264 VDVSA-DFAKCIQEVRPTsymapprfyqkfatqIINHVngsSEAERrnYTLALGIAREVLADRQDAGTGDPFKEQLYAIC 342
Cdd:cd05937 161 RKFSAsQFWKDVRDSGAT---------------IIQYV---GELCR--YLLSTPPSPYDRDHKVRVAWGNGLRPDIWERF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 343 RERvfkpllarIGFDDLRYPYTASAPVppevVTLFQL----WGVNLKENYGQTE--MVGGNLAQV-----TD--WSRPGN 409
Cdd:cd05937 221 RER--------FNVPEIGEFYAATEGV----FALTNHnvgdFGAGAIGHHGLIRrwKFENQVVLVkmdpeTDdpIRDPKT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 410 S---GVPLDDPawetrvlpdGEMIVRGP----GLFIGYWNKEAETKAAL-------RDGWLYTGDIVDVGADGSYKLIDR 475
Cdd:cd05937 289 GfcvRAPVGEP---------GEMLGRVPfknrEAFQGYLHNEDATESKLvrdvfrkGDIYFRTGDLLRQDADGRWYFLDR 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 981242995 476 kkeLINTAAGKS--ISPVQIENELRQSPYITEALVIG------EGR 513
Cdd:cd05937 360 ---LGDTFRWKSenVSTTEVADVLGAHPDIAEANVYGvkvpghDGR 402
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
186-504 |
4.77e-07 |
|
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: 52.67 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 186 ARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFTWPTFCPAILSEPQrmVIHLPLSHTVA--------------RIQAT 251
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVF--LNWVPLDHVGGlvelhlravylgcqQVHVP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 252 TlPLIAKTVPYFVDVsadfakcIQEVRPTSYMAPPRFYqkfatqiiNHVNGSSEaERRNYTLALGIAREVLadrqDAGtg 331
Cdd:cd05906 242 T-EEILADPLRWLDL-------IDRYRVTITWAPNFAF--------ALLNDLLE-EIEDGTWDLSSLRYLV----NAG-- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 332 dpfkEQLYA-ICRErvFKPLLARIGfddlrypytasapVPPEVVtlfqlwgvnlKENYGQTEMVGG---NLAQVTDWSRP 407
Cdd:cd05906 299 ----EAVVAkTIRR--LLRLLEPYG-------------LPPDAI----------RPAFGMTETCSGviySRSFPTYDHSQ 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 408 GNS----GVPLddPAWETRVLPD----------GEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDI--VDvgaDGSY 470
Cdd:cd05906 350 ALEfvslGRPI--PGVSMRIVDDegqllpegevGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLgfLD---NGNL 424
|
330 340 350
....*....|....*....|....*....|....
gi 981242995 471 KLIDRKKELINTaAGKSISPVQIENELRQSPYIT 504
Cdd:cd05906 425 TITGRTKDTIIV-NGVNYYSHEIEAAVEEVPGVE 457
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
415-508 |
7.36e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 52.30 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 415 DDPAW----ETRVLPDGE---MIVRGPGLFIGYWNKEAETKAAL-RDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGK 486
Cdd:PRK10946 362 DDEVWvadaDGNPLPQGEvgrLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINR-GGE 440
|
90 100
....*....|....*....|...
gi 981242995 487 SISPVQIENELRQSPYITE-ALV 508
Cdd:PRK10946 441 KIAAEEIENLLLRHPAVIHaALV 463
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
427-506 |
1.06e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 51.55 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEA 506
Cdd:PRK05857 375 GTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRIAEGVSGVREA 453
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
16-480 |
2.03e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 50.71 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 16 TIPALLIERVKNDADANAF-F----QRRAGAWVPTTWKGYANAVCSVSAALGAAGVArGDRIAIMGDVSREWLIADMATI 90
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFtFidyeQDPAGVAETLTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 91 CSGAVTVGV---YFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADTSS-----RLLKIVVLDPDWKRSPDetgmnvv 162
Cdd:PRK05850 81 QAGLIAVPLsvpQGGAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPgqsapPVIEVDLLDLDSPRGSD------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 163 slaefASHFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTH-------VSMLAGAFtwpTFCPAILSEPQRM 235
Cdd:PRK05850 154 -----ARPRDLPSTAYLQ---------------YTSGSTRTPAGVMVSHrnvianfEQLMSDYF---GDTGGVPPPDTTV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 236 VIHLPLSHTVARIQATTLPLIAKtvpyfvdvsadfakciqevRPTSYMAPPRFYQKFA---TQIINHVNGSSEAErrNYT 312
Cdd:PRK05850 211 VSWLPFYHDMGLVLGVCAPILGG-------------------CPAVLTSPVAFLQRPArwmQLLASNPHAFSAAP--NFA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 313 LALGIAREVLADRQDAGTGDpfkeqLYAICR--ERV-------FKPLLARIGFDD--LRyP---------YTASAPV--P 370
Cdd:PRK05850 270 FELAVRKTSDDDMAGLDLGG-----VLGIISgsERVhpatlkrFADRFAPFNLREtaIR-PsyglaeatvYVATREPgqP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 371 PEVVTlFQLWG-----VNLKENYGQTEMVGgnlaqvtdWSRPGNSGVPLDDPawETRV-LPD---GEMIVRGPGLFIGYW 441
Cdd:PRK05850 344 PESVR-FDYEKlsaghAKRCETGGGTPLVS--------YGSPRSPTVRIVDP--DTCIeCPAgtvGEIWVHGDNVAAGYW 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 981242995 442 NKEAETK----AALRDG--------WLYTGDIvDVGADGSYKLIDRKKELI 480
Cdd:PRK05850 413 QKPEETErtfgATLVDPspgtpegpWLRTGDL-GFISEGELFIVGRIKDLL 462
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-518 |
2.11e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.11 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADTSSR 139
Cdd:PRK12316 2044 RLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARL 2123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 LLKivvlDPDWkrspdetgmnvvsLAEFASHfdgdevaylREQSELArPTDLVSLGYTSGTTGAPKGAMLTHVSMLAgaf 219
Cdd:PRK12316 2124 PLD----RDAE-------------WADYPDT---------APAVQLA-GENLAYVIYTSGSTGLPKGVAVSHGALVA--- 2173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 220 twptFCPAI-----LSEPQRMVIHLPLSHTVARIQATTlPLIAKTVPYFVDVS----ADFAKCIQEVRPTSYMAPPRFYQ 290
Cdd:PRK12316 2174 ----HCQAAgeryeLSPADCELQFMSFSFDGAHEQWFH-PLLNGARVLIRDDElwdpEQLYDEMERHGVTILDFPPVYLQ 2248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 291 KFAtqiinhvngsSEAERRNYTLALgiarevladRQDAGTGDPFKEQLYAICRERvfkpllarigfddlrypytasapvp 370
Cdd:PRK12316 2249 QLA----------EHAERDGRPPAV---------RVYCFGGEAVPAASLRLAWEA------------------------- 2284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 371 pevvtlfqLWGVNLKENYGQTEMVGGNLAQVTDWSRP-GNSGVPLDDPAWETR---------VLPD---GEMIVRGPGLF 437
Cdd:PRK12316 2285 --------LRPVYLFNGYGPTEAVVTPLLWKCRPQDPcGAAYVPIGRALGNRRayildadlnLLAPgmaGELYLGGEGLA 2356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 438 IGYWNKEAETkaALR---------DGWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEAL 507
Cdd:PRK12316 2357 RGYLNRPGLT--AERfvpdpfsasGERLYrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAV 2433
|
490
....*....|....
gi 981242995 508 VI---GEGRKYLTA 518
Cdd:PRK12316 2434 VVaqdGASGKQLVA 2447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
18-510 |
2.20e-06 |
|
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: 50.51 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 18 PALLIERvkndadANAFFQRRAGAWVPTTWKGYANAVCSVSAALGAAGVARGDRIAIMGD----VSREWLIADMAticsG 93
Cdd:cd05915 4 AAALFGR------KEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFnhfrHLEAYFAVPGM----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 94 AVTVGVYFTASVEEVRYYLEDSGATLAFAGSaeqlRVMKAADTSSRLLKIVVLDPDwKRSPDETGMNVVSLAEfashfdg 173
Cdd:cd05915 74 AVLHTANPRLSPKEIAYILNHAEDKVLLFDP----NLLPLVEAIRGELKTVQHFVV-MDEKAPEGYLAYEEAL------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 174 DEVAYLREQSElarpTDLVSLGYTSGTTGAPKGAMLTHvsmlAGAFTWPTfCPAILSE--PQRMVIHL---PLSHTVARI 248
Cdd:cd05915 142 GEEADPVRVPE----RAACGMAYTTGTTGLPKGVVYSH----RALVLHSL-AASLVDGtaLSEKDVVLpvvPMFHVNAWC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 249 QATTLPLIAKTVPYFVDVSAD---FAKCIQEVRPTSYMAPPrfyqkfatqIINHVNGSSEAERRNYTLALGIarevladr 325
Cdd:cd05915 213 LPYAATLVGAKQVLPGPRLDPaslVELFDGEGVTFTAGVPT---------VWLALADYLESTGHRLKTLRRL-------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 326 QDAGTGDPfkEQLYAICRERVFKPLLArIGFDDLrYPYTASAPVPPEVVTLFQLWGVNLKENYGQTemvggNLAQVTDWS 405
Cdd:cd05915 276 VVGGSAAP--RSLIARFERMGVEVRQG-YGLTET-SPVVVQNFVKSHLESLSEEEKLTLKAKTGLP-----IPLVRLRVA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 406 RPGNSGVPLDDPAweTRVLPdgemiVRGPGLFIGYW-NKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAA 484
Cdd:cd05915 347 DEEGRPVPKDGKA--LGEVQ-----LKGPWITGGYYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI-KSG 418
|
490 500
....*....|....*....|....*.
gi 981242995 485 GKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
56-600 |
4.04e-06 |
|
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: 49.62 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 56 SVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAeqlrvmkaad 135
Cdd:cd17653 34 ALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS---------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 136 tssrllkivvldpdwkrspdetgmnvvslaefashfdGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSML 215
Cdd:cd17653 104 -------------------------------------PDDLAYII---------------FTSGSTGIPKGVMVPHRGVL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 216 AgaftwptfcpAILSEPQRMviHLPLSHTVARIqattlpliaktvpyfvdVSADFAKCIQEVrptsymapprfyqkFATQ 295
Cdd:cd17653 132 N----------YVSQPPARL--DVGPGSRVAQV-----------------LSIAFDACIGEI--------------FSTL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 296 iinhVNGSseaerrnyTLalgiareVLADrqdagTGDPFkEQLYAICRERVFKP-LLARI---GFDDLRYPYTASAPVPP 371
Cdd:cd17653 169 ----CNGG--------TL-------VLAD-----PSDPF-AHVARTVDALMSTPsILSTLspqDFPNLKTIFLGGEAVPP 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 372 EVVtlfQLW--GVNLKENYGQTEM-VGGNLAQVtdwsRPG----------NSGVPLDDPawETRVLPD---GEMIVRGPG 435
Cdd:cd17653 224 SLL---DRWspGRRLYNAYGPTECtISSTMTEL----LPGqpvtigkpipNSTCYILDA--DLQPVPEgvvGEICISGVQ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 436 LFIGYWNKEAETKAA-----LRDGW-LY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQS-PYITEAl 507
Cdd:cd17653 295 VARGYLGNPALTASKfvpdpFWPGSrMYrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQSqPEVTQA- 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 508 vigegrkyltALIEVDGTLamdwarthdpsvtqYADLASSPPVIDLIREEVEKANARLARAEQIKAFRIFPeeltpengv 587
Cdd:cd17653 373 ----------AAIVVNGRL--------------VAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFP--------- 419
|
570
....*....|...
gi 981242995 588 MTATRKKRRKALM 600
Cdd:cd17653 420 LTANGKVDRKALR 432
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
381-510 |
4.20e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 49.64 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 381 GVNLKENYGQTEmvGGNLAQVTDWSRPGNSGVPLDDPAW---ET-------------RVL-PD---GEMIVR-GPGLFIG 439
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAPGVAIynpETltecavarfdahgALLnADeaiGELVNTaGAGFFEG 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981242995 440 YWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:PRK13388 366 YYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-520 |
6.53e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.57 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFagsaeqlrvmkaadTSSR 139
Cdd:PRK12316 552 ALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL--------------SQSH 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 LLKIVVLDpdwkrspdeTGMNVVSLAEFASHFDGdevaYLREQSELA-RPTDLVSLGYTSGTTGAPKGAMLTHvSMLAGA 218
Cdd:PRK12316 618 LGRKLPLA---------AGVQVLDLDRPAAWLEG----YSEENPGTElNPENLAYVIYTSGSTGKPKGAGNRH-RALSNR 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 219 FTWptfcpailsepQRMVIHLPLSHTVAriqattlpliAKTvPYFVDVSAdfakciqevrptsymapprfYQKFatqiin 298
Cdd:PRK12316 684 LCW-----------MQQAYGLGVGDTVL----------QKT-PFSFDVSV--------------------WEFF------ 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 299 hvngsseaerrnYTLALGiAREVLADRQDAGTGDPFKEqlyAICRERV----FKP--LLARIGFDD------LRYPYTAS 366
Cdd:PRK12316 716 ------------WPLMSG-ARLVVAAPGDHRDPAKLVE---LINREGVdtlhFVPsmLQAFLQDEDvasctsLRRIVCSG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 367 APVPPEVV-TLFQ-LWGVNLKENYGQTEMVGGnlaqVTDWS--RPGNSGVPLDDPAWETR---------VLP---DGEMI 430
Cdd:PRK12316 780 EALPADAQeQVFAkLPQAGLYNLYGPTEAAID----VTHWTcvEEGGDSVPIGRPIANLAcyildanlePVPvgvLGELY 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 431 VRGPGLFIGYWNKEAETK-----AALRDG-WLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYI 503
Cdd:PRK12316 856 LAGRGLARGYHGRPGLTAerfvpSPFVAGeRMYrTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWV 934
|
490
....*....|....*..
gi 981242995 504 TEALVIGEGRKYLTALI 520
Cdd:PRK12316 935 REAAVLAVDGKQLVGYV 951
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
15-211 |
7.18e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.97 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 15 TTIPALLIERVKNDADANA-----FFQRRAGAWVPTTWKGYANAVCSVSAALGAAgVARGDRIAIMGDVSREWLIADMAT 89
Cdd:PRK12476 34 TTLISLIERNIANVGDTVAyryldHSHSAAGCAVELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 90 ICSGAVTVGVY---FTASVEEVRYYLEDSGAT--LAFAGSAEQLRVMKAADTSSRLLKIVVLDpdwkRSPDETGMNVVsl 164
Cdd:PRK12476 113 IKAGTIAVPLFapeLPGHAERLDTALRDAEPTvvLTTTAAAEAVEGFLRNLPRLRRPRVIAID----AIPDSAGESFV-- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 981242995 165 aefASHFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTH 211
Cdd:PRK12476 187 ---PVELDTDDVSHLQ---------------YTSGSTRPPVGVEITH 215
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
351-510 |
7.71e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 48.99 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 351 LARIGFDDLRYPYTASAPVPPEVVTLFQ-LWGVNLKENYGQTEMVGGNLAQVTDWSR-PGNSGVP--------LDDpawE 420
Cdd:PRK13382 306 RNRYSGRSLRFAAASGSRMRPDVVIAFMdQFGDVIYNNYNATEAGMIATATPADLRAaPDTAGRPaegteiriLDQ---D 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 421 TRVLPDGE---MIVRGPGLFIGYwnKEAETKAaLRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENEL 497
Cdd:PRK13382 383 FREVPTGEvgtIFVRNDTQFDGY--TSGSTKD-FHDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTL 458
|
170
....*....|...
gi 981242995 498 RQSPYITEALVIG 510
Cdd:PRK13382 459 ATHPDVAEAAVIG 471
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
171-522 |
8.90e-06 |
|
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: 48.70 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 171 FDGDEVAYLREQSE----LARPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFtWPTFCPAILSEpQRMVIHLPLSHTVA 246
Cdd:cd17645 82 YPGERIAYMLADSSakilLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCE-WHRPYFGVTPA-DKSLVYASFSFDAS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 247 RIQ-------ATTLPLIAKTVPYFVDVSADFakCIQEVRPTSYMaPPRFYQKFaTQIINHVngsseaerrnytlalgiAR 319
Cdd:cd17645 160 AWEifphltaGAALHVVPSERRLDLDALNDY--FNQEGITISFL-PTGAAEQF-MQLDNQS-----------------LR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 320 EVLADrqdagtGDPFKeqlyaicrerVFKpllarigfddlRYPYTasapvppevvtlfqlwgvnLKENYGQTEmvggNLA 399
Cdd:cd17645 219 VLLTG------GDKLK----------KIE-----------RKGYK-------------------LVNNYGPTE----NTV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 400 QVTDWS-RPGNSGVPLDDPAWETRVL------------PDGEMIVRGPGLFIGYWNKEAETKAAL-------RDGWLYTG 459
Cdd:cd17645 249 VATSFEiDKPYANIPIGKPIDNTRVYildealqlqpigVAGELCIAGEGLARGYLNRPELTAEKFivhpfvpGERMYRTG 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981242995 460 DIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI----GEGRKYLTALIEV 522
Cdd:cd17645 329 DLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIELAAVLakedADGRKYLVAYVTA 394
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
185-520 |
1.06e-05 |
|
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: 48.20 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 185 LARPTDLVSLGYTSGTTGAPKGAMLTHVSMLagAFTWPTFCPAILSEPQRMVIHLPLSHTVA--RIQATTLP---LIAKT 259
Cdd:cd17644 102 LTQPENLAYVIYTSGSTGKPKGVMIEHQSLV--NLSHGLIKEYGITSSDRVLQFASIAFDVAaeEIYVTLLSgatLVLRP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 260 VPYFVDvSADFAKCIQEVRPTSYMAPPRFYQKFatqiinhvngsseaerrnytlalgiareVLADRQDAGTGdPFKEQLY 339
Cdd:cd17644 180 EEMRSS-LEDFVQYIQQWQLTVLSLPPAYWHLL----------------------------VLELLLSTIDL-PSSLRLV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 340 AICRERVfkpllarigfddlrypytasapVPPEVVTLFQLWG--VNLKENYGQTE-MVGGNLAQVTDWSRPGNSGVPLDD 416
Cdd:cd17644 230 IVGGEAV----------------------QPELVRQWQKNVGnfIQLINVYGPTEaTIAATVCRLTQLTERNITSVPIGR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 417 PAWETRV---------LP---DGEMIVRGPGLFIGYWNKEAETK--------AALRDGWLY-TGDIVDVGADGSYKLIDR 475
Cdd:cd17644 288 PIANTQVyildenlqpVPvgvPGELHIGGVGLARGYLNRPELTAekfishpfNSSESERLYkTGDLARYLPDGNIEYLGR 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 981242995 476 KKELINTaAGKSISPVQIENELRQSPYITEALVIGE----GRKYLTALI 520
Cdd:cd17644 368 IDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVIVRedqpGNKRLVAYI 415
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
15-211 |
1.36e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.50 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 15 TTIPALLIERVKNDADANAF-FQRRAgawvpTTWKGYANAVCSVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSG 93
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALaDARYQ-----FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAG 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 94 AVTVGVYFTASVEEVRYYLEDSGATLAFAgsaeqlrvmkAADTSSRLLKIVVLDPDWKRSPDETGmnvvslaefashfdg 173
Cdd:PRK10252 533 AAWLPLDTGYPDDRLKMMLEDARPSLLIT----------TADQLPRFADVPDLTSLCYNAPLAPQ--------------- 587
|
170 180 190
....*....|....*....|....*....|....*...
gi 981242995 174 dEVAYLReqseLARPTDLVSLGYTSGTTGAPKGAMLTH 211
Cdd:PRK10252 588 -GAAPLQ----LSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-518 |
2.05e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.03 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFagSAEQLRVMKAADTSSR 139
Cdd:PRK12316 3098 RLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL--SQSHLRLPLAQGVQVL 3175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 LLkivvldpdwkrspdETGMNVVSLAEFASHFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSMlaGAF 219
Cdd:PRK12316 3176 DL--------------DRGDENYAEANPAIRTMPENLAYVI---------------YTSGSTGKPKGVGIRHSAL--SNH 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 220 TWPTFCPAILSEPQRMVIHLPLSHTVARIQA-TTLPLIAKTVPYFVDVSADFAKCIQEVRPTSYMAPPRFYQKFATqiin 298
Cdd:PRK12316 3225 LCWMQQAYGLGVGDRVLQFTTFSFDVFVEELfWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQA---- 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 299 hvngsseaerrnyTLALGIAREVLADRQDAGTGDPFKEQLYAicRERVFKPLLARIGfddlrypytasapvPPEVVTLFQ 378
Cdd:PRK12316 3301 -------------FLEEEDAHRCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYG--------------PTEATITVT 3351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 379 LWgvNLKENYGQTEMVGGNLaqvtdwsrPGNSGVPLDDPAWETRVLPDGEMIVRGPGLFIGYWNKEAETKAAL------R 452
Cdd:PRK12316 3352 HW--QCVEEGKDAVPIGRPI--------ANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvP 3421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981242995 453 DGWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIGEGRKYLTA 518
Cdd:PRK12316 3422 GERLYrTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVA 3487
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
188-494 |
2.57e-05 |
|
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: 47.10 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 188 PTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAFtwptfcpAIL-----SEPQRMVIHLPLSHTVARIQATTLPLIAKTVPY 262
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMF-------AILnstewKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 263 FVDvSADFAkciqeVRPTSYM-----------APPRFYQKF-----ATQIINHVNGSS------EAERRNYTLAlgiarE 320
Cdd:cd05908 178 LMP-TRLFI-----RRPILWLkkasehkativSSPNFGYKYflktlKPEKANDWDLSSirmilnGAEPIDYELC-----H 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 321 VLADRQDagtgdPFKeqLYAICRERVFKPLLARIGfddLRYPYTASAPVPPEVVTLFQLWGVNLKEnYGQTEMVGGNLAQ 400
Cdd:cd05908 247 EFLDHMS-----KYG--LKRNAILPVYGLAEASVG---ASLPKAQSPFKTITLGRRHVTHGEPEPE-VDKKDSECLTFVE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 401 VtdwsrpgnsGVPLDDPAW-----ETRVLPD---GEMIVRGPGLFIGYWNKEAETKAALR-DGWLYTGDIvDVGADGSYK 471
Cdd:cd05908 316 V---------GKPIDETDIricdeDNKILPDgyiGHIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTGDL-GFIRNGRLV 385
|
330 340
....*....|....*....|...
gi 981242995 472 LIDRKKELInTAAGKSISPVQIE 494
Cdd:cd05908 386 ITGREKDII-FVNGQNVYPHDIE 407
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
58-216 |
3.52e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.46 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 58 SAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADts 137
Cdd:PRK12467 1613 AHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDG-- 1690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 138 srlLKIVVLDP--DWKRSPDETGMNVVslaefashFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSML 215
Cdd:PRK12467 1691 ---LRSLVLDQedDWLEGYSDSNPAVN--------LAPQNLAYVI---------------YTSGSTGRPKGAGNRHGALV 1744
|
.
gi 981242995 216 A 216
Cdd:PRK12467 1745 N 1745
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
57-518 |
4.08e-05 |
|
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: 46.53 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 57 VSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLafagsaeqlrvmkaadt 136
Cdd:cd17643 25 LARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSL----------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 137 ssrllkiVVLDPDwkrspdetgmnvvslaefashfdgdevaylreqselarptDLVSLGYTSGTTGAPKGAMLTH---VS 213
Cdd:cd17643 88 -------LLTDPD----------------------------------------DLAYVIYTSGSTGRPKGVVVSHanvLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 214 MLAGAFTWPTFcpailSEPQRMV-------------IHLPLSHTvARIqattlpLIaktVPYfvdvsadfakciqEVRPT 280
Cdd:cd17643 121 LFAATQRWFGF-----NEDDVWTlfhsyafdfsvweIWGALLHG-GRL------VV---VPY-------------EVARS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 281 symaPPRFYQKFATQIINHVNGSSEAERRNYTLALGIAREVLADRQDAGTGDPfkeqlyaiCRERVFKPLLARIGFDDlr 360
Cdd:cd17643 173 ----PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEA--------LEAAMLRPWAGRFGLDR-- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 361 ypytasapvpPEVVTLfqlwgvnlkenYGQTEM---VGGNLAQVTDWSRPGNS--GVPLddPAWETRVLPD--------- 426
Cdd:cd17643 239 ----------PQLVNM-----------YGITETtvhVTFRPLDAADLPAAAASpiGRPL--PGLRVYVLDAdgrpvppgv 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 -GEMIVRGPGLFIGYWNKEAETK------AALRDGWLY--TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENEL 497
Cdd:cd17643 296 vGELYVSGAGVARGYLGRPELTAerfvanPFGGPGSRMyrTGDLARRLPDGELEYLGRADEQVKI-RGFRIELGEIEAAL 374
|
490 500
....*....|....*....|....*
gi 981242995 498 RQSPYITEALVI----GEGRKYLTA 518
Cdd:cd17643 375 ATHPSVRDAAVIvredEPGDTRLVA 399
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
421-510 |
5.13e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 46.31 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 421 TRVLPD--GEMIVRGPGLFIGYWNKEAETKAALRDGWLYTGDIVDVGADGSYKLIDRKKELInTAAGKSISPVQIENELR 498
Cdd:PRK07638 326 EEVQKGeiGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLH 404
|
90
....*....|..
gi 981242995 499 QSPYITEALVIG 510
Cdd:PRK07638 405 EHPAVDEIVVIG 416
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
22-258 |
1.16e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.11 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 22 IER-VKNDADANAF----FQR-RAGAWVPTTWKGYANAVCSVSAALGAAGvARGDRIAIMGDVSREWLIADMATICSGAV 95
Cdd:PRK07769 27 VERwAKVRGDKLAYrfldFSTeRDGVARDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 96 TVGVYFTAS---VEEVRYYLEDS--GATLAFAGSAEQLRVMKAADTSSRLLKIVVLDPdwkrSPDETGMNVVSLAefash 170
Cdd:PRK07769 106 AVPLFDPAEpghVGRLHAVLDDCtpSAILTTTDSAEGVRKFFRARPAKERPRVIAVDA----VPDEVGATWVPPE----- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 171 FDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSMLAGAFtwpTFCPAI-LSEPQRMVIHLPLSHTVARIQ 249
Cdd:PRK07769 177 ANEDTIAYLQ---------------YTSGSTRIPAGVQITHLNLPTNVL---QVIDALeGQEGDRGVSWLPFFHDMGLIT 238
|
....*....
gi 981242995 250 ATTLPLIAK 258
Cdd:PRK07769 239 VLLPALLGH 247
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
60-216 |
3.19e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 43.76 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSReWLIADMAticsGAVTVGVyftasveevRYYLEDSGAtlafagSAEQLrvmkaADTSSR 139
Cdd:PRK07788 90 GLLALGVRAGDGVAVLARNHR-GFVLALY----AAGKVGA---------RIILLNTGF------SGPQL-----AEVAAR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 L-LKIVVLD-----------PD------WKRSPDETGMNVVSLAEFASHFDGDEVAYLREQSelaRPTDLVSLgyTSGTT 201
Cdd:PRK07788 145 EgVKALVYDdeftdllsalpPDlgrlraWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPP---KPGGIVIL--TSGTT 219
|
170
....*....|....*
gi 981242995 202 GAPKGAMLTHVSMLA 216
Cdd:PRK07788 220 GTPKGAPRPEPSPLA 234
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
196-520 |
4.55e-04 |
|
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: 43.11 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 196 YTSGTTGAPKGAMLTH---VSMLAGAFTWptfcpAILSEPQRMVIHLPLSHTVARIQATTLPLIA-KTVPYFVDVSA-DF 270
Cdd:cd05940 88 YTSGTTGLPKAAIISHrraWRGGAFFAGS-----GGALPSDVLYTCLPLYHSTALIVGWSACLASgATLVIRKKFSAsNF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 271 AKCIQEvrptsymapprfYQKFATQIInhvngsseAERRNYTLAlgiAREVLADRqdagtgdpfKEQLYAIC----RERV 346
Cdd:cd05940 163 WDDIRK------------YQATIFQYI--------GELCRYLLN---QPPKPTER---------KHKVRMIFgnglRPDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 347 FKPLLARIGFDDLRYPYTASapvppEVVTLFqlwgVNLkenYGQTEMVGGNLAQVTDWSRPG------NSGVPLDDPAWE 420
Cdd:cd05940 211 WEEFKERFGVPRIAEFYAAT-----EGNSGF----INF---FGKPGAIGRNPSLLRKVAPLAlvkydlESGEPIRDAEGR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 421 TRVLPDGEmivrgPGL----------FIGYWNKEAETKAALR------DGWLYTGDIVDVGADGSYKLIDRkkeLINTA- 483
Cdd:cd05940 279 CIKVPRGE-----PGLlisrinplepFDGYTDPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYFVDR---LGDTFr 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 981242995 484 -AGKSISPVQIENELRQSPYITEALVIG------EGRKYLTALI 520
Cdd:cd05940 351 wKGENVSTTEVAAVLGAFPGVEEANVYGvqvpgtDGRAGMAAIV 394
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-214 |
5.99e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 65 GVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAGSAEQLRVMKAADTSSRLLKIV 144
Cdd:PRK05691 1177 GVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSL 1256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 145 VLDpDWKRSPDetgmnvvslaefASHFDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHVSM 214
Cdd:PRK05691 1257 HLD-SWPSQAP------------GLHLHGDNLAYVI---------------YTSGSTGQPKGVGNTHAAL 1298
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
60-549 |
6.64e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 43.23 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 60 ALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAFAgsaeQLRVMKAADTSSR 139
Cdd:PRK12467 3136 RLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT----QAHLLEQLPAPAG 3211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 140 LLKIVVLDPDWKRSPDETGMNVVslaefashfDGDEVAYLReqselarptdlvslgYTSGTTGAPKGAMLTHvsmlaGAF 219
Cdd:PRK12467 3212 DTALTLDRLDLNGYSENNPSTRV---------MGENLAYVI---------------YTSGSTGKPKGVGVRH-----GAL 3262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 220 TwpTFCPAI-----LSEPQRMVIHLPLSHTVARIQATTlPLIAktvpyfvdvsadfAKCIQeVRPTSYMAPPRFYQKfat 294
Cdd:PRK12467 3263 A--NHLCWIaeayeLDANDRVLLFMSFSFDGAQERFLW-TLIC-------------GGCLV-VRDNDLWDPEELWQA--- 3322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 295 qiINhvngsseaeRRNYTLALGIAREVLADRQDAGTGDPFKEQLYAICRERVFKPLLARIgfddlrypytaSAPVPPevv 374
Cdd:PRK12467 3323 --IH---------AHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQV-----------KRKLKP--- 3377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 375 tlfqlwgVNLKENYGQTEMVggnlAQVTDWSRPGNS---------GVP--------LDDPAWETRVLPDGEMIVRGPGLF 437
Cdd:PRK12467 3378 -------RGLTNGYGPTEAV----VTVTLWKCGGDAvceapyapiGRPvagrsiyvLDGQLNPVPVGVAGELYIGGVGLA 3446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 438 IGYWNKEAETkaALR---------DGWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEAL 507
Cdd:PRK12467 3447 RGYHQRPSLT--AERfvadpfsgsGGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLLQHPSVREAV 3523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 981242995 508 VI---GEGRKYLTALIeVDGTLAMDWArthdpsVTQYADLASSPP 549
Cdd:PRK12467 3524 VLardGAGGKQLVAYV-VPADPQGDWR------ETLRDHLAASLP 3561
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
185-532 |
1.46e-03 |
|
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: 41.47 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 185 LARPTDLVSLGYTSGTTGAPKGAMLTH--VSMLAGAFtwptfcpailsepqrmvihlplshtVARIQattlpliaktvpy 262
Cdd:cd17652 89 LTTPDNLAYVIYTSGSTGRPKGVVVTHrgLANLAAAQ-------------------------IAAFD------------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 263 fvdvsadfakciqeVRPTSymappRFYQkFATQiinhvngSSEAERRNYTLALGI-AREVLADRQDAGTGDPFKEQLYAI 341
Cdd:cd17652 131 --------------VGPGS-----RVLQ-FASP-------SFDASVWELLMALLAgATLVLAPAEELLPGEPLADLLREH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 342 CRERVFKP--LLARI---GFDDLRYPYTASAPVPPEVVtlfQLW--GVNLKENYGQTEM-VGGNLAQVTdwsrPGNSGVP 413
Cdd:cd17652 184 RITHVTLPpaALAALppdDLPDLRTLVVAGEACPAELV---DRWapGRRMINAYGPTETtVCATMAGPL----PGGGVPP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 414 LDDPAWETRV---------LP---DGEMIVRGPGLFIGYWNKEAETkaALR---------DGWLY-TGDIVDVGADGSYK 471
Cdd:cd17652 257 IGRPVPGTRVyvldarlrpVPpgvPGELYIAGAGLARGYLNRPGLT--AERfvadpfgapGSRMYrTGDLARWRADGQLE 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242995 472 LIDRKKELINTaAGKSISPVQIENELRQSPYITEALVI----GEGRKYLTALIEVDGTLAMDWAR 532
Cdd:cd17652 335 FLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEAVVVvrddRPGDKRLVAYVVPAPGAAPTAAE 398
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
196-246 |
2.07e-03 |
|
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: 41.12 E-value: 2.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 981242995 196 YTSGTTGAPKGAMLTHVSMLAGAFTWPtFCPAilsePQRMVIH--LPLSHTVA 246
Cdd:cd05938 151 YTSGTTGLPKAARISHLRVLQCSGFLS-LCGV----TADDVIYitLPLYHSSG 198
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
57-246 |
2.14e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 41.01 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 57 VSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVtVGVYFTASVEEV-RYYLEDSGATLAFAGSAEQLRVMKAAD 135
Cdd:PRK08279 75 YAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV-VALLNTQQRGAVlAHSLNLVDAKHLIVGEELVEAFEEARA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 136 TSSRLLKIVVLDPDWKRSPDEtgmnVVSLAEFASHFDGDEVAyLREQSELARPTDLVslgYTSGTTGAPKGAMLTHVS-M 214
Cdd:PRK08279 154 DLARPPRLWVAGGDTLDDPEG----YEDLAAAAAGAPTTNPA-SRSGVTAKDTAFYI---YTSGTTGLPKAAVMSHMRwL 225
|
170 180 190
....*....|....*....|....*....|...
gi 981242995 215 LAGAftwpTFCPAI-LSEPQRMVIHLPLSHTVA 246
Cdd:PRK08279 226 KAMG----GFGGLLrLTPDDVLYCCLPLYHNTG 254
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
427-527 |
2.43e-03 |
|
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: 40.76 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETKAALR------DGWLY-TGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQ 499
Cdd:cd12115 295 GELYIGGAGVARGYLGRPGLTAERFLpdpfgpGARLYrTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRS 373
|
90 100 110
....*....|....*....|....*....|..
gi 981242995 500 SPYITEALVI----GEGRKYLTALIEVDGTLA 527
Cdd:cd12115 374 IPGVREAVVVaigdAAGERRLVAYIVAEPGAA 405
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
359-508 |
2.98e-03 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 40.65 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 359 LRYPYTASAPVPPEVVTLFQLW---GVNLKENYGQTE-----MVGGN--LAQVTDWSRPGN--------SGV-----PLD 415
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAMlppDAEILTPYGATEalpisSIESReiLFATRAATDNGAgicvgrpvDGVevriiAIS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 416 D---PAW-ETRVLPD---GEMIVRGPGLFIGYWNKEAETKAA-LRDG----WLYTGDIVDVGADGSYKLIDRKKELINTA 483
Cdd:PRK09274 370 DapiPEWdDALRLATgeiGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETA 449
|
170 180
....*....|....*....|....*.
gi 981242995 484 AGkSISPVQIENELRQSPYITE-ALV 508
Cdd:PRK09274 450 GG-TLYTIPCERIFNTHPGVKRsALV 474
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
56-219 |
3.18e-03 |
|
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: 40.38 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 56 SVSAALGAAGVARGDRIAIMGDVSREWLIADMATICSGAVTVGVYFTASVEEVRYYLEDSGATLAfagsaeqlrvmkaad 135
Cdd:cd12115 36 RLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV--------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 136 tssrllkivvldpdwkrspdetgmnvvslaefashfdgdevaylreqseLARPTDLVSLGYTSGTTGAPKGAMLTHVSml 215
Cdd:cd12115 101 -------------------------------------------------LTDPDDLAYVIYTSGSTGRPKGVAIEHRN-- 129
|
....
gi 981242995 216 AGAF 219
Cdd:cd12115 130 AAAF 133
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
381-510 |
3.71e-03 |
|
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: 40.38 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 381 GVNLKENYGQTE----MVGGNLAQVTDWSRPGNSGVPLddPAWETRVLPD----------GEMIVRGP---GLFIGYW-N 442
Cdd:cd05967 380 GVPVIDHWWQTEtgwpITANPVGLEPLPIKAGSPGKPV--PGYQVQVLDEdgepvgpnelGNIVIKLPlppGCLLTLWkN 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 443 KEAETKAALRD--GWLYTGDIVDVGADGSYKLIDRKKELINTaAGKSISPVQIENELRQSPYITEALVIG 510
Cdd:cd05967 458 DERFKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINV-AGHRLSTGEMEESVLSHPAVAECAVVG 526
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
196-248 |
4.84e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 39.72 E-value: 4.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 981242995 196 YTSGTTGAPKGAMLTH---VSMLAGAFTwpTFCpaiLSEPQRMVIHLPLSHTVARI 248
Cdd:cd05939 111 YTSGTTGLPKAAVIVHsryYRIAAGAYY--AFG---MRPEDVVYDCLPLYHSAGGI 161
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
185-215 |
5.45e-03 |
|
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: 39.69 E-value: 5.45e-03
10 20 30
....*....|....*....|....*....|.
gi 981242995 185 LARPTDLVSLGYTSGTTGAPKGAMLTHVSML 215
Cdd:cd17648 90 ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVV 120
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
427-512 |
6.06e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 39.75 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 427 GEMIVRGPGLFIGYWNKEAETkaalRDGWLYTGDIVDVGaDGSYKLIDRKKELInTAAGKSISPVQIENELRQSPYITEA 506
Cdd:PRK05851 373 GEIEIRGASMMSGYLGQAPID----PDDWFPTGDLGYLV-DGGLVVCGRAKELI-TVAGRNIFPTEIERVAAQVRGVREG 446
|
....*.
gi 981242995 507 LVIGEG 512
Cdd:PRK05851 447 AVVAVG 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
187-461 |
7.19e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 39.77 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 187 RPTDLVSLGYTSGTTGAPKGAMLTHVSMLAGAftWPTFCP-AILSEPQRMVIH-LPLSHTVARIQATTLPlIAKTVPyfv 264
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANE--QLIRHGfGIDLNPDDVIVSwLPLYHDMGLIGGLLQP-IFSGVP--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 265 dvsadfakCIqevrptsYMAPprfyqkfatqiinhvngsseaerrNYTLALGIaREVLADRQDAGT--GDPfkEQLYAIC 342
Cdd:PRK05691 238 --------CV-------LMSP------------------------AYFLERPL-RWLEAISEYGGTisGGP--DFAYRLC 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 343 RERVFKPLLARIGFDDLRYPYTASAPVPPEVVTLF--QLWGVNLKEN-----YGQTE----MVGG--------------- 396
Cdd:PRK05691 276 SERVSESALERLDLSRWRVAYSGSEPIRQDSLERFaeKFAACGFDPDsffasYGLAEatlfVSGGrrgqgipaleldaea 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 397 ---NLAQVTD--------WSRPGNsGVPLDDPAwETRVLPD---GEMIVRGPGLFIGYW-NKEAETKAAL-RDG--WLYT 458
Cdd:PRK05691 356 larNRAEPGTgsvlmscgRSQPGH-AVLIVDPQ-SLEVLGDnrvGEIWASGPSIAHGYWrNPEASAKTFVeHDGrtWLRT 433
|
...
gi 981242995 459 GDI 461
Cdd:PRK05691 434 GDL 436
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
422-510 |
8.23e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.21 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242995 422 RVLP----------DGEMIVRGPGLFIGYWNKEAETkaalrDGWLYTGDIVDVGADGSYKLIDRKKELINTAaGKSISPV 491
Cdd:PRK07445 287 QVLPhaqitipanqTGNITIQAQSLALGYYPQILDS-----QGIFETDDLGYLDAQGYLHILGRNSQKIITG-GENVYPA 360
|
90
....*....|....*....
gi 981242995 492 QIENELRQSPYITEALVIG 510
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLG 379
|
|
| |
