|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-600 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 726.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 3 SDIDSANNLVELFLKRAAEKGDLPFLGARIGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLA 82
Cdd:COG1022 5 SDVPPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 83 IMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTEKLLRPLHGALQASGIADHVIGIDDLHRQQSSGflFHRWDSMFA 162
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPR--LLSLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 163 -GDAAEARQAVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLSHAYE 241
Cdd:COG1022 163 lGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFLPLAHVFE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 242 HTGGQFLpISVGAQIYYAEGLEKLASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTALEVGERRAA--- 318
Cdd:COG1022 239 RTVSYYA-LAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARarl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 319 --GKPKFGDGLRDALVGRLLKPKIRQRFGGRIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAgIA 396
Cdd:COG1022 318 agKSPSLLLRLKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGD-NR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 397 MHSVGPAMRGVDIRIAEDGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDN 475
Cdd:COG1022 397 IGTVGPPLPGVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 476 VAPQKVEGMLTLQPEIGQAMVAGDKKPYIVGLIVPDAEWTLEWCREQGKQFDckKVQEL---PEFRNAVRAAVDRVNKDL 552
Cdd:COG1022 477 VAPQPIENALKASPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYT--SYAELaqdPEVRALIQEEVDRANAGL 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2786869514 553 SVVEKVRQFAFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYRG 600
Cdd:COG1022 555 SRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
34-586 |
2.02e-173 |
|
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: 499.43 E-value: 2.02e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKA 113
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVSTekllrplhgalqasgiADhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGT 193
Cdd:cd05907 81 LFVED----------------PD----------------------------------------------DLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 194 GGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLEKLASNIEETR 273
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERL----PATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 274 PTIMVVVPRLFEVLRTRImkQVQKQGGLAEKLMNTALevgerraagkpkfgdglrdalvgrllkpkirqrfGGRIKAMVS 353
Cdd:cd05907 175 PTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAV----------------------------------GGRLRFAAS 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 354 GGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAgIAMHSVGPAMRGVDIRIAEDGEILVRGELVMQGYWHNEA 433
Cdd:cd05907 219 GGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGD-NRIGTVGKPLPGVEVRIADDGEILVRGPNVMLGYYKNPE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 434 ET-ERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPYIVGLIVPDA 512
Cdd:cd05907 298 ATaEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDP 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 513 EWTLEWCREQGKQF-DCKKVQELPEFRNAVRAAVDRVNKDLSVVEKVRQFAFADEPFTIENEEMTPSMKIRRHKI 586
Cdd:cd05907 378 EALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
34-599 |
3.18e-120 |
|
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: 366.93 E-value: 3.18e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLRALGLR--DGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGA 111
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 112 KAVIVStekllrplhgalqaSGIAdhVIGIDDLHRQqssgflfhrwdsmfagdAAEARQAVEQRiagiGRGDTACIIYTS 191
Cdd:cd05927 81 SIVFCD--------------AGVK--VYSLEEFEKL-----------------GKKNKVPPPPP----KPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 192 GTGGAPRGVMQHHGAILCNVAGAAEILIEDFGIADDERFLSFLPLSHAYEHTgGQFLPISVGAQI-YYAEGLEKLASNIE 270
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERV-VEALFLYHGAKIgFYSGDIRLLLDDIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 271 ETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTALEVGERRAagkpKFGDGLRDALVGRLLKPKIRQRFGGRIKA 350
Cdd:cd05927 203 ALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAEL----RSGVVRASPFWDKLVFNKIKQALGGNVRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 MVSGGAPLNPEVGIFFES-MGLTMLQGYGQTEAGPVISCNRPAAGIAMHsVGPAMRGVDIRI---------AED----GE 416
Cdd:cd05927 279 MLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGH-VGGPLPCAEVKLvdvpemnydAKDpnprGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 417 ILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAM 495
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 496 VAGD-KKPYIVGLIVPDAEWTLEWCREQ-GKQFDCKKVQELPEFRNAVRAAVDRVNKD--LSVVEKVRQFAFADEPFTIE 571
Cdd:cd05927 438 VYGDsLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKEngLKGFEQVKAIHLEPEPFSVE 517
|
570 580
....*....|....*....|....*...
gi 2786869514 572 NEEMTPSMKIRRHKIKERYAERLDALYR 599
Cdd:cd05927 518 NGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
15-469 |
2.52e-99 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 308.47 E-value: 2.52e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 15 FLKRAAEKGDLPFLGariGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTY 94
Cdd:pfam00501 1 LERQAARTPDKTALE---VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 95 ITNTERDHAHILDNSGAKAVIVSTEKLLRPLHGALQASGIADHVIGIDDLHRQQSSGFLFhrwdsmfagdAAEARQAVEQ 174
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPE----------EAKPADVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 175 RIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGA 254
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 255 QIYYAEG-----LEKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrd 329
Cdd:pfam00501 228 TVVLPPGfpaldPAALLELIERYKVTVLYGVPTLLNML------------------------------------------ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 330 alvgrLLKPKIRQRFGGRIKAMVSGGAPLNPEVGIFFES-MGLTMLQGYGQTEAGPVISCNRPAAGIA--MHSVGPAMRG 406
Cdd:pfam00501 266 -----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLDEDLrsLGSVGRPLPG 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 407 VDIRIAED-----------GEILVRGELVMQGYWHNEAETERTIK-DGWLHTGDIGHVDDKGRIVITDRKKDMIV 469
Cdd:pfam00501 341 TEVKIVDDetgepvppgepGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
34-590 |
1.50e-97 |
|
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: 308.97 E-value: 1.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKA 113
Cdd:cd17641 7 GIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVSTEKLLRPLHGALQASGIADHVIGIDDL-HRQQSSGFLFHRWDSMFAGDAAEARQ--AVEQRIAGIGRGDTACIIYT 190
Cdd:cd17641 87 VIAEDEEQVDKLLEIADRIPSVRYVIYCDPRgMRKYDDPRLISFEDVVALGRALDRRDpgLYEREVAAGKGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 191 SGTGGAPRGVMQHHGAILCNVAGAAEIlieDFGIADDErFLSFLPLSHAYEH--TGGQflPISVGAQIYYAEGLEKLASN 268
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLGHCAAYLAA---DPLGPGDE-YVSVLPLPWIGEQmySVGQ--ALVCGFIVNFPEEPETMMED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 269 IEETRPTIMVVVPRLFEVL----RTRIMKQVQKQGGLAEKLMNTALEVGERRAAGKP-KFGDGLRDALVGRLLKPKIRQR 343
Cdd:cd17641 241 LREIGPTFVLLPPRVWEGIaadvRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPvSLWLRLASWLADALLFRPLRDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 344 FG-GRIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGpVISCNRPAAGIAMHSVGPAMRGVDIRIAEDGEILVRGE 422
Cdd:cd17641 321 LGfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELA-GAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILVRSP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 423 LVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKK 501
Cdd:cd17641 400 GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 502 PYIVGLIVPDAEWTLEWCREQGKQFdcKKVQEL---PEFRNAVRAAVDRVNKDLSVVEKVRQFAFADEPFTIENEEMTPS 578
Cdd:cd17641 480 PYLTAFICIDYAIVGKWAEQRGIAF--TTYTDLasrPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELTRT 557
|
570
....*....|..
gi 2786869514 579 MKIRRHKIKERY 590
Cdd:cd17641 558 RKVRRGVIAEKY 569
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
33-590 |
1.49e-96 |
|
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: 304.39 E-value: 1.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAK 112
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 113 AVIVSteKLlrpLHGALQASGIADHVIGIddLHRQQSSGFLFHRWDSMFagdaaeARQAVEQRIAGIGRGDTACIIYTSG 192
Cdd:cd05932 81 ALFVG--KL---DDWKAMAPGVPEGLISI--SLPPPSAANCQYQWDDLI------AQHPPLEERPTRFPEQLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 193 TGGAPRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLEKLASNIEET 272
Cdd:cd05932 148 TTGQPKGVMLTFG----SFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 273 RPTIMVVVPRLFEVLRTRIMKQVQKQgglaeklmntalevgerraagkpKFGDGLRDALVGRLLKPKIRQRFG-GRIKAM 351
Cdd:cd05932 224 RPTLFFSVPRLWTKFQQGVQDKIPQQ-----------------------KLNLLLKIPVVNSLVKRKVLKGLGlDQCRLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 352 VSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGiAMHSVGPAMRGVDIRIAEDGEILVRGELVMQGYWHN 431
Cdd:cd05932 281 GCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRD-KIGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 432 EAET-ERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPYIVGLIVP 510
Cdd:cd05932 360 PEATaEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 511 DAEwtlewCREQGKQFDCKkvqelpEFRNAVRAAVDRVNKDLSVVEKVRQFAFADEPFTIENEEMTPSMKIRRHKIKERY 590
Cdd:cd05932 440 SEE-----ARLRADAFARA------ELEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
34-586 |
3.66e-96 |
|
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: 301.97 E-value: 3.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKA 113
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIV-STEKllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSG 192
Cdd:cd17640 81 LVVeNDSD--------------------------------------------------------------DLATIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 193 TGGAPRGVMQHHGAILCNVAGAAEILIEDFGiaddERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAegLEKLASNIEET 272
Cdd:cd17640 99 TTGNPKGVMLTHANLLHQIRSLSDIVPPQPG----DRFLSILPIWHSYERSAEYFIFACGCSQAYTS--IRTLKDDLKRV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 273 RPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTALevgerraagkpkfgdglrdalvgrllkpkirqrFGGRIKAMV 352
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFL---------------------------------SGGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 353 SGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAmHSVGPAMRGVDIRI-----------AEDGEILVRG 421
Cdd:cd17640 220 SGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVR-GSVGRPLPGTEIKIvdpegnvvlppGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 422 ELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDK 500
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 501 KPYIVGLIVPDAEWTLEWCREQGKQFDCKKVQ------ELPEFRNAVRaavDRVNKDL--SVVEKVRQFAFADEPFtIEN 572
Cdd:cd17640 379 QKRLGALIVPNFEELEKWAKESGVKLANDRSQllaskkVLKLYKNEIK---DEISNRPgfKSFEQIAPFALLEEPF-IEN 454
|
570
....*....|....
gi 2786869514 573 EEMTPSMKIRRHKI 586
Cdd:cd17640 455 GEMTQTMKIKRNVV 468
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
11-600 |
2.03e-95 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 305.87 E-value: 2.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGDLPFLGARIG-----GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMA 85
Cdd:PLN02736 46 LHDNFVYAVETFRDYKYLGTRIRvdgtvGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 86 SGCITVPTYITNTERDHAHILDNSGAKAVIVSTEKLLRPLHGALQASGIADHVI--GIDDL--HRQQSSGFLFHRWDSMF 161
Cdd:PLN02736 126 YSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPSVRLIVVvgGADEPlpSLPSGTGVEIVTYSKLL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 162 AGDAAEARQAVEQRiagigRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAeiLIEDFGIADdeRFLSFLPLSHAYE 241
Cdd:PLN02736 206 AQGRSSPQPFRPPK-----PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSS--LSTKFYPSD--VHISYLPLAHIYE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 242 HTGgQFLPISVGAQI-YYAEGLEKLASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTALEVgERRAAGK 320
Cdd:PLN02736 277 RVN-QIVMLHYGVAVgFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNA-KKQALEN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 321 PKFGDGLRDalvgRLLKPKIRQRFGGRIKAMVSGGAPLNPEVGIFFE-SMGLTMLQGYGQTEAGPVISCNRPAAGIAMHs 399
Cdd:PLN02736 355 GKNPSPMWD----RLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRiCFGGRVLEGYGMTETSCVISGMDEGDNLSGH- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 400 VGPAMRGVDIRIA---------ED-----GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRK 464
Cdd:PLN02736 430 VGSPNPACEVKLVdvpemnytsEDqpyprGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRK 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 465 KDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDK-KPYIVGLIVPDAEWTLEWCREQGKQF-DCKKVQELPEFRNAVR 542
Cdd:PLN02736 510 KNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSlNSSLVAVVVVDPEVLKAWAASEGIKYeDLKQLCNDPRVRAAVL 589
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 543 AAVDRVNKDlsvvEKVRQFAFA------DEPFTIENEEMTPSMKIRRHKIKERYAERLDALYRG 600
Cdd:PLN02736 590 ADMDAVGRE----AQLRGFEFAkavtlvPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
11-593 |
2.47e-94 |
|
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: 296.72 E-value: 2.47e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGDLPFLGARiggsWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCIT 90
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 91 VPTYITNTERDHAHILDNSGAKAVIvstekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearq 170
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 171 aveqriagigrgdTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEilieDFGIADDERFLSFLPLSHAYEHTGGQFLPI 250
Cdd:COG0318 102 -------------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAA----ALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 251 SVGAQIYYAEGL--EKLASNIEETRPTIMVVVPRLFEvlrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglr 328
Cdd:COG0318 165 LAGATLVLLPRFdpERVLELIERERVTVLFGVPTMLA------------------------------------------- 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 329 dalvgRLLK-PKIRQRFGGRIKAMVSGGAPLNPEVG-IFFESMGLTMLQGYGQTEAGPVISCNRPAAGIA-MHSVGPAMR 405
Cdd:COG0318 202 -----RLLRhPEFARYDLSSLRLVVSGGAPLPPELLeRFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrPGSVGRPLP 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 406 GVDIRIA----------EDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDN 475
Cdd:COG0318 277 GVEVRIVdedgrelppgEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GEN 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 476 VAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEWTLEWC----REQGKQFDckkvqeLPEFRNAVRAAVDRVnkd 551
Cdd:COG0318 356 VYPAEVEEVLAAHPGVAEAAVVG----------VPDEKWGERVVafvvLRPGAELD------AEELRAFLRERLARY--- 416
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2786869514 552 lsvveKV-RQFAFADE-PftieneeMTPSMKIRRHKIKERYAER 593
Cdd:COG0318 417 -----KVpRRVEFVDElP-------RTASGKIDRRALRERYAAG 448
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
38-583 |
1.47e-92 |
|
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: 292.42 E-value: 1.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVS 117
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 118 TEKllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTGGAP 197
Cdd:cd05914 87 DED--------------------------------------------------------------DVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 198 RGVMQHHGAILCNVAGAAEILIedfgIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYaegLEKLASNI------EE 271
Cdd:cd05914 105 KGVMLTYRNIVSNVDGVKEVVL----LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVF---LDKIPSAKiialafAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 272 TRPTIMVvvPRLFEVLRTRIMKQVQKQGG------LAEKLMNTALevgeRRAAGKpkfgdglrdalvgrllkpKIRQRFG 345
Cdd:cd05914 178 VTPTLGV--PVPLVIEKIFKMDIIPKLTLkkfkfkLAKKINNRKI----RKLAFK------------------KVHEAFG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 346 GRIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAgIAMHSVGPAMRGVDIRIA------EDGEILV 419
Cdd:cd05914 234 GNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNR-IRLGSAGKVIDGVEVRIDspdpatGEGEIIV 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 420 RGELVMQGYWHNEAET-ERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVA- 497
Cdd:cd05914 313 RGPNVMKGYYKNPEATaEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVv 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 498 GDKKpyIVGLIVPDAEwtlewcREQGKQfdcKKVQELPEfrNAVRAAVDRVNKDLSVVEKVRQFAFADEPFtieneEMTP 577
Cdd:cd05914 393 QEKK--LVALAYIDPD------FLDVKA---LKQRNIID--AIKWEVRDKVNQKVPNYKKISKVKIVKEEF-----EKTP 454
|
....*.
gi 2786869514 578 SMKIRR 583
Cdd:cd05914 455 KGKIKR 460
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
33-598 |
1.11e-86 |
|
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: 281.17 E-value: 1.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADL-AIMASGcITVPTYITNTERDHAHILDNSGA 111
Cdd:cd05933 3 GDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVgAIFAGG-IAVGIYTTNSPEACQYVAETSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 112 KAVIVSTEKLLRPLHgalQASGIADHVIGI----DDLHRQQSSgflFHRWDSMFAGDAAEARQAVEQRIAGIGRGDTACI 187
Cdd:cd05933 82 NILVVENQKQLQKIL---QIQDKLPHLKAIiqykEPLKEKEPN---LYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 188 IYTSGTGGAPRGVMQHHGAILCNVAGAAEILieDFGIADD--ERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAE---GL 262
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHM--DLRPATVgqESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQpdaLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 EKLASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKL----MNTALEVGERRAAGK--PKFGDGLRDALVGRll 336
Cdd:cd05933 234 GTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIaswaKGVGLETNLKLMGGEspSPLFYRLAKKLVFK-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 337 kpKIRQRFG-GRIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTE-AGPVISCNRPAAGIamHSVGPAMRGVDIRIAE- 413
Cdd:cd05933 312 --KVRKALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSEtSGPHTISNPQAYRL--LSCGKALPGCKTKIHNp 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 414 ----DGEILVRGELVMQGYWHNEAETERTIK-DGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQ 488
Cdd:cd05933 388 dadgIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 489 -PEIGQAMVAGDKKPYIVGLI-----------VPDAEWTLE---WCREQGKQfdCKKVQEL-----PEFRNAVRAAVDRV 548
Cdd:cd05933 468 lPIISNAMLIGDKRKFLSMLLtlkcevnpetgEPLDELTEEaieFCRKLGSQ--ATRVSEIaggkdPKVYEAIEEGIKRV 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 549 NKD-LSVVEKVRQFAFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALY 598
Cdd:cd05933 546 NKKaISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
34-586 |
1.24e-86 |
|
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: 278.33 E-value: 1.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKA 113
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVSTEKllrplhgalqasgiadhvigiDDLhrqqssgflfhrwdsmfagdaaearqaveqriagigrgdtACIIYTSGT 193
Cdd:cd17639 81 IFTDGKP---------------------DDL----------------------------------------ACIMYTSGS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 194 GGAPRGVMQHHGAILCNVAGAAEILIEDFGiaDDERFLSFLPLSHAYEHTGgQFLPISVGAQIYYAEGL---EKLASN-- 268
Cdd:cd17639 100 TGNPKGVMLTHGNLVAGIAGLGDRVPELLG--PDDRYLAYLPLAHIFELAA-ENVCLYRGGTIGYGSPRtltDKSKRGck 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 269 --IEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTALEVgeRRAAGKPKFGDGLRDALVGRllkpKIRQRFGG 346
Cdd:cd17639 177 gdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQS--KLKALKEGPGTPLLDELVFK----KVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 347 RIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTE---AGPVISCNRPAAGiamhSVGPAMRGVDIR---IAE------- 413
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTEtcaGGTVQDPGDLETG----RVGPPLPCCEIKlvdWEEggystdk 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 414 ---DGEILVRGELVMQGYWHNEAETERTIK-DGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQP 489
Cdd:cd17639 327 pppRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 490 EIGQAMVAGD-KKPYIVGLIVPDAEWTLEWCREQGKQFD-----CKKvqelPEFRNAVRAAVDRVNKD--LSVVEKVRQF 561
Cdd:cd17639 407 LVNNICVYADpDKSYPVAIVVPNEKHLTKLAEKHGVINSeweelCED----KKLQKAVLKSLAETARAagLEKFEIPQGV 482
|
570 580
....*....|....*....|....*
gi 2786869514 562 AFADEPFTIENEEMTPSMKIRRHKI 586
Cdd:cd17639 483 VLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
11-522 |
7.37e-80 |
|
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: 259.42 E-value: 7.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGDLP---FLGariggswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG 87
Cdd:cd05936 1 LADLLEEAARRFPDKTaliFMG-------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 88 CITVPTYITNTERDHAHILDNSGAKAVIVstekllrplhgalqasgiadhvigiddlhrqqssgflFHRWDSMFAGDAAE 167
Cdd:cd05936 74 AVVVPLNPLYTPRELEHILNDSGAKALIV-------------------------------------AVSFTDLLAAGAPL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 168 arqaveQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDFGiaDDERFLSFLPLSHAYEHTGGQF 247
Cdd:cd05936 117 ------GERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLE--GDDVVLAALPLFHVFGLTVALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 248 LPISVGAQI-----YYAEGLEKLasnIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEVGERRAAGKPk 322
Cdd:cd05936 189 LPLALGATIvliprFRPIGVLKE---IRKHRVTIFPGVPTMYIAL----------------------LNAPEFKKRDFS- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 323 fgdglrdalvgrllkpkirqrfggRIKAMVSGGAPLNPEVGIFFESM-GLTMLQGYGQTEAGPVISCNRPAAGIAMHSVG 401
Cdd:cd05936 243 ------------------------SLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 402 PAMRGVDIRIAED----------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNd 471
Cdd:cd05936 299 IPLPGTEVKIVDDdgeelppgevGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIV- 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 472 KGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY----IVGLIVP------DAEWTLEWCREQ 522
Cdd:cd05936 378 GGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYsgeaVKAFVVLkegaslTEEEIIAFCREQ 438
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-540 |
1.50e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 241.73 E-value: 1.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 10 NLVELFLKRAAEKGDLPflgARIGGSwQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCI 89
Cdd:PRK07656 6 TLPELLARAARRFGDKE---AYVFGD-QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 90 TVPTYITNTERDHAHILDNSGAKAVIVSTE--KLLRPLHGALQAsgiADHVIGIDDLHrQQSSGFLFHRWDSMFA-GDAA 166
Cdd:PRK07656 82 VVPLNTRYTADEAAYILARGDAKALFVLGLflGVDYSATTRLPA---LEHVVICETEE-DDPHTEKMKTFTDFLAaGDPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 167 EarqaveqRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYEHTGGQ 246
Cdd:PRK07656 158 E-------RAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYL----GLTEGDRYLAANPFFHVFGYKAGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 247 FLPISVGAQIYYAE--GLEKLASNIEETRPTIMVVVPRLFevlrtrimkqvqkqgglaeklmNTALEVGERRAagkpkfg 324
Cdd:PRK07656 227 NAPLMRGATILPLPvfDPDEVFRLIETERITVLPGPPTMY----------------------NSLLQHPDRSA------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 325 DGLRDalvgrllkpkirqrfggrIKAMVSGGAPLNPEVGIFFESM-GL-TMLQGYGQTEAGPVISCNRP---AAGIAmHS 399
Cdd:PRK07656 278 EDLSS------------------LRLAVTGAASMPVALLERFESElGVdIVLTGYGLSEASGVTTFNRLdddRKTVA-GT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 400 VGPAMRGVDIRIA----------EDGEILVRGELVMQGYWHNEAETERTIK-DGWLHTGDIGHVDDKGRIVITDRKKDMI 468
Cdd:PRK07656 339 IGTAIAGVENKIVnelgeevpvgEVGELLVRGPNVMKGYYDDPEATAAAIDaDGWLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 469 VNDkGDNVAPQKVEGMLTLQPEIGQAMVAG--DK------KPYIVGLIVP--DAEWTLEWCREQGKQFDCKK----VQEL 534
Cdd:PRK07656 419 IVG-GFNVYPAEVEEVLYEHPAVAEAAVIGvpDErlgevgKAYVVLKPGAelTEEELIAYCREHLAKYKVPRsiefLDEL 497
|
....*.
gi 2786869514 535 PefRNA 540
Cdd:PRK07656 498 P--KNA 501
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
37-592 |
3.00e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 240.86 E-value: 3.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:PRK06187 30 RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STE--KLLRPLHGALQASgiaDHVIGIDDLHRQQSSGFLfHRWDSMFAGdAAEARQAVEqriagIGRGDTACIIYTSGTG 194
Cdd:PRK06187 110 DSEfvPLLAAILPQLPTV---RTVIVEGDGPAAPLAPEV-GEYEELLAA-ASDTFDFPD-----IDENDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 195 GAPRGVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLSHAYEhTGGQFLPISVGAQIYYAEGL--EKLASNIEET 272
Cdd:PRK06187 180 GHPKGVVLSHRNLFLHSLAVCAW----LKLSRDDVYLVIVPMFHVHA-WGLPYLALMAGAKQVIPRRFdpENLLDLIETE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 273 RPTIMVVVPrlfevlrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrDALVGRLLKPKIRQRFGGRIKAMV 352
Cdd:PRK06187 255 RVTFFFAVP-----------------------------------------------TIWQMLLKAPRAYFVDFSSLRLVI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 353 SGGAPLNPE-VGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIA-----MHSVGPAMRGVDIRIAED------------ 414
Cdd:PRK06187 288 YGGAALPPAlLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPgqwtkRRSAGRPLPGVEARIVDDdgdelppdggev 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQA 494
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVI-ISGGENIYPRELEDALYGHPAVAEV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 495 MVAGdkkpyivgliVPDAEW--------TLewcrEQGKQFDckkVQELPEFrnavraAVDRVNKdlsvvEKV-RQFAFAD 565
Cdd:PRK06187 447 AVIG----------VPDEKWgerpvavvVL----KPGATLD---AKELRAF------LRGRLAK-----FKLpKRIAFVD 498
|
570 580
....*....|....*....|....*...
gi 2786869514 566 E-PftieneeMTPSMKIRRHKIKERYAE 592
Cdd:PRK06187 499 ElP-------RTSVGKILKRVLREQYAE 519
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
37-498 |
1.36e-67 |
|
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: 227.87 E-value: 1.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKaVIV 116
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK-VIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLRPLHGALQASGIADHVIGIDDlhRQQSSGFLFHRWDSmFAGDAAEARQAVEQRiagiGRGDTACIIYTSGTGGA 196
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPKDKIIVLDD--KPDGVLSIEDLLSP-TLGEEDEDLPPPLKD----GKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGAILCNVAGAAEILIEDFGiaDDERFLSFLPLSHAYehtggqflpisvGAQIYYAEGL-------------E 263
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFLYGNDG--SNDVILGFLPLYHIY------------GLFTTLASLLngatviimpkfdsE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 264 KLASNIEETRPTIMVVVPRLFEVLRTriMKQVQKqgglaEKLMNtalevgerraagkpkfgdglrdalvgrllkpkirqr 343
Cdd:cd05911 227 LFLDLIEKYKITFLYLVPPIAAALAK--SPLLDK-----YDLSS------------------------------------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 344 fggrIKAMVSGGAPLNPEVGIFFESM--GLTMLQGYGQTEAGPVISCNrPAAGIAMHSVGPAMRGVDIRIAED------- 414
Cdd:cd05911 264 ----LRVILSGGAPLSKELQELLAKRfpNATIKQGYGMTETGGILTVN-PDGDDKPGSVGRLLPNVEAKIVDDdgkdslg 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 ----GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQP 489
Cdd:cd05911 339 pnepGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELI-KYKGFQVAPAELEAVLLEHP 417
|
....*....
gi 2786869514 490 EIGQAMVAG 498
Cdd:cd05911 418 GVADAAVIG 426
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
3-599 |
1.63e-67 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 232.01 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 3 SDIDSANNLvelfLKRAAEK-------GDLPFLGARIGG-SWQTisWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRP 74
Cdd:PLN02430 39 SDITTAWDI----FSKSVEKypdnkmlGWRRIVDGKVGPyMWKT--YKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 75 EWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTEK---LLRP-LHGALQASGIADHVIGIDDL-HRQQS 149
Cdd:PLN02430 113 QWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKikeLLEPdCKSAKRLKAIVSFTSVTEEEsDKASQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 150 SGFLFHRW-DSMFAGDAAEARQAVEQRIagigrgDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAaEILIEDF--GIAD 226
Cdd:PLN02430 193 IGVKTYSWiDFLHMGKENPSETNPPKPL------DICTIMYTSGTSGDPKGVVLTHEAVATFVRGV-DLFMEQFedKMTH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 227 DERFLSFLPLSHAYEHTGGQFL---PISVGaqiYYAEGLEKLASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAE 303
Cdd:PLN02430 266 DDVYLSFLPLAHILDRMIEEYFfrkGASVG---YYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 304 KLMNtAL---EVGERRAAGKPKFGDGLRDALVGRllkpKIRQRFGGRIKAMVSGGAPLNPEVGIFFESMGLTML-QGYGQ 379
Cdd:PLN02430 343 LIFN-ALykyKLAWMNRGYSHKKASPMADFLAFR----KVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVvQGYGL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 380 TEA-GPVISCnRPAAGIAMHSVGPAMRGVDIRIAE-------------DGEILVRGELVMQGYWHNEAETERTIKDGWLH 445
Cdd:PLN02430 418 TETlGPTTLG-FPDEMCMLGTVGAPAVYNELRLEEvpemgydplgeppRGEICVRGKCLFSGYYKNPELTEEVMKDGWFH 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 446 TGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDK-KPYIVGLIVPDAEWTLEWCREQGK 524
Cdd:PLN02430 497 TGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSfKSMLVAVVVPNEENTNKWAKDNGF 576
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786869514 525 QFDCKKVQELPEFRNAV----RAAVDRvNKdLSVVEKVRQFAFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYR 599
Cdd:PLN02430 577 TGSFEELCSLPELKEHIlselKSTAEK-NK-LRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYR 653
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
8-598 |
8.33e-67 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 230.77 E-value: 8.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 8 ANNLVELFLKRAAEKGDLPFLGAR--IG-----------------GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCL 68
Cdd:PLN02387 57 ATTLAALFEQSCKKYSDKRLLGTRklISrefetssdgrkfeklhlGEYEWITYGQVFERVCNFASGLVALGHNKEERVAI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 69 VSENRPEWCIAdlaimASGC----ITVPT-YITNTERDHAHILDNSGAKAVIVSTeKLLRPLHGALQASGIADHVIGIDD 143
Cdd:PLN02387 137 FADTRAEWLIA-----LQGCfrqnITVVTiYASLGEEALCHSLNETEVTTVICDS-KQLKKLIDISSQLETVKRVIYMDD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 144 LH-RQQSSGFLFHRWDSMFAGDAAEARQ--AVEQRIAGigRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEIlIE 220
Cdd:PLN02387 211 EGvDSDSSLSGSSNWTVSSFSEVEKLGKenPVDPDLPS--PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTV-VP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 221 DFGIADdeRFLSFLPLSHAYEHTgGQFLPISVGAQIYY--AEGLEKLASNIE--------ETRPTIMVVVPRLFEVLRTR 290
Cdd:PLN02387 288 KLGKND--VYLAYLPLAHILELA-AESVMAAVGAAIGYgsPLTLTDTSNKIKkgtkgdasALKPTLMTAVPAILDRVRDG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 291 IMKQVQKQGGLAEKLMNTALevgERR--AAGKPKFGD-GLR----DALVGRllkpKIRQRFGGRIKAMVSGGAPLNPEVG 363
Cdd:PLN02387 365 VRKKVDAKGGLAKKLFDIAY---KRRlaAIEGSWFGAwGLEkllwDALVFK----KIRAVLGGRIRFMLSGGAPLSGDTQ 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 364 IFFE-SMGLTMLQGYGQTE--AGPVIS-CNRPAAGiamhSVGPAM-----RGVD-----IRIAED----GEILVRGELVM 425
Cdd:PLN02387 438 RFINiCLGAPIGQGYGLTEtcAGATFSeWDDTSVG----RVGPPLpccyvKLVSweeggYLISDKpmprGEIVIGGPSVT 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 426 QGYWHNEAETERTIKDG-----WLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDK 500
Cdd:PLN02387 514 LGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADP 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 501 -KPYIVGLIVPDAEWTLEWCREQGKQFD-----CKKVQELPEfrnaVRAAVDRVNKD--LSVVEKVRQFAFADEPFTIEN 572
Cdd:PLN02387 594 fHSYCVALVVPSQQALEKWAKKAGIDYSnfaelCEKEEAVKE----VQQSLSKAAKAarLEKFEIPAKIKLLPEPWTPES 669
|
650 660
....*....|....*....|....*.
gi 2786869514 573 EEMTPSMKIRRHKIKERYAERLDALY 598
Cdd:PLN02387 670 GLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
36-599 |
4.90e-65 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 225.11 E-value: 4.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 36 WQTisWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVI 115
Cdd:PLN02861 77 WLT--YKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 VSTEKLLRPLHGALQASGIADHVIGIDDLHRQQS--------SGFLFHRWDSMFAGDAAEARQAveqriagigRGDTACI 187
Cdd:PLN02861 155 VQESKISSILSCLPKCSSNLKTIVSFGDVSSEQKeeaeelgvSCFSWEEFSLMGSLDCELPPKQ---------KTDICTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 188 IYTSGTGGAPRGVMQHHGAILCNVAGAAEILIE-DFGIADDERFLSFLPLSHAYEHTGGQFLpISVGAQIYYAEG-LEKL 265
Cdd:PLN02861 226 MYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVtDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGdIRYL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 266 ASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTA-------LEVGERRAAGKPKFGdglrdalvgRLLKP 338
Cdd:PLN02861 305 MEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAynyklgnLRKGLKQEEASPRLD---------RLVFD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 339 KIRQRFGGRIKAMVSGGAPLNPEVGIFFESMGLTML-QGYGQTEagpviSCNRPAAGIA-----MHSVGPAMRGVDIRIA 412
Cdd:PLN02861 376 KIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLsQGYGLTE-----SCGGCFTSIAnvfsmVGTVGVPMTTIEARLE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 413 E-------------DGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQ 479
Cdd:PLN02861 451 SvpemgydalsdvpRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 480 KVEGMLTLQPEIGQAMVAGDK-KPYIVGLIVPDAEWTLEWCREQGKQFDCKKVQELPEFRNAVRAAVDRVNKDLSV--VE 556
Cdd:PLN02861 531 NLENTYSRCPLIASIWVYGNSfESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLrgFE 610
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2786869514 557 KVRQFAFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYR 599
Cdd:PLN02861 611 MLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
183-522 |
8.65e-63 |
|
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: 210.22 E-value: 8.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLSHAYEHTGGqFLPISVGAQIYYAEGL 262
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS----GGLTEGDVFLSTLPLFHIGGLFGL-LGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 --EKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEVGERRAAGKPkfgdglrdalvgrllkpki 340
Cdd:cd04433 76 dpEAALELIEREKVTILLGVPTLLARL----------------------LKAPESAGYDLS------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 341 rqrfggRIKAMVSGGAPLNPEVGIFFESM-GLTMLQGYGQTEAGPVISCNRPAAGIA-MHSVGPAMRGVDIRIA------ 412
Cdd:cd04433 115 ------SLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDDARkPGSVGRPVPGVEVRIVdpdgge 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 413 ----EDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQ 488
Cdd:cd04433 189 lppgEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMI-KSGGENVYPAEVEAVLLGH 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2786869514 489 PEIGQAMVAGDKKPY----IVGLIVP------DAEWTLEWCREQ 522
Cdd:cd04433 268 PGVAEAAVVGVPDPEwgerVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
37-514 |
2.29e-62 |
|
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: 212.47 E-value: 2.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIv 116
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 stekllrplhgalqasgiadhvigiDDLhrqqssgflfhrwdsmfagdaaearqaveqriagigrgdtACIIYTSGTGGA 196
Cdd:cd17631 98 -------------------------DDL----------------------------------------ALLMYTSGTTGR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGAILCNVAGAaeilIEDFGIADDERFLSFLPLSHAYEhTGGQFLP-ISVGAQIYYAEGLE--KLASNIEETR 273
Cdd:cd17631 113 PKGAMLTHRNLLWNAVNA----LAALDLGPDDVLLVVAPLFHIGG-LGVFTLPtLLRGGTVVILRKFDpeTVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 274 PTIMVVVPRLFEVLRTRimkqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrllkPKIRQRFGGRIKAMVS 353
Cdd:cd17631 188 VTSFFLVPTMIQALLQH-----------------------------------------------PRFATTDLSSLRAVIY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 354 GGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIA-MHSVGPAMRGVDIRI----------AEDGEILVRGE 422
Cdd:cd17631 221 GGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRkLGSAGRPVFFVEVRIvdpdgrevppGEVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 423 LVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkkp 502
Cdd:cd17631 301 HVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISG-GENVYPAEVEDVLYEHPAVAEVAVIG---- 375
|
490
....*....|..
gi 2786869514 503 yivgliVPDAEW 514
Cdd:cd17631 376 ------VPDEKW 381
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
37-599 |
2.75e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 204.82 E-value: 2.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLRPLhgALQASGIADH--VIGIDDLHRQ-QSSGFLFHRW-DSMFAGDAAEARQAVeqRIAGiGRGDTACIIYTSG 192
Cdd:PTZ00216 200 NGKNVPNLL--RLMKSGGMPNttIIYLDSLPASvDTEGCRLVAWtDVVAKGHSAGSHHPL--NIPE-NNDDLALIMYTSG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 193 TGGAPRGVMQHHGAILCNVAGAAEILIEDFG-IADDERFLSFLPLSHAYEHTGGQFLpISVGAQIYYA------EGLEKL 265
Cdd:PTZ00216 275 TTGDPKGVMHTHGSLTAGILALEDRLNDLIGpPEEDETYCSYLPLAHIMEFGVTNIF-LARGALIGFGsprtltDTFARP 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 266 ASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTALEvgERRAAGKpkfgDGLRDALVGRLLKPKIRQRFG 345
Cdd:PTZ00216 354 HGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQ--SRLRALK----EGKDTPYWNEKVFSAPRAVLG 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 346 GRIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAgIAMHSVGPAMRGVDIRIAE-------D---- 414
Cdd:PTZ00216 428 GRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGD-LEPNAVGQLLKGVEMKLLDteeykhtDtpep 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 -GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLT----LQ 488
Cdd:PTZ00216 507 rGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGqnelVV 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 489 PEiGQAMVAGDKKPYIVGLIVPDAEWTLEWCREQGKQFDCKKVQELPEFRNAV--------RAAvDRvnKDLSVVEKVRq 560
Cdd:PTZ00216 587 PN-GVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKAteslqetaRAA-GR--KSFEIVRHVR- 661
|
570 580 590
....*....|....*....|....*....|....*....
gi 2786869514 561 faFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYR 599
Cdd:PTZ00216 662 --VLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
36-599 |
3.99e-57 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 203.71 E-value: 3.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 36 WQTisWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVI 115
Cdd:PLN02614 79 WQT--YQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 VSTEKLLRPLHGALQASGIADHVIGIDDLHRQQSS-----GFLFHRWDSMFA-GDAAEARQAVEQRiagigrGDTACIIY 189
Cdd:PLN02614 157 VEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEeaetfGLVIYAWDEFLKlGEGKQYDLPIKKK------SDICTIMY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 190 TSGTGGAPRGVMQHHGAILCNVAGAAEILIE-DFGIADDERFLSFLPLSHAYEHTGGQFLpISVGAQIYYAEG-LEKLAS 267
Cdd:PLN02614 231 TSGTTGDPKGVMISNESIVTLIAGVIRLLKSaNAALTVKDVYLSYLPLAHIFDRVIEECF-IQHGAAIGFWRGdVKLLIE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 268 NIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTA-------LEVGERRAAGKPkfgdglrdaLVGRLLKPKI 340
Cdd:PLN02614 310 DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAfsykfgnMKKGQSHVEASP---------LCDKLVFNKV 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 341 RQRFGGRIKAMVSGGAPLNPEVGIFFESMGL-TMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIAE------ 413
Cdd:PLN02614 381 KQGLGGNVRIILSGAAPLASHVESFLRVVACcHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESvpemey 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 414 -------DGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLT 486
Cdd:PLN02614 461 dalastpRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYG 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 487 LQPEIGQAMVAGDK-KPYIVGLIVPDAEWTLEWCREQGKQFDCKKVQELPEFRNAVRAAVDRVNKD--LSVVEKVRQFAF 563
Cdd:PLN02614 541 EVQAVDSVWVYGNSfESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEkkMKGFEIIKAIHL 620
|
570 580 590
....*....|....*....|....*....|....*.
gi 2786869514 564 ADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYR 599
Cdd:PLN02614 621 DPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
38-514 |
4.68e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 200.60 E-value: 4.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVS 117
Cdd:PRK06188 37 RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 118 TEKLL-RPLHGALQASGIAdHVIGIDDLHRQQssgflfhrwDSMFAGDAAEARQAVeqriAGIGRGDTACIIYTSGTGGA 196
Cdd:PRK06188 117 PAPFVeRALALLARVPSLK-HVLTLGPVPDGV---------DLLAAAAKFGPAPLV----AAALPPDIAGLAYTGGTTGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGAIlcnvAGAAEILIEDFGIADDERFLSFLPLSHAyehTGGQFLPISV-GAQIYYAEGL--EKLASNIEETR 273
Cdd:PRK06188 183 PKGVMGTHRSI----ATMAQIQLAEWEWPADPRFLMCTPLSHA---GGAFFLPTLLrGGTVIVLAKFdpAEVLRAIEEQR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 274 PTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrLLKPKIRQRFGGRIKAMVS 353
Cdd:PRK06188 256 ITATFLVPTMIYAL-----------------------------------------------LDHPDLRTRDLSSLETVYY 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 354 GGAPLNP---EVGIffESMGLTMLQGYGQTEAGPVI-----------------SCNRPAAGIAMHSVGPAMRGVDIriAE 413
Cdd:PRK06188 289 GASPMSPvrlAEAI--ERFGPIFAQYYGQTEAPMVItylrkrdhdpddpkrltSCGRPTPGLRVALLDEDGREVAQ--GE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 414 DGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQ 493
Cdd:PRK06188 365 VGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTG-GFNVFPREVEDVLAEHPAVAQ 443
|
490 500
....*....|....*....|.
gi 2786869514 494 AMVAGdkkpyivgliVPDAEW 514
Cdd:PRK06188 444 VAVIG----------VPDEKW 454
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
51-498 |
2.93e-54 |
|
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: 192.45 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 51 LAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVST---EKLlrplhg 127
Cdd:cd05904 45 LAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAelaEKL------ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 128 alqaSGIADHVIGIDDLHrqqssGFLFHRWDSMFAGDAAEARQAVeqriagIGRGDTACIIYTSGTGGAPRGVMQHHGAI 207
Cdd:cd05904 119 ----ASLALPVVLLDSAE-----FDSLSFSDLLFEADEAEPPVVV------IKQDDVAALLYSSGTTGRSKGVMLTHRNL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 208 LCNVAGAAEIliEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEG--LEKLASNIEETRPTIMVVVPRlfe 285
Cdd:cd05904 184 IAMVAQFVAG--EGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRfdLEELLAAIERYKVTHLPVVPP--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 286 vlrtrIMKQVQKQgglaeklmntalevgerraagkpkfgdglrdALVGRLLKPKIRQrfggrikaMVSGGAPLNPEVGIF 365
Cdd:cd05904 259 -----IVLALVKS-------------------------------PIVDKYDLSSLRQ--------IMSGAAPLGKELIEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 366 FESM--GLTMLQGYGQTEAGPVISCNRPAAGIAMH--SVGPAMRGVDIRIA-----------EDGEILVRGELVMQGYWH 430
Cdd:cd05904 295 FRAKfpNVDLGQGYGMTESTGVVAMCFAPEKDRAKygSVGRLVPNVEAKIVdpetgeslppnQTGELWIRGPSIMKGYLN 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786869514 431 NEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAG 498
Cdd:cd05904 375 NPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELI-KYKGFQVAPAELEALLLSHPEILDAAVIP 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
11-522 |
1.44e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 189.44 E-value: 1.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGDLP---FLGAriggswqTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG 87
Cdd:PRK05605 34 LVDLYDNAVARFGDRPaldFFGA-------TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 88 CITV---PTYitnTERDHAHILDNSGAKAVIV--STEKLLRPLHGALQAsgiaDHVIGIDDLH----------------- 145
Cdd:PRK05605 107 AVVVehnPLY---TAHELEHPFEDHGARVAIVwdKVAPTVERLRRTTPL----ETIVSVNMIAampllqrlalrlpipal 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 146 ---RQQSSGFL--FHRWDSMFAGDAAEARQAVEQRiaGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVA-GAAEILi 219
Cdd:PRK05605 180 rkaRAALTGPApgTVPWETLVDAAIGGDGSDVSHP--RPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqGKAWVP- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 220 edfGIAD-DERFLSFLPLSHAYEHTGGQFLPISVGAQI--YYAEGLEKLASNIEETRPTIMVVVPRLFEvlrtRIMKQVQ 296
Cdd:PRK05605 257 ---GLGDgPERVLAALPMFHAYGLTLCLTLAVSIGGELvlLPAPDIDLILDAMKKHPPTWLPGVPPLYE----KIAEAAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 297 KQGglaeklmntaLEVgerraagkpkfgDGLRDALvgrllkpkirqrfggrikamvSGGAPLNPEVGIFFESM-GLTMLQ 375
Cdd:PRK05605 330 ERG----------VDL------------SGVRNAF---------------------SGAMALPVSTVELWEKLtGGLLVE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 376 GYGQTEAGPVISCN------RPAagiamhSVGPAMRGVDIRIA------------EDGEILVRGELVMQGYWHNEAETER 437
Cdd:PRK05605 367 GYGLTETSPIIVGNpmsddrRPG------YVGVPFPDTEVRIVdpedpdetmpdgEEGELLVRGPQVFKGYWNRPEETAK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 438 TIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAG----DKKPYIVGLIVP--- 510
Cdd:PRK05605 441 SFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITG-GFNVYPAEVEEVLREHPGVEDAAVVGlpreDGSEEVVAAVVLepg 519
|
570
....*....|....*
gi 2786869514 511 ---DAEWTLEWCREQ 522
Cdd:PRK05605 520 aalDPEGLRAYCREH 534
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
17-522 |
8.37e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 186.70 E-value: 8.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 17 KRAAEKGDLPFLGARIggswqtiSWNEAAEQVCLLAENL-RALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYI 95
Cdd:PRK08314 21 RRYPDKTAIVFYGRAI-------SYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 96 TNTERDHAHILDNSGAKAVIVSTEKL--LRPLHGAL---------------QASGIADHVIGIDDLHRQQSSGFLFHRW- 157
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSELApkVAPAVGNLrlrhvivaqysdylpAEPEIAVPAWLRAEPPLQALAPGGVVAWk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 158 DSMFAGDAAEARQAveqriagiGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLS 237
Cdd:PRK08314 174 EALAAGLAPPPHTA--------GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW----SNSTPESVVLAVLPLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 238 HAyehTGGQFlpiSVGAQIYYAegleklasnieetrpTIMVVVPRLfevlrtrimkqvqkqgglaeklmntalevgERRA 317
Cdd:PRK08314 242 HV---TGMVH---SMNAPIYAG---------------ATVVLMPRW------------------------------DREA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 318 AGKpkfgdglrdaLVGR----------------LLKPKIRQRFGGRIKAMVSGGAPLNPEVG-IFFESMGLTMLQGYGQT 380
Cdd:PRK08314 271 AAR----------LIERyrvthwtniptmvvdfLASPGLAERDLSSLRYIGGGGAAMPEAVAeRLKELTGLDYVEGYGLT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 381 E-AGPVIScnRPAAGIAMHSVGPAMRGVDIRI-----------AEDGEILVRGELVMQGYWHNEAETER---TIkDG--W 443
Cdd:PRK08314 341 EtMAQTHS--NPPDRPKLQCLGIPTFGVDARVidpetleelppGEVGEIVVHGPQVFKGYWNRPEATAEafiEI-DGkrF 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 444 LHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY----IVGLIVPDAEWT---- 515
Cdd:PRK08314 418 FRTGDLGRMDEEGYFFITDRLKRMI-NASGFKVWPAEVENLLYKHPAIQEACVIATPDPRrgetVKAVVVLRPEARgktt 496
|
570
....*....|.
gi 2786869514 516 ----LEWCREQ 522
Cdd:PRK08314 497 eeeiIAWAREH 507
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
10-593 |
1.77e-48 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 177.61 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 10 NLVELFLKR-AAEKGDLP-FLGARIGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG 87
Cdd:COG0365 9 NIAYNCLDRhAEGRGDKVaLIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 88 CITVPTYITNTERDHAHILDNSGAKAVIVSTEkLLRP---------LHGALQASGIADHVIGIDDLHRQQSSGfLFHRWD 158
Cdd:COG0365 89 AVHSPVFPGFGAEALADRIEDAEAKVLITADG-GLRGgkvidlkekVDEALEELPSLEHVIVVGRTGADVPME-GDLDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 159 SMFAGDAAEArQAVEqriagIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedFGIADDERFLSFLPLSH 238
Cdd:COG0365 167 ELLAAASAEF-EPEP-----TDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV---LDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 239 AYEHTGGQFLPISVGAQIYYAEG------LEKLASNIEETRPTIMVVVPRLFevlrtRIMKqvqkqgglaeklmntalev 312
Cdd:COG0365 238 ATGHSYIVYGPLLNGATVVLYEGrpdfpdPGRLWELIEKYGVTVFFTAPTAI-----RALM------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 313 gerraagkpKFGDGLRDALvgRLlkpkirqrfgGRIKAMVSGGAPLNPEVGI-FFESMGLTMLQGYGQTEAGPVISCNRP 391
Cdd:COG0365 294 ---------KAGDEPLKKY--DL----------SSLRLLGSAGEPLNPEVWEwWYEAVGVPIVDGWGQTETGGIFISNLP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 392 aaGIAMH--SVGPAMRGVDIRIA-EDGEIL---VRGELV--------MQGYWHNEAETERTIKD---GWLHTGDIGHVDD 454
Cdd:COG0365 353 --GLPVKpgSMGKPVPGYDVAVVdEDGNPVppgEEGELVikgpwpgmFRGYWNDPERYRETYFGrfpGWYRTGDGARRDE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 455 KGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAG----DKKPYIVGLIVPDAEWTLEwcreqgkqfdckk 530
Cdd:COG0365 431 DGYFWILGRSDDVI-NVSGHRIGTAEIESALVSHPAVAEAAVVGvpdeIRGQVVKAFVVLKPGVEPS------------- 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 531 vQELpefrnaVRAAVDRVNKDLSVVEKVRQFAFADE-PftieneeMTPSMKIRRHKIKERYAER 593
Cdd:COG0365 497 -DEL------AKELQAHVREELGPYAYPREIEFVDElP-------KTRSGKIMRRLLRKIAEGR 546
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
32-535 |
4.86e-46 |
|
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: 169.42 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 32 IGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGA 111
Cdd:cd05926 8 VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 112 KAVIVSTEKLLrPLHGALQASGIADHVIGIDD--LHRQQSSGFL-FHRWDSMFAGDAAEARqaveqriagigRGDTACII 188
Cdd:cd05926 88 KLVLTPKGELG-PASRAASKLGLAILELALDVgvLIRAPSAESLsNLLADKKNAKSEGVPL-----------PDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 189 YTSGTGGAPRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLEKLA-- 266
Cdd:cd05926 156 HTSGTTGRPKGVPLTHR----NLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTfw 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 267 SNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaekLMntalevgerRAAGKPKfgdglrdalvgrllKPKIRQRFgg 346
Cdd:cd05926 232 PDVRDYNATWYTAVPTIHQIL-----------------LN---------RPEPNPE--------------SPPPKLRF-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 347 rIKamvSGGAPLNPEVGIFFE-SMGLTMLQGYGQTEAGPVISCNR-PAAGIAMHSVGPAMrGVDIRIAED---------- 414
Cdd:cd05926 270 -IR---SCSASLPPAVLEALEaTFGAPVLEAYGMTEAAHQMTSNPlPPGPRKPGSVGKPV-GVEVRILDEdgeilppgvv 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 GEILVRGELVMQGYWHNEAET-ERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQ 493
Cdd:cd05926 345 GEICLRGPNVTRGYLNNPEANaEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI-NRGGEKISPLEVDGVLLSHPAVLE 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 494 AMVAGDKKP-Y---IVGLIVP------DAEWTLEWCREQGKQFDCKK----VQELP 535
Cdd:cd05926 424 AVAFGVPDEkYgeeVAAAVVLregasvTEEELRAFCRKHLAAFKVPKkvyfVDELP 479
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
40-594 |
1.33e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 169.57 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 40 SWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITV---PTYITnTERDHAhiLDNSGAKAVIV 116
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVninPAYRA-SELEYA--LGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLRPLHGALQ--ASGIAD------------HVIGIDDLHRQQSSGFLfhRWDSMFAGDAAEARQAVEQRIAGIGRG 182
Cdd:PRK12583 124 ADAFKTSDYHAMLQelLPGLAEgqpgalacerlpELRGVVSLAPAPPPGFL--AWHELQARGETVSREALAERQASLDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYY-AEG 261
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESL----GLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNEA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 262 LEKLAS--NIEETRPTIMVVVPRLFevlrtrimkqvqkqggLAEklmntaLEvgerraagKPKFGDGLRDALvgrllkpk 339
Cdd:PRK12583 278 FDPLATlqAVEEERCTALYGVPTMF----------------IAE------LD--------HPQRGNFDLSSL-------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 340 irqRFGgrikamVSGGAPLNPEV-GIFFESMGLTMLQ-GYGQTEAGPVISCNRPAAGIA--MHSVGPAMRGVDIRI---- 411
Cdd:PRK12583 320 ---RTG------IMAGAPCPIEVmRRVMDEMHMAEVQiAYGMTETSPVSLQTTAADDLErrVETVGRTQPHLEVKVvdpd 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 ------AEDGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGM 484
Cdd:PRK12583 391 gatvprGEIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRG-GENIYPREIEEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 485 LTLQPEIGQAMVAGdkkpyivgliVPD---AEWTLEWCR-EQGKQFDckkvqeLPEFRNAVRAAVDRVnkdlsvveKV-R 559
Cdd:PRK12583 470 LFTHPAVADVQVFG----------VPDekyGEEIVAWVRlHPGHAAS------EEELREFCKARIAHF--------KVpR 525
|
570 580 590
....*....|....*....|....*....|....*.
gi 2786869514 560 QFAFADE-PftieneeMTPSMKIRRHKIKERYAERL 594
Cdd:PRK12583 526 YFRFVDEfP-------MTVTGKVQKFRMREISIEEL 554
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
4-503 |
5.23e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 167.90 E-value: 5.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 4 DIDSANNLVELFLKRAAEKGDLPFLGariggswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAI 83
Cdd:PRK06710 22 DIQPLHKYVEQMASRYPEKKALHFLG-------KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 84 MASGCITVPTYITNTERDHAHILDNSGAKAVIVSteKLLRPLHGALQASGIADHVI--GIDD------------LHRQQS 149
Cdd:PRK06710 95 LLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL--DLVFPRVTNVQSATKIEHVIvtRIADflpfpknllypfVQKKQS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 150 S-------GFLFHRWDSMfagdAAEARQAVEqrIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEdf 222
Cdd:PRK06710 173 NlvvkvseSETIHLWNSV----EKEVNTGVE--VPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYN-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 223 GIADDERFLSFLPLSHAYEHTGGQFLPISVGAQiyyaegleklasnieetrptiMVVVPRlFEVlrTRIMKQVQKQggla 302
Cdd:PRK06710 245 CKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYK---------------------MVLIPK-FDM--KMVFEAIKKH---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 303 eklmntalevgerraagKPKFGDGLRDALVGRLLKPKIRQRFGGRIKAMVSGGAPLNPEVGIFFESM-GLTMLQGYGQTE 381
Cdd:PRK06710 297 -----------------KVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVtGGKLVEGYGLTE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 382 AGPVISCNRPAAGIAMHSVGPAMRGVDIRI-----------AEDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIG 450
Cdd:PRK06710 360 SSPVTHSNFLWEKRVPGSIGVPWPDTEAMImsletgealppGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVG 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2786869514 451 HVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY 503
Cdd:PRK06710 440 YMDEDGFFYVKDRKKDMIVA-SGFNVYPREVEEVLYEHEKVQEVVTIGVPDPY 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
39-522 |
1.14e-44 |
|
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: 164.19 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 39 ISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVST 118
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 119 EkllrplhgalqasgiadhvigIDDLhrqqssgflfhrwdsmfagdaaearqaveqriagigrgdtACIIYTSGTGGAPR 198
Cdd:cd05935 82 E---------------------LDDL----------------------------------------ALIPYTSGTTGLPK 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 199 GVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLEK--LASNIEETRPTI 276
Cdd:cd05935 101 GCMHTHFSAAANALQSAVW----TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRetALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 277 MVVVPRLFEVLrtrimkqvqkqgglaeklMNTalevgerraagkpkfgdglrdalvgrllkPKIRQRFGGRIKAMVSGGA 356
Cdd:cd05935 177 WTNIPTMLVDL------------------LAT-----------------------------PEFKTRDLSSLKVLTGGGA 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 357 PLNPEVG-IFFESMGLTMLQGYGQTEAGPVISCNRPAAgIAMHSVGPAMRGVDIRI-----------AEDGEILVRGELV 424
Cdd:cd05935 210 PMPPAVAeKLLKLTGLRFVEGYGLTETMSQTHTNPPLR-PKLQCLGIP*FGVDARVidietgrelppNEVGEIVVRGPQI 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 425 MQGYWHNEAETERT-IKDG---WLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDK 500
Cdd:cd05935 289 FKGYWNRPEETEESfIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMI-NVSGFKVWPAEVEAKLYKHPAI*EVCVISVP 367
|
490 500 510
....*....|....*....|....*....|....
gi 2786869514 501 KPYIV----GLIVPDAEWT--------LEWCREQ 522
Cdd:cd05935 368 DERVGeevkAFIVLRPEYRgkvteediIEWAREQ 401
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
37-522 |
6.08e-44 |
|
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: 162.08 E-value: 6.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 stekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTGGA 196
Cdd:cd05934 82 ------------------------------------------------------------------DPASILYTSGTTGP 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLEklASN----IEET 272
Cdd:cd05934 96 PKGVVITHA----NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFS--ASRfwsdVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 273 RPTIMVVVPRLFEVLrtriMKQvqkqgglaeklmntalEVGERRAAGKpkfgdgLRdalvgrllkpkirqrfggrikamV 352
Cdd:cd05934 170 GATVTNYLGAMLSYL----LAQ----------------PPSPDDRAHR------LR-----------------------A 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 353 SGGAPLNPE-VGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMhSVGPAMRGVDIRIAED----------GEILVRG 421
Cdd:cd05934 201 AYGAPNPPElHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPG-SIGRPAPGYEVRIVDDdgqelpagepGELVIRG 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 422 E---LVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAG 498
Cdd:cd05934 280 LrgwGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAAVVA 358
|
490 500 510
....*....|....*....|....*....|....
gi 2786869514 499 DKKPY-----IVGLIVPDAEWTL-----EWCREQ 522
Cdd:cd05934 359 VPDEVgedevKAVVVLRPGETLDpeelfAFCEGQ 392
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
38-512 |
2.99e-42 |
|
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: 159.07 E-value: 2.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVS 117
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 118 TEkLLRPLHGALQASGIADHVIGIDDLHRQQSSgflfHRWDSMFAGDAAEARQAveqriAGIGRGDTACIIYTSGTGGAP 197
Cdd:cd05959 109 GE-LAPVLAAALTKSEHTLVVLIVSGGAGPEAG----ALLLAELVAAEAEQLKP-----AATHADDPAFWLYSSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 198 RGVMQ-HHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQ-IYYAEGLE--KLASNIEETR 273
Cdd:cd05959 179 KGVVHlHADIYWTAELYARNVL----GIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATtVLMPERPTpaAVFKRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 274 PTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrLLKPKIRQRFGGRIKAMVS 353
Cdd:cd05959 255 PTVFFGVPTLYAAM-----------------------------------------------LAAPNLPSRDLSSLRLCVS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 354 GGAPLNPEVGIFFESM-GLTMLQGYGQTEAGPVISCNRPAA-----------GIAMHSVGPAmrGVDIRIAEDGEILVRG 421
Cdd:cd05959 288 AGEALPAEVGERWKARfGLDILDGIGSTEMLHIFLSNRPGRvrygttgkpvpGYEVELRDED--GGDVADGEPGELYVRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 422 ELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKK 501
Cdd:cd05959 366 PSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDML-KVSGIWVSPFEVESALVQHPAVLEAAVVGVED 444
|
490
....*....|.
gi 2786869514 502 PyiVGLIVPDA 512
Cdd:cd05959 445 E--DGLTKPKA 453
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
40-514 |
5.21e-42 |
|
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: 157.23 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 40 SWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSgakavivste 119
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 120 kllrPLHGALQASGIADHVIGIDDLHRQQSSGFLFHRWDSMFAGDaaearqaveqriagigrgDTACIIYTSGTGGAPRG 199
Cdd:TIGR01923 71 ----DVQLLLTDSLLEEKDFQADSLDRIEAAGRYETSLSASFNMD------------------QIATLMFTSGTTGKPKA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 200 VMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHayehTGGQ---FLPISVGAQIYYAEGLEKLASNIEETRPTI 276
Cdd:TIGR01923 129 VPHTFRNHYASAVGSKENL----GFTEDDNWLLSLPLYH----ISGLsilFRWLIEGATLRIVDKFNQLLEMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 277 MVVVPRLFevlrTRIMKQvqkqgglaeklmntalevgerraagkpkfgdGLRDALVGRLLkpkirqrfggrikamvSGGA 356
Cdd:TIGR01923 201 ISLVPTQL----NRLLDE-------------------------------GGHNENLRKIL----------------LGGS 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 357 PLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRI-----AEDGEILVRGELVMQGYWHN 431
Cdd:TIGR01923 230 AIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIkvdnkEGHGEIMVKGANLMKGYLYQ 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 432 EAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPD 511
Cdd:TIGR01923 310 GELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISG-GENIYPEEIETVLYQHPGIQEAVVVP----------KPD 378
|
...
gi 2786869514 512 AEW 514
Cdd:TIGR01923 379 AEW 381
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
183-540 |
6.20e-42 |
|
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: 154.20 E-value: 6.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILcnvaGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGL 262
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL----RAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 EKLA--SNIEETRPTIMVVVPRLFEVLrtrimkqvqkqggLAEklmntalevgerraAGKPKFG-DGLRDALVGRLLKPK 339
Cdd:cd17638 77 DVDAilEAIERERITVLPGPPTLFQSL-------------LDH--------------PGRKKFDlSSLRAAVTGAATVPV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 340 IRqrfggrIKAMVSggaplnpEVGIffesmgLTMLQGYGQTEAGPVISCnRPA--AGIAMHSVGPAMRGVDIRIAEDGEI 417
Cdd:cd17638 130 EL------VRRMRS-------ELGF------ETVLTAYGLTEAGVATMC-RPGddAETVATTCGRACPGFEVRIADDGEV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 418 LVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMV 496
Cdd:cd17638 190 LVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMYIVG-GFNVYPAEVEGALAEHPGVAQVAV 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786869514 497 AG--DK------KPYIVGL--IVPDAEWTLEWCREQGKQFDCKK----VQELPefRNA 540
Cdd:cd17638 269 IGvpDErmgevgKAFVVARpgVTLTEEDVIAWCRERLANYKVPRfvrfLDELP--RNA 324
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
37-552 |
4.09e-41 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 154.76 E-value: 4.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALG-LRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVI 115
Cdd:cd05941 10 DSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 vstekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTGG 195
Cdd:cd05941 90 -------------------------------------------------------------------DPALILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 196 APRGVMQHHGAILCNVagaaEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIyyaEGLEKLASNIEETRP- 274
Cdd:cd05941 103 RPKGVVLTHANLAANV----RALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASV---EFLPKFDPKEVAISRl 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 275 ----TIMVVVPRLFevlrTRIMKQVQKQgglaEKLMNTALEVGERRAagkpkfgdglrdalvgRLlkpkirqrfggrika 350
Cdd:cd05941 176 mpsiTVFMGVPTIY----TRLLQYYEAH----FTDPQFARAAAAERL----------------RL--------------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 MVSGGAPLNPEVGIFFES-MGLTMLQGYGQTEAGPVISCnrPAAGIAMH-SVGPAMRGVDIRIAED-----------GEI 417
Cdd:cd05941 217 MVSGSAALPVPTLEEWEAiTGHTLLERYGMTEIGMALSN--PLDGERRPgTVGMPLPGVQARIVDEetgeplprgevGEI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 418 LVRGELVMQGYWHNEAET-ERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMV 496
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATkEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 497 AGDKKP----YIVGLIVPDAE---WTLE----WCREQGKQFDCKK----VQELPefRNavraAVDRVNKDL 552
Cdd:cd05941 375 IGVPDPdwgeRVVAVVVLRAGaaaLSLEelkeWAKQRLAPYKRPRrlilVDELP--RN----AMGKVNKKE 439
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
42-540 |
1.58e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 154.71 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 42 NEAAEQVcllAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTEkL 121
Cdd:PRK08316 43 DAAVNRV---AAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA-L 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 122 LRPLHGALQASGIADhvIGIDDLHRQQSSGFLFHRWDSMFAGDAAEArqaVEQRIAGigrGDTACIIYTSGTGGAPRGVM 201
Cdd:PRK08316 119 APTAEAALALLPVDT--LILSLVLGGREAPGGWLDFADWAEAGSVAE---PDVELAD---DDLAQILYTSGTESLPKGAM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 202 QHHGAILCNVAGAaeilIEDFGIADDERFLSFLPLSH-AYEHTggqFL-P-ISVGAQIYYAEG--LEKLASNIEETRPTI 276
Cdd:PRK08316 191 LTHRALIAEYVSC----IVAGDMSADDIPLHALPLYHcAQLDV---FLgPyLYVGATNVILDApdPELILRTIEAERITS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 277 MVVVPRLFEVLrtrimkqvqkqgglaeklmntalevgerraAGKPKFG----DGLRDALVGRLLKP-----KIRQRFggr 347
Cdd:PRK08316 264 FFAPPTVWISL------------------------------LRHPDFDtrdlSSLRKGYYGASIMPvevlkELRERL--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 348 ikamvsggaplnPEVGIFfesmgltmlQGYGQTEAGPVI-------------SCNRPAAGIAMHSVGPAMRgvDIRIAED 414
Cdd:PRK08316 311 ------------PGLRFY---------NCYGQTEIAPLAtvlgpeehlrrpgSAGRPVLNVETRVVDDDGN--DVAPGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQA 494
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMI-KTGGENVASREVEEALYTHPAVAEV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 495 MVAGDKKPY----IVGLIVPDAEWTL------EWCREQGKQFDCKK----VQELPefRNA 540
Cdd:PRK08316 447 AVIGLPDPKwieaVTAVVVPKAGATVtedeliAHCRARLAGFKVPKrvifVDELP--RNP 504
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
38-465 |
1.58e-39 |
|
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: 151.33 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRAlGLRDGDRVCLVSENRPEWCIADLAIMASGciTVPTYI--TNTERDHAHILDNSGAKAVI 115
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLnyTAGLRELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 VSTE--KLLRPLHGALQASGIadHVIGIDDLhRQQSSGflfhrWDSMFAGDAAEARQAVEQRIAGIGR---GDTACIIYT 190
Cdd:cd05909 84 TSKQfiEKLKLHHLFDVEYDA--RIVYLEDL-RAKISK-----ADKCKAFLAGKFPPKWLLRIFGVAPvqpDDPAVILFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 191 SGTGGAPRGVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEG---LEKLAS 267
Cdd:cd05909 156 SGSEGLPKGVVLSHKNLLANVEQITAI----FDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpldYKKIPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 268 NIEETRPTIMVVVPRLFevlrtrimkqvqkqGGLAeklmntalevgerRAAGKPKFgDGLRDALVG-RLLKPKIRQrfgg 346
Cdd:cd05909 232 LIYDKKATILLGTPTFL--------------RGYA-------------RAAHPEDF-SSLRLVVAGaEKLKDTLRQ---- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 347 rikamvsggaplnpevgIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRI-----------AEDG 415
Cdd:cd05909 280 -----------------EFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIvsvetheevpiGEGG 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2786869514 416 EILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKK 465
Cdd:cd05909 343 LLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLS 392
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-535 |
3.98e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 149.51 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 48 VCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGC----ITVPTYITNTERDHAHILDNSGAKAVIVStEKLLR 123
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLAD-AGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 124 PLHGALQASGIADHVIGIDDLhrqqssgflfhrWDsmfAGDAAEARQAVEQriagigrgDTACIIYTSGTGGAPRGVMQH 203
Cdd:cd05922 82 RLRDALPASPDPGTVLDADGI------------RA---ARASAPAHEVSHE--------DLALLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 204 HGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYehtGGQFLPISV--GAQIYYAEGL---EKLASNIEETRPTIMV 278
Cdd:cd05922 139 HQNLLANARSIAEYL----GITADDRALTVLPLSYDY---GLSVLNTHLlrGATLVLTNDGvldDAFWEDLREHGATGLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 279 VVPRLFEVLRTRIMKQVqkqgGLAEKLMNTalevgerRAAGKpkfgdgLRDALVGRLlkpkiRQRF-GGRIKAMvsggap 357
Cdd:cd05922 212 GVPSTYAMLTRLGFDPA----KLPSLRYLT-------QAGGR------LPQETIARL-----RELLpGAQVYVM------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 358 lnpevgiffesmgltmlqgYGQTEAGPVISCNRPA-AGIAMHSVGPAMRGVDIRIAED----------GEILVRGELVMQ 426
Cdd:cd05922 264 -------------------YGQTEATRRMTYLPPErILEKPGSIGLAIPGGEFEILDDdgtptppgepGEIVHRGPNVMK 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 427 GYWHNEA-ETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPYIV 505
Cdd:cd05922 325 GYWNDPPyRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMI-KLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2786869514 506 GLIV-------PDAEWTLEWCREQGKQF----DCKKVQELP 535
Cdd:cd05922 404 KLALfvtapdkIDPKDVLRSLAERLPPYkvpaTVRVVDELP 444
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
4-498 |
4.37e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 150.97 E-value: 4.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 4 DIDSANNLVELFLKRAAEKGDLPflgARIGGSwQTISWNEAAEQVCLLAENLR-ALGLRDGDRVCLVSENRPEWCIADLA 82
Cdd:PRK08974 18 NPDRYQSLVDMFEQAVARYADQP---AFINMG-EVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 83 IMASGCITV---PTYitnTERDHAHILDNSGAKA-VIVST-----EKLLrplhgalqASGIADHVIgIDDLHRQQSSG-- 151
Cdd:PRK08974 94 ILRAGMIVVnvnPLY---TPRELEHQLNDSGAKAiVIVSNfahtlEKVV--------FKTPVKHVI-LTRMGDQLSTAkg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 152 ----FLFHRWDSMFAG----DAAEARQAVE-----QRI-AGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNV---AGA 214
Cdd:PRK08974 162 tlvnFVVKYIKRLVPKyhlpDAISFRSALHkgrrmQYVkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqaKAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 215 AEILIEDfgiaDDERFLSFLPLSHAYEHTGGQFLPISVGAQiyyaegleklasnieetrpTIMVVVPRLFEVLrtriMKQ 294
Cdd:PRK08974 242 YGPLLHP----GKELVVTALPLYHIFALTVNCLLFIELGGQ-------------------NLLITNPRDIPGF----VKE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 295 VQKQGGLAEKLMNTalevgerraagkpkfgdgLRDALVGrllKPKIRQRFGGRIKAMVSGGAPLNPEVGIFFESM-GLTM 373
Cdd:PRK08974 295 LKKYPFTAITGVNT------------------LFNALLN---NEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLtGQYL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 374 LQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIAED----------GEILVRGELVMQGYWHNEAETERTIKDGW 443
Cdd:PRK08974 354 LEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDdgnevppgepGELWVKGPQVMLGYWQRPEATDEVIKDGW 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 444 LHTGDIGHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAG 498
Cdd:PRK08974 434 LATGDIAVMDEEGFLRIVDRKKDMILV-SGFNVYPNEIEDVVMLHPKVLEVAAVG 487
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
37-514 |
1.76e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 148.19 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVptyITNTERDHAHI---LDNSGAKA 113
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAV---LLNTRLSREELlwqLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVSTEKLlrplhgalqasgiADHVIGIddlhrqqssgflFHRWDSMFAGDAAEArqaveQRIAGIGRGDTACIIYTSGT 193
Cdd:PRK03640 103 LITDDDFE-------------AKLIPGI------------SVKFAELMNGPKEEA-----EIQEEFDLDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 194 GGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAyehTGGQFLPISV--GAQIYYAEGL--EKLASNI 269
Cdd:PRK03640 153 TGKPKGVIQTYGNHWWSAVGSALNL----GLTEDDCWLAAVPIFHI---SGLSILMRSViyGMRVVLVEKFdaEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 270 EETRPTIMVVVPRLFEVLrtrimkqvqkqggLAEklmntalevgerraagkpkFGDGlrdalvgrllkpkirqRFGGRIK 349
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRL-------------LER-------------------LGEG----------------TYPSSFR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 350 AMVSGGAPLNPEVGIFFESMGLTMLQGYGQTE-AGPVISCNRPAAGIAMHSVGPAMRGVDIRIAED---------GEILV 419
Cdd:PRK03640 258 CMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDgvvvppfeeGEIVV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 420 RGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGd 499
Cdd:PRK03640 338 KGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISG-GENIYPAEIEEVLLSHPGVAEAGVVG- 415
|
490
....*....|....*
gi 2786869514 500 kkpyivgliVPDAEW 514
Cdd:PRK03640 416 ---------VPDDKW 421
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
14-535 |
3.14e-38 |
|
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: 147.45 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 14 LFLKRAAE-KGDLPflgARI-GGSWQTisWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITV 91
Cdd:cd12118 8 SFLERAAAvYPDRT---SIVyGDRRYT--WRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 92 PTYITNTERDHAHILDNSGAKAVIVSTEkllrplhgalqasgiadhvigiddlhrqqssgflFHRWDSMFAGDA-AEARQ 170
Cdd:cd12118 83 ALNTRLDAEEIAFILRHSEAKVLFVDRE----------------------------------FEYEDLLAEGDPdFEWIP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 171 AVEQRiagigrgDTACIIYTSGTGGAPRGVMQHH-GAILCNVAGAAEiliedFGIADDERFLSFLPLSHAyehtGGQFLP 249
Cdd:cd12118 129 PADEW-------DPIALNYTSGTTGRPKGVVYHHrGAYLNALANILE-----WEMKQHPVYLWTLPMFHC----NGWCFP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 250 ISVGA--------------QIYyaegleklaSNIEETRPTIMVVVPrlfEVLRTrimkqvqkqgglaekLMNTAlevger 315
Cdd:cd12118 193 WTVAAvggtnvclrkvdakAIY---------DLIEKHKVTHFCGAP---TVLNM---------------LANAP------ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 316 raagkpkfgdglrdalvgrllkPKIRQRFGGRIKAMVSGGAPlnPEVGIF-FESMGLTMLQGYGQTEA-GPVISC----- 388
Cdd:cd12118 240 ----------------------PSDARPLPHRVHVMTAGAPP--PAAVLAkMEELGFDVTHVYGLTETyGPATVCawkpe 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 389 --NRPAA---------GIAMHSVGPaMRGVDIRIAED--------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDI 449
Cdd:cd12118 296 wdELPTEerarlkarqGVRYVGLEE-VDVLDPETMKPvprdgktiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDL 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 450 GHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW--------TL----- 516
Cdd:cd12118 375 AVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGVLYKHPAVLEAAVVA----------RPDEKWgevpcafvELkegak 443
|
570 580
....*....|....*....|....*....
gi 2786869514 517 -------EWCREQGKQFDCKK---VQELP 535
Cdd:cd12118 444 vteeeiiAFCREHLAGFMVPKtvvFGELP 472
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
38-514 |
3.66e-38 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 145.57 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTyitNTERDHAHILDNsgakavivs 117
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLL---NTRLTPNELAFQ--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 118 tekllrplhgalqasgiadhvigIDDlhrqqssgflfhrwdsmfagdaaearqaveqriAGIGRGDTACIIYTSGTGGAP 197
Cdd:cd05912 69 -----------------------LKD---------------------------------SDVKLDDIATIMYTSGTTGKP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 198 RGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHayehTGGqfLPISVGAQIY---------YAEglEKLASN 268
Cdd:cd05912 93 KGVQQTFGNHWWSAIGSALNL----GLTEDDNWLCALPLFH----ISG--LSILMRSVIYgmtvylvdkFDA--EQVLHL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 269 IEETRPTIMVVVPrlfevlrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrdALVGRLLKpKIRQRFGGRI 348
Cdd:cd05912 161 INSGKVTIISVVP------------------------------------------------TMLQRLLE-ILGEGYPNNL 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 349 KAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTE-AGPVISCNRPAAGIAMHSVGPAMRGVDIRIA-------EDGEILVR 420
Cdd:cd05912 192 RCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELKIEddgqppyEVGEILLK 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 421 GELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdk 500
Cdd:cd05912 272 GPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISG-GENIYPAEIEEVLLSHPAIKEAGVVG-- 348
|
490
....*....|....
gi 2786869514 501 kpyivgliVPDAEW 514
Cdd:cd05912 349 --------IPDDKW 354
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
2-500 |
3.75e-38 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 148.20 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 2 LSDIDSANN--LVELFLKRAAEKGDLPFLgarI-GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCI 78
Cdd:PLN02246 14 LPDIYIPNHlpLHDYCFERLSEFSDRPCL---IdGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 79 ADLAIMASGCITV---PTYitnTERDHAHILDNSGAKaVIVSTEKLLRPLHGALQASGIAdhVIGIDDlhrqQSSGFLfH 155
Cdd:PLN02246 91 AFLGASRRGAVTTtanPFY---TPAEIAKQAKASGAK-LIITQSCYVDKLKGLAEDDGVT--VVTIDD----PPEGCL-H 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 156 RWDSMFAgDAAEARQAVeqriagIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDFGIADDERFLSFLP 235
Cdd:PLN02246 160 FSELTQA-DENELPEVE------ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 236 LSHAYEHTGGQFLPISVGAQIyyaegleklasnieetrptimVVVPRlFEVlrTRIMKQVQKQGGLAeklmntalevger 315
Cdd:PLN02246 233 MFHIYSLNSVLLCGLRVGAAI---------------------LIMPK-FEI--GALLELIQRHKVTI------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 316 rAAGKPkfgdglrdALVGRLLKPKIRQRFG-GRIKAMVSGGAPLNPEVGIFFESM--GLTMLQGYGQTEAGPVISCNRPA 392
Cdd:PLN02246 276 -APFVP--------PIVLAIAKSPVVEKYDlSSIRMVLSGAAPLGKELEDAFRAKlpNAVLGQGYGMTEAGPVLAMCLAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 393 AG----IAMHSVGPAMRGVDIRIAED-----------GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKG 456
Cdd:PLN02246 347 AKepfpVKSGSCGTVVRNAELKIVDPetgaslprnqpGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDD 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2786869514 457 RIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAGDK 500
Cdd:PLN02246 427 ELFIVDRLKELIKY-KGFQVAPAELEALLISHPSIADAAVVPMK 469
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
40-594 |
7.06e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 147.65 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 40 SWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITV---PTYitnteRDH--AHILDNSGAKAV 114
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVtinPAY-----RLSelEYALNQSGCKAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 115 I----------VSTEKLLRP-----LHGALQASGIAD--HVIGIDDlhrQQSSGFLfhRWDSMFAGDAAEARQAVEQRIA 177
Cdd:PRK08315 120 IaadgfkdsdyVAMLYELAPelatcEPGQLQSARLPElrRVIFLGD---EKHPGML--NFDELLALGRAVDDAELAARQA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 178 GIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYEHTGGQFLPISVGA-QI 256
Cdd:PRK08315 195 TLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAM----KLTEEDRLCIPVPLYHCFGMVLGNLACVTHGAtMV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 257 YYAEGLEKLA--SNIEETRPTIMVVVPRLF--------------EVLRTRI----------MKQVQKQgglaeklMNTAl 310
Cdd:PRK08315 271 YPGEGFDPLAtlAAVEEERCTALYGVPTMFiaeldhpdfarfdlSSLRTGImagspcpievMKRVIDK-------MHMS- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 311 evgerraagkpkfgdglrdalvgrllkpkirqrfggrikamvsggaplnpEVGIffesmgltmlqGYGQTEAGPVISCNR 390
Cdd:PRK08315 343 --------------------------------------------------EVTI-----------AYGMTETSPVSTQTR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 391 PAAGIA--MHSVGPAMRGVDIRI--AEDGEIL---VRGEL------VMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKG 456
Cdd:PRK08315 362 TDDPLEkrVTTVGRALPHLEVKIvdPETGETVprgEQGELctrgysVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 457 RIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAG--DKKpY--IVGLIV---PDAEWTLE----WCREQGKQ 525
Cdd:PRK08315 442 YVNIVGRIKDMIIRG-GENIYPREIEEFLYTHPKIQDVQVVGvpDEK-YgeEVCAWIilrPGATLTEEdvrdFCRGKIAH 519
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 526 FdckkvqelpefrnavraavdrvnkdlsvveKV-RQFAFADE-PftieneeMTPSMKIRRHKIKERYAERL 594
Cdd:PRK08315 520 Y------------------------------KIpRYIRFVDEfP-------MTVTGKIQKFKMREMMIEEL 553
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
18-572 |
1.82e-37 |
|
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: 146.83 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 18 RAAEKGDLPFLG---ARIGGSWQTISWNEAAEQVCLLA-ENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPT 93
Cdd:cd17632 44 RATELVTDPATGrttLRLLPRFETITYAELWERVGAVAaAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 94 YiTNTERDH-AHILDNSGAKAVIVSTEKLlrPLHGALQASGIADHVIGIDDLHRQQSSgflfHRwdsmFAGDAAEARQA- 171
Cdd:cd17632 124 Q-AGASAAQlAPILAETEPRLLAVSAEHL--DLAVEAVLEGGTPPRLVVFDHRPEVDA----HR----AALESARERLAa 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 172 ------VEQRIAGIGRGDT--------------ACIIYTSGTGGAPRGVMQHHGailcNVAGAAeiLIEDFGIADDERF- 230
Cdd:cd17632 193 vgipvtTLTLIAVRGRDLPpaplfrpepdddplALLIYTSGSTGTPKGAMYTER----LVATFW--LKVSSIQDIRPPAs 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 231 --LSFLPLSHAYehtGGQFL--PISVGAQIYYAEG--LEKLASNIEETRPTIMVVVPRLFEVLRTRIMKqvqkqgglaek 304
Cdd:cd17632 267 itLNFMPMSHIA---GRISLygTLARGGTAYFAAAsdMSTLFDDLALVRPTELFLVPRVCDMLFQRYQA----------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 305 lmntalEVGERRAAGkpkfgdGLRDALVGRlLKPKIRQR-FGGRIKAMVSGGAPLNPEVGIFFES-MGLTMLQGYGQTEA 382
Cdd:cd17632 333 ------ELDRRSVAG------ADAETLAER-VKAELRERvLGGRLLAAVCGSAPLSAEMKAFMESlLDLDLHDGYGSTEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 383 GPVISCN---RPAAgiamhsvgpamrgVDIRIAE--------------DGEILVRGELVMQGYWHN-EAETERTIKDGWL 444
Cdd:cd17632 400 GAVILDGvivRPPV-------------LDYKLVDvpelgyfrtdrphpRGELLVKTDTLFPGYYKRpEVTAEVFDEDGFY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 445 HTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGD-KKPYIVGLIVPDAEWTLEWCREQg 523
Cdd:cd17632 467 RTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNsERAYLLAVVVPTQDALAGEDTAR- 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 524 kqfdckkvqelpeFRNAVRAAVDRVNKD--LSVVEKVRQFAFADEPFTIEN 572
Cdd:cd17632 546 -------------LRAALAESLQRIAREagLQSYEIPRDFLIETEPFTIAN 583
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
34-514 |
4.40e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 141.54 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLR-ALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAK 112
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 113 AVIVSTEklLRPLHGALQASGIADHVIGIDDLhrqqsSGFLFHRWDSMFAGdaaearqaveqriagiGRGDTACIIYTSG 192
Cdd:PRK06839 103 VLFVEKT--FQNMALSMQKVSYVQRVISITSL-----KEIEDRKIDNFVEK----------------NESASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 193 TGGAPRG-VMQHHGAILCNVAGAAEIliedfGIADDERFLSFLPLSHayehTGG----QFLPISVGAQIYYAEGLE--KL 265
Cdd:PRK06839 160 TTGKPKGaVLTQENMFWNALNNTFAI-----DLTMHDRSIVLLPLFH----IGGiglfAFPTLFAGGVIIVPRKFEptKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 266 ASNIEETRPTIMVVVPRLFEVLRTrimkqvqkqgglaeklmntalevgerraagKPKFgdglrdalvgrlLKPKIRQrfg 345
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALIN------------------------------CSKF------------ETTNLQS--- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 346 grIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVI-------------SCNRPAAGIAMHSVGPAmrGVDIRIA 412
Cdd:PRK06839 266 --VRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVfmlseedarrkvgSIGKPVLFCDYELIDEN--KNKVEVG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 413 EDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIG 492
Cdd:PRK06839 342 EVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISG-GENIYPLEVEQVINKLSDVY 420
|
490 500
....*....|....*....|..
gi 2786869514 493 QAMVAGdkkpyivgliVPDAEW 514
Cdd:PRK06839 421 EVAVVG----------RQHVKW 432
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
183-463 |
2.08e-35 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 142.76 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYY---- 258
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDV----FNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYhpdp 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 259 --AEGLEKLasnIEETRPTIMVVVPRLFEvLRTRIMKqvqkqgglAEKLMntalevgerraagkpkFGDgLRdaLVgrll 336
Cdd:PRK08633 859 tdALGIAKL---VAKHRATILLGTPTFLR-LYLRNKK--------LHPLM----------------FAS-LR--LV---- 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 337 kpkirqrfggrikamVSGGAPLNPEVGIFF-ESMGLTMLQGYGQTEAGPVISCNRP---AAGIAMH------SVGPAMRG 406
Cdd:PRK08633 904 ---------------VAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPdvlAADFKRQtgskegSVGMPLPG 968
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786869514 407 VDIRI-----------AEDGEILVRGELVMQGYWHNEAETERTIKD----GWLHTGDIGHVDDKGRIVITDR 463
Cdd:PRK08633 969 VAVRIvdpetfeelppGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
17-591 |
2.98e-35 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 139.68 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 17 KRAAEKGDLPFLG--ARIGGSWQTISWNEAAEQVCLLAENLRALGLRdGDRVCLVSENRPEWCIADLAIMASGCITVPTY 94
Cdd:cd05931 1 RRAAARPDRPAYTflDDEGGREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 95 ITNTERDHAH---ILDNSGAKAVIVSTEKL-LRPLHGALQASGIADHVIGIDDLhrqqssgflfhrwdsmfagDAAEARQ 170
Cdd:cd05931 80 PPTPGRHAERlaaILADAGPRVVLTTAAALaAVRAFAASRPAAGTPRLLVVDLL-------------------PDTSAAD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 171 AVEqriAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVagaaEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPI 250
Cdd:cd05931 141 WPP---PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANV----RQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 251 SVGAQIYYAEGLEKLAS------NIEETRPTIMVVVPRLFEVLRTRIMkqVQKQGGLAEKLMNTALEVGER-RAAGKPKF 323
Cdd:cd05931 214 YSGGPSVLMSPAAFLRRplrwlrLISRYRATISAAPNFAYDLCVRRVR--DEDLEGLDLSSWRVALNGAEPvRPATLRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 324 GDGLRdalvgrllkpkirqRFGGRIKAM------------VSGGAPLNPEVGIFFESMGLtmlqgygqtEAGPVISCNRP 391
Cdd:cd05931 292 AEAFA--------------PFGFRPEAFrpsyglaeatlfVSGGPPGTGPVVLRVDRDAL---------AGRAVAVAADD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 392 AAGIAMHSVGPAMRGVDIRIAED-----------GEILVRGELVMQGYWHNEAETERTIK-------DGWLHTGDIGHVD 453
Cdd:cd05931 349 PAARELVSCGRPLPDQEVRIVDPetgrelpdgevGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 454 DkGRIVITDRKKDMIVNDkGDNVAPQKVEgmLTLQ---PEIGQAMVA----GDKKPYIVGLIVPDAEWTLEwcreqgkqf 526
Cdd:cd05931 429 D-GELYITGRLKDLIIVR-GRNHYPQDIE--ATAEeahPALRPGCVAafsvPDDGEERLVVVAEVERGADP--------- 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 527 dckkvQELPEFRNAVRAAVDRvNKDLsvveKVRQFAFAdEPFTIENeemTPSMKIRRHKIKERYA 591
Cdd:cd05931 496 -----ADLAAIAAAIRAAVAR-EHGV----APADVVLV-RPGSIPR---TSSGKIQRRACRAAYL 546
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
51-587 |
3.39e-35 |
|
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: 137.85 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 51 LAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTEkllrplhgalq 130
Cdd:cd05972 13 AANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 131 asgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTGGAPRGVMQHHGAILCN 210
Cdd:cd05972 82 ----------------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 211 VAGAAEILiedfGIADDERFLSFLPLSHAYEHTGGQFLPISVGAqiyyaegleklasnieetrPTIMVVVPRlFEvlrtr 290
Cdd:cd05972 110 IPTAAYWL----GLRPDDIHWNIADPGWAKGAWSSFFGPWLLGA-------------------TVFVYEGPR-FD----- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 291 imkqvqkqgglAEKLMNTALEVGERRAAGKPKfgdGLRdalvgRLLKPKIRQRFGGRIKAMVSGGAPLNPEV-GIFFESM 369
Cdd:cd05972 161 -----------AERILELLERYGVTSFCGPPT---AYR-----MLIKQDLSSYKFSHLRLVVSAGEPLNPEViEWWRAAT 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 370 GLTMLQGYGQTEAGPVIScNRPAAGIAMHSVGPAMRGVDIRIA-EDGEILVRGEL-----------VMQGYWHNEAETER 437
Cdd:cd05972 222 GLPIRDGYGQTETGLTVG-NFPDMPVKPGSMGRPTPGYDVAIIdDDGRELPPGEEgdiaiklpppgLFLGYVGDPEKTEA 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 438 TIKDGWLHTGDIGHVDDKGRIVITDRKKDmIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkKPYIVGLIVPDAEWTLe 517
Cdd:cd05972 301 SIRGDYYLTGDRAYRDEDGYFWFVGRADD-IIKSSGYRIGPFEVESALLEHPAVAEAAVVG--SPDPVRGEVVKAFVVL- 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 518 wcrEQGKQFDCKKVQELPEFrnavraavdrVNKDLSVVEKVRQFAFADE-PFTIeneemtpSMKIRRHKIK 587
Cdd:cd05972 377 ---TSGYEPSEELAEELQGH----------VKKVLAPYKYPREIEFVEElPKTI-------SGKIRRVELR 427
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
7-588 |
1.10e-34 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 138.04 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 7 SANNLVELFLKRAAEKGD-LPFLGARIGgswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMA 85
Cdd:cd17642 15 TAGEQLHKAMKRYASVPGtIAFTDAHTG---VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 86 SGCITVPTYITNTERDHAHILDNSGAKAVIVSTEKLLRPLHGALQASGIADHVI--GIDDLHRQQSSGFLFHRWD----- 158
Cdd:cd17642 92 IGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIIldSKEDYKGYQCLYTFITQNLppgfn 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 159 -SMFAGDAAEARQAVeqriagigrgdtACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedFG--IADDERFLSFLP 235
Cdd:cd17642 172 eYDFKPPSFDRDEQV------------ALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPI---FGnqIIPDTAILTVIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 236 LSHAYehtgGQFLPIS---VGAQIYYAEGLEK--LASNIEETRPTIMVVVPRLFEVLrtrimkqvqKQGGLAEKLMNTAL 310
Cdd:cd17642 237 FHHGF----GMFTTLGyliCGFRVVLMYKFEEelFLRSLQDYKVQSALLVPTLFAFF---------AKSTLVDKYDLSNL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 311 EVgerraagkpkfgdglrdalvgrllkpkirqrfggrikaMVSGGAPLNPEVG-IFFESMGLTML-QGYGQTEAGPVI-- 386
Cdd:cd17642 304 HE--------------------------------------IASGGAPLSKEVGeAVAKRFKLPGIrQGYGLTETTSAIli 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 387 ---------SCNRPAAGIAMHSVGPAMrGVDIRIAEDGEILVRGELVMQGYWHN-EAETERTIKDGWLHTGDIGHVDDKG 456
Cdd:cd17642 346 tpegddkpgAVGKVVPFFYAKVVDLDT-GKTLGPNERGELCVKGPMIMKGYVNNpEATKALIDKDGWLHSGDIAYYDEDG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 457 RIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkKPYIVGLIVPDAEWTLewcrEQGKQFDCKKVQelpe 536
Cdd:cd17642 425 HFFIVDRLKSLI-KYKGYQVPPAELESILLQHPKIFDAGVAG--IPDEDAGELPAAVVVL----EAGKTMTEKEVM---- 493
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 537 frnavraavDRVNKDLSVVEKVR-QFAFADE-PftieneeMTPSMKIRRHKIKE 588
Cdd:cd17642 494 ---------DYVASQVSTAKRLRgGVKFVDEvP-------KGLTGKIDRRKIRE 531
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
25-515 |
3.23e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 136.83 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 25 LPFLGariggswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAH 104
Cdd:PRK07786 36 LRFLG-------NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 105 ILDNSGAKAVIvsTEKLLRPLHGALQAS------------GIADHVIGIDDLHRQqssgflfhrwdsmfagdAAEARQAV 172
Cdd:PRK07786 109 LVSDCGAHVVV--TEAALAPVATAVRDIvpllstvvvaggSSDDSVLGYEDLLAE-----------------AGPAHAPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 173 EqriagIGRGDTACIIYTSGTGGAPRGVMQHHgailCNVAGAAEILIEDFG--IADDERFLSfLPLSH-AYEHTGGQFLP 249
Cdd:PRK07786 170 D-----IPNDSPALIMYTSGTTGRPKGAVLTH----ANLTGQAMTCLRTNGadINSDVGFVG-VPLFHiAGIGSMLPGLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 250 ISVGAQIYYAEGLE--KLASNIEETRPTIMVVVPrlfevlrtrimkqVQKQGGLAEklmntalevgerraagkpkfgdgl 327
Cdd:PRK07786 240 LGAPTVIYPLGAFDpgQLLDVLEAEKVTGIFLVP-------------AQWQAVCAE------------------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 328 rdalvgrllkPKIRQRfGGRIKAMVSGGAPLNPEVgifFESMGLT-----MLQGYGQTEAGPVI-------------SCN 389
Cdd:PRK07786 283 ----------QQARPR-DLALRVLSWGAAPASDTL---LRQMAATfpeaqILAAFGQTEMSPVTcmllgedairklgSVG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 390 RPAAGIAMHSVGPAMRgvDIRIAEDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIV 469
Cdd:PRK07786 349 KVIPTVAARVVDENMN--DVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMII 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2786869514 470 NDkGDNVAPQKVEGMLTLQPEIGQAMVAGDkkpyivglivPDAEWT 515
Cdd:PRK07786 427 SG-GENIYCAEVENVLASHPDIVEVAVIGR----------ADEKWG 461
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
37-517 |
3.86e-34 |
|
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: 134.90 E-value: 3.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEkllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTGGA 196
Cdd:cd05919 89 SAD---------------------------------------------------------------DIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGailcNVAGAAEIL-IEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGL---EKLASNIEET 272
Cdd:cd05919 106 PKGVMHAHR----DPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWptaERVLATLARF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 273 RPTIMVVVPRLFEVLRTRimkqvqkqgglaeklmntalevgerraagkpkfGDGLRDALVGrllkpkirqrfggrIKAMV 352
Cdd:cd05919 182 RPTVLYGVPTFYANLLDS---------------------------------CAGSPDALRS--------------LRLCV 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 353 SGGAPLNPEVGIFF-ESMGLTMLQGYGQTEAGPVISCNRPAAgIAMHSVGPAMRGVDIRIAED----------GEILVRG 421
Cdd:cd05919 215 SAGEALPRGLGERWmEHFGGPILDGIGATEVGHIFLSNRPGA-WRLGSTGRPVPGYEIRLVDEeghtippgeeGDLLVRG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 422 ELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkK 501
Cdd:cd05919 294 PSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVVA--V 370
|
490
....*....|....*.
gi 2786869514 502 PYIVGLIVPDAEWTLE 517
Cdd:cd05919 371 PESTGLSRLTAFVVLK 386
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
38-498 |
4.61e-34 |
|
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: 134.43 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVS 117
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 118 TekllrplhgalqasgiadhvigiddlhrqqssgflfhRWDSMfagdaaearqaveqRIAGIGrGDTACIIYTSGTGGAP 197
Cdd:cd05903 81 E-------------------------------------RFRQF--------------DPAAMP-DAVALLLFTSGTTGEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 198 RGVMQHHGAILCNVAGaaeiLIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLE--KLASNIEETRPT 275
Cdd:cd05903 109 KGVMHSHNTLSASIRQ----YAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDpdKALALMREHGVT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 276 IMVVVPRLFEvlrtrimkqvqkqgglaeKLMNTALEVGERRAagkpkfgdglrdalvgrllkpkirqrfggRIKAMVSGG 355
Cdd:cd05903 185 FMMGATPFLT------------------DLLNAVEEAGEPLS-----------------------------RLRTFVCGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 356 APLNPEVGI-FFESMGLTMLQGYGQTE-AGPVISCNRPAAGIAMHSVGPAMRGVDIRIAED----------GEILVRGEL 423
Cdd:cd05903 218 ATVPRSLARrAAELLGAKVCSAYGSTEcPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDtgatlapgveGELLSRGPS 297
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 424 VMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAG 498
Cdd:cd05903 298 VFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRG-GENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
30-514 |
1.12e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 134.65 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 30 ARIGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP--TYITNTERdhAHILD 107
Cdd:PRK08276 3 VIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPinWHLTAAEI--AYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 108 NSGAKAVIVStEKLLRPLHGALQASGIADHVIGIDDlhrQQSSGFLfhRWDSMFAGDAAEarqaveqRIAGIGRGDTacI 187
Cdd:PRK08276 81 DSGAKVLIVS-AALADTAAELAAELPAGVPLLLVVA---GPVPGFR--SYEEALAAQPDT-------PIADETAGAD--M 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 188 IYTSGTGGAPRGVM--QHHGAILCNVAGAAEILIEDFGIADDERFLSFLPLSHA-------YEHTGGQFLpisVGAQIYY 258
Cdd:PRK08276 146 LYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrfgmSALALGGTV---VVMEKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 259 AEGLEKLasnIEETRPTIMVVVPRLFevlrTRIMKqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrlLKP 338
Cdd:PRK08276 223 AEEALAL---IERYRVTHSQLVPTMF----VRMLK------------------------------------------LPE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 339 KIRQRFG-GRIKAMVSGGAPLNPEVGiffESM----GLTMLQGYGQTEAGPVISCNrpAAGIAMH--SVGPAMRGVdIRI 411
Cdd:PRK08276 254 EVRARYDvSSLRVAIHAAAPCPVEVK---RAMidwwGPIIHEYYASSEGGGVTVIT--SEDWLAHpgSVGKAVLGE-VRI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 -AEDGEILVRGE--LV---MQGY---WHNEAETERTI--KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQK 480
Cdd:PRK08276 328 lDEDGNELPPGEigTVyfeMDGYpfeYHNDPEKTAAArnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISG-GVNIYPQE 406
|
490 500 510
....*....|....*....|....*....|....
gi 2786869514 481 VEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:PRK08276 407 IENLLVTHPKVADVAVFG----------VPDEEM 430
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
11-596 |
1.65e-33 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 134.72 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGD-LPFLGARIGgswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCI 89
Cdd:PLN02330 30 LPDFVLQDAELYADkVAFVEAVTG---KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 90 TVPTYITNTERDHAHILDNSGAKAVIVSTEKllrplHGALQASGIADHVIGiddlhRQQSSGFLfhRWDSMF-AGDAAEA 168
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTNDTN-----YGKVKGLGLPVIVLG-----EEKIEGAV--NWKELLeAADRAGD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 169 RQAVEQriagIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAeiliedFGIADDE----RFLSFLPLSHAYEHTG 244
Cdd:PLN02330 175 TSDNEE----ILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSL------FSVGPEMigqvVTLGLIPFFHIYGITG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 245 gqflpisvgaqIYYAEgleklasnieeTRPTIMVVVPRLFEvLRTRIMKQVQKQGGLAEKLMNTALEVgerraagkpkfg 324
Cdd:PLN02330 245 -----------ICCAT-----------LRNKGKVVVMSRFE-LRTFLNALITQEVSFAPIVPPIILNL------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 325 dgLRDALVGRLLKPKIRqrfggrIKAMVSGGAPLNPEVGIFFESM--GLTMLQGYGQTEAGPV-ISCNRPAAG--IAM-H 398
Cdd:PLN02330 290 --VKNPIVEEFDLSKLK------LQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHSCItLTHGDPEKGhgIAKkN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 399 SVGPAMRGVDIRIAE-----------DGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKD 466
Cdd:PLN02330 362 SVGFILPNLEVKFIDpdtgrslpkntPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 467 MIvNDKGDNVAPQKVEGMLTLQPEIGQAMVagdkkpyivgLIVPDaewtlewcrEQGKQFDCKKVQELPEFRNAVRAAVD 546
Cdd:PLN02330 442 LI-KYKGFQVAPAELEAILLTHPSVEDAAV----------VPLPD---------EEAGEIPAACVVINPKAKESEEDILN 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2786869514 547 RVNKDLSVVEKVRQFAFADepfTIENeemTPSMKIRRHKIKERYAERLDA 596
Cdd:PLN02330 502 FVAANVAHYKKVRVVQFVD---SIPK---SLSGKIMRRLLKEKMLSINKA 545
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
183-535 |
1.93e-33 |
|
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: 130.14 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHayehTGGQ---FLPISVGAQIYYA 259
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL----GFGGGDSWLLSLPLYH----VGGLailVRSLLAGAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 260 EGLEKLASNIEETRPTIMVVVPRlfevlrtrimkQVQKqgglaeklmntALEVGERRAAGKpkfgdglrdalvgrllkpk 339
Cdd:cd17630 73 ERNQALAEDLAPPGVTHVSLVPT-----------QLQR-----------LLDSGQGPAALK------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 340 irqrfggRIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVIsCNRPAAGIAMHSVGPAMRGVDIRIAEDGEILV 419
Cdd:cd17630 112 -------SLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQV-ATKRPDGFGRGGVGVLLPGRELRIVEDGEIWV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 420 RGELVMQGYWHNEAETERTiKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGD 499
Cdd:cd17630 184 GGASLAMGYLRGQLVPEFN-EDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVVGV 261
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2786869514 500 KKPY----IVGLIVPDAEWTLE----WCREQGKQFDCKK----VQELP 535
Cdd:cd17630 262 PDEElgqrPVAVIVGRGPADPAelraWLKDKLARFKLPKriypVPELP 309
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
38-512 |
4.28e-33 |
|
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: 133.04 E-value: 4.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVS 117
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 118 TEklLRPLhgalqasgIADHVIGIDDLHRQQSSGFLFHRWDSMFAGDAAEArqavEQRIAGIGRGDTACI-IYTSGTGGA 196
Cdd:TIGR02262 110 GA--LLPV--------IKAALGKSPHLEHRVVVGRPEAGEVQLAELLATES----EQFKPAATQADDPAFwLYSSGSTGM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGailcNVAGAAEILIED-FGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQ-IYYAEgleklasnieetRP 274
Cdd:TIGR02262 176 PKGVVHTHS----NPYWTAELYARNtLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATtVLMGE------------RP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 275 TimvvVPRLFEVLRTRimkqvqkqgglaeklmntalevgerraagKPKFGDGLRDALVGRLLKPKIRQRFGGRIKAMVSG 354
Cdd:TIGR02262 240 T----PDAVFDRLRRH-----------------------------QPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 355 GAPLNPEVGIFFES-MGLTMLQGYGQTEAGPVISCNRPAA-----------GIAMHSVGPamRGVDIRIAEDGEILVRGE 422
Cdd:TIGR02262 287 GEALPAEVGQRWQArFGVDIVDGIGSTEMLHIFLSNLPGDvrygtsgkpvpGYRLRLVGD--GGQDVADGEPGELLISGP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 423 LVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKP 502
Cdd:TIGR02262 365 SSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDML-KVSGIYVSPFEIESALIQHPAVLEAAVVGVADE 443
|
490
....*....|
gi 2786869514 503 YivGLIVPDA 512
Cdd:TIGR02262 444 D--GLIKPKA 451
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
17-496 |
8.87e-33 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 132.57 E-value: 8.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 17 KRAAEKGDLPFLgaRIGGSWQTisWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTyit 96
Cdd:PRK06155 29 RQAERYPDRPLL--VFGGTRWT--YAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 97 NTERDHA---HILDNSGAKAVIVSTEkLLRPLHGALQASGIADHVIGIDdlhrQQSSGFLFHRWD--SMFAGDAAEArqa 171
Cdd:PRK06155 102 NTALRGPqleHILRNSGARLLVVEAA-LLAALEAADPGDLPLPAVWLLD----APASVSVPAGWStaPLPPLDAPAP--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 172 veqrIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAIL---CNVAgaaeiliEDFGIADDERFLSFLPLSHayehtggqfl 248
Cdd:PRK06155 174 ----AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYwwgRNSA-------EDLEIGADDVLYTTLPLFH---------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 249 pisVGAQIYYAEGLEKLASnieetrptiMVVVPRlFEVlrTRIMKQVQKQGGLAEKLMNtalevgerraagkpkfgdglr 328
Cdd:PRK06155 233 ---TNALNAFFQALLAGAT---------YVLEPR-FSA--SGFWPAVRRHGATVTYLLG--------------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 329 dALVGRLL-KPKIRQRFGGRIKAMVSGGAPlnPEVGI-FFESMGLTMLQGYGQTEAGPVISCNRPA--AGiamhSVGPAM 404
Cdd:PRK06155 277 -AMVSILLsQPARESDRAHRVRVALGPGVP--AALHAaFRERFGVDLLDGYGSTETNFVIAVTHGSqrPG----SMGRLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 405 RGVDIRIAED----------GEILVRGE---LVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvND 471
Cdd:PRK06155 350 PGFEARVVDEhdqelpdgepGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAI-RR 428
|
490 500
....*....|....*....|....*
gi 2786869514 472 KGDNVAPQKVEGMLTLQPEIGQAMV 496
Cdd:PRK06155 429 RGENISSFEVEQVLLSHPAVAAAAV 453
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
7-498 |
3.92e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 130.00 E-value: 3.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 7 SANNLVELFLKRAAEKgDLPFLGARIGgswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMAS 86
Cdd:PRK07514 1 MNNNLFDALRAAFADR-DAPFIETPDG---LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 87 GCITVP--TYITNTERDHahILDNSGAKAVIVSTEKL--LRPLHGALQASgiadHVIGIDDlhrqQSSGFLFHRwdsmfA 162
Cdd:PRK07514 77 GAVFLPlnTAYTLAELDY--FIGDAEPALVVCDPANFawLSKIAAAAGAP----HVETLDA----DGTGSLLEA-----A 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 163 GDAAEARQAVEQriagiGRGDTACIIYTSGTGGAPRGVMQHHGAILCNvagaAEILIEDFGIADDERFLSFLPLSHayeh 242
Cdd:PRK07514 142 AAAPDDFETVPR-----GADDLAAILYTSGTTGRSKGAMLSHGNLLSN----ALTLVDYWRFTPDDVLIHALPIFH---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 243 TGGQFLPISV----GAQIYY------AEGLEKLAsnieetRPTIMVVVPRLFevlrTRIMKQvqkqgglaeklmntalev 312
Cdd:PRK07514 209 THGLFVATNVallaGASMIFlpkfdpDAVLALMP------RATVMMGVPTFY----TRLLQE------------------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 313 gerraagkPKFGdglRDALVG-RLLkpkirqrfggrikamVSGGAPLNPEVGI-FFESMGLTMLQGYGQTEAGPVIScnR 390
Cdd:PRK07514 261 --------PRLT---REAAAHmRLF---------------ISGSAPLLAETHReFQERTGHAILERYGMTETNMNTS--N 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 391 PAAG--IAmHSVGPAMRGVDIRIA--EDGEILVRGEL---------VMQGYWHNEAET-ERTIKDGWLHTGDIGHVDDKG 456
Cdd:PRK07514 313 PYDGerRA-GTVGFPLPGVSLRVTdpETGAELPPGEIgmievkgpnVFKGYWRMPEKTaEEFRADGFFITGDLGKIDERG 391
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2786869514 457 RIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAG 498
Cdd:PRK07514 392 YVHIVGRGKDLIISG-GYNVYPKEVEGEIDELPGVVESAVIG 432
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-501 |
3.95e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 127.01 E-value: 3.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYEHTGGQFLPISVGA-QIYYAEG 261
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERL----GLTEQDRLCIPVPLFHCFGSVLGVLACLTHGAtMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 262 LEKLAS--NIEETRPTIMVVVPRLFEVLRTRIMKqvqkqgglaeklmntalevgerraagkPKFGDGlrdalvgrllkpk 339
Cdd:cd05917 79 FDPLAVleAIEKEKCTALHGVPTMFIAELEHPDF---------------------------DKFDLS------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 340 irqrfggRIKAMVSGGAPLNPEV--GIFfESMGLTMLQ-GYGQTEAGPVISCNRPAAGI--AMHSVGPAMRGVDIRI--- 411
Cdd:cd05917 119 -------SLRTGIMAGAPCPPELmkRVI-EVMNMKDVTiAYGMTETSPVSTQTRTDDSIekRVNTVGRIMPHTEAKIvdp 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 --------AEDGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVE 482
Cdd:cd05917 191 eggivppvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRG-GENIYPREIE 269
|
330 340
....*....|....*....|.
gi 2786869514 483 GMLTLQPEIGQAMVAG--DKK 501
Cdd:cd05917 270 EFLHTHPKVSDVQVVGvpDER 290
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
40-513 |
5.69e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 129.82 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 40 SWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTE 119
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 120 kLLRPLHGALQAsGIADHVI----------GIDDLHRQQSSGFLfhRWDSMFAGDAAEARQAVEQRiagigrgdtACIIY 189
Cdd:PRK12406 93 -LLHGLASALPA-GVTVLSVptppeiaaayRISPALLTPPAGAI--DWEGWLAQQEPYDGPPVPQP---------QSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 190 TSGTGGAPRGVmQHHGAILCNVAGAAEILIEDFGIADDERFLSFLPLSH----AYEHTGGQFLPISVGAQIYYAEGLEKL 265
Cdd:PRK12406 160 TSGTTGHPKGV-RRAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYGLRAGRLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 266 asnIEETRPTIMVVVPRLFevlrTRIMKqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrlLKPKIRQRFG 345
Cdd:PRK12406 239 ---IERHRITHMHMVPTMF----IRLLK------------------------------------------LPEEVRAKYD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 346 -GRIKAMVSGGAPLNPEVG-IFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIAED--------- 414
Cdd:PRK12406 270 vSSLRHVIHAAAPCPADVKrAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEdgrplpqge 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 -GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIG 492
Cdd:PRK12406 350 iGEIYSRIAGNPDFTYHNKPEKRAEIdRGGFITSGDVGYLDADGYLFLCDRKRDMVISG-GVNIYPAEIEAVLHAVPGVH 428
|
490 500
....*....|....*....|.
gi 2786869514 493 QAMVAGdkkpyivgliVPDAE 513
Cdd:PRK12406 429 DCAVFG----------IPDAE 439
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
4-541 |
2.50e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 128.34 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 4 DIDSANNLVELF---LKRAAEKGDLPFLGAriggswqTISWNEAAEQVCLLAENLRAL-GLRDGDRVCLVSENRPEWCIA 79
Cdd:PRK05677 19 NPDEYPNIQAVLkqsCQRFADKPAFSNLGK-------TLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 80 DLAIMASGCITVPTYITNTERDHAHILDNSGAKA----------------------VIVsTE--KLLRPLHGALQASGIA 135
Cdd:PRK05677 92 VFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKAlvclanmahlaekvlpktgvkhVIV-TEvaDMLPPLKRLLINAVVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 136 DHVIGIDDLHRQQSSGFLfhrwDSMFAGdaaeARQAVEQriAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAA 215
Cdd:PRK05677 171 HVKKMVPAYHLPQAVKFN----DALAKG----AGQPVTE--ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 216 EILIEDFGIADdERFLSFLPLSHAYEHTGGQFLPISVGAQiyyaegleklasnieetrpTIMVVVPRLFEVLrtriMKQV 295
Cdd:PRK05677 241 ALMGSNLNEGC-EILIAPLPLYHIYAFTFHCMAMMLIGNH-------------------NILISNPRDLPAM----VKEL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 296 QKQgglaeklmntalevgerraagkpKFGD--GLRDALVGRLLKPKIRQRFGGRIKAMVSGGAPLNPEVGIFFESM-GLT 372
Cdd:PRK05677 297 GKW-----------------------KFSGfvGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVtGCA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 373 MLQGYGQTEAGPVISCNrPAAGIAMHSVG---PAM-------RGVDIRIAEDGEILVRGELVMQGYWHNEAETERTI-KD 441
Cdd:PRK05677 354 ICEGYGMTETSPVVSVN-PSQAIQVGTIGipvPSTlckviddDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 442 GWLHTGDIGHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAG--DKKP--YIVGLIVP------D 511
Cdd:PRK05677 433 GWLKTGDIALIQEDGYMRIVDRKKDMILV-SGFNVYPNELEDVLAALPGVLQCAAIGvpDEKSgeAIKVFVVVkpgetlT 511
|
570 580 590
....*....|....*....|....*....|
gi 2786869514 512 AEWTLEWCREQGKQFdckKVQELPEFRNAV 541
Cdd:PRK05677 512 KEQVMEHMRANLTGY---KVPKAVEFRDEL 538
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
41-496 |
2.42e-30 |
|
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: 123.14 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 41 WNEAAEQvclLAENLRAL-GLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTe 119
Cdd:TIGR01733 5 LDERANR---LARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 120 kllrplHGALQASGIADHVIGIDDLHrqqssgflfhrwdsmfaGDAAEARQAVEQRIAGIGRGDTACIIYTSGTGGAPRG 199
Cdd:TIGR01733 81 ------ALASRLAGLVLPVILLDPLE-----------------LAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 200 VMQHHGAILCNVAGAAeiliEDFGIADDERFLSFLPLSH---AYEhtggQFLPISVGAQIYYAEG------LEKLASNIE 270
Cdd:TIGR01733 138 VVVTHRSLVNLLAWLA----RRYGLDPDDRVLQFASLSFdasVEE----IFGALLAGATLVVPPEdeerddAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 271 ETRPTIMVVVPRLFEVLrtrIMKQVQKQGGLaeKLMNTAlevgerraagkpkfGDGLRDALVGRLlkpkiRQRFGGRika 350
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALL---AAALPPALASL--RLVILG--------------GEALTPALVDRW-----RARGPGA--- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 mvsggaplnpevgiffesmglTMLQGYGQTEAGPVISCN----------------RPAAGIAMHSVGPAMRGVDirIAED 414
Cdd:TIGR01733 263 ---------------------RLINLYGPTETTVWSTATlvdpddaprespvpigRPLANTRLYVLDDDLRPVP--VGVV 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 GEILVRGELVMQGYWHNEAET-ERTIKDG--------WLHTGDIGHVDDKGRIVITDRkKDMIVNDKGDNVAPQKVEGML 485
Cdd:TIGR01733 320 GELYIGGPGVARGYLNRPELTaERFVPDPfaggdgarLYRTGDLVRYLPDGNLEFLGR-IDDQVKIRGYRIELGEIEAAL 398
|
490
....*....|.
gi 2786869514 486 TLQPEIGQAMV 496
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
37-514 |
2.52e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 124.61 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEkllrplhgaLQASGIADHVIGIDDLHRQQSSGFLFhrwdsmfAGDAAEARQAVeqriagIGRGDTACIIYTSGTGGA 196
Cdd:PRK06145 106 DEE---------FDAIVALETPKIVIDAAAQADSRRLA-------QGGLEIPPQAA------VAPTDLVRLMYTSGTTDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPLSHayehTGGQFLPisvGAQIYYAEGLeklasnieetrpti 276
Cdd:PRK06145 164 PKGVMHSYG----NLHWKSIDHVIALGLTASERLLVVGPLYH----VGAFDLP---GIAVLWVGGT-------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 277 mvvvprlfevlrTRIMKQVQKQGGLAeklmntALEvGERRAAGkpkfgdGLRDALVGRLLKPKIRQRFGGRIKAMVSGGA 356
Cdd:PRK06145 219 ------------LRIHREFDPEAVLA------AIE-RHRLTCA------WMAPVMLSRVLTVPDRDRFDLDSLAWCIGGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 357 PLNPEVGIF-FESM--GLTMLQGYGQTEA---GPVISCNRPAAGIAmhSVGPAMRGVDIRIAED----------GEILVR 420
Cdd:PRK06145 274 EKTPESRIRdFTRVftRARYIDAYGLTETcsgDTLMEAGREIEKIG--STGRALAHVEIRIADGagrwlppnmkGEICMR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 421 GELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdk 500
Cdd:PRK06145 352 GPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISG-GENIASSEVERVIYELPEVAEAAVIG-- 428
|
490
....*....|....
gi 2786869514 501 kpyivgliVPDAEW 514
Cdd:PRK06145 429 --------VHDDRW 434
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
183-515 |
3.35e-29 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 118.53 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRG-VMQHHGAILCNVAgaaeiLIEDFGIADDERFLSFLPLSHayehTGGQFLPISV----GAQIY 257
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGaVLSHGNLIAANLQ-----LIHAMGLTEADVYLNMLPLFH----IAGLNLALATfhagGANVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 258 YAEGLEKLASN-IEETRPTIMVVVPRLFevlrTRIMKQVQKQGGLAEKLMNTAlevgerraagkpkfgdGLrDAlvgrll 336
Cdd:cd17637 72 MEKFDPAEALElIEEEKVTLMGSFPPIL----SNLLDAAEKSGVDLSSLRHVL----------------GL-DA------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 337 kpkirqrfggrikamvsggaplnPEVGIFFESM-GLTMLQGYGQTEAGPVISC----NRPAagiamhSVGPAMRGVDIRI 411
Cdd:cd17637 125 -----------------------PETIQRFEETtGATFWSLYGQTETSGLVTLspyrERPG------SAGRPGPLVRVRI 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 AED----------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRK--KDMIvndK--GDNVA 477
Cdd:cd17637 176 VDDndrpvpagetGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELI---KpgGENVY 252
|
330 340 350
....*....|....*....|....*....|....*...
gi 2786869514 478 PQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEWT 515
Cdd:cd17637 253 PAEVEKVILEHPAIAEVCVIG----------VPDPKWG 280
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
19-600 |
3.84e-29 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 121.77 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 19 AAEKGDLPFLGARIG-GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG---CITVPTY 94
Cdd:cd05921 5 ARQAPDRTWLAEREGnGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaAPVSPAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 95 ITNTeRDHA---HILDNSGAKAVIVSTEKllrPLHGALQAsgiadhvigIDDLHRQQ--SSGFLFHRWDSMFAGDAA-EA 168
Cdd:cd05921 85 SLMS-QDLAklkHLFELLKPGLVFAQDAA---PFARALAA---------IFPLGTPLvvSRNAVAGRGAISFAELAAtPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 169 RQAVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGailcNVAGAAEILIEDFGIADDE--RFLSFLPLSHAYehtGGQ 246
Cdd:cd05921 152 TAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQR----MLCANQAMLEQTYPFFGEEppVLVDWLPWNHTF---GGN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 247 --FLPISVGAQIYY-------AEGLEKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaleVGERRa 317
Cdd:cd05921 225 hnFNLVLYNGGTLYiddgkpmPGGFEETLRNLREISPTVYFNVPAGWEML------------------------VAALE- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 318 agkpkfgdglRDalvgrllkPKIRQRFGGRIKAMVSGGAPLNPEV-----GIFFESMG--LTMLQGYGQTEAGPVIS-CN 389
Cdd:cd05921 280 ----------KD--------EALRRRFFKRLKLMFYAGAGLSQDVwdrlqALAVATVGerIPMMAGLGATETAPTATfTH 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 390 RPAAGIAMhsVGPAMRGVDIRIAEDG---EILVRGELVMQGYWHNeaeTERTIK----DGWLHTGDIGHVDD-------- 454
Cdd:cd05921 342 WPTERSGL--IGLPAPGTELKLVPSGgkyEVRVKGPNVTPGYWRQ---PELTAQafdeEGFYCLGDAAKLADpddpakgl 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 455 --KGRIViTDRKKdmivnDKGDNVA--PQKVEGMLTLQPEIGQAMVAGDKKPYIVGLIVPDaewtLEWCRE--QGKQFDC 528
Cdd:cd05921 417 vfDGRVA-EDFKL-----ASGTWVSvgPLRARAVAACAPLVHDAVVAGEDRAEVGALVFPD----LLACRRlvGLQEASD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786869514 529 KKVQELPEFRNAVRAAVDRVNKDLS-VVEKVRQFAFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYRG 600
Cdd:cd05921 487 AEVLRHAKVRAAFRDRLAALNGEATgSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
2-522 |
5.08e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 121.99 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 2 LSDIDSANNLVELFLKRAAEKGDLPFLGARI-GGSW---QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWC 77
Cdd:PRK07529 18 LAARDLPASTYELLSRAAARHPDAPALSFLLdADPLdrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 78 IADLAIMASGcITVPtyIT-NTERDH-AHILDNSGAKAVIVsteklLRPLHG---ALQASGIADH---------VIGIDD 143
Cdd:PRK07529 98 FALWGGEAAG-IANP--INpLLEPEQiAELLRAAGAKVLVT-----LGPFPGtdiWQKVAEVLAAlpelrtvveVDLARY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 144 LHRQQSSGFLFHRWDS---MFAGDAAEARQAVEQRIAG--IGRGDTACIIYTSGTGGAPRGVMQHHGAILCNvagaAEIL 218
Cdd:PRK07529 170 LPGPKRLAVPLIRRKAharILDFDAELARQPGDRLFSGrpIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN----AWLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 219 IEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGL----EKLASN----IEETRPTIMVVVPRLFEVLrtr 290
Cdd:PRK07529 246 ALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQgyrgPGVIANfwkiVERYRINFLSGVPTVYAAL--- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 291 imkqvqkqgglaeklmnTALEVGERRAagkpkfgDGLRDALvgrllkpkirqrfggrikamvSGGAPLNPEVGIFFES-M 369
Cdd:PRK07529 323 -----------------LQVPVDGHDI-------SSLRYAL---------------------CGAAPLPVEVFRRFEAaT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 370 GLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIA---------------EDGEILVRGELVMQGYwhNEAE 434
Cdd:PRK07529 358 GVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVilddagrylrdcavdEVGVLCIAGPNVFSGY--LEAA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 435 TERTI--KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY-------IV 505
Cdd:PRK07529 436 HNKGLwlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRG-GHNIDPAAIEEALLRHPAVALAAAVGRPDAHagelpvaYV 514
|
570 580
....*....|....*....|.
gi 2786869514 506 GLiVPDAEWT----LEWCREQ 522
Cdd:PRK07529 515 QL-KPGASATeaelLAFARDH 534
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
39-539 |
7.09e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 120.90 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 39 ISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITV---PTYitnTERDHAHILDNSGAKAVI 115
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLY---TPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 VsTEKLLRPLHGALQASGIAdHVI--GIDDLHRQQSS--GFLFHRWDSM-----------FAGDAAEARQAVEQRIAgIG 180
Cdd:PRK07059 126 V-LENFATTVQQVLAKTAVK-HVVvaSMGDLLGFKGHivNFVVRRVKKMvpawslpghvrFNDALAEGARQTFKPVK-LG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 181 RGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDFGIADDERFLSF---LPLSHAYEHTGGQFLPISVGAQ-- 255
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPDQLNFvcaLPLYHIFALTVCGLLGMRTGGRni 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 256 -IYYAEGLEKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklMNTalevgerraagkPKFGdglrdalvgR 334
Cdd:PRK07059 283 lIPNPRDIPGFIKELKKYQVHIFPAVNTLYNAL------------------LNN------------PDFD---------K 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 335 LLKPKIRQRFGGrikamvsGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAA-------GIAMHSVGPAMR-- 405
Cdd:PRK07059 324 LDFSKLIVANGG-------GMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDAtefsgtiGLPLPSTEVSIRdd 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 406 -GVDIRIAEDGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEG 483
Cdd:PRK07059 397 dGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILV-SGFNVYPNEIEE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 484 MLTLQPEIGQAMVAGDKKPY---IVGLIV----PD--AEWTLEWCREQGKQFdckKVQELPEFRN 539
Cdd:PRK07059 476 VVASHPGVLEVAAVGVPDEHsgeAVKLFVvkkdPAltEEDVKAFCKERLTNY---KRPKFVEFRT 537
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
40-514 |
8.93e-29 |
|
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: 120.43 E-value: 8.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 40 SWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCI--TV-----PTYItnterdhAHILDNSGAK 112
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlhTInprlfPEQI-------AYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 113 AVIV--STEKLLRPLHGALQAsgIADHVIGIDDLHRQQSSGFLFHRWDSMFAGDAAEARQAVeqriagIGRGDTACIIYT 190
Cdd:cd12119 100 VVFVdrDFLPLLEAIAPRLPT--VEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPD------FDENTAAAICYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 191 SGTGGAPRGVMQHHGAIlcnVAGAAEILIED-FGIADDERFLSFLPLSHAyeHTGGqfLPIS---VGA-QIY---YAEGl 262
Cdd:cd12119 172 SGTTGNPKGVVYSHRSL---VLHAMAALLTDgLGLSESDVVLPVVPMFHV--NAWG--LPYAaamVGAkLVLpgpYLDP- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 EKLASNIEETRPTImvvvprlfevlrtrimkqvqkqgglaeklmntalevgerrAAGKPKFGDGLRDALvgrllKPKIRQ 342
Cdd:cd12119 244 ASLAELIEREGVTF----------------------------------------AAGVPTVWQGLLDHL-----EANGRD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 343 RFGGRikAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSV----------GPAMRGVDIRIA 412
Cdd:cd12119 279 LSSLR--RVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPGVELRIV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 413 ED------------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvndK--GDNVAP 478
Cdd:cd12119 357 DDdgrelpwdgkavGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVI---KsgGEWISS 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 2786869514 479 QKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:cd12119 434 VELENAIMAHPAVAEAAVIG----------VPHPKW 459
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
10-547 |
1.32e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 119.99 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 10 NLVELFLKRAAEKGDLPFLGARIggswqTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCI 89
Cdd:PRK05852 20 DLVEVAATRLPEAPALVVTADRI-----AISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 90 TVPTYITNTERDHAHILDNSGAKAVIVSTEKLLRPLHGALQASGIADHVIGIDDlhrQQSSGFLFHRwdsmfaGDAAE-- 167
Cdd:PRK05852 95 VVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSG---PSGGTLSVHL------DAATEpt 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 168 ARQAVEQRIagigRGDTACIIYTSGTGGAPRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPLSHAYE------ 241
Cdd:PRK05852 166 PATSTPEGL----RPDDAMIMFTGGTTGLPKMVPWTHA----NIASSVRAIITGYRLSPRDATVAVMPLYHGHGliaall 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 242 ---HTGGQFLPISVG---AQIYYAEgleklasnIEETRPTIMVVVPRLFEVLRTRimkqvqkqgglaeklmntALEVGER 315
Cdd:PRK05852 238 atlASGGAVLLPARGrfsAHTFWDD--------IKAVGATWYTAVPTIHQILLER------------------AATEPSG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 316 RAAGKPKFgdglrdalvgrllkpkIRqrfggrikamvSGGAPLNPEVGIFFE-SMGLTMLQGYGQTEAGPVISCNRPAAG 394
Cdd:PRK05852 292 RKPAALRF----------------IR-----------SCSAPLTAETAQALQtEFAAPVVCAFGMTEATHQVTTTQIEGI 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 395 IAMH----SVGPAMR--GVDIRI----------AEDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRI 458
Cdd:PRK05852 345 GQTEnpvvSTGLVGRstGAQIRIvgsdglplpaGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 459 VITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGD-KKPY---IVGLIVP------DAEWTLEWCREQGKQFDC 528
Cdd:PRK05852 425 SIRGRIKELI-NRGGEKISPERVEGVLASHPNVMEAAVFGVpDQLYgeaVAAVIVPresappTAEELVQFCRERLAAFEI 503
|
570 580
....*....|....*....|
gi 2786869514 529 -KKVQELPEFRNAVRAAVDR 547
Cdd:PRK05852 504 pASFQEASGLPHTAKGSLDR 523
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
39-514 |
2.08e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 118.76 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 39 ISWNEAA--EQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPT--YITNTERDhahildnsgakAV 114
Cdd:PRK09088 21 RRWTYAEldALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwRLSASELD-----------AL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 115 IVSTEKLLRpLHGALQASGIADhVIGIDDLHrqqssgflfhrwDSMFAGDAAEARQAVEQRIAgigrgdtaCIIYTSGTG 194
Cdd:PRK09088 90 LQDAEPRLL-LGDDAVAAGRTD-VEDLAAFI------------ASADALEPADTPSIPPERVS--------LILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 195 GAPRGVM-----QHHGAILCNVAGAAEiliedfgiaDDERFLSFLPLSHAyehtggqflpisVGaqiyyaeglekLASNI 269
Cdd:PRK09088 148 GQPKGVMlsernLQQTAHNFGVLGRVD---------AHSSFLCDAPMFHI------------IG-----------LITSV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 270 eetRPTIM----VVVPRLFEVLRTrimkqvqkqgglAEKLMNTALevGERRAAGKPKFGDGLRDalvgrllKPKIRQRFG 345
Cdd:PRK09088 196 ---RPVLAvggsILVSNGFEPKRT------------LGRLGDPAL--GITHYFCVPQMAQAFRA-------QPGFDAAAL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 346 GRIKAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPV---------ISCNRPAAGIAMHSVGPAM---RGVDIRIAE 413
Cdd:PRK09088 252 RHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVfgmsvdcdvIRAKAGAAGIPTPTVQTRVvddQGNDCPAGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 414 DGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIG 492
Cdd:PRK09088 332 PGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISG-GENVYPAEIEAVLADHPGIR 410
|
490 500
....*....|....*....|..
gi 2786869514 493 QAMVAGdkkpyivgliVPDAEW 514
Cdd:PRK09088 411 ECAVVG----------MADAQW 422
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
15-514 |
2.61e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 118.99 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 15 FLKRAAEKgdlpfLGARIGGSW--QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP 92
Cdd:PRK07470 12 FLRQAARR-----FPDRIALVWgdRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 93 TYITNTERDHAHILDNSGAKAVIVSTEkllRPLHGAL--QASGIADHVIGIDDlhrqqssGFLFHRWDSMFAG--DAAEA 168
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHAD---FPEHAAAvrAASPDLTHVVAIGG-------ARAGLDYEALVARhlGARVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 169 RQAVEQriagigrgDTAC-IIYTSGTGGAPRGVMQHHGAI-------LCNVAGaaeiliedfGIADDERFLSFLPLSH-A 239
Cdd:PRK07470 157 NAAVDH--------DDPCwFFFTSGTTGRPKAAVLTHGQMafvitnhLADLMP---------GTTEQDASLVVAPLSHgA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 240 YEHtggQFLPISVGAQ--IYYAEGLE-----KLasnIEETRPTIMVVVPRLFevlrtrimkqvqkqgglaeKLMNTALEV 312
Cdd:PRK07470 220 GIH---QLCQVARGAAtvLLPSERFDpaevwAL---VERHRVTNLFTVPTIL-------------------KMLVEHPAV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 313 GERRA--------AGKPKFGDGLRDALvgRLLKPKIRQRFGgriKAMVSGGaplnpevgiffesmgLTMLQGYGQT-EAG 383
Cdd:PRK07470 275 DRYDHsslryviyAGAPMYRADQKRAL--AKLGKVLVQYFG---LGEVTGN---------------ITVLPPALHDaEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 384 P---VISCNRPAAGIAMhSVGPAmRGVDIRIAEDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVI 460
Cdd:PRK07470 335 PdarIGTCGFERTGMEV-QIQDD-EGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYI 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 461 TDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:PRK07470 413 TGRASDMYISG-GSNVYPREIEEKLLTHPAVSEVAVLG----------VPDPVW 455
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
37-522 |
3.15e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 118.99 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVI- 115
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLa 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 ----------VSTEKLLRP-LHGALQASGIADHVIGIDDLH---RQQSSGflfhrWDSMFAGDAAeARQAVEQRIAGIGr 181
Cdd:PRK06178 137 ldqlapvveqVRAETSLRHvIVTSLADVLPAEPTLPLPDSLrapRLAAAG-----AIDLLPALRA-CTAPVPLPPPALD- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 182 gDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEdfgIADDERFLSFLPLSH-AYEHTGGQFlPISVGAQI---- 256
Cdd:PRK06178 210 -ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVV---GGEDSVFLSFLPEFWiAGENFGLLF-PLFSGATLvlla 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 257 -YYAEGLeklASNIEETRPTIMVVvprlfevlrtrimkqvqkqgglaekLMNTALEVGERraagkPKFGD----GLRDAL 331
Cdd:PRK06178 285 rWDAVAF---MAAVERYRVTRTVM-------------------------LVDNAVELMDH-----PRFAEydlsSLRQVR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 332 VG---RLLKPKIRQRFGgrikamvsggaplnpevgiffESMGLTMLQG-YGQTEAGpviSCNRPAAGIA-----MHS--- 399
Cdd:PRK06178 332 VVsfvKKLNPDYRQRWR---------------------ALTGSVLAEAaWGMTETH---TCDTFTAGFQdddfdLLSqpv 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 400 -VGPAMRGVDIRI-----------AEDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDM 467
Cdd:PRK06178 388 fVGLPVPGTEFKIcdfetgellplGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEM 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 468 I-VNdkGDNVAPQKVEGMLTLQPEIGQAMVAG----DKKPYIVGLIVPDAEWTL------EWCREQ 522
Cdd:PRK06178 468 LkVN--GMSVFPSEVEALLGQHPAVLGSAVVGrpdpDKGQVPVAFVQLKPGADLtaaalqAWCREN 531
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-583 |
3.89e-28 |
|
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: 117.53 E-value: 3.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 51 LAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVstekllrplhgalq 130
Cdd:cd05971 19 FANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 131 asgiadhvigiddlhrqqssgflfhrwdsmfagDAAEarqaveqriagigrgDTACIIYTSGTGGAPRGVMQHHGAILCN 210
Cdd:cd05971 85 ---------------------------------DGSD---------------DPALIIYTSGTTGPPKGALHAHRVLLGH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 211 VAGAaEILIEDFGIADDerfLSFLPLSHAYehTGGQF---LPISvgaqiYYaeGLEKLASNieetrptimvvvPRLFEVl 287
Cdd:cd05971 117 LPGV-QFPFNLFPRDGD---LYWTPADWAW--IGGLLdvlLPSL-----YF--GVPVLAHR------------MTKFDP- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 288 rTRIMKQVQKQGGLAEKLMNTALEVgeRRAAGKPkfgdglrdalvgrllkpkiRQRFGGRIKAMVSGGAPLNPE-VGIFF 366
Cdd:cd05971 171 -KAALDLMSRYGVTTAFLPPTALKM--MRQQGEQ-------------------LKHAQVKLRAIATGGESLGEElLGWAR 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 367 ESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIAED-GEILVRGE-----------LVMQGYWHNEAE 434
Cdd:cd05971 229 EQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDnGTPLPPGEvgeiavelpdpVAFLGYWNNPSA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 435 TERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:cd05971 309 TEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVI-TSSGYRIGPAEIEECLLKHPAVLMAAVVG----------IPDPIR 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 515 TlewcrEQGKQFDCKKVQELP------EFRNAVRAAvdrvnkdLSVVEKVRQFAFADE-PftieneeMTPSMKIRR 583
Cdd:cd05971 378 G-----EIVKAFVVLNPGETPsdalarEIQELVKTR-------LAAHEYPREIEFVNElP-------RTATGKIRR 434
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-535 |
4.03e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 118.26 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGC--ITVPTYITNTERdhAHILDNSG 110
Cdd:PRK13391 19 ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLyyTCVNSHLTPAEA--AYIVDDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 111 AKAVIVSTEKllrplhgALQASGIADHVIGIddLHRqqssgFLFHRWDSM--FAGDAAEARQAVEQRIAGIGRGDTacII 188
Cdd:PRK13391 97 ARALITSAAK-------LDVARALLKQCPGV--RHR-----LVLDGDGELegFVGYAEAVAGLPATPIADESLGTD--ML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 189 YTSGTGGAPRGVMQH--HGAILCNVaGAAEILIEDFGIADDERFLSFLPLSHAyehtGGQF---LPISVGAQIYYAEGL- 262
Cdd:PRK13391 161 YSSGTTGRPKGIKRPlpEQPPDTPL-PLTAFLQRLWGFRSDMVYLSPAPLYHS----APQRavmLVIRLGGTVIVMEHFd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 -EKLASNIEETRPTIMVVVPRLFevlrTRIMKqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrlLKPKIR 341
Cdd:PRK13391 236 aEQYLALIEEYGVTHTQLVPTMF----SRMLK------------------------------------------LPEEVR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 342 QRFG-GRIKAMVSGGAPLNPEVGiffESM----GLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGvDIRIAED-- 414
Cdd:PRK13391 270 DKYDlSSLEVAIHAAAPCPPQVK---EQMidwwGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDdg 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 --------GEILVRGELVMQgYWHNEAETE--RTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGM 484
Cdd:PRK13391 346 aelppgepGTIWFEGGRPFE-YLNDPAKTAeaRHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISG-GVNIYPQEAENL 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786869514 485 LTLQPEIGQAMVAG----DKKPYIVGLIVPD---------AEWTLEWCREQGKQFDCKK----VQELP 535
Cdd:PRK13391 424 LITHPKVADAAVFGvpneDLGEEVKAVVQPVdgvdpgpalAAELIAFCRQRLSRQKCPRsidfEDELP 491
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
4-540 |
4.08e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 118.25 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 4 DIDSANNLVELFLKRAAEKGDLPFLGAR-IGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEW--CIAD 80
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVYGHKTALIFEsSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFifCWFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 81 LAIMasGCITVPTYITNTERDHAHILDNSGAKAVIVSTEKLlrPLHGALQASGIA--DHVIgIDDLHRQQSSGFlfHRWD 158
Cdd:PRK08008 82 LAKI--GAIMVPINARLLREESAWILQNSQASLLVTSAQFY--PMYRQIQQEDATplRHIC-LTRVALPADDGV--SSFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 159 SMFAGDAAEARQAVEqriagIGRGDTACIIYTSGTGGAPRGVMQHHgailCNVAGAAEILIEDFGIADDERFLSFLPLSH 238
Cdd:PRK08008 155 QLKAQQPATLCYAPP-----LSTDDTAEILFTSGTTSRPKGVVITH----YNLRFAGYYSAWQCALRDDDVYLTVMPAFH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 239 AYEHTGGQFLPISVGAQIYYaegLEKLA-----SNIEETRPTIMVVVPRLfevLRTRIMKQVQ---KQGGLAEKLMNTAL 310
Cdd:PRK08008 226 IDCQCTAAMAAFSAGATFVL---LEKYSarafwGQVCKYRATITECIPMM---IRTLMVQPPSandRQHCLREVMFYLNL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 311 EVGERRAagkpkfgdglrdalvgrllkpkIRQRFGGRikamvsggaplnpevgiffesmgltMLQGYGQTEAGPVISCNR 390
Cdd:PRK08008 300 SDQEKDA----------------------FEERFGVR-------------------------LLTSYGMTETIVGIIGDR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 391 PAAGIAMHSVGPAMRGVDIRIAED----------GEILVRGE---LVMQGYWHNEAETERTIK-DGWLHTGDIGHVDDKG 456
Cdd:PRK08008 333 PGDKRRWPSIGRPGFCYEAEIRDDhnrplpageiGEICIKGVpgkTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEG 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 457 RIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY----IVGLIVPDA------EWTLEWCREQGKQF 526
Cdd:PRK08008 413 FFYFVDRRCNMI-KRGGENVSCVELENIIATHPKIQDIVVVGIKDSIrdeaIKAFVVLNEgetlseEEFFAFCEQNMAKF 491
|
570
....*....|....
gi 2786869514 527 dckKVQELPEFRNA 540
Cdd:PRK08008 492 ---KVPSYLEIRKD 502
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
15-544 |
6.98e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 117.74 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 15 FLKRAAE-KGDLPflgARIGGSwQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCI--TV 91
Cdd:PRK08162 23 FLERAAEvYPDRP---AVIHGD-RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVlnTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 92 ptyitNTERDH---AHILDNSGAKAVIVSTEkLLRPLHGALQASGiADHVIGIDDLHRQQSSGFLFHRWDS---MFAGDA 165
Cdd:PRK08162 99 -----NTRLDAasiAFMLRHGEAKVLIVDTE-FAEVAREALALLP-GPKPLVIDVDDPEYPGGRFIGALDYeafLASGDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 166 AEARQAVE---QRIAgigrgdtacIIYTSGTGGAPRGVMQHH-GAILCNVAGAAEiliedFGIADDERFLSFLPLSHAye 241
Cdd:PRK08162 172 DFAWTLPAdewDAIA---------LNYTSGTTGNPKGVVYHHrGAYLNALSNILA-----WGMPKHPVYLWTLPMFHC-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 242 htGGQFLPISVGAQIYYAEGLEKlasnieetrptimvVVPRL-FEVLRTrimKQVQKQGGlAEKLMNTalevgerraagk 320
Cdd:PRK08162 236 --NGWCFPWTVAARAGTNVCLRK--------------VDPKLiFDLIRE---HGVTHYCG-APIVLSA------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 321 pkfgdgLRDAlvgrllKPKIRQRFGGRIKAMVSGGAPlnPEVGIF-FESMGLTMLQGYGQTEA-GPVISC-------NRP 391
Cdd:PRK08162 284 ------LINA------PAEWRAGIDHPVHAMVAGAAP--PAAVIAkMEEIGFDLTHVYGLTETyGPATVCawqpewdALP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 392 AA---------GIAMHSVGpAMRGVDIRIAED--------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDD 454
Cdd:PRK08162 350 LDeraqlkarqGVRYPLQE-GVTVLDPDTMQPvpadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHP 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 455 KGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW-------------------- 514
Cdd:PRK08162 429 DGYIKIKDRSKDIIISG-GENISSIEVEDVLYRHPAVLVAAVVA----------KPDPKWgevpcafvelkdgasateee 497
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2786869514 515 TLEWCREQGKQFDCKKV---QELP----------EFRNAVRAA 544
Cdd:PRK08162 498 IIAHCREHLAGFKVPKAvvfGELPktstgkiqkfVLREQAKSL 540
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
33-498 |
1.58e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 116.77 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQvclLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAK 112
Cdd:PRK06087 47 GASYTYSALDHAASR---LANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 113 AVIVST-------EKLLRPLHGALQAsgiADHVIGIDDLHRQQSSGFLFHRWDSMFAGDAAearqaveqriAGIGRGDTA 185
Cdd:PRK06087 124 MFFAPTlfkqtrpVDLILPLQNQLPQ---LQQIVGVDKLAPATSSLSLSQIIADYEPLTTA----------ITTHGDELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 186 CIIYTSGTGGAPRGVMQHHGAILcnvagAAE-ILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGA-----QIYYA 259
Cdd:PRK06087 191 AVLFTSGTEGLPKGVMLTHNNIL-----ASErAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGArsvllDIFTP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 260 EGLEKLasnIEETRPTIMV-VVPRLFEVLrtrimKQVQKQGGLAEKLmntalevgerraagkpkfgdglrdalvgrllkp 338
Cdd:PRK06087 266 DACLAL---LEQQRCTCMLgATPFIYDLL-----NLLEKQPADLSAL--------------------------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 339 kirqRFggrikaMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNrPAAGIA--MHSVGPAMRGVDIRIAED-- 414
Cdd:PRK06087 305 ----RF------FLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVN-LDDPLSrfMHTDGYAAAGVEIKVVDEar 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 --------GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGML 485
Cdd:PRK06087 374 ktlppgceGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRG-GENISSREVEDIL 452
|
490
....*....|...
gi 2786869514 486 TLQPEIGQAMVAG 498
Cdd:PRK06087 453 LQHPKIHDACVVA 465
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
6-600 |
2.38e-27 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 116.90 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 6 DSANNLVELFLKRAAEKGDLPFLGARI-GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIM 84
Cdd:PRK08180 36 DYPRRLTDRLVHWAQEAPDRVFLAERGaDGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 85 ASG---CITVPTYITnTERDHA---HILDNSGAKAVIVSTEKLLRPlhgALQASGIAD-HVIGIddlhRQQSSGFLFHRW 157
Cdd:PRK08180 116 YAGvpyAPVSPAYSL-VSQDFGklrHVLELLTPGLVFADDGAAFAR---ALAAVVPADvEVVAV----RGAVPGRAATPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 158 DSMFagdAAEARQAVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGaILCNVAGAAEILIEDFGIaDDERFLSFLPLS 237
Cdd:PRK08180 188 AALL---ATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHR-MLCANQQMLAQTFPFLAE-EPPVLVDWLPWN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 238 HAYehtGGQF---LPISVGAQIYYAEG------LEKLASNIEETRPTIMVVVPRLFEVLRtrimkqvqkqgglaeklmnT 308
Cdd:PRK08180 263 HTF---GGNHnlgIVLYNGGTLYIDDGkptpggFDETLRNLREISPTVYFNVPKGWEMLV-------------------P 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 309 ALEvgerraagkpkfgdglRDalvgrllkPKIRQRFGGRIKAMVSGGAPLNP-------EVGIffESMG--LTMLQGYGQ 379
Cdd:PRK08180 321 ALE----------------RD--------AALRRRFFSRLKLLFYAGAALSQdvwdrldRVAE--ATCGerIRMMTGLGM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 380 TEAGPV-ISCNRPAAGIAMhsVGPAMRGVDIRIAEDG---EILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDD 454
Cdd:PRK08180 375 TETAPSaTFTTGPLSRAGN--IGLPAPGCEVKLVPVGgklEVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGDAVRFVD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 455 ----------KGRIViTDRKkdmIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPYIVGLIVPDaewtLEWCRE--- 521
Cdd:PRK08180 453 padperglmfDGRIA-EDFK---LSSGTWVSVGPLRARAVSAGAPLVQDVVITGHDRDEIGLLVFPN----LDACRRlag 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 522 QGKQFDCKKVQELPEFRNAVRAAVDRVNKDLS-VVEKVRQFAFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYRG 600
Cdd:PRK08180 525 LLADASLAEVLAHPAVRAAFRERLARLNAQATgSSTRVARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVEALYAD 604
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
40-509 |
5.72e-27 |
|
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: 114.14 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 40 SWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKaVIVSTE 119
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAK-VLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 120 KLLRplhgalqasgiadhvigiddlHRQQSSGFLFHrwdsmfagdaaearqaveqriagigrgdtaciiYTSGTGGAPRG 199
Cdd:cd05969 81 ELYE---------------------RTDPEDPTLLH---------------------------------YTSGTTGTPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 200 VMQHHGAILCNVAGAAEIliedFGIADDERFLsflplshayeHTG----------GQFLPISVGAQIYYAEG---LEKLA 266
Cdd:cd05969 107 VLHVHDAMIFYYFTGKYV----LDLHPDDIYW----------CTAdpgwvtgtvyGIWAPWLNGVTNVVYEGrfdAESWY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 267 SNIEETRPTIMVVVPRLFevlrtRIMKqvqkqgglaeklmntalevgerraagkpKFGDGLrdalvgrllkpkIRQRFGG 346
Cdd:cd05969 173 GIIERVKVTVWYTAPTAI-----RMLM----------------------------KEGDEL------------ARKYDLS 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 347 RIKAMVSGGAPLNPEVGIF-FESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGV----------DIRIAEDG 415
Cdd:cd05969 208 SLRFIHSVGEPLNPEAIRWgMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVkaavvdengnELPPGTKG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 416 EILVRGEL--VMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQ 493
Cdd:cd05969 288 ILALKPGWpsMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDII-KTSGHRVGPFEVESALMEHPAVAE 366
|
490
....*....|....*.
gi 2786869514 494 AMVAGDKKPyIVGLIV 509
Cdd:cd05969 367 AGVIGKPDP-LRGEII 381
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
4-498 |
9.85e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 114.53 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 4 DIDSANNLVELF---LKRAAEKGDLPFLGAriggswqTISWNEAAEQVCLLAENLRA-LGLRDGDRVCLVSENRPEWCIA 79
Cdd:PRK12492 19 DLAAYKSVVEVFersCKKFADRPAFSNLGV-------TLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 80 DLAIMASGCITVPTYITNTERDHAHILDNSGAKAVI-----------------------VSTEKLLRPLHGALqASGIAD 136
Cdd:PRK12492 92 VFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVylnmfgklvqevlpdtgieylieAKMGDLLPAAKGWL-VNTVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 137 HVIG-IDDLHRQQSSGFlfhrwdsmfagdAAEARQAVEQRIAGIGRG--DTACIIYTSGTGGAPRGVMQHHGAILCNVAG 213
Cdd:PRK12492 171 KVKKmVPAYHLPQAVPF------------KQALRQGRGLSLKPVPVGldDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 214 A----------AEILIEDfgiaDDERFLSFLPLSHAYEHTGGQFLPISVGAQiyyaegleklasnieetrpTIMVVVPRl 283
Cdd:PRK12492 239 VraclsqlgpdGQPLMKE----GQEVMIAPLPLYHIYAFTANCMCMMVSGNH-------------------NVLITNPR- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 284 fevlrtrimkqvqKQGGLAEKLmntalevgerraaGKPKFGD--GLRDALVGRLLKPKIRQRFGGRIKAMVSGGAPLNPE 361
Cdd:PRK12492 295 -------------DIPGFIKEL-------------GKWRFSAllGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 362 VGIFFESM-GLTMLQGYGQTEAGPVISCNR------------PAAGIAMHSVGPAmrGVDIRIAEDGEILVRGELVMQGY 428
Cdd:PRK12492 349 TAERWEQLtGCTIVEGYGLTETSPVASTNPygelarlgtvgiPVPGTALKVIDDD--GNELPLGERGELCIKGPQVMKGY 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 429 WHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAG 498
Cdd:PRK12492 427 WQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIV-SGFNVYPNEIEDVVMAHPKVANCAAIG 496
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
10-599 |
2.83e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 113.60 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 10 NLVELFLKRAAEKGDLPFLGARIG--GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG 87
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 88 CITVP---TYITNTErDHA---HILDNSGAKAVIVStekllrplHGALQASGIadHVIGIDDLHRQQSSGFLFHRWDSMF 161
Cdd:PRK12582 130 VPAAPvspAYSLMSH-DHAklkHLFDLVKPRVVFAQ--------SGAPFARAL--AALDLLDVTVVHVTGPGEGIASIAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 162 AGDAAEA-RQAVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDfgiADDE--RFLSFLPLSH 238
Cdd:PRK12582 199 ADLAATPpTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPRE---PDPPppVSLDWMPWNH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 239 AYehtGGQ--FLPISVGAQIYY-------AEGLEKLASNIEETRPTIMVVVPRLFevlrtrimkqvqkqGGLAEklmntA 309
Cdd:PRK12582 276 TM---GGNanFNGLLWGGGTLYiddgkplPGMFEETIRNLREISPTVYGNVPAGY--------------AMLAE-----A 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 310 LEvgerraagkpkfgdglRDalvgrllkPKIRQRFGGRIKAMVSGGAPLNPEVgifFESMG----------LTMLQGYGQ 379
Cdd:PRK12582 334 ME----------------KD--------DALRRSFFKNLRLMAYGGATLSDDL---YERMQalavrttghrIPFYTGYGA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 380 TEAGPvISCNRPAAGIAMHSVGPAMRGVDIRIAEDG---EILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGH-VDD 454
Cdd:PRK12582 387 TETAP-TTTGTHWDTERVGLIGLPLPGVELKLAPVGdkyEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARfVDP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 455 K---------GRIViTDRKKDmivNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPYIVGLIVPDaewtLEWCREQGKQ 525
Cdd:PRK12582 466 DdpekglifdGRVA-EDFKLS---TGTWVSVGTLRPDAVAACSPVIHDAVVAGQDRAFIGLLAWPN----PAACRQLAGD 537
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786869514 526 FDCK--KVQELPEFRNAVRAAVDRVNKDL-SVVEKVRQFAFADEPFTIENEEMTPSMKIRRHKIKERYAERLDALYR 599
Cdd:PRK12582 538 PDAApeDVVKHPAVLAILREGLSAHNAEAgGSSSRIARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERLYA 614
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
33-588 |
3.09e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.84 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAK 112
Cdd:PRK13295 50 TGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 113 AVIVST-------EKLLRPLHGALQAsgiADHVIGIDdlhrqqssGFLFHRWDSMFAGDAAEARQAVEQRIAGI--GRGD 183
Cdd:PRK13295 130 VLVVPKtfrgfdhAAMARRLRPELPA---LRHVVVVG--------GDGADSFEALLITPAWEQEPDAPAILARLrpGPDD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 184 TACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILieDFGiADDERFLSFlPLSHayeHTG---GQFLPISVGAQIYYAE 260
Cdd:PRK13295 199 VTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL--GLG-ADDVILMAS-PMAH---QTGfmyGLMMPVMLGATAVLQD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 261 GLE--KLASNIEETRPTI-MVVVPRLFEVLRTrimkqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrllk 337
Cdd:PRK13295 272 IWDpaRAAELIRTEGVTFtMASTPFLTDLTRA------------------------------------------------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 338 PKIRQRFGGRIKAMVSGGAPLNPE-VGIFFESMGLTMLQGYGQTEAGPViSCNRPAAG--IAMHSVGPAMRGVDIRI--- 411
Cdd:PRK13295 304 VKESGRPVSSLRTFLCAGAPIPGAlVERARAALGAKIVSAWGMTENGAV-TLTKLDDPdeRASTTDGCPLPGVEVRVvda 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 -------AEDGEILVRGELVMQGYWHNEaETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGM 484
Cdd:PRK13295 383 dgaplpaGQIGRLQVRGCSNFGGYLKRP-QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRG-GENIPVVEIEAL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 485 LTLQPEIgqAMVAgdkkpyIVGliVPDAEWTLEWCR----EQGKQFDckkVQELPEFRNAVRAAVDRVNKDLSVVEKVRQ 560
Cdd:PRK13295 461 LYRHPAI--AQVA------IVA--YPDERLGERACAfvvpRPGQSLD---FEEMVEFLKAQKVAKQYIPERLVVRDALPR 527
|
570 580
....*....|....*....|....*...
gi 2786869514 561 fafadepftieneemTPSMKIRRHKIKE 588
Cdd:PRK13295 528 ---------------TPSGKIQKFRLRE 540
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
6-587 |
3.34e-25 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 109.93 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 6 DSANNLVELFLKRAAEKGDLPFLGARIGGSwqtISWNEAAEQVCLLAENL-RALGLRDGDRVCLVSENRPEWCIADLAIM 84
Cdd:PLN02574 37 DPNLDAVSFIFSHHNHNGDTALIDSSTGFS---ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 85 ASGCITVPTYITNTERDHAHILDNSGAKAVIVSTEKLlrplhGALQASGIAdhVIGIDDLHRQQSSGFLFHRWDSMFAGD 164
Cdd:PLN02574 114 SLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV-----EKLSPLGVP--VIGVPENYDFDSKRIEFPKFYELIKED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 165 AAEARQAVeqriagIGRGDTACIIYTSGTGGAPRGVMQHHGAIlcnvagaaeiliedfgIADDERFLSFLPLSHAYEHTG 244
Cdd:PLN02574 187 FDFVPKPV------IKQDDVAAIMYSSGTTGASKGVVLTHRNL----------------IAMVELFVRFEASQYEYPGSD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 245 GQFLPISVGAQIY----YAEGLEKLASNIeetrptimvVVPRLFEVlrtrimkqvqkqgglaeklmNTALEVGERRAAGK 320
Cdd:PLN02574 245 NVYLAALPMFHIYglslFVVGLLSLGSTI---------VVMRRFDA--------------------SDMVKVIDRFKVTH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 321 PKFGDGLRDALVgRLLKPKIRQRFGGrIKAMVSGGAPLNPE-VGIFFESMG-LTMLQGYGQTEAGPVISCNRPAAGIAMH 398
Cdd:PLN02574 296 FPVVPPILMALT-KKAKGVCGEVLKS-LKQVSCGAAPLSGKfIQDFVQTLPhVDFIQGYGMTESTAVGTRGFNTEKLSKY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 399 -SVG---PAMRG--VDIRIA------EDGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKK 465
Cdd:PLN02574 374 sSVGllaPNMQAkvVDWSTGcllppgNCGELWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYLYIVDRLK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 466 DmIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEwtlewCREQGKQFDCKKvqelPEFRNAVRAAV 545
Cdd:PLN02574 454 E-IIKYKGFQIAPADLEAVLISHPEIIDAAVTA----------VPDKE-----CGEIPVAFVVRR----QGSTLSQEAVI 513
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2786869514 546 DRVNKDLSVVEKVRQFAFadepftIENEEMTPSMKIRRHKIK 587
Cdd:PLN02574 514 NYVAKQVAPYKKVRKVVF------VQSIPKSPAGKILRRELK 549
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
37-509 |
1.27e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 108.04 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRA-LGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVI 115
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 VSTEkllrplHGALQASGIAD----HVI--GIDDL---HRQQSSGFLFHRWDSMFA----GDAAEARQAVEQ------RI 176
Cdd:PRK08751 129 VIDN------FGTTVQQVIADtpvkQVIttGLGDMlgfPKAALVNFVVKYVKKLVPeyriNGAIRFREALALgrkhsmPT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 177 AGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDFGIAD-DERFLSFLPLSHAYEHTGGQFLPISVGaq 255
Cdd:PRK08751 203 LQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEgCEVVITALPLYHIFALTANGLVFMKIG-- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 256 iyyaeGLEKLASNIEETRPTIMvvvprlfEVLRTRiMKQVQKQGGLAEKLMNTalevgerraagkpkfgdglrdalvgrl 335
Cdd:PRK08751 281 -----GCNHLISNPRDMPGFVK-------ELKKTR-FTAFTGVNTLFNGLLNT--------------------------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 336 lkPKIRQRFGGRIKAMVSGGAPLNPEVGIFFESM-GLTMLQGYGQTEAGPViSCNRP--------AAGIAMHSVGPAMR- 405
Cdd:PRK08751 321 --PGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVtGLTLVEAYGLTETSPA-ACINPltlkeyngSIGLPIPSTDACIKd 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 406 --GVDIRIAEDGEILVRGELVMQGYWHNEAETERTIK-DGWLHTGDIGHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVE 482
Cdd:PRK08751 398 daGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILV-SGFNVYPNEIE 476
|
490 500 510
....*....|....*....|....*....|
gi 2786869514 483 GMLTLQP---EIGQAMVAGDKKPYIVGLIV 509
Cdd:PRK08751 477 DVIAMMPgvlEVAAVGVPDEKSGEIVKVVI 506
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-521 |
1.35e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 105.64 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 182 GDTACIIYTSGTGGAPRGVMQHHGAILCNvagaAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQI----- 256
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVvlagp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 257 --YYAEGL-EKLASNIEETRPTIMVVVPRLFEVLRTRIMkqvqkqgglaeklmntalevgerraagkpkfgdglrDALVG 333
Cdd:cd05944 78 agYRNPGLfDNFWKLVERYRITSLSTVPTVYAALLQVPV------------------------------------NADIS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 334 RLlkpkirqrfggriKAMVSGGAPLNPEVGIFFE-SMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIA 412
Cdd:cd05944 122 SL-------------RFAMSGAAPLPVELRARFEdATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 413 ---------------EDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVA 477
Cdd:cd05944 189 vldgvgrllrdcapdEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRG-GHNID 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 478 PQKVEGMLTLQPEIGQAMVAGDKKPYIVGL------IVPDAEWT----LEWCRE 521
Cdd:cd05944 268 PALIEEALLRHPAVAFAGAVGQPDAHAGELpvayvqLKPGAVVEeeelLAWARD 321
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-513 |
2.43e-24 |
|
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: 106.59 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 12 VELFLKRAAEKGDLPflgARIGGSwQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITV 91
Cdd:cd17646 1 HALVAEQAARTPDAP---AVVDEG-RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 92 PTYITNTERDHAHILDNSGAKAVIVStekllRPLHGALQASGIADHVigiddlhrqqssgflfhrwdsmfaGDAAEARQA 171
Cdd:cd17646 77 PLDPGYPADRLAYMLADAGPAVVLTT-----ADLAARLPAGGDVALL------------------------GDEALAAPP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 172 VEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGaaeiLIEDFGIADDERFLSFLPLS---HAYEhtggQFL 248
Cdd:cd17646 128 ATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLW----MQDEYPLGPGDRVLQKTPLSfdvSVWE----LFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 249 PISVGAQIYYAE-GLEK----LASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaleVGERRAAGkpkf 323
Cdd:cd17646 200 PLVAGARLVVARpGGHRdpayLAALIREHGVTTCHFVPSMLRVF------------------------LAEPAAGS---- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 324 GDGLRdaLVgrllkpkirqrfggrikamVSGGAPLNPEVGI-FFESMGLTMLQGYGQTEA--------------GPVISC 388
Cdd:cd17646 252 CASLR--RV-------------------FCSGEALPPELAArFLALPGAELHNLYGPTEAaidvthwpvrgpaeTPSVPI 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 389 NRPAAGIAMHSVGPAMRGVDIRIAedGEILVRGELVMQGYWHNEAET-ERTIKDGWLH------TGDIGHVDDKGRIVIT 461
Cdd:cd17646 311 GRPVPNTRLYVLDDALRPVPVGVP--GELYLGGVQLARGYLGRPALTaERFVPDPFGPgsrmyrTGDLARWRPDGALEFL 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 462 DRkKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMV----AGDKKPYIVGLIVPDAE 513
Cdd:cd17646 389 GR-SDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVvaraAPAGAARLVGYVVPAAG 443
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
57-512 |
2.46e-24 |
|
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: 106.02 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 57 ALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSG-AKAVIVstekllrplhGALQASGia 135
Cdd:cd05958 30 ELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARiTVALCA----------HALTASD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 136 dhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTGGAPRGVMQHHGAILCNVAG-A 214
Cdd:cd05958 98 -----------------------------------------------DICILAFTSGTTGAPKATMHFHRDPLASADRyA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 215 AEILiedfGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGL--EKLASNIEETRPTIMVVVPrlfevlrtrim 292
Cdd:cd05958 131 VNVL----RLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEAtpDLLLSAIARYKPTVLFTAP----------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 293 kqvqkqgglaeklmntaleVGERRAAGKPKFGdglrdalvgrllkpkirQRFGGRIKAMVSGGAPLNPEV-GIFFESMGL 371
Cdd:cd05958 196 -------------------TAYRAMLAHPDAA-----------------GPDLSSLRKCVSAGEALPAALhRAWKEATGI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 372 TMLQGYGQTEAGPVISCNRPAAgIAMHSVGPAMRGVDIRIAED----------GEILVRGElvmQGYWHNEAETERT-IK 440
Cdd:cd05958 240 PIIDGIGSTEMFHIFISARPGD-ARPGATGKPVPGYEAKVVDDegnpvpdgtiGRLAVRGP---TGCRYLADKRQRTyVQ 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786869514 441 DGWLHTGDIGHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAGdkKPYIVGLIVPDA 512
Cdd:cd05958 316 GGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVLLQHPAVAECAVVG--HPDESRGVVVKA 384
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
15-560 |
3.17e-24 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 107.03 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 15 FLKRAAEKgdLPFLGARIGGSWQtISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTy 94
Cdd:PLN03102 19 FLKRASEC--YPNRTSIIYGKTR-FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 95 itNTERDH---AHILDNSGAKAVIV--STEKLLRPLHGALQA--SGIADHVIGIDDLHRQQSSGFLFHRWDSMF-AGDAA 166
Cdd:PLN03102 95 --NTRLDAtsiAAILRHAKPKILFVdrSFEPLAREVLHLLSSedSNLNLPVIFIHEIDFPKRPSSEELDYECLIqRGEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 167 EARQAVEQRIAGigRGDTACIIYTSGTGGAPRGV-MQHHGAILCNVAGaaeILIEDFGIAddERFLSFLPLSHAyehtGG 245
Cdd:PLN03102 173 PSLVARMFRIQD--EHDPISLNYTSGTTADPKGVvISHRGAYLSTLSA---IIGWEMGTC--PVYLWTLPMFHC----NG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 246 QFLPISVGAQ------IYYAEGLEkLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEvgerraag 319
Cdd:PLN03102 242 WTFTWGTAARggtsvcMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNIL----------------------LK-------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 320 kpkfGDGLRdalvgrlLKPKirqrfGGRIKAMVSGGAPlnPEVGIF-FESMGLTMLQGYGQTEA-GPVISC------NRP 391
Cdd:PLN03102 291 ----GNSLD-------LSPR-----SGPVHVLTGGSPP--PAALVKkVQRLGFQVMHAYGLTEAtGPVLFCewqdewNRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 392 AAGIAMH---SVGPAMRG---VDIRIAED-----------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDD 454
Cdd:PLN03102 353 PENQQMElkaRQGVSILGladVDVKNKETqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHP 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 455 KGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGDKKP--------YIV------------GLIVPDAEW 514
Cdd:PLN03102 433 DGHVEIKDRSKDIIISG-GENISSVEVENVLYKYPKVLETAVVAMPHPtwgetpcaFVVlekgettkedrvDKLVTRERD 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 515 TLEWCREQGKQFDC-KKV---QELP----------EFRNAVRAAVdrVNKDLSVVEKVRQ 560
Cdd:PLN03102 512 LIEYCRENLPHFMCpRKVvflQELPkngngkilkpKLRDIAKGLV--VEDEDNVIKKVHQ 569
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
16-469 |
3.93e-24 |
|
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: 106.60 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 16 LKRAAEKGDLPFLgARIG--GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPT 93
Cdd:cd05906 16 LLRAAERGPTKGI-TYIDadGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 94 --YITNTERDHA-----HILDNSGaKAVIVSTEKLLRPLHGALQASGI-ADHVIGIDDLHRqqssgflfhrwdsmfAGDA 165
Cdd:cd05906 95 tvPPTYDEPNARlrklrHIWQLLG-SPVVLTDAELVAEFAGLETLSGLpGIRVLSIEELLD---------------TAAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 166 AEARQAVEQriagigrgDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAaeilIEDFGIADDERFLSFLPLSHayehtgg 245
Cdd:cd05906 159 HDLPQSRPD--------DLALLMLTSGSTGFPKAVPLTHRNILARSAGK----IQHNGLTPQDVFLNWVPLDH------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 246 qflpisVGAQIYYaegleklasnieetrptimvvvpRLFEVLRTriMKQVQKQggLAEKLMNTA--LEVGERRAAGK--- 320
Cdd:cd05906 220 ------VGGLVEL-----------------------HLRAVYLG--CQQVHVP--TEEILADPLrwLDLIDRYRVTItwa 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 321 PKFGDglrdALVGRLLKPKIRQRFG-GRIKAMVSGGAPLNPEVGIFFESM----GL---TMLQGYGQTE--AGpVISCNR 390
Cdd:cd05906 267 PNFAF----ALLNDLLEEIEDGTWDlSSLRYLVNAGEAVVAKTIRRLLRLlepyGLppdAIRPAFGMTEtcSG-VIYSRS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 391 PAAGIAMH-----SVGPAMRGVDIRI----------AEDGEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDD 454
Cdd:cd05906 342 FPTYDHSQalefvSLGRPIPGVSMRIvddegqllpeGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLDN 421
|
490
....*....|....*
gi 2786869514 455 kGRIVITDRKKDMIV 469
Cdd:cd05906 422 -GNLTITGRTKDTII 435
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-517 |
7.14e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 101.84 E-value: 7.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP---TYitNTERdHAHILDNSGAKA 113
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPldpSY--PAER-LAYILEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVstekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagiGRGDTACIIYTSGT 193
Cdd:cd05930 88 VLT---------------------------------------------------------------DPDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 194 GGAPRGVMQHHGAILCNVAGaaeiLIEDFGIADDERFLSFLPLSHAYeHTGGQFLPISVGAQIYYAEG-----LEKLASN 268
Cdd:cd05930 105 TGKPKGVMVEHRGLVNLLLW----MQEAYPLTPGDRVLQFTSFSFDV-SVWEIFGALLAGATLVVLPEevrkdPEALADL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 269 IEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEVGERRAAGKpkfgdgLRDALVgrllkpkirqrfggri 348
Cdd:cd05930 180 LAEEGITVLHLTPSLLRLL----------------------LQELELAALPS------LRLVLV---------------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 349 kamvsGGAPLNPE-VGIFFESM-GLTMLQGYGQTEAGPVISCN---------------RPAAGIAMHSVGPAMRGVdiRI 411
Cdd:cd05930 216 -----GGEALPPDlVRRWRELLpGARLVNLYGPTEATVDATYYrvppddeedgrvpigRPIPNTRVYVLDENLRPV--PP 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 AEDGEILVRGELVMQGYWHNEAET-ERTIKD-----GWLH-TGDIGHVDDKGRIVITDRkKDMIVNDKGDNVAPQKVEGM 484
Cdd:cd05930 289 GVPGELYIGGAGLARGYLNRPELTaERFVPNpfgpgERMYrTGDLVRWLPDGNLEFLGR-IDDQVKIRGYRIELGEIEAA 367
|
490 500 510
....*....|....*....|....*....|....*..
gi 2786869514 485 LTLQPEIGQAMV----AGDKKPYIVGLIVPDAEWTLE 517
Cdd:cd05930 368 LLAHPGVREAAVvareDGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
46-497 |
7.17e-23 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 102.78 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 46 EQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP-----------TYITNTERdhahILDNSGAKAV 114
Cdd:PRK09192 57 ARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlplpmgfggreSYIAQLRG----MLASAQPAAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 115 IVSTEklLRPLhgalqasgIADHVIGIDDLHRqqssgflfhrwdsmFAGDAAEARQAVEQRIAGIGRGDTACIIYTSGTG 194
Cdd:PRK09192 133 ITPDE--LLPW--------VNEATHGNPLLHV--------------LSHAWFKALPEADVALPRPTPDDIAYLQYSSGST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 195 GAPRGVMQHHGAILCNVAGaaeILIEDFGIADDERFLSFLPLSHAYEHTGgqFLPISVGAQIyyaeGLEKLASN------ 268
Cdd:PRK09192 189 RFPRGVIITHRALMANLRA---ISHDGLKVRPGDRCVSWLPFYHDMGLVG--FLLTPVATQL----SVDYLPTRdfarrp 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 269 ------IEETRPTIMVVVPRLFEVLRTRIMKQvqkqgGLAEklmntaLEVGERRAAGkpkfgdglrdaLVGRLLKPKIRQ 342
Cdd:PRK09192 260 lqwldlISRNRGTISYSPPFGYELCARRVNSK-----DLAE------LDLSCWRVAG-----------IGADMIRPDVLH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 343 RFGGRI-------KAMV-SGG----------APLNPevGIFFESMGLTMLQGYGQTEAGPviscNRPAAGIAMHSVGPAM 404
Cdd:PRK09192 318 QFAEAFapagfddKAFMpSYGlaeatlavsfSPLGS--GIVVEEVDRDRLEYQGKAVAPG----AETRRVRTFVNCGKAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 405 RGVDIRIAED----------GEILVRGELVMQGYWHNEaETERTIK-DGWLHTGDIGHVDDkGRIVITDRKKDMI-VNdk 472
Cdd:PRK09192 392 PGHEIEIRNEagmplpervvGHICVRGPSLMSGYFRDE-ESQDVLAaDGWLDTGDLGYLLD-GYLYITGRAKDLIiIN-- 467
|
490 500
....*....|....*....|....*
gi 2786869514 473 GDNVAPQKVEGMLTLQPEIGQAMVA 497
Cdd:PRK09192 468 GRNIWPQDIEWIAEQEPELRSGDAA 492
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
39-514 |
1.01e-22 |
|
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: 101.82 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 39 ISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVST 118
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 119 ekllrplhGALQASGIADHVIGIDDLHRQQSSGFLFHrwdsmfAGDAAEARQAveqriagiGRGDTACIIYTSGTGGAPR 198
Cdd:cd05923 109 --------DAQVMDAIFQSGVRVLALSDLVGLGEPES------AGPLIEDPPR--------EPEQPAFVFYTSGTTGLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 199 GVMQHHGAILCNVAGAAEILIEDFGiaDDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLE--KLASNIEETRPTI 276
Cdd:cd05923 167 GAVIPQRAAESRVLFMSTQAGLRHG--RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDpaDALKLIEQERVTS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 277 MVVVPRLFEVLRTRIMKQVQKQGGLaEKLMNTalevgerraagkpkfGDGLRDALVGRL--LKPkirqrfggrikamvsg 354
Cdd:cd05923 245 LFATPTHLDALAAAAEFAGLKLSSL-RHVTFA---------------GATMPDAVLERVnqHLP---------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 355 gaplNPEVGIffesmgltmlqgYGQTEAGPVISCNRPAAGIAM----HS---VGPAMRGVDIRIA--EDGEILVR--GEL 423
Cdd:cd05923 293 ----GEKVNI------------YGTTEAMNSLYMRDARTGTEMrpgfFSevrIVRIGGSPDEALAngEEGELIVAaaADA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 424 VMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpy 503
Cdd:cd05923 357 AFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG----- 430
|
490
....*....|.
gi 2786869514 504 ivgliVPDAEW 514
Cdd:cd05923 431 -----VADERW 436
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
37-513 |
2.21e-22 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 100.40 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP-TYITNTERDHAhILDNSGAKAVI 115
Cdd:cd05945 15 RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPlDASSPAERIRE-ILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 VstekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfAGDaaearqaveqriagigrgDTACIIYTSGTGG 195
Cdd:cd05945 94 A---------------------------------------------DGD------------------DNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 196 APRGVMQHHGAILCNVAGAaeilIEDFGIADDERFLSFLPLS-----HAYEHT---GGQFLPISVGAQIYYAEglekLAS 267
Cdd:cd05945 111 RPKGVQISHDNLVSFTNWM----LSDFPLGPGDVFLNQAPFSfdlsvMDLYPAlasGATLVPVPRDATADPKQ----LFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 268 NIEETRPTIMVVVPRLFEVLRTRimkqvqkqGGLAEKLMNTALEV---GErraagkpkfgdglrdALVGRLLKpKIRQRF 344
Cdd:cd05945 183 FLAEHGITVWVSTPSFAAMCLLS--------PTFTPESLPSLRHFlfcGE---------------VLPHKTAR-ALQQRF 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 345 ggrikamvsggaplnPEVGIFfesmgltmlQGYGQTEAGPVISCNR----PAAGIAMHSVGPAMRGVDIRI--------- 411
Cdd:cd05945 239 ---------------PDARIY---------NTYGPTEATVAVTYIEvtpeVLDGYDRLPIGYAKPGAKLVIldedgrpvp 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 -AEDGEILVRGELVMQGYWHNEAETERTI----KDGWLHTGDIGHVDDKGRIVITDRKKDMI-VNdkGDNVAPQKVEGML 485
Cdd:cd05945 295 pGEKGELVISGPSVSKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVkLN--GYRIELEEIEAAL 372
|
490 500 510
....*....|....*....|....*....|..
gi 2786869514 486 TLQPEIGQAMV----AGDKKPYIVGLIVPDAE 513
Cdd:cd05945 373 RQVPGVKEAVVvpkyKGEKVTELIAFVVPKPG 404
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
11-458 |
3.30e-22 |
|
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: 101.86 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGDLPflgARIGGSwQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCIT 90
Cdd:COG1020 478 LHELFEAQAARTPDAV---AVVFGD-QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 91 VP---TYitNTERdHAHILDNSGAKAVIVSTEkllrpLHGALQASGIadHVIGIDDLhrqqssgflfhrwdsmfagdaAE 167
Cdd:COG1020 554 VPldpAY--PAER-LAYMLEDAGARLVLTQSA-----LAARLPELGV--PVLALDAL---------------------AL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 168 ARQAVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAeiliEDFGIADDERFLSFLPLSH---AYEhtg 244
Cdd:COG1020 603 AAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQ----RRYGLGPGDRVLQFASLSFdasVWE--- 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 245 gQFLPISVGAQIYYAE-----GLEKLASNIEETRPTIMVVVPRLFEVLRtrimkQVQKQGGLAEKLMNTAlevgerraag 319
Cdd:COG1020 676 -IFGALLSGATLVLAPpearrDPAALAELLARHRVTVLNLTPSLLRALL-----DAAPEALPSLRLVLVG---------- 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 320 kpkfGDGLRDALVGRLlkpkiRQRFGGRikamvsggaplnpevgiffesmglTMLQGYGQTEA---------------GP 384
Cdd:COG1020 740 ----GEALPPELVRRW-----RARLPGA------------------------RLVNLYGPTETtvdstyyevtppdadGG 786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 385 VISCNRPAAGIAMHSVGPAMRGVDIRIAedGEILVRGELVMQGYWHNEAET-ERTIKDGWLH-------TGDIGHVDDKG 456
Cdd:COG1020 787 SVPIGRPIANTRVYVLDAHLQPVPVGVP--GELYIGGAGLARGYLNRPELTaERFVADPFGFpgarlyrTGDLARWLPDG 864
|
..
gi 2786869514 457 RI 458
Cdd:COG1020 865 NL 866
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
183-465 |
3.72e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 101.58 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILieDFGIADdeRFLSFLPLSHAYEHTGGQFLPISVGAQIY-YAEG 261
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI--DFSPED--KVFNALPVFHSFGLTGGLVLPLLSGVKVFlYPSP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 262 LE-----KLasnIEETRPTIMVvvprlfevlrtrimkqvqkqgGLAEKLMNTAlevgerRAAGKPKFGdglrdalvgrll 336
Cdd:PRK06814 870 LHyriipEL---IYDTNATILF---------------------GTDTFLNGYA------RYAHPYDFR------------ 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 337 kpkirqrfggRIKAMVSGGAPLNPEV-GIFFESMGLTMLQGYGQTEAGPVISCNRPaagiaMH----SVGPAMRGVDIR- 410
Cdd:PRK06814 908 ----------SLRYVFAGAEKVKEETrQTWMEKFGIRILEGYGVTETAPVIALNTP-----MHnkagTVGRLLPGIEYRl 972
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786869514 411 -----IAEDGEILVRGELVMQGYWHneAETERTIK---DGWLHTGDIGHVDDKGRIVITDRKK 465
Cdd:PRK06814 973 epvpgIDEGGRLFVRGPNVMLGYLR--AENPGVLEppaDGWYDTGDIVTIDEEGFITIKGRAK 1033
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
37-513 |
8.45e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 98.93 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG--CITVPTYITNTERDHahILDNSGAKAV 114
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGlyITAINHHLTAPEADY--IVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 115 IVStekllrplhGALqaSGIADHVIGidDLHRQQSSGFLFHRWDSMFAGDAAEARQAVEQRIAgigrgdtACIIYTSGTG 194
Cdd:PRK13390 101 VAS---------AAL--DGLAAKVGA--DLPLRLSFGGEIDGFGSFEAALAGAGPRLTEQPCG-------AVMLYSSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 195 GAPRGV--------MQHHGAILCNVAGAAeiliedFGIADDERFLSFLPLSHAyehtggqfLPI-------SVGAQIYYA 259
Cdd:PRK13390 161 GFPKGIqpdlpgrdVDAPGDPIVAIARAF------YDISESDIYYSSAPIYHA--------APLrwcsmvhALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 260 EGLEKLAS--NIEETRPTIMVVVPRLFevlrTRIMKqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrlLK 337
Cdd:PRK13390 227 KRFDAQATlgHVERYRITVTQMVPTMF----VRLLK------------------------------------------LD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 338 PKIRQRFG-GRIKAMVSGGAPLNPEVG-IFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGvDIRIAED- 414
Cdd:PRK13390 261 ADVRTRYDvSSLRAVIHAAAPCPVDVKhAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDd 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 GEILVRGEL--------VMQGYWHNE----AETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVE 482
Cdd:PRK13390 340 GNELPAGRIgtvyferdRLPFRYLNDpektAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISG-GVNIYPQETE 418
|
490 500 510
....*....|....*....|....*....|.
gi 2786869514 483 GMLTLQPEIGQAMVAGdkkpyivgliVPDAE 513
Cdd:PRK13390 419 NALTMHPAVHDVAVIG----------VPDPE 439
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
5-556 |
1.00e-21 |
|
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: 99.49 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 5 IDSANNLVELFLKRAAEKGDLPFLGARigGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIM 84
Cdd:cd05968 60 MNIVEQLLDKWLADTRTRPALRWEGED--GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 85 ASGCITVPTYITNTERDHAHILDNSGAKAVIVS-----TEKLLRPLHGALQASGIA---DHVIgiddLHRQQSSGFLFHR 156
Cdd:cd05968 138 RIGGIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrRGREVNLKEEADKACAQCptvEKVV----VVRHLGNDFTPAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 157 WDSMFAGDAAEARQAveqRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAIlcNVAGAAEILIEdFGIADDERFLSFLPL 236
Cdd:cd05968 214 GRDLSYDEEKETAGD---GAERTESEDPLMIIYTSGTTGKPKGTVHVHAGF--PLKAAQDMYFQ-FDLKPGDLLTWFTDL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 237 SHAYehtgGQFL---PISVGAQIYYAEGL------EKLASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAeklmn 307
Cdd:cd05968 288 GWMM----GPWLifgGLILGATMVLYDGApdhpkaDRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSS----- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 308 talevgeRRAAGkpkfgdglrdalvgrllkpkirqrfggrikamvSGGAPLNPEVGI-FFESMG---LTMLQGYGQTEAG 383
Cdd:cd05968 359 -------LRVLG---------------------------------STGEPWNPEPWNwLFETVGkgrNPIINYSGGTEIS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 384 PVISCN---RPAAGIAMHSVGPAMRGVdiRIAEDGEILVR--GELVM--------QGYWHNEAETERT----IKDGWLHt 446
Cdd:cd05968 399 GGILGNvliKPIKPSSFNGPVPGMKAD--VLDESGKPARPevGELVLlapwpgmtRGFWRDEDRYLETywsrFDNVWVH- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 447 GDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY----IVGLIV--PDAEWTLEW-- 518
Cdd:cd05968 476 GDFAYYDEEGYFYILGRSDDTI-NVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVkgeaIVCFVVlkPGVTPTEALae 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 519 ------CREQGKQFDCKK---VQELPEFRNA------VRAA-VDRVNKDLSVVE 556
Cdd:cd05968 555 elmervADELGKPLSPERilfVKDLPKTRNAkvmrrvIRAAyLGKELGDLSSLE 608
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
39-584 |
1.35e-21 |
|
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: 97.59 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 39 ISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSt 118
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 119 ekllrplhgalqasgiadhvigIDDLHRQQSSGFLFhrwdsMFagdaaearqaveqriagigrgdtaciiyTSGTGGAPR 198
Cdd:cd05973 80 ----------------------AANRHKLDSDPFVM-----MF----------------------------TSGTTGLPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 199 GVMQHHGAILCNVAgaaeILIEDFGIADDERFLSFLPLSHAYehtggqflpisvgaQIYYAeglekLASNIEETRPTIMV 278
Cdd:cd05973 105 GVPVPLRALAAFGA----YLRDAVDLRPEDSFWNAADPGWAY--------------GLYYA-----ITGPLALGHPTILL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 279 VVPrlFEVLRT-RIMkqvqkqgglaEKLMNTALevgerraAGKPKFGDGLRDAlvgrllKPKIRQRFGGRIKAMVSGGAP 357
Cdd:cd05973 162 EGG--FSVESTwRVI----------ERLGVTNL-------AGSPTAYRLLMAA------GAEVPARPKGRLRRVSSAGEP 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 358 LNPEVGIFFES-MGLTMLQGYGQTEAGPVIsCNRPAAGIAMH--SVGPAMRGVDIRI-AEDGEILVRGE----------- 422
Cdd:cd05973 217 LTPEVIRWFDAaLGVPIHDHYGQTELGMVL-ANHHALEHPVHagSAGRAMPGWRVAVlDDDGDELGPGEpgrlaidians 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 423 --LVMQGYWHNEaetERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAGdk 500
Cdd:cd05973 296 plMWFRGYQLPD---TPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITM-SGYRIGPFDVESALIEHPAVAEAAVIG-- 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 501 kpyivgliVPDAEWTlewcrEQGKQFD--CKKVQELPEFRNAVRAavdRVNKDLSVVEKVRQFAFADE-PftieneeMTP 577
Cdd:cd05973 370 --------VPDPERT-----EVVKAFVvlRGGHEGTPALADELQL---HVKKRLSAHAYPRTIHFVDElP-------KTP 426
|
....*..
gi 2786869514 578 SMKIRRH 584
Cdd:cd05973 427 SGKIQRF 433
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
183-465 |
2.97e-21 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 98.24 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAgaaEI-LIEDFGIADdeRFLSFLPLSHAYEHTGGQFLPISVGAQIY-YAE 260
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKSLLANVE---QIkTIADFTPND--RFMSALPLFHSFGLTVGLFTPLLTGAEVFlYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 261 gleklasnieetrPTIMVVVPRLF-----EVLRtrimkqvqkqgGLAEKLMNTAlevgerRAAGKPKFGdglrdalvgrl 335
Cdd:PRK08043 441 -------------PLHYRIVPELVydrncTVLF-----------GTSTFLGNYA------RFANPYDFA----------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 336 lkpkirqrfggRIKAMVSGGAPLNPEVG-IFFESMGLTMLQGYGQTEAGPVISCNRPAAGiAMHSVGPAMRGVDIR---- 410
Cdd:PRK08043 480 -----------RLRYVVAGAEKLQESTKqLWQDKFGLRILEGYGVTECAPVVSINVPMAA-KPGTVGRILPGMDARllsv 547
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786869514 411 --IAEDGEILVRGELVMQGYWHNE---------AETERTIKD-GWLHTGDIGHVDDKGRIVITDRKK 465
Cdd:PRK08043 548 pgIEQGGRLQLKGPNIMNGYLRVEkpgvlevptAENARGEMErGWYDTGDIVRFDEQGFVQIQGRAK 614
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
37-516 |
3.20e-21 |
|
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: 96.98 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTyitntERDH-----AHILDNSGA 111
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL-----DPDYpadrlRYILEDAEP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 112 kAVIVSTEKLLRPLHGALQASGIAdhvigiddlhrqqssgflfhrwdsmfaGDAAEArqAVEQRIAGIGRGDTACIIYTS 191
Cdd:cd12116 86 -ALVLTDDALPDRLPAGLPVLLLA---------------------------LAAAAA--APAAPRTPVSPDDLAYVIYTS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 192 GTGGAPRGVMQHHGAILCNVAGaaeiLIEDFGIADDERFL---------SFLPLshayehtggqFLPISVGAQIYYAEG- 261
Cdd:cd12116 136 GSTGRPKGVVVSHRNLVNFLHS----MRERLGLGPGDRLLavttyafdiSLLEL----------LLPLLAGARVVIAPRe 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 262 ----LEKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEVGERRAAgkpkfgdGLRdALVgrllk 337
Cdd:cd12116 202 tqrdPEALARLIEAHSITVMQATPATWRML----------------------LDAGWQGRA-------GLT-ALC----- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 338 pkirqrfggrikamvsGGAPLNPEVGIFFESMGLTMLQGYGQTE------------AGPVISCNRPAAGIAMHSVGPAMR 405
Cdd:cd12116 247 ----------------GGEALPPDLAARLLSRVGSLWNLYGPTEttiwstaarvtaAAGPIPIGRPLANTQVYVLDAALR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 406 GVDIRIAedGEILVRGELVMQGYWHNEAET-ERTIKDGWLH-------TGDIGHVDDKGRIVITDRkKDMIVNDKGDNVA 477
Cdd:cd12116 311 PVPPGVP--GELYIGGDGVAQGYLGRPALTaERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGR-ADGQVKIRGHRIE 387
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2786869514 478 PQKVEGMLTLQPEIGQAMV---AGDKKPYIVGLIVPDAEWTL 516
Cdd:cd12116 388 LGEIEAALAAHPGVAQAAVvvrEDGGDRRLVAYVVLKAGAAP 429
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
38-498 |
9.19e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 95.98 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 38 TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCiadLAIMASGCITVPTYITNTE---RDHAHILDNSGAKAV 114
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFV---EALLAANRIGADILLLNTSfagPALAEVVTREGVDTV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 115 IVS---TEKLLRPLHGALQASGIADhvigiddlhrqqssgflfhrWDSMFAGDAAEARQA--VEQRIAGIGR-GDTacII 188
Cdd:PRK13382 145 IYDeefSATVDRALADCPQATRIVA--------------------WTDEDHDLTVEVLIAahAGQRPEPTGRkGRV--IL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 189 YTSGTGGAPRGVmQHHGAilcNVAGAAEILIEDFGIADDERFLSFLPLSHAYEHtggqflpisvgAQIYYAEGL------ 262
Cdd:PRK13382 203 LTSGTTGTPKGA-RRSGP---GGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGF-----------SQLVLAASLactivt 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 ------EKLASNIEETRPTIMVVVPRLFEvlrtRIMKqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrlL 336
Cdd:PRK13382 268 rrrfdpEATLDLIDRHRATGLAVVPVMFD----RIMD------------------------------------------L 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 337 KPKIRQRFGGR-IKAMVSGGAPLNPEVGI-FFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRI--- 411
Cdd:PRK13382 302 PAEVRNRYSGRsLRFAAASGSRMRPDVVIaFMDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRIldq 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 -------AEDGEILVRGELVMQGYwhnEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGM 484
Cdd:PRK13382 382 dfrevptGEVGTIFVRNDTQFDGY---TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSG-GENVYPIEVEKT 457
|
490
....*....|....
gi 2786869514 485 LTLQPEIGQAMVAG 498
Cdd:PRK13382 458 LATHPDVAEAAVIG 471
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
33-517 |
1.29e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 95.62 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLR-ALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP--TYITNTERdhAHILDNS 109
Cdd:PRK05620 33 GAEQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPlnKQLMNDQI--VHIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 110 GAKAVIVS---TEKLLRPLHGALQASGIAdhVIG---IDDLHRQQSSGFLFHRWDSMFAGDAAEAR-QAVEQRIAgigrg 182
Cdd:PRK05620 111 EDEVIVADprlAEQLGEILKECPCVRAVV--FIGpsdADSAAAHMPEGIKVYSYEALLDGRSTVYDwPELDETTA----- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 dtACIIYTSGTGGAPRGVMQHHGAILCNvagAAEILIED-FGIADDERFLSFLPLSHAYEHTggqfLPISV---GAQIYY 258
Cdd:PRK05620 184 --AAICYSTGTTGAPKGVVYSHRSLYLQ---SLSLRTTDsLAVTHGESFLCCVPIYHVLSWG----VPLAAfmsGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 259 AE---GLEKLASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEklmntalevgerraagkpkfgdglrdalvgrl 335
Cdd:PRK05620 255 PGpdlSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQE-------------------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 336 lkpkirqrfggrikaMVSGGAPLNPE-VGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIA-------MHSVGPAMRGV 407
Cdd:PRK05620 303 ---------------IYVGGSAVPPIlIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSgearwayRVSQGRFPASL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 408 DIRIAED-----------GEILVRGELVMQGYWHNEAET-----------------ERTIKDGWLHTGDIGHVDDKGRIV 459
Cdd:PRK05620 368 EYRIVNDgqvmestdrneGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedanDRFTADGWLRTGDVGSVTRDGFLT 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 460 ITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAG--DKK----PYIVGLIVPDAEWTLE 517
Cdd:PRK05620 448 IHDRARDVI-RSGGEWIYSAQLENYIMAAPEVVECAVIGypDDKwgerPLAVTVLAPGIEPTRE 510
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
37-515 |
1.53e-20 |
|
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: 95.03 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 StekllrpLHGALQASGIADHVIGIDDLhrqqssgflfhrwdsmfagDAAEARQAVeqriAGIGRGDTACIIYTSGTGGA 196
Cdd:cd12114 91 D-------GPDAQLDVAVFDVLILDLDA-------------------LAAPAPPPP----VDVAPDDLAYVIFTSGSTGT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGAILcNVAGAaeiLIEDFGIADDERFLSFLPLSH---AYEhtggQFLPISVGAQIYYAEGLEK-----LASN 268
Cdd:cd12114 141 PKGVMISHRAAL-NTILD---INRRFAVGPDDRVLALSSLSFdlsVYD----IFGALSAGATLVLPDEARRrdpahWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 269 IEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEVGERRAAGKPkfgdGLRDALV-GRL----LKPKIRQR 343
Cdd:cd12114 213 IERHGVTLWNSVPALLEML----------------------LDVLEAAQALLP----SLRLVLLsGDWipldLPARLRAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 344 F-GGRIKAMvsGGAplnPEVGIFfesmglTMLQGYGQTEAGPV-ISCNRPAAGIAMHSVGPAMRGVDIRIAedGEILVRG 421
Cdd:cd12114 267 ApDARLISL--GGA---TEASIW------SIYHPIDEVPPDWRsIPYGRPLANQRYRVLDPRGRDCPDWVP--GELWIGG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 422 ELVMQGYWHNEAETER---TIKDG--WLHTGDIGHVDDKGRIVITDRkKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMV 496
Cdd:cd12114 334 RGVALGYLGDPELTAArfvTHPDGerLYRTGDLGRYRPDGTLEFLGR-RDGQVKVRGYRIELGEIEAALQAHPGVARAVV 412
|
490 500
....*....|....*....|..
gi 2786869514 497 AGDKKPY---IVGLIVPDAEWT 515
Cdd:cd12114 413 VVLGDPGgkrLAAFVVPDNDGT 434
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
16-514 |
2.78e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 94.61 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 16 LKRAAEKGDLPFLGARIGGSWQ-------TISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRpEWCIadLAIMASGC 88
Cdd:PRK07788 45 IRRYGPFAGLVAHAARRAPDRAalidergTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNH-RGFV--LALYAAGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 89 ITVPTYITNTERDHAHILDNS---GAKAVIVSTE--KLLRPLHGAL-QASGIADHVigiDDLHRQQSSGFLFhrwDSMFA 162
Cdd:PRK07788 122 VGARIILLNTGFSGPQLAEVAareGVKALVYDDEftDLLSALPPDLgRLRAWGGNP---DDDEPSGSTDETL---DDLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 163 GDAAEARQAVEQRiAGIgrgdtacIIYTSGTGGAPRGVMQHHGAILCNVAGaaeiliedfgiadderFLSFLPLshayeh 242
Cdd:PRK07788 196 GSSTAPLPKPPKP-GGI-------VILTSGTTGTPKGAPRPEPSPLAPLAG----------------LLSRVPF------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 243 tgGQFLPISVGAQIYYAEGL---------------------EKLASNIEETRPTIMVVVPrlfeVLRTRImkqvqkqggl 301
Cdd:PRK07788 246 --RAGETTLLPAPMFHATGWahltlamalgstvvlrrrfdpEATLEDIAKHKATALVVVP----VMLSRI---------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 302 aeklmntaLEVGerraagkpkfgdglrdalvgrllkPKIRQRFG-GRIKAMVSGGAPLNPEVGI-FFESMGLTMLQGYGQ 379
Cdd:PRK07788 310 --------LDLG------------------------PEVLAKYDtSSLKIIFVSGSALSPELATrALEAFGPVLYNLYGS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 380 TEAGpVISCNRPAA-GIAMHSVGPAMRGVDIRIAED----------GEILVRGELVMQGYWHNEaetERTIKDGWLHTGD 448
Cdd:PRK07788 358 TEVA-FATIATPEDlAEAPGTVGRPPKGVTVKILDEngnevprgvvGRIFVGNGFPFEGYTDGR---DKQIIDGLLSSGD 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 449 IGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:PRK07788 434 VGYFDEDGLLFVDGRDDDMIVSG-GENVFPAEVEDLLAGHPDVVEAAVIG----------VDDEEF 488
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
43-515 |
4.35e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.10 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 43 EAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP-TYITNTERDHAHILDnsgAKAVIVSTEKL 121
Cdd:PLN02860 37 EFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPlNYRWSFEEAKSAMLL---VRPVMLVTDET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 122 LRPLHGALQASGIAD---HVIgIDDlhrqqSSGFLFHRWDSMFAGDAAEARQAVEQRIAGIGRGDTACII-YTSGTGGAP 197
Cdd:PLN02860 114 CSSWYEELQNDRLPSlmwQVF-LES-----PSSSVFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLIcFTSGTTGRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 198 RGVMQHHGAILcnVAGAAEILIedFGIADDERFLSFLPLSHayehTGGqflpIS-------VGAQIYYAEGLE-KLASN- 268
Cdd:PLN02860 188 KGVTISHSALI--VQSLAKIAI--VGYGEDDVYLHTAPLCH----IGG----LSsalamlmVGACHVLLPKFDaKAALQa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 269 IEETRPTIMVVVPRLF-EVLRTRIMKQVQKQGGLAEKLMNtalevgerraaGKPKFGDGLRDALVGRLLKPKIRQRFGgr 347
Cdd:PLN02860 256 IKQHNVTSMITVPAMMaDLISLTRKSMTWKVFPSVRKILN-----------GGGSLSSRLLPDAKKLFPNAKLFSAYG-- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 348 ikaMVSGGAPLNpevgifFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIAED-----GEILVRGE 422
Cdd:PLN02860 323 ---MTEACSSLT------FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDessrvGRILTRGP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 423 LVMQGYWHNEAET-ERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkk 501
Cdd:PLN02860 394 HVMLGYWGQNSETaSVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRI-KTGGENVYPEEVEAVLSQHPGVASVVVVG--- 469
|
490
....*....|....
gi 2786869514 502 pyivgliVPDAEWT 515
Cdd:PLN02860 470 -------VPDSRLT 476
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
185-468 |
9.34e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 93.63 E-value: 9.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 185 ACIIYTSGTGGAPRGVMQHHGAI------LCNVAgaaeiLIEDFGIaddERFLSFLPLSHAYEHTGGqFLPISVGAQIY- 257
Cdd:PTZ00342 307 TSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHS-----IFKKYNP---KTHLSYLPISHIYERVIA-YLSFMLGGTINi 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 258 YAEGLEKLASNIEETRPTIMVVVPRLFEVLRTRIMKQVQKQGGLAEKLMNTALEVgeRRAAGKPKFGDGLrDALVGrlLK 337
Cdd:PTZ00342 378 WSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSL--RKSNNNGGFSKFL-EGITH--IS 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 338 PKIRQRFGGRIKAMVSGGAPLNPEVgiffeSMGLTML------QGYGQTE-AGPVI-----SCNRPAAGIAMH-SVGPAM 404
Cdd:PTZ00342 453 SKIKDKVNPNLEVILNGGGKLSPKI-----AEELSVLlnvnyyQGYGLTEtTGPIFvqhadDNNTESIGGPISpNTKYKV 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786869514 405 RGVDIRIAED----GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMI 468
Cdd:PTZ00342 528 RTWETYKATDtlpkGELLIKSDSIFSGYFLEKEQTKNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
13-513 |
1.24e-19 |
|
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: 92.52 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 13 ELFLKRAAEKGDLPflgARIGGSwQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP 92
Cdd:COG1021 29 DLLRRRAERHPDRI---AVVDGE-RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 93 TYITNTERDHAHILDNSGAKAVIVSTEKLL---RPLHGALQASGIA-DHVIGIDDLHRqqssgflFHRWDSMFAGDAaea 168
Cdd:COG1021 105 ALPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyRALARELQAEVPSlRHVLVVGDAGE-------FTSLDALLAAPA--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 169 rqavEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYehtggqfl 248
Cdd:COG1021 175 ----DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEIC----GLDADTVYLAALPAAHNF-------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 249 PISV-GAQ-IYYAEGLEKLASN---------IEETRPTIMVVVPrlfevlrtrimkqvqkqgGLAEKLMNTAlevGERRA 317
Cdd:COG1021 239 PLSSpGVLgVLYAGGTVVLAPDpspdtafplIERERVTVTALVP------------------PLALLWLDAA---ERSRY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 318 AgkpkfgdglRDALvgRLLkpkirqrfggrikamVSGGAPLNPE----VGiffESMGLTMLQGYGQTEaGPViSCNRPAA 393
Cdd:COG1021 298 D---------LSSL--RVL---------------QVGGAKLSPElarrVR---PALGCTLQQVFGMAE-GLV-NYTRLDD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 394 G--IAMHSVGPAMRGVD-IRIAED----------GEILVRGELVMQGYWHNEAETER--TiKDGWLHTGDIGHVDDKGRI 458
Cdd:COG1021 347 PeeVILTTQGRPISPDDeVRIVDEdgnpvppgevGELLTRGPYTIRGYYRAPEHNARafT-PDGFYRTGDLVRRTPDGYL 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 459 VITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVagdkkpyiVGliVPDAE 513
Cdd:COG1021 426 VVEGRAKDQI-NRGGEKIAAEEVENLLLAHPAVHDAAV--------VA--MPDEY 469
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
39-482 |
2.12e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 88.51 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 39 ISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEwcIADLAI---MASGCITV---PTYITNTER---DHAHILDNS 109
Cdd:PRK07768 30 HTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVE--IAPTAQglwMRGASLTMlhqPTPRTDLAVwaeDTLRVIGMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 110 GAKAVIVSTEKLlrPLHGALQASGIAdhVIGIDDLhrqqssgflfhrwdsmfagDAAEARQAVEqriagIGRGDTACIIY 189
Cdd:PRK07768 108 GAKAVVVGEPFL--AAAPVLEEKGIR--VLTVADL-------------------LAADPIDPVE-----TGEDDLALMQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 190 TSGTGGAPRGVMQHHGAILCNVAG---AAEILIEDfgiaddERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLEKLA 266
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAmfvAAEFDVET------DVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 267 S------NIEETRPTiMVVVPrlfevlrtrimkqvqkqgglaeklmNTALEVGERRAAGKPKFGD----GLRDALVG-RL 335
Cdd:PRK07768 234 DpllwaeLISKYRGT-MTAAP-------------------------NFAYALLARRLRRQAKPGAfdlsSLRFALNGaEP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 336 LKPKIRQRFggrikamVSGGAP--LNPEVgiffesmgltMLQGYGQTEAGPVISCNRPAAGI-----------AMH---- 398
Cdd:PRK07768 288 IDPADVEDL-------LDAGARfgLRPEA----------ILPAYGMAEATLAVSFSPCGAGLvvdevdadllaALRravp 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 399 ----------SVGPAMRGVDIRIAED----------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRI 458
Cdd:PRK07768 351 atkgntrrlaTLGPPLPGLEVRVVDEdgqvlpprgvGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEV 430
|
490 500
....*....|....*....|....
gi 2786869514 459 VITDRKKDMIVNdKGDNVAPQKVE 482
Cdd:PRK07768 431 VVCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
34-589 |
2.21e-18 |
|
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: 88.71 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKA 113
Cdd:cd05970 43 GEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVSTEK-LLRPLHGALQASGIadhvigidDLHRQQSSGFLFHRWDSmFAGDAAEARQAVEQRIAGI-GRGDTACIIY-T 190
Cdd:cd05970 123 IVAIAEDnIPEEIEKAAPECPS--------KPKLVWVGDPVPEGWID-FRKLIKNASPDFERPTANSyPCGEDILLVYfS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 191 SGTGGAPRGVMQHHGAILCNVAGAAeiliedF--GIADDERFLSFLPLSHAYEHTG---GQFLpisVGAQIY-YAEGL-- 262
Cdd:cd05970 194 SGTTGMPKMVEHDFTYPLGHIVTAK------YwqNVREGGLHLTVADTGWGKAVWGkiyGQWI---AGAAVFvYDYDKfd 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 -EKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqggLAEKLMNTALEvgerraagkpkfgdGLRDAlvgrllkpkir 341
Cdd:cd05970 265 pKALLEKLSKYGVTTFCAPPTIYRFL-------------IREDLSRYDLS--------------SLRYC----------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 342 qrfggrikamVSGGAPLNPEV-GIFFESMGLTMLQGYGQTEAGPVI---SCNRPAAGiamhSVGPAMRGVDIRI------ 411
Cdd:cd05970 307 ----------TTAGEALNPEVfNTFKEKTGIKLMEGFGQTETTLTIatfPWMEPKPG----SMGKPAPGYEIDLidregr 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 ----AEDGEILVR---GELV--MQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVE 482
Cdd:cd05970 373 sceaGEEGEIVIRtskGKPVglFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLI-KSSGYRIGPFEVE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 483 GMLTLQPEIGQAMVAGDKKPyIVGLIVpDAEWTLEWCREQGKQFDcKKVQelpefrnavraavDRVNKDLSVVEKVRQFA 562
Cdd:cd05970 452 SALIQHPAVLECAVTGVPDP-IRGQVV-KATIVLAKGYEPSEELK-KELQ-------------DHVKKVTAPYKYPRIVE 515
|
570 580
....*....|....*....|....*...
gi 2786869514 563 FADE-PFTIeneemtpSMKIRRHKIKER 589
Cdd:cd05970 516 FVDElPKTI-------SGKIRRVEIRER 536
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
37-540 |
2.97e-18 |
|
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: 88.40 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STE--------KLLRPLHGALQASGIA-DHVIGIDdlhRQQSS-GFLFHRWdsmFAGDAAEARQAVEQRIAGIGRGDTAC 186
Cdd:cd17634 163 ADGgvragrsvPLKKNVDDALNPNVTSvEHVIVLK---RTGSDiDWQEGRD---LWWRDLIAKASPEHQPEAMNAEDPLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 187 IIYTSGTGGAPRGVMQHHGAILcnvAGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGlekla 266
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGYL---VYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEG----- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 267 sniEETRPTimvvvprlfevlRTRIMKQVQKQGGLAEKLMNTALEVgeRRAAGKpkfgdglrDALVGRLLKpkirqrfgg 346
Cdd:cd17634 309 ---VPNWPT------------PARMWQVVDKHGVNILYTAPTAIRA--LMAAGD--------DAIEGTDRS--------- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 347 RIKAMVSGGAPLNPEVGIFF----ESMGLTMLQGYGQTEAGPVISCNRP-----AAGIAMHSV-GPAMRGVDIR-----I 411
Cdd:cd17634 355 SLRILGSVGEPINPEAYEWYwkkiGKEKCPVVDTWWQTETGGFMITPLPgaielKAGSATRPVfGVQPAVVDNEghpqpG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 AEDGEILVRGELVMQ--GYWHNEAETE----RTIKDGWLHtGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGML 485
Cdd:cd17634 435 GTEGNLVITDPWPGQtrTLFGDHERFEqtyfSTFKGMYFS-GDGARRDEDGYYWITGRSDDVI-NVAGHRLGTAEIESVL 512
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786869514 486 TLQPEIGQAMVAGDKKP--------YIV---GLIVPD--AEWTLEWCREQ-GKQF---DCKKVQELPEFRNA 540
Cdd:cd17634 513 VAHPKVAEAAVVGIPHAikgqapyaYVVlnhGVEPSPelYAELRNWVRKEiGPLAtpdVVHWVDSLPKTRSG 584
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
183-497 |
5.49e-18 |
|
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: 85.39 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAIlcnVAGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAE-- 260
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTF---FAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEnt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 261 GLEKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglAEKLMNTALEVGERRAAGkpkfgdglrdalvgrllkpki 340
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKL--------------VSELKSANATVPSLRLIG--------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 341 rqrfggrikamVSGGAPLNPEVGiFFESMGLT-MLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRI-------- 411
Cdd:cd17635 124 -----------YGGSRAIAADVR-FIEATGLTnTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLaatdgiag 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 --AEDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQP 489
Cdd:cd17635 192 psASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDEVERIAEGVS 270
|
....*...
gi 2786869514 490 EIGQAMVA 497
Cdd:cd17635 271 GVQECACY 278
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
10-514 |
5.72e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 87.25 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 10 NLVELFLKRAAEKGDLPFL--GARiggswqTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG 87
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALvcGDR------RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 88 CITVPTYITNTERDHAHILDNSGAKAVIVSTEklLRP-LHGALQASGIADHVIGIDDlhrqQSSGFLF---HRWDSMFAG 163
Cdd:PRK07798 78 AVPVNVNYRYVEDELRYLLDDSDAVALVYERE--FAPrVAEVLPRLPKLRTLVVVED----GSGNDLLpgaVDYEDALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 164 DAAEarqaveqRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDFgIADDERFLSFlplshAYEHT 243
Cdd:PRK07798 152 GSPE-------RDFGERSPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEP-IEDEEELAKR-----AAAGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 244 GGQFLPISvgaQIYYAEGLEKLASNIEETRPTIMVVVPRL--FEVLRTrimkqVQKqgglaEKLMNTALeVGErrAAGKP 321
Cdd:PRK07798 219 GMRRFPAP---PLMHGAGQWAAFAALFSGQTVVLLPDVRFdaDEVWRT-----IER-----EKVNVITI-VGD--AMARP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 322 kfgdgLRDALVGRllkpkiRQRFGGRIKAMVSGGAPLNPEV-GIFFESM-GLTMLQGYGQTEAGpviscnrpAAGIAMHS 399
Cdd:PRK07798 283 -----LLDALEAR------GPYDLSSLFAIASGGALFSPSVkEALLELLpNVVLTDSIGSSETG--------FGGSGTVA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 400 VGPAMRG---VDIR-----IAEDGEILVRGE----------LVMQGYWHNEAETERTIK--DG--WLHTGDIGHVDDKGR 457
Cdd:PRK07798 344 KGAVHTGgprFTIGprtvvLDEDGNPVEPGSgeigwiarrgHIPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGT 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786869514 458 IVITDRkKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:PRK07798 424 ITLLGR-GSVCINTGGEKVFPEEVEEALKAHPDVADALVVG----------VPDERW 469
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
176-463 |
9.50e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.79 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 176 IAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNvagaAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQ 255
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLAN----QRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 256 IYYAEG---LEKLASNIEETRPTIMVVVPRLFEVlrtrIMKQVQKQgglaeklmNTALEVGERRAAGkpkfGDGLRDALV 332
Cdd:PRK06334 253 VVFAYNplyPKKIVEMIDEAKVTFLGSTPVFFDY----ILKTAKKQ--------ESCLPSLRFVVIG----GDAFKDSLY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 333 GRLLKpkirqrfggrikamvsggapLNPEVgiffesmglTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRI- 411
Cdd:PRK06334 317 QEALK--------------------TFPHI---------QLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIv 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786869514 412 ----------AEDGEILVRGELVMQGYWHNEaETERTIK---DGWLHTGDIGHVDDKGRIVITDR 463
Cdd:PRK06334 368 seetkvpvssGETGLVLTRGTSLFSGYLGED-FGQGFVElggETWYVTGDLGYVDRHGELFLKGR 431
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
13-522 |
2.26e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 84.95 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 13 ELFLKRAAEKGDLPFLgaRIGGswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP 92
Cdd:cd12117 1 ELFEEQAARTPDAVAV--VYGD--RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 93 TYITNTERDHAHILDNSGAKAVIvsTEKLLRPLHGALQASGIADhvigiddlhrqqssgflfhrwDSMFAGDAAEARqav 172
Cdd:cd12117 77 LDPELPAERLAFMLADAGAKVLL--TDRSLAGRAGGLEVAVVID---------------------EALDAGPAGNPA--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 173 eqriAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEIliedfGIADDERFLSFLPLS---HAYEHTGgqflP 249
Cdd:cd12117 131 ----VPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-----TLGPDDRVLQTSPLAfdaSTFEIWG----A 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 250 ISVGAQIYYAEG-----LEKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntalevgerrAAGKPKFG 324
Cdd:cd12117 198 LLNGARLVLAPKgtlldPDALGALIAEEGVTVLWLTAALFNQL-----------------------------ADEDPECF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 325 DGLRDALVG--RLLKPKIRQrfggrikamVSGGAPlnpevgiffesmGLTMLQGYGQTE---------------AGPVIS 387
Cdd:cd12117 249 AGLRELLTGgeVVSPPHVRR---------VLAACP------------GLRLVNGYGPTEnttfttshvvteldeVAGSIP 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 388 CNRPAAGIAMHSVGPAMRGVdiRIAEDGEILVRGELVMQGYWHNEAET-ERTIKDGWL------HTGDIGHVDDKGRIVI 460
Cdd:cd12117 308 IGRPIANTRVYVLDEDGRPV--PPGVPGELYVGGDGLALGYLNRPALTaERFVADPFGpgerlyRTGDLARWLPDGRLEF 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786869514 461 TDRKKDMiVNDKGDNVAPQKVEGMLTLQPEIGQAMVA------GDKkpYIVGLIVPDAEWTLE----WCREQ 522
Cdd:cd12117 386 LGRIDDQ-VKIRGFRIELGEIEAALRAHPGVREAVVVvredagGDK--RLVAYVVAEGALDAAelraFLRER 454
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
13-537 |
2.77e-17 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 85.07 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 13 ELFLKRAAEKGDLPflgARIGGSwQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP 92
Cdd:cd17655 1 ELFEEQAEKTPDHT---AVVFED-QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 93 TYITNTERDHAHILDNSGAKaVIVSTEKLLRPLHGAlqasgiaDHVIGIDDlhrqqssgflfhrwDSMFAGDAAEARQAV 172
Cdd:cd17655 77 IDPDYPEERIQYILEDSGAD-ILLTQSHLQPPIAFI-------GLIDLLDE--------------DTIYHEESENLEPVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 173 EQRiagigrgDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDFGIaddeRFLSFLPLShaYEHTGGQ-FLPIS 251
Cdd:cd17655 135 KSD-------DLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHL----RVALFASIS--FDASVTEiFASLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 252 VGAQIYYAEG-----LEKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntalevgerraagkpkfgdg 326
Cdd:cd17655 202 SGNTLYIVRKetvldGQALTQYIRQNRITIIDLTPAHLKLL--------------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 327 lrdalvgrllkPKIRQRFGGRIKAMVSGGAPLNPE-VGIFFESMGL--TMLQGYGQTEA---------------GPVISC 388
Cdd:cd17655 243 -----------DAADDSEGLSLKHLIVGGEALSTElAKKIIELFGTnpTITNAYGPTETtvdasiyqyepetdqQVSVPI 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 389 NRPAAGIAMHSVGPAMRGVDIRIAedGEILVRGELVMQGYWHNEAET-ERTIKDGWL------HTGDI------GHVDDK 455
Cdd:cd17655 312 GKPLGNTRIYILDQYGRPQPVGVA--GELYIGGEGVARGYLNRPELTaEKFVDDPFVpgermyRTGDLarwlpdGNIEFL 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 456 GRIvitdrkkDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAG----DKKPYIVGLIVPDAEWTLEWCREQGKqfdckkv 531
Cdd:cd17655 390 GRI-------DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIArkdeQGQNYLCAYIVSEKELPVAQLREFLA------- 455
|
....*.
gi 2786869514 532 QELPEF 537
Cdd:cd17655 456 RELPDY 461
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
185-482 |
3.32e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 84.85 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 185 ACIIYTSGTGGAPRGVM-QHHGAI--LCNVAGAAEILIEDfgiaddeRFLSFLPLSHAYEHTGGQFLPISVGAQIYYAeg 261
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMlTHENLVhnMFAILNSTEWKTKD-------RILSWMPLTHDMGLIAFHLAPLIAGMNQYLM-- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 262 leklasnieetrPTimvvvpRLFEVLRTRIMKQVQKQgglaeKLMNTAlevgerraagKPKFGDGLrdaLVGRLLKPKIR 341
Cdd:cd05908 180 ------------PT------RLFIRRPILWLKKASEH-----KATIVS----------SPNFGYKY---FLKTLKPEKAN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 342 QRFGGRIKAMVSGGAPLNPEV-GIFFESM---GL---TMLQGYGQTEAGPVIS---CNRPAAGIAMH------------- 398
Cdd:cd05908 224 DWDLSSIRMILNGAEPIDYELcHEFLDHMskyGLkrnAILPVYGLAEASVGASlpkAQSPFKTITLGrrhvthgepepev 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 399 -----------SVGPAMRGVDIRIAED----------GEILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDkG 456
Cdd:cd05908 304 dkkdsecltfvEVGKPIDETDIRICDEdnkilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIRN-G 382
|
330 340
....*....|....*....|....*..
gi 2786869514 457 RIVITDRKKDMI-VNdkGDNVAPQKVE 482
Cdd:cd05908 383 RLVITGREKDIIfVN--GQNVYPHDIE 407
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-482 |
6.24e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.22 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGD---LPFLGARIGGSWQtISWNEAAEQVCLLAENLRALGlRDGDRVCLVSENRPEWCIADLAIMASG 87
Cdd:PRK05691 11 LVQALQRRAAQTPDrlaLRFLADDPGEGVV-LSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 88 CITVPTYITNTERDHAHildnsgakavivstEKLLRPLHGA-----LQASGIADHVIGIDDLHRQQSSGFLfhrwdsmfA 162
Cdd:PRK05691 89 VIAVPAYPPESARRHHQ--------------ERLLSIIADAeprllLTVADLRDSLLQMEELAAANAPELL--------C 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 163 GDAAEARQAVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNvagaaEILI-EDFGIA--DDERFLSFLPLSHA 239
Cdd:PRK05691 147 VDTLDPALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVAN-----EQLIrHGFGIDlnPDDVIVSWLPLYHD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 240 YEHTGGQFLPISVGAqiyyaegleklasnieetrPTIMVVvPRLFEVLRTRIMKQVQKQGGL------------AEKLMN 307
Cdd:PRK05691 222 MGLIGGLLQPIFSGV-------------------PCVLMS-PAYFLERPLRWLEAISEYGGTisggpdfayrlcSERVSE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 308 TALEVGERraagkpkfgDGLRDALVGRllKPkIRQ----RFGGRIKAmvSGGAPLNpevgiFFESMGL---TMLQGYGQT 380
Cdd:PRK05691 282 SALERLDL---------SRWRVAYSGS--EP-IRQdsleRFAEKFAA--CGFDPDS-----FFASYGLaeaTLFVSGGRR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 381 EAGP--------VISCNR--PAAGIAMHSVGPAMRGVDIRIAED-----------GEILVRGELVMQGYWHNEAETERTI 439
Cdd:PRK05691 343 GQGIpaleldaeALARNRaePGTGSVLMSCGRSQPGHAVLIVDPqslevlgdnrvGEIWASGPSIAHGYWRNPEASAKTF 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2786869514 440 --KDG--WLHTGDIGHVDDkGRIVITDRKKDMIVNdKGDNVAPQKVE 482
Cdd:PRK05691 423 veHDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIV-RGHNLYPQDIE 467
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
6-498 |
6.70e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.16 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 6 DSANNLVELFLKRAAEKGDLPFLgaRIGGswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMA 85
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPAL--LFED--QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 86 SGCITvpTYITNTERDH--AHILDNSGAKAVIVSTE---------KLLRPLHGALQASGI-ADHVIGIDDLHRQQSSgfl 153
Cdd:PRK08279 110 LGAVV--ALLNTQQRGAvlAHSLNLVDAKHLIVGEElveafeearADLARPPRLWVAGGDtLDDPEGYEDLAAAAAG--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 154 fhrwdsmFAGDAAEARQAVEQRiagigrgDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedfGIADDERFLSF 233
Cdd:PRK08279 185 -------APTTNPASRSGVTAK-------DTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLL----RLTPDDVLYCC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 234 LPLSHAyehTGGQflpISVGAQIyyAEGleklASnieetrptimVVVPRLF-------EVLRTRImKQVQKQGGLAEKLM 306
Cdd:PRK08279 247 LPLYHN---TGGT---VAWSSVL--AAG----AT----------LALRRKFsasrfwdDVRRYRA-TAFQYIGELCRYLL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 307 NTALEVGERRAAGKPKFGDGLRdalvgrllkPKI----RQRFG-GRIkamvsggaplnpevgiffesmgltmLQGYGQTE 381
Cdd:PRK08279 304 NQPPKPTDRDHRLRLMIGNGLR---------PDIwdefQQRFGiPRI-------------------------LEFYAASE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 382 aGPVISCN---RPaagiamHSVG--PAMRGVDIRI--------------------AEDGEIlvrGELV--------MQGY 428
Cdd:PRK08279 350 -GNVGFINvfnFD------GTVGrvPLWLAHPYAIvkydvdtgepvrdadgrcikVKPGEV---GLLIgritdrgpFDGY 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 429 wHNEAETERTI-----KDG--WLHTGDIGHVDDKGRIVITDRkkdmiVND----KGDNVAPQKVEGMLTLQPEIGQAMVA 497
Cdd:PRK08279 420 -TDPEASEKKIlrdvfKKGdaWFNTGDLMRDDGFGHAQFVDR-----LGDtfrwKGENVATTEVENALSGFPGVEEAVVY 493
|
.
gi 2786869514 498 G 498
Cdd:PRK08279 494 G 494
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
32-511 |
8.57e-17 |
|
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: 83.13 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 32 IGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGA 111
Cdd:cd17653 16 VESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 112 KaVIVSTekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagDAAEarqaveqriagigrgDTACIIYTS 191
Cdd:cd17653 96 T-LLLTT---------------------------------------------DSPD---------------DLAYIIFTS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 192 GTGGAPRGVMQHHGAILcNVAGAAEILiedFGIADDERFLSFLplSHAYEHTGGQ-FLPISVGAQIYYAEGLEKLASNIE 270
Cdd:cd17653 115 GSTGIPKGVMVPHRGVL-NYVSQPPAR---LDVGPGSRVAQVL--SIAFDACIGEiFSTLCNGGTLVLADPSDPFAHVAR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 271 ETrpTIMVVVPRLFEVLRtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrllkpkiRQRFGgRIKA 350
Cdd:cd17653 189 TV--DALMSTPSILSTLS----------------------------------------------------PQDFP-NLKT 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 MVSGGAPLNPEVgIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHsVGPAMRGVDIRI----------AEDGEILVR 420
Cdd:cd17653 214 IFLGGEAVPPSL-LDRWSPGRRLYNAYGPTECTISSTMTELLPGQPVT-IGKPIPNSTCYIldadlqpvpeGVVGEICIS 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 421 GELVMQGYWHNEAETER-----TIKDGWLH--TGDIGHVDDKGRIVITDRkKDMIVNDKGDNVA-PQKVEGMLTLQPEIG 492
Cdd:cd17653 292 GVQVARGYLGNPALTASkfvpdPFWPGSRMyrTGDYGRWTEDGGLEFLGR-EDNQVKVRGFRINlEEIEEVVLQSQPEVT 370
|
490 500
....*....|....*....|.
gi 2786869514 493 Q--AMVAGDKkpyIVGLIVPD 511
Cdd:cd17653 371 QaaAIVVNGR---LVAFVTPE 388
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
37-521 |
1.69e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 82.64 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKaVIV 116
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAK-VLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLRPLhgalqasgIAD------HVIGIDDlHRQQSSGFL-FHRwdsmfagdaaEARQAVEQ-RIAGIGRGDTACII 188
Cdd:PRK04319 151 TTPALLERK--------PADdlpslkHVLLVGE-DVEEGPGTLdFNA----------LMEQASDEfDIEWTDREDGAILH 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 189 YTSGTGGAPRGVMQHHGAILCNVAGAAEILieDFgiADDERFLS--------------FLPLSHAYEHT--GGQFLPisv 252
Cdd:PRK04319 212 YTSGSTGKPKGVLHVHNAMLQHYQTGKYVL--DL--HEDDVYWCtadpgwvtgtsygiFAPWLNGATNVidGGRFSP--- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 253 gaqiyyaeglEKLASNIEETRPTIMVVVPRLFEVLrtriMKQvqkQGGLAEKLMNTALevgerraagkpkfgdglrdalv 332
Cdd:PRK04319 285 ----------ERWYRILEDYKVTVWYTAPTAIRML----MGA---GDDLVKKYDLSSL---------------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 333 grllkpkirqRFggrikaMVSGGAPLNPEVGIF-FESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRI 411
Cdd:PRK04319 326 ----------RH------ILSVGEPLNPEVVRWgMKVFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 412 AED----GEILVRGELV--------MQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQ 479
Cdd:PRK04319 390 VDDqgneLPPNRMGNLAikkgwpsmMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVI-KTSGERVGPF 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2786869514 480 KVEGMLTLQPEIGQAMVAGDKKPyIVGLIV-------PDAEWTLEWCRE 521
Cdd:PRK04319 469 EVESKLMEHPAVAEAGVIGKPDP-VRGEIIkafvalrPGYEPSEELKEE 516
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
51-596 |
1.04e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 80.17 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 51 LAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTyitNTE-RDH--AHILDNSGAKAVIVSTE----KLLR 123
Cdd:PRK06164 48 LAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV---NTRyRSHevAHILGRGRARWLVVWPGfkgiDFAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 124 PLHGALQASGIADHVIGIDDLHRQQSSGFLFHRWDSMFAGDAAEARQAVEQRIAGIGRGdtACIIYTSGTGGAPRGVMQH 203
Cdd:PRK06164 125 ILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAG--ALLFTTSGTTSGPKLVLHR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 204 HGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYehtggqflpisvgaqiyyaeGLEKLASNIEETRPTIMVVVprl 283
Cdd:PRK06164 203 QATLLRHARAIARAY----GYDPGAVLLAALPFCGVF--------------------GFSTLLGALAGGAPLVCEPV--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 284 FEVLRTriMKQVQKQG-----GLAEKLMNTALEVGERRA------AGKPKFGDGLRDalvgrlLKPKIRQRfggrikamv 352
Cdd:PRK06164 256 FDAART--ARALRRHRvthtfGNDEMLRRILDTAGERADfpsarlFGFASFAPALGE------LAALARAR--------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 353 sgGAPLNpevgiffesmGLtmlqgYGQTEAGPVISCNRPAAGIAMHSVG---PAMRGVDIRIA-----------EDGEIL 418
Cdd:PRK06164 319 --GVPLT----------GL-----YGSSEVQALVALQPATDPVSVRIEGggrPASPEARVRARdpqdgallpdgESGEIE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 419 VRGELVMQGYWHNEAETERTIK-DGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVA 497
Cdd:PRK06164 382 IRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSL-RLGGFLVNPAEIEHALEALPGVAAAQVV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 498 G---DKKPYIVGLIVP------DAEWTLEWCREQgkqfdckkvqeLPEFRnaVRAAVDRVNkdlsvvekvrqfAFadePF 568
Cdd:PRK06164 461 GatrDGKTVPVAFVIPtdgaspDEAGLMAACREA-----------LAGFK--VPARVQVVE------------AF---PV 512
|
570 580
....*....|....*....|....*...
gi 2786869514 569 TieneEMTPSMKIRRHKIKERYAERLDA 596
Cdd:PRK06164 513 T----ESANGAKIQKHRLREMAQARLAA 536
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
10-501 |
1.05e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 80.46 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 10 NLVELFLKRAAEKG--DLPFLGARiggswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG 87
Cdd:PRK06060 5 NLAGLLAEQASEAGwyDRPAFYAA-----DVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 88 CITvptYITNTE--RDHAHILDNSGAKAVIVSTEkllrPLHGALQASGIADHVIGIDDLHRQQSSGFlfhrwdSMFAGDA 165
Cdd:PRK06060 80 VMA---FLANPElhRDDHALAARNTEPALVVTSD----ALRDRFQPSRVAEAAELMSEAARVAPGGY------EPMGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 166 AearqaveqriagigrgdtACIIYTSGTGGAPRGVMQHHG-------AILCNvagAAEILIEDFGIADDERFLSF----- 233
Cdd:PRK06060 147 L------------------AYATYTSGTTGPPKAAIHRHAdpltfvdAMCRK---ALRLTPEDTGLCSARMYFAYglgns 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 234 --LPLShayehTGGQFL--PISVGAqiyyaEGLEKLASNIEetrPTIMVVVPRLFevlrTRIMKQVQKQGGLAEKLMNTA 309
Cdd:PRK06060 206 vwFPLA-----TGGSAVinSAPVTP-----EAAAILSARFG---PSVLYGVPNFF----ARVIDSCSPDSFRSLRCVVSA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 310 levgerraagkpkfGDGLRDALVGRLLKpkirqrfggrikamvsggaplnpevgiFFEsmGLTMLQGYGQTEAGPVISCN 389
Cdd:PRK06060 269 --------------GEALELGLAERLME---------------------------FFG--GIPILDGIGSTEVGQTFVSN 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 390 -----RPAagiamhSVGPAMRGVDIRIAE----------DGEILVRGELVMQGYWhNEAETERTiKDGWLHTGDIGHVDD 454
Cdd:PRK06060 306 rvdewRLG------TLGRVLPPYEIRVVApdgttagpgvEGDLWVRGPAIAKGYW-NRPDSPVA-NEGWLDTRDRVCIDS 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2786869514 455 KGRIVITDRKKDM-IVNdkGDNVAPQKVEGMLTLQPEIGQAMVAGDKK 501
Cdd:PRK06060 378 DGWVTYRCRADDTeVIG--GVNVDPREVERLIIEDEAVAEAAVVAVRE 423
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
37-513 |
1.15e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 79.53 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:PRK09029 27 EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEkllrplhgalqasgiADHVIGIDDLHRQQSSGFLFHRWDSmfagdaaearqaveQRIAgigrgdtaCIIYTSGTGGA 196
Cdd:PRK09029 107 LEG---------------ENTFSALTSLHLQLVEGAHAVAWQP--------------QRLA--------TMTLTSGSTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGAILCNVAGAAEILieDFGiADDERFLSfLPLshaYeHTGGQ-----FLpiSVGAQIYYAEGlEKLASNIEE 271
Cdd:PRK09029 150 PKAAVHTAQAHLASAEGVLSLM--PFT-AQDSWLLS-LPL---F-HVSGQgivwrWL--YAGATLVVRDK-QPLEQALAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 272 TrpTIMVVVPrlfevlrTrimkQVQkqgglaeklmntalevgerraagkpkfgdglrdalvgRLLKPKIRQrfgGRIKAM 351
Cdd:PRK09029 219 C--THASLVP-------T----QLW-------------------------------------RLLDNRSEP---LSLKAV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 352 VSGGAPLNPEVGIFFESMGLTMLQGYGQTEAGPVIsCNRPAAGIAmhSVGPAMRGVDIRIaEDGEILVRGELVMQGYWHN 431
Cdd:PRK09029 246 LLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTV-CAKRADGLA--GVGSPLPGREVKL-VDGEIWLRGASLALGYWRQ 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 432 EAETERTIKDGWLHTGDIGHVDDkGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVagdkkpyivgLIVPD 511
Cdd:PRK09029 322 GQLVPLVNDEGWFATRDRGEWQN-GELTILGRLDNLFFSG-GEGIQPEEIERVINQHPLVQQVFV----------VPVAD 389
|
..
gi 2786869514 512 AE 513
Cdd:PRK09029 390 AE 391
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
110-498 |
1.23e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 80.04 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 110 GAKAVIVSTEKLLRPLHGALQASGIAdhVIGIDDLHRQQSSGflfhRWDSMFAGDAAE--ARQAVEQ-RIAGIGRgdtaC 186
Cdd:PRK13383 109 GADVVPISTEFRSDALAAALRAHHIS--TVVADNEFAERIAG----ADDAVAVIDPATagAEESGGRpAVAAPGR----I 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 187 IIYTSGTGGAPRGVMQhhGAILCNVAGAAEILIEDFGIADDERFLSFLPLSHAYeHTGGQFLPISVGAQIYYAEGLEKLA 266
Cdd:PRK13383 179 VLLTSGTTGKPKGVPR--APQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGL-GLGMLMLTIALGGTVLTHRHFDAEA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 267 SNIEET--RPTIMVVVPrlfeVLRTRIMKqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrlLKPKIRQRF 344
Cdd:PRK13383 256 ALAQASlhRADAFTAVP----VVLARILE------------------------------------------LPPRVRARN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 345 G-GRIKAMVSGGAPLNPEVGI-FFESMGLTMLQGYGQTEAG------PVI------SCNRPAAGIAMHSVGPAMRGVDIR 410
Cdd:PRK13383 290 PlPQLRVVMSSGDRLDPTLGQrFMDTYGDILYNGYGSTEVGigalatPADlrdapeTVGKPVAGCPVRILDRNNRPVGPR 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 411 IAedGEILVRGELVMQGYWHNEAeteRTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPE 490
Cdd:PRK13383 370 VT--GRIFVGGELAGTRYTDGGG---KAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISG-GENVYPRAVENALAAHPA 443
|
....*...
gi 2786869514 491 IGQAMVAG 498
Cdd:PRK13383 444 VADNAVIG 451
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
367-515 |
1.36e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 78.11 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 367 ESMGLTMLQGYGQTEAGPVISCN---RPAAGIAMHSvGPAMR-------GVDIRIAEDGEILVRGELVMQGYWHNEAETE 436
Cdd:cd17636 133 TSPWGRKPGGYGQTEVMGLATFAalgGGAIGGAGRP-SPLVQvrildedGREVPDGEVGEIVARGPTVMAGYWNRPEVNA 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786869514 437 RTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEWT 515
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMI-KSGAENIYPAEVERCLRQHPAVADAAVIG----------VPDPRWA 279
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
37-502 |
1.37e-15 |
|
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: 79.40 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLR-ALGLRDGDRVCLVSENRPEWCIADLAIMASGCitVPTYITNTERDHA--HILDNSGAKA 113
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGA--APAFINYNLSGDPliHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVSTEKLlrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgdtACIIYTSGT 193
Cdd:cd05937 82 VIVDPDDP---------------------------------------------------------------AILIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 194 GGAPRGVMQHHGAILCnvagAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAE--GLEKLASNIEE 271
Cdd:cd05937 99 TGLPKAAAISWRRTLV----TSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRkfSASQFWKDVRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 272 TRPTIMVVVprlfevlrtrimkqvqkqGGLAEKLMNTALEVGERRAAGKPKFGDGLRDALVGRLlkpkiRQRFGgrikam 351
Cdd:cd05937 175 SGATIIQYV------------------GELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERF-----RERFN------ 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 352 vsggaplNPEVGIFFESmgltmlqgygqTEaGPVISCNRPAAGIAMHSVGpaMRGVDIR-IAEDGEILVR---------- 420
Cdd:cd05937 226 -------VPEIGEFYAA-----------TE-GVFALTNHNVGDFGAGAIG--HHGLIRRwKFENQVVLVKmdpetddpir 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 421 ---------------GELVM----------QGYWHNEAETERTI-------KDGWLHTGDIGHVDDKGRIVITDRKKDMI 468
Cdd:cd05937 285 dpktgfcvrapvgepGEMLGrvpfknreafQGYLHNEDATESKLvrdvfrkGDIYFRTGDLLRQDADGRWYFLDRLGDTF 364
|
490 500 510
....*....|....*....|....*....|....
gi 2786869514 469 vNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKP 502
Cdd:cd05937 365 -RWKSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
15-496 |
1.49e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 79.89 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 15 FLKRAAEKGdlPFLGARIGGSWQtISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTY 94
Cdd:PLN02479 25 FLERAAVVH--PTRKSVVHGSVR-YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 95 ITNTERDHAHILDNSGAKAVIVS------TEKLLRPLHGALQAS-------GIADHVIGIDDLHRQQSSGFLFHRwDSMF 161
Cdd:PLN02479 102 IRLNAPTIAFLLEHSKSEVVMVDqefftlAEEALKILAEKKKSSfkpplliVIGDPTCDPKSLQYALGKGAIEYE-KFLE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 162 AGDAAEARQAVEQRIAGIGRGdtaciiYTSGTGGAPRGVMQHH-GAILCNVAGAaeiLIedFGIADDERFLSFLPLSHAy 240
Cdd:PLN02479 181 TGDPEFAWKPPADEWQSIALG------YTSGTTASPKGVVLHHrGAYLMALSNA---LI--WGMNEGAVYLWTLPMFHC- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 241 ehtGGQFLPISVGAQIyyaegleklASNIeetrptimvvvpRLFEVLRTRIMKQVQKQGglaeklmntaleVGERRAAgk 320
Cdd:PLN02479 249 ---NGWCFTWTLAALC---------GTNI------------CLRQVTAKAIYSAIANYG------------VTHFCAA-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 321 PKFGDGLRDALVGRLLKPKIRQrfggrIKAMVSGGAPlNPEVGIFFESMGLTMLQGYGQTEA-GPVISC----------- 388
Cdd:PLN02479 291 PVVLNTIVNAPKSETILPLPRV-----VHVMTAGAAP-PPSVLFAMSEKGFRVTHTYGLSETyGPSTVCawkpewdslpp 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 389 ---NRPAAGIAMHSVGpaMRGVDI-------RIAEDG----EILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDD 454
Cdd:PLN02479 365 eeqARLNARQGVRYIG--LEGLDVvdtktmkPVPADGktmgEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHP 442
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2786869514 455 KGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMV 496
Cdd:PLN02479 443 DGYIEIKDRSKDIIISG-GENISSLEVENVVYTHPAVLEASV 483
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
183-473 |
2.85e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.79 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPLshayehtggqFLPISVgaqiyyAEGL 262
Cdd:PRK09274 175 DMAAILFTSGSTGTPKGVVYTHG----MFEAQIEALREDYGIEPGEIDLPTFPL----------FALFGP------ALGM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 EKLASNIEETRPTimVVVPRlfevlrtRIMKQVQKQGglaeklmntalevgERRAAGKPkfgdglrdALVGRLLkpkirq 342
Cdd:PRK09274 235 TSVIPDMDPTRPA--TVDPA-------KLFAAIERYG--------------VTNLFGSP--------ALLERLG------ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 343 RFGGR-------IKAMVSGGAPLNPEVGIFFESM---GLTMLQGYGQTEAGPVIS----------CNRPAAGiAMHSVGP 402
Cdd:PRK09274 278 RYGEAngiklpsLRRVISAGAPVPIAVIERFRAMlppDAEILTPYGATEALPISSiesreilfatRAATDNG-AGICVGR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 403 AMRGVDIRI-------------------AEDGEILVRGELVMQGYWHNEAETERT-IKDG----WLHTGDIGHVDDKGRI 458
Cdd:PRK09274 357 PVDGVEVRIiaisdapipewddalrlatGEIGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRL 436
|
330
....*....|....*
gi 2786869514 459 VITDRKKDMIVNDKG 473
Cdd:PRK09274 437 WFCGRKAHRVETAGG 451
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
40-514 |
5.28e-15 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 77.75 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 40 SWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVste 119
Cdd:cd05920 42 TYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIV--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 120 kllrplhgalqasgiadhvigiDDLHRQQSSGFLFHrwdsmfagdaaEARQAVeqriagigrGDTACIIYTSGTGGAPRG 199
Cdd:cd05920 119 ----------------------PDRHAGFDHRALAR-----------ELAESI---------PEVALFLLSGGTTGTPKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 200 VMQHHGAILCNVAGAAEILiedfGIADDERFLSFLPLSHAYEHTGgqflPISVGAqiYYAEGLEKLASN---------IE 270
Cdd:cd05920 157 IPRTHNDYAYNVRASAEVC----GLDQDTVYLAVLPAAHNFPLAC----PGVLGT--LLAGGRVVLAPDpspdaafplIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 271 ETRPTIMVVVPrlfevlrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrdALVGRLLKPKIRQRFG-GRIK 349
Cdd:cd05920 227 REGVTVTALVP------------------------------------------------ALVSLWLDAAASRRADlSSLR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 350 AMVSGGAPLNPEVG-IFFESMGLTMLQGYGQTEAgpVISCNRP--AAGIAMHSVG-PAMRGVDIRIA----------EDG 415
Cdd:cd05920 259 LLQVGGARLSPALArRVPPVLGCTLQQVFGMAEG--LLNYTRLddPDEVIIHTQGrPMSPDDEIRVVdeegnpvppgEEG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 416 EILVRGELVMQGYWHNEAETERTI-KDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQA 494
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVENLLLRHPAVHDA 415
|
490 500
....*....|....*....|
gi 2786869514 495 MVAGdkkpyivgliVPDAEW 514
Cdd:cd05920 416 AVVA----------MPDELL 425
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
37-513 |
7.00e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.41 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDR-VCLVSENRPEWCIADLAIMASGciTVPTYITNTERDHAHILDNSGAKAVI 115
Cdd:PRK07867 27 SFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSG--IVPVGLNPTRRGAALARDIAHADCQL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 116 VSTEKLLRPLhgaLQASGIADHVIGIDDLHrqqssgflfhrWDSMFAGDA-AEARQAVEQRiagigrGDTACIIYTSGTG 194
Cdd:PRK07867 105 VLTESAHAEL---LDGLDPGVRVINVDSPA-----------WADELAAHRdAEPPFRVADP------DDLFMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 195 GAPRGVMQHHGailcNVAGAAEILIEDFGI-ADDERFLSfLPLSHAYEHTGGQFLPISVGAQIyyaegleklasnieetr 273
Cdd:PRK07867 165 GDPKAVRCTHR----KVASAGVMLAQRFGLgPDDVCYVS-MPLFHSNAVMAGWAVALAAGASI----------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 274 ptimvVVPRLFEVlrTRIMKQVQKQGglaeklMNTALEVGERRA---AGKPKFGDglRDAlvgrllkpKIRQRFGGRika 350
Cdd:PRK07867 223 -----ALRRKFSA--SGFLPDVRRYG------ATYANYVGKPLSyvlATPERPDD--ADN--------PLRIVYGNE--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 mvsgGAPlnPEVGIFFESMGLTMLQGYGQTEAGPVI---------SCNRPAAGIAMHSV------GPAMRGVDIRIAEDG 415
Cdd:PRK07867 277 ----GAP--GDIARFARRFGCVVVDGFGSTEGGVAItrtpdtppgALGPLPPGVAIVDPdtgtecPPAEDADGRLLNADE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 416 EIlvrGELV-------MQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQ 488
Cdd:PRK07867 351 AI---GELVntagpggFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD-GENLGTAPIERILLRY 426
|
490 500
....*....|....*....|....*
gi 2786869514 489 PEIGQAMVAGdkkpyivgliVPDAE 513
Cdd:PRK07867 427 PDATEVAVYA----------VPDPV 441
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
31-513 |
9.97e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 76.95 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 31 RIGGswQTISWNEAAEQVCLLAENLRALglrdgDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSG 110
Cdd:PRK07787 20 RIGG--RVLSRSDLAGAATAVAERVAGA-----RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 111 AKAVIvstekllrplhGALQASGIADHVIGIDdlhrqqssgfLFHRWDSMFAGDAAEArqaveqriagigrgdTACIIYT 190
Cdd:PRK07787 93 AQAWL-----------GPAPDDPAGLPHVPVR----------LHARSWHRYPEPDPDA---------------PALIVYT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 191 SGTGGAPRGVMQHHGAIlcnvAGAAEILIEDFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIY---------YAEG 261
Cdd:PRK07787 137 SGTTGPPKGVVLSRRAI----AADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVhtgrptpeaYAQA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 262 LEklasnieeTRPTIMVVVPRLFEvlrtrimkqvqkqgglaeklmntalevgerRAAGKPKFGDGLRDAlvgRLLkpkir 341
Cdd:PRK07787 213 LS--------EGGTLYFGVPTVWS------------------------------RIAADPEAARALRGA---RLL----- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 342 qrfggrikamVSGGAPLNPEVgifFESM----GLTMLQGYGQTEAGPVISC-----NRPAagiamhSVGPAMRGVDIRIA 412
Cdd:PRK07787 247 ----------VSGSAALPVPV---FDRLaaltGHRPVERYGMTETLITLSTradgeRRPG------WVGLPLAGVETRLV 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 413 ED------------GEILVRGELVMQGYWHN-EAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDKGDNVAPQ 479
Cdd:PRK07787 308 DEdggpvphdgetvGELQVRGPTLFDGYLNRpDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAG 387
|
490 500 510
....*....|....*....|....*....|....*...
gi 2786869514 480 KVEGMLTLQPEIGQAMVAGDKKP----YIVGLIVPDAE 513
Cdd:PRK07787 388 EIETALLGHPGVREAAVVGVPDDdlgqRIVAYVVGADD 425
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
33-596 |
1.04e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 77.29 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLRALGlRDGDRVCLVSENRPEWCIADLAIMASGCITVP----TYITNTERDHAHILDN 108
Cdd:PRK05850 30 AGVAETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVPlsvpQGGAHDERVSAVLRDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 109 SgaKAVIVSTekllrplhgalqaSGIADHVIGIDDLHRQQSSGflfhrwdSMFAGDAAEARQAVEQRIAGIGRGDTACII 188
Cdd:PRK05850 109 S--PSVVLTT-------------SAVVDDVTEYVAPQPGQSAP-------PVIEVDLLDLDSPRGSDARPRDLPSTAYLQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 189 YTSGTGGAPRGVMQHHGAILCNVagaaEILIEDF-----GIA-DDERFLSFLPLSHAYEHTGGQFLPISVGaqiyyaegl 262
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANF----EQLMSDYfgdtgGVPpPDTTVVSWLPFYHDMGLVLGVCAPILGG--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 263 eklasnieetRPTIMVVvPRLFevLR--TRIMKQVQKQGGLAEKLMNTALEVGERRAAGKPKFGDGLRDALV---G--RL 335
Cdd:PRK05850 234 ----------CPAVLTS-PVAF--LQrpARWMQLLASNPHAFSAAPNFAFELAVRKTSDDDMAGLDLGGVLGiisGseRV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 336 LKPKIRQ------RFGGRIKAM------------VSGGAPLNPEVGIFFESMGLTmlqgygqteAGPVISCnRPAAGIAM 397
Cdd:PRK05850 301 HPATLKRfadrfaPFNLRETAIrpsyglaeatvyVATREPGQPPESVRFDYEKLS---------AGHAKRC-ETGGGTPL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 398 HSVG----PAMRGVD----IRIAED--GEILVRGELVMQGYWHNEAETERT-----------IKDG-WLHTGDIGHVDDk 455
Cdd:PRK05850 371 VSYGsprsPTVRIVDpdtcIECPAGtvGEIWVHGDNVAAGYWQKPEETERTfgatlvdpspgTPEGpWLRTGDLGFISE- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 456 GRIVITDRKKDMIVNDkGDNVAPQKVEGmlTLQpEIGQAMVAgdkkpyivGLIVPDAEW----TLEWCREQGKQfDCKKV 531
Cdd:PRK05850 450 GELFIVGRIKDLLIVD-GRNHYPDDIEA--TIQ-EITGGRVA--------AISVPDDGTeklvAIIELKKRGDS-DEEAM 516
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786869514 532 QELPEFRNAVRAAVDRVNKdLSVvekvrqfafAD----EPFTIeneEMTPSMKIRRHKIKERYA----ERLDA 596
Cdd:PRK05850 517 DRLRTVKREVTSAISKSHG-LSV---------ADlvlvAPGSI---PITTSGKIRRAACVEQYRqdefTRLDA 576
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
332-589 |
1.21e-14 |
|
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: 76.45 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 332 VGRLLKPKIRQRFGGRIKAMVSGGAPLNPEV-GIFFESMGLTMLQGYGQTEAGPVIScNRPAAGIAMHSVGPAMRGVDIR 410
Cdd:cd05974 186 VWRMLIQQDLASFDVKLREVVGAGEPLNPEViEQVRRAWGLTIRDGYGQTETTALVG-NSPGQPVKAGSMGRPLPGYRVA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 411 IAE-DGEILVRGEL-----------VMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDmIVNDKGDNVAP 478
Cdd:cd05974 265 LLDpDGAPATEGEValdlgdtrpvgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISP 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 479 QKVEGMLTLQPEIGQAMVAgdKKPYIVGLIVPDAEWTLewcrEQGKQFDCKKVQELPEFRNAVRAAVDRvnkdlsvvekV 558
Cdd:cd05974 344 FELESVLIEHPAVAEAAVV--PSPDPVRLSVPKAFIVL----RAGYEPSPETALEIFRFSRERLAPYKR----------I 407
|
250 260 270
....*....|....*....|....*....|.
gi 2786869514 559 RQFAFADEPFTIeneemtpSMKIRRHKIKER 589
Cdd:cd05974 408 RRLEFAELPKTI-------SGKIRRVELRRR 431
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
46-513 |
1.76e-14 |
|
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: 75.88 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 46 EQVCLLaenlRALGLRDGDRVCLVSENRPEWciADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTEKLlRPL 125
Cdd:cd05929 9 AQVFHQ----RRLLLLDVYSIALNRNARAAA--AEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPR-AEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 126 HGALQASGIADHVIGIDDlhrqqssGFLFHRWDSMFAgdaAEARQAVEQrIAGIGRGDTacIIYTSGTGGAPRGVMQHHG 205
Cdd:cd05929 82 CAIIEIKAAALVCGLFTG-------GGALDGLEDYEA---AEGGSPETP-IEDEAAGWK--MLYSGGTTGRPKGIKRGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 206 AILCNVA-GAAEILIedFGIADDERFLSFLPLSHAYEHT--------GGQflpiSVGAQIYYAEGLEKLasnIEETRPTI 276
Cdd:cd05929 149 GGPPDNDtLMAAALG--FGPGADSVYLSPAPLYHAAPFRwsmtalfmGGT----LVLMEKFDPEEFLRL---IERYRVTF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 277 MVVVPRLFevlrTRIMKqvqkqgglaeklmntalevgerraagkpkfgdglrdalvgrlLKPKIRQRFG-GRIKAMVSGG 355
Cdd:cd05929 220 AQFVPTMF----VRLLK------------------------------------------LPEAVRNAYDlSSLKRVIHAA 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 356 APLNPEVG-IFFESMGLTMLQGYGQTEAGPVISCN------------RPAAGiAMHSVGPAMRGVDIRiaEDGEILVRGE 422
Cdd:cd05929 254 APCPPWVKeQWIDWGGPIIWEYYGGTEGQGLTIINgeewlthpgsvgRAVLG-KVHILDEDGNEVPPG--EIGEVYFANG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 423 LVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkkp 502
Cdd:cd05929 331 PGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISG-GVNIYPQEIENALIAHPKVLDAAVVG---- 405
|
490
....*....|.
gi 2786869514 503 yivgliVPDAE 513
Cdd:cd05929 406 ------VPDEE 410
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-514 |
2.34e-14 |
|
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: 74.73 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 182 GDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAeiliedfGIADDERFLSFLPLSHAYEHTGGQFLPISV---GAQIYY 258
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGA-------DFGTGEFTPSEDAHKAAAAAAGTVMFPAPPlmhGTGSWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 259 AEGLEKlasnieeTRPTIMVVVPRL--FEVLRTrimkqVQKQGglaeklMNTALEVGErrAAGKPkfgdgLRDALVGRll 336
Cdd:cd05924 76 AFGGLL-------GGQTVVLPDDRFdpEEVWRT-----IEKHK------VTSMTIVGD--AMARP-----LIDALRDA-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 337 kpkirqrfGGR----IKAMVSGGAPLNPEV-GIFFESM-GLTMLQGYGQTEAGpviscnrpAAGIAMHSVGPAMRGVDIR 410
Cdd:cd05924 129 --------GPYdlssLFAISSGGALLSPEVkQGLLELVpNITLVDAFGSSETG--------FTGSGHSAGSGPETGPFTR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 411 IAED------------------GEILVRGeLVMQGYWHNEAETERTIK--DG--WLHTGDIGHVDDKGRIVITDRKkDMI 468
Cdd:cd05924 193 ANPDtvvldddgrvvppgsggvGWIARRG-HIPLGYYGDEAKTAETFPevDGvrYAVPGDRATVEADGTVTLLGRG-SVC 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2786869514 469 VNDKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:cd05924 271 INTGGEKVFPEEVEEALKSHPAVYDVLVVG----------RPDERW 306
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
51-513 |
3.47e-14 |
|
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: 75.07 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 51 LAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTyitntERDH-----AHILDNSGAKAVivstekLLRPL 125
Cdd:cd17651 33 LAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL-----DPAYpaerlAFMLADAGPVLV------LTHPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 126 HGALQAsGIADHVIGIDDlhrqqssgflfhrwdsmfAGDAAEARQAveqRIAGIGRGDTACIIYTSGTGGAPRGVMQHHG 205
Cdd:cd17651 102 LAGELA-VELVAVTLLDQ------------------PGAAAGADAE---PDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 206 AILCNVAGAAEIliedFGIADDERFLSFLPLSH--AYEHTggqFLPISVGAQIYYAEgleklasniEETRPTimvvVPRL 283
Cdd:cd17651 160 SLANLVAWQARA----SSLGPGARTLQFAGLGFdvSVQEI---FSTLCAGATLVLPP---------EEVRTD----PPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 284 FEVLRTRIMKQVQKQGGLAEKLMNTALEVGERRAAgkpkfgdgLRDALVG--RL-LKPKIRQRFGGRikamvsggaplnP 360
Cdd:cd17651 220 AAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAA--------LRYLLTGgeQLvLTEDLREFCAGL------------P 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 361 evgiffesmGLTMLQGYGQTEAgPVISC----NRPAAGIAMHSVGPAMRGVDIRIAED----------GEILVRGELVMQ 426
Cdd:cd17651 280 ---------GLRLHNHYGPTET-HVVTAlslpGDPAAWPAPPPIGRPIDNTRVYVLDAalrpvppgvpGELYIGGAGLAR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 427 GYWHNEAET-ERTIKDGWL------HTGDIGHVDDKGRIVITDRKKDMiVNDKGDNVAPQKVEGMLTLQPEIGQAMV--- 496
Cdd:cd17651 350 GYLNRPELTaERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQ-VKIRGFRIELGEIEAALARHPGVREAVVlar 428
|
490 500
....*....|....*....|
gi 2786869514 497 ---AGDKKpyIVGLIVPDAE 513
Cdd:cd17651 429 edrPGEKR--LVAYVVGDPE 446
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
377-514 |
3.48e-14 |
|
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: 73.98 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 377 YGQTEAGpVISCNRPAAGIAMHSVGPAMRGVDIRI-----AEDGEILVRGELVMQGYWHNEAETertiKDGWLHTGDIGH 451
Cdd:cd17633 143 YGTSELS-FITYNFNQESRPPNSVGRPFPNVEIEIrnadgGEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGY 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786869514 452 VDDKGRIVITDRKKDMIVNdKGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPDAEW 514
Cdd:cd17633 218 VDEEGYLYLVGRESDMIII-GGINIFPTEIESVLKAIPGIEEAIVVG----------IPDARF 269
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
16-509 |
5.51e-14 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 74.81 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 16 LKRAAEKGDLPFLGArIGGSWQTISWN--EAAEQVCLLAENLR-ALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP 92
Cdd:cd05928 18 KEKAGKRPPNPALWW-VNGKGDEVKWSfrELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 93 TYITNTERDHAHILDNSGAKAVIVSTEKLLRPLHGALQASGIADHVIGIDdlhrqqssgflfHRWDSM-----FAGDAAE 167
Cdd:cd05928 97 GTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSE------------KSRDGWlnfkeLLNEAST 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 168 ARQAVEQriagiGRGDTACIIYTSGTGGAPRGVMQHHGAILcnvagaaeiliedFGIADDERFLSFLPLSHAYEHT---- 243
Cdd:cd05928 165 EHHCVET-----GSQEPMAIYFTSGTTGSPKMAEHSHSSLG-------------LGLKVNGRYWLDLTASDIMWNTsdtg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 244 ------GGQFLPISVGAQIYyAEGLEKLASNI----EETRP-TIMVVVPRLFEVLRTRIMKQVQKQgglaeklmntalev 312
Cdd:cd05928 227 wiksawSSLFEPWIQGACVF-VHHLPRFDPLVilktLSSYPiTTFCGAPTVYRMLVQQDLSSYKFP-------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 313 gerraagkpkfgdglrdalvgrllkpkirqrfggRIKAMVSGGAPLNPEV-GIFFESMGLTMLQGYGQTEAGpVISCNRP 391
Cdd:cd05928 292 ----------------------------------SLQHCVTGGEPLNPEVlEKWKAQTGLDIYEGYGQTETG-LICANFK 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 392 AAGIAMHSVGPAMRGVDIRIAED-GEILVRGE--------------LVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKG 456
Cdd:cd05928 337 GMKIKPGSMGKASPPYDVQIIDDnGNVLPPGTegdigirvkpirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDG 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2786869514 457 RIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPyIVGLIV 509
Cdd:cd05928 417 YFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEVV 467
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
37-525 |
1.47e-13 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 73.17 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIv 116
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 stekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdAAEARQAveqriagigrgdtACIIYTSGTGGA 196
Cdd:cd17649 90 ------------------------------------------------THHPRQL-------------AYVIYTSGSTGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGAIlcnvAGAAEILIEDFGIADDERFLSFLPLSH--AYEhtgGQFLPISVGAQIYYA-----EGLEKLASNI 269
Cdd:cd17649 109 PKGVAVSHGPL----AAHCQATAERYGLTPGDRELQFASFNFdgAHE---QLLPPLICGACVVLRpdelwASADELAEMV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 270 EETRPTIMVVVPR-LFEVLRtrimkqvqkqgglaeklmnTALEVGERRAagkpkfgdglrdalvgrllkpkirqrfgGRI 348
Cdd:cd17649 182 RELGVTVLDLPPAyLQQLAE-------------------EADRTGDGRP----------------------------PSL 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 349 KAMVSGGAPLNPEVGIFFESMGLTMLQGYGQTEA----------------GPVISCNRPAAGIAMHSVGPAMRGVDirIA 412
Cdd:cd17649 215 RLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEAtvtplvwkceagaaraGASMPIGRPLGGRSAYILDADLNPVP--VG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 413 EDGEILVRGELVMQGYwHNEAET--ERTIKDG-------WLHTGDI------GHVDDKGRIvitdrkkDMIVNDKGDNVA 477
Cdd:cd17649 293 VTGELYIGGEGLARGY-LGRPELtaERFVPDPfgapgsrLYRTGDLarwrddGVIEYLGRV-------DHQVKIRGFRIE 364
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2786869514 478 PQKVEGMLTLQPEIGQAMV---AGDKKPYIVGLIVPDAEWTLEWCREQGKQ 525
Cdd:cd17649 365 LGEIEAALLEHPGVREAAVvalDGAGGKQLVAYVVLRAAAAQPELRAQLRT 415
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
37-502 |
1.68e-13 |
|
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: 72.77 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCitVPTYITNTERDH--AHILDNSGAKAV 114
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA--VAALINYNLRGEslAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 115 IVstekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTG 194
Cdd:cd05940 80 VV------------------------------------------------------------------DAALYIYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 195 GAPRGVMQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLSHAYEHTGGQFLPISVGAQIYYAEGLEklASN----IE 270
Cdd:cd05940 94 GLPKAAIISHRRAWRGGAFFAGS----GGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFS--ASNfwddIR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 271 ETRPTIMVVVprlfevlrtrimkqvqkqGGLAEKLMNTALEVGERRAAGKPKFGDGLRdalvgrllkPKIRQRFGGRIKA 350
Cdd:cd05940 168 KYQATIFQYI------------------GELCRYLLNQPPKPTERKHKVRMIFGNGLR---------PDIWEEFKERFGV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 mvsggaplnPEVGIFfesmgltmlqgYGQTEaGPVISCNRP----AAGIAMHSVGPAMRGVDIRIAEDGEILVR------ 420
Cdd:cd05940 221 ---------PRIAEF-----------YAATE-GNSGFINFFgkpgAIGRNPSLLRKVAPLALVKYDLESGEPIRdaegrc 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 421 --------GELV--------MQGYWHNEAETERTIK------DGWLHTGDIGHVDDKGRIVITDRkkdmiVND----KGD 474
Cdd:cd05940 280 ikvprgepGLLIsrinplepFDGYTDPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYFVDR-----LGDtfrwKGE 354
|
490 500
....*....|....*....|....*...
gi 2786869514 475 NVAPQKVEGMLTLQPEIGQAMVAGDKKP 502
Cdd:cd05940 355 NVSTTEVAAVLGAFPGVEEANVYGVQVP 382
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
37-537 |
2.52e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 73.66 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:PRK12467 536 QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLR-PLHGALQASGIADhvigiddlhrqqssgflfhrwdsmfAGDAAEARQAVEQRIAgIGRGDTACIIYTSGTGG 195
Cdd:PRK12467 616 QSHLLAQlPVPAGLRSLCLDE-------------------------PADLLCGYSGHNPEVA-LDPDNLAYVIYTSGSTG 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 196 APRGVMQHHGAILCNVAGAAeiliEDFGIADDERFLSFLPLSHAYEHTgGQFLPISVGAQIY-----YAEGLEKLASNIE 270
Cdd:PRK12467 670 QPKGVAISHGALANYVCVIA----ERLQLAADDSMLMVSTFAFDLGVT-ELFGALASGATLHllppdCARDAEAFAALMA 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 271 ETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntalevgerraagkpkfgdgLRDALVGrLLKPKIRQRFGGRIKA 350
Cdd:PRK12467 745 DQGVTVLKIVPSHLQAL---------------------------------------LQASRVA-LPRPQRALVCGGEALQ 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 mVSGGAPlnpevgIFFESMGLTMLQGYGQTEAGPVIS---CNRPAAGIAMHSVGPAMRGVDIRIAED----------GEI 417
Cdd:PRK12467 785 -VDLLAR------VRALGPGARLINHYGPTETTVGVStyeLSDEERDFGNVPIGQPLANLGLYILDHylnpvpvgvvGEL 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 418 LVRGELVMQGYWHNEAET-ERTIKD------GWLH-TGDIGHVDDKGRIVITDRkKDMIVNDKGDNVAPQKVEGMLTLQP 489
Cdd:PRK12467 858 YIGGAGLARGYHRRPALTaERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGR-MDHQVKIRGFRIELGEIEARLLAQP 936
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2786869514 490 EIGQAMV---AGDKKPYIVGLIVPDAewTLEWCREQGKQFDCKKV--QELPEF 537
Cdd:PRK12467 937 GVREAVVlaqPGDAGLQLVAYLVPAA--VADGAEHQATRDELKAQlrQVLPDY 987
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-554 |
3.22e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 13 ELFLKRAAEKGDLPflgARIGGSwQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVP 92
Cdd:PRK12316 4555 QLVAERARMTPDAV---AVVFDE-EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 93 TYITNTERDHAHILDNSGAKAVIVSTEKLLR-PLhgalqASGIADHVIGIDDlhrqqssgflfhRWDSMfaGDAAEARQA 171
Cdd:PRK12316 4631 LDPEYPRERLAYMMEDSGAALLLTQSHLLQRlPI-----PDGLASLALDRDE------------DWEGF--PAHDPAVRL 4691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 172 VEQRIagigrgdtACIIYTSGTGGAPRGVMQHHGAILCNVAGAAeiliEDFGIADDERFLSFLPLSHAYEHTgGQFLPIS 251
Cdd:PRK12316 4692 HPDNL--------AYVIYTSGSTGRPKGVAVSHGSLVNHLHATG----ERYELTPDDRVLQFMSFSFDGSHE-GLYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 252 VGAQIYYAE-GL---EKLASNIEETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEVGERRaaGKPkfgdgl 327
Cdd:PRK12316 4759 NGASVVIRDdSLwdpERLYAEIHEHRVTVLVFPPVYLQQL----------------------AEHAERD--GEP------ 4808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 328 rdalvgrllkPKIRQR-FGGriKAMVSGGAPLnpevgIFFESMGLTMLQGYGQTEAGPVISCNR----PAAGIAMHSVGP 402
Cdd:PRK12316 4809 ----------PSLRVYcFGG--EAVAQASYDL-----AWRALKPVYLFNGYGPTETTVTVLLWKardgDACGAAYMPIGT 4871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 403 AMRGVDIRIAED----------GEILVRGELVMQGYWHNEAET-ERTIKD------GWLH-TGDI------GHVDDKGRI 458
Cdd:PRK12316 4872 PLGNRSGYVLDGqlnplpvgvaGELYLGGEGVARGYLERPALTaERFVPDpfgapgGRLYrTGDLaryradGVIDYLGRV 4951
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 459 vitdrkkDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVA---GDKKPYIVGLIVPDAEWTLEWCREQGkqfdckkvqelp 535
Cdd:PRK12316 4952 -------DHQVKIRGFRIELGEIEARLREHPAVREAVVIaqeGAVGKQLVGYVVPQDPALADADEAQA------------ 5012
|
570
....*....|....*....
gi 2786869514 536 EFRNAVRAAVDRVNKDLSV 554
Cdd:PRK12316 5013 ELRDELKAALRERLPEYMV 5031
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
398-536 |
8.07e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 70.96 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 398 HSVGPAMRGVDIRI----------AEDGEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDM 467
Cdd:PRK07638 307 NSVGRPFHNVQVRIcneageevqkGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNM 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786869514 468 IVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY---IVGLIV---PDAEWTLEWCREQGKQFDCKK----VQELPE 536
Cdd:PRK07638 387 ILFG-GINIFPEEIESVLHEHPAVDEIVVIGVPDSYwgeKPVAIIkgsATKQQLKSFCLQRLSSFKIPKewhfVDEIPY 464
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1-517 |
8.64e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.89 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 1 MLSDIDSANNLVELFLKRAAEK-GDLPFLGARIGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIA 79
Cdd:PRK07008 1 LLGQMMDMPLLISSLIAHAARHaGDTEIVSRRVEGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 80 DLAIMASG--CITV-P-------TYITNTERDHAHILDNSGAKavivstekLLRPLHGalQASGIADHVIGIDDLHRQQS 149
Cdd:PRK07008 81 YYGVSGSGavCHTInPrlfpeqiAYIVNHAEDRYVLFDLTFLP--------LVDALAP--QCPNVKGWVAMTDAAHLPAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 150 SGFLFHRWDSMFAGDAAEARQAVEQRIAgigrgdtACIIYTSGTGGAPRGVMQHHGAILCNVAGAAeiLIEDFGIADDER 229
Cdd:PRK07008 151 STPLLCYETLVGAQDGDYDWPRFDENQA-------SSLCYTSGTTGNPKGALYSHRSTVLHAYGAA--LPDAMGLSARDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 230 FLSFLPLSHAyeHTGGqfLPIS---VGAQIYY------AEGLEKLasnIEETRPTIMVVVPRLFEVLRTRImkqvqKQGG 300
Cdd:PRK07008 222 VLPVVPMFHV--NAWG--LPYSaplTGAKLVLpgpdldGKSLYEL---IEAERVTFSAGVPTVWLGLLNHM-----REAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 301 LaeklmntalevgerraagkpkfgdglrdalvgrllkpkirqRFGgRIKAMVSGGAPLNPE-VGIFFESMGLTMLQGYGQ 379
Cdd:PRK07008 290 L-----------------------------------------RFS-TLRRTVIGGSACPPAmIRTFEDEYGVEVIHAWGM 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 380 TEAGPV-ISCNRPAAGIAM-----HSV----GPAMRGVDIRIAED------------GEILVRGELVMQGYWHNEAETer 437
Cdd:PRK07008 328 TEMSPLgTLCKLKWKHSQLpldeqRKLlekqGRVIYGVDMKIVGDdgrelpwdgkafGDLQVRGPWVIDRYFRGDASP-- 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 438 tIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAG------DKKPYIVGLIVPD 511
Cdd:PRK07008 406 -LVDGWFPTGDVATIDADGFMQITDRSKDVI-KSGGEWISSIDIENVAVAHPAVAEAACIAcahpkwDERPLLVVVKRPG 483
|
....*.
gi 2786869514 512 AEWTLE 517
Cdd:PRK07008 484 AEVTRE 489
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
11-513 |
1.32e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGDLPFLGARIGGSwqTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCIT 90
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRRCDGTS--ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 91 VptyitnterdhahILDNSGAKAVIVSTEKLLRPLHGALQASGIADHVIGIDDLHRQQSSGFLFHRWDSMFAGDAAEARQ 170
Cdd:PRK05857 94 V-------------MADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 171 AVEqriAGIGRGDTACIIYTSGTGGAPRGVMqhhgaiLCNVAGAA--EILIEDfGIA-----DDERFLSFLPLSHayehT 243
Cdd:PRK05857 161 AGN---ADQGSEDPLAMIFTSGTTGEPKAVL------LANRTFFAvpDILQKE-GLNwvtwvVGETTYSPLPATH----I 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 244 GGQFLPISV----GAQIYYAEGLEKLASNIEETRPTIMVVVPRLFevlrTRIMKQVqkqgglaeklmntalevgerraag 319
Cdd:PRK05857 227 GGLWWILTClmhgGLCVTGGENTTSLLEILTTNAVATTCLVPTLL----SKLVSEL------------------------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 320 kpKFGDGLRDALvgRLLKpkirqrFGGR--IKAMVSggaplnpevgiFFESMGLTMLQGYGQTEAGPVISC----NRPAA 393
Cdd:PRK05857 279 --KSANATVPSL--RLVG------YGGSraIAADVR-----------FIEATGVRTAQVYGLSETGCTALClptdDGSIV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 394 GIAMHSVGPAMRGVDIRIAED----------------GEILVRGELVMQGYWHNEAETERTIKDGWLHTGDIGHVDDKGR 457
Cdd:PRK05857 338 KIEAGAVGRPYPGVDVYLAATdgigptapgagpsasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGF 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 458 IVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY---IVGL-IVPDAE 513
Cdd:PRK05857 418 FYIKGRSSEMIICG-GVNIAPDEVDRIAEGVSGVREAACYEIPDEEfgaLVGLaVVASAE 476
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
34-546 |
6.52e-12 |
|
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: 68.50 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 34 GSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKa 113
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPK- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VIVSTEKLLRP---------LHGALQASGI-ADHVIgidDLHRQQSSGFLFHR-----WDSMFAGdaAEARQAVEqriag 178
Cdd:cd05967 157 LIVTASCGIEPgkvvpykplLDKALELSGHkPHHVL---VLNRPQVPADLTKPgrdldWSELLAK--AEPVDCVP----- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 179 IGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILiedFGIADDERFLSFLPL----SHAYehtggqflpisvga 254
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNI---YGIKPGDVWWAASDVgwvvGHSY-------------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 255 qIYYAEGLEKLASNIEETRPtimVVVP------RLFEVLRTRIMKQVQkqgglaeklmnTALevgerRAAGK-PKFGDGL 327
Cdd:cd05967 290 -IVYGPLLHGATTVLYEGKP---VGTPdpgafwRVIEKYQVNALFTAP-----------TAI-----RAIRKeDPDGKYI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 328 RDALVGRLlkpkirqrfggriKAMVSGGAPLNPEVGIFFE-SMGLTMLQGYGQTEAGPVISCNrpAAGIAMHSV-----G 401
Cdd:cd05967 350 KKYDLSSL-------------RTLFLAGERLDPPTLEWAEnTLGVPVIDHWWQTETGWPITAN--PVGLEPLPIkagspG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 402 PAMRGVDIRIAED----------GEILVRGEL---VMQGYWHNEaetERTIK------DGWLHTGDIGHVDDKGRIVITD 462
Cdd:cd05967 415 KPVPGYQVQVLDEdgepvgpnelGNIVIKLPLppgCLLTLWKND---ERFKKlylskfPGYYDTGDAGYKDEDGYLFIMG 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 463 RKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKPY----IVGLIVPDAewtlewcreqgkqfDCKKVQElpEFR 538
Cdd:cd05967 492 RTDDVI-NVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELkgqvPLGLVVLKE--------------GVKITAE--ELE 554
|
....*...
gi 2786869514 539 NAVRAAVD 546
Cdd:cd05967 555 KELVALVR 562
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
37-513 |
8.63e-12 |
|
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: 67.33 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEkllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagigrgDTACIIYTSGTGGA 196
Cdd:cd17643 91 DPD---------------------------------------------------------------DLAYVIYTSGSTGR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFlplsHAY-------EhtggQFLPISVGAQiyyaegleklasni 269
Cdd:cd17643 108 PKGVVVSHA----NVLALFAATQRWFGFNEDDVWTLF----HSYafdfsvwE----IWGALLHGGR-------------- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 270 eetrptiMVVVPRlfEVLRT-RIMKQVQKQGGLA---------EKLMNTALEVGERRAAgkpkfgdgLRdaLVgrllkpk 339
Cdd:cd17643 162 -------LVVVPY--EVARSpEDFARLLRDEGVTvlnqtpsafYQLVEAADRDGRDPLA--------LR--YV------- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 340 irqrfggrikamVSGGAPLNPE-VGIFFESMGL---TMLQGYGQTEAgPVISCNRP-----AAGIAMHSVGPAMRGVDIR 410
Cdd:cd17643 216 ------------IFGGEALEAAmLRPWAGRFGLdrpQLVNMYGITET-TVHVTFRPldaadLPAAAASPIGRPLPGLRVY 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 411 IAED----------GEILVRGELVMQGYWHNEAET-ERTIKDGW-------LHTGDIGHVDDKGRIVITDRkKDMIVNDK 472
Cdd:cd17643 283 VLDAdgrpvppgvvGELYVSGAGVARGYLGRPELTaERFVANPFggpgsrmYRTGDLARRLPDGELEYLGR-ADEQVKIR 361
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2786869514 473 GDNVAPQKVEGMLTLQPEIGQAMVA----GDKKPYIVGLIVPDAE 513
Cdd:cd17643 362 GFRIELGEIEAALATHPSVRDAAVIvredEPGDTRLVAYVVADDG 406
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-502 |
1.83e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 66.33 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 182 GDTACIIYTSGTGGAPRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPL-------------SHAYEHTGgqfl 248
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHG----TFAAQIDALRQLYGIRPGEVDLATFPLfalfgpalgltsvIPDMDPTR---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 249 PISVGAQiyyaegleKLASNIEETRPTIMVVVPRLFEVLrTRIMKQVQKQGGLAEKLMntalevgerrAAGKPkfgdgLR 328
Cdd:cd05910 157 PARADPQ--------KLVGAIRQYGVSIVFGSPALLERV-ARYCAQHGITLPSLRRVL----------SAGAP-----VP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 329 DALVGRLlkpkirqrfggriKAMVSGGAP-LNPevgiffesmgltmlqgYGQTEAGPVISCN---------RPAAGIAMH 398
Cdd:cd05910 213 IALAARL-------------RKMLSDEAEiLTP----------------YGATEALPVSSIGsrellatttAATSGGAGT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 399 SVGPAMRGVDIRI-------------------AEDGEILVRGELVMQGYWHNEAETERT-IKDG----WLHTGDIGHVDD 454
Cdd:cd05910 264 CVGRPIPGVRVRIieiddepiaewddtlelprGEIGEITVTGPTVTPTYVNRPVATALAkIDDNsegfWHRMGDLGYLDD 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2786869514 455 KGRIVITDRKKDMIVNDKGdNVAPQKVEGMLTLQPEIGQAMVAGDKKP 502
Cdd:cd05910 344 EGRLWFCGRKAHRVITTGG-TLYTEPVERVFNTHPGVRRSALVGVGKP 390
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-525 |
7.15e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLR-PLHGALQAsgiadhvigiddlhrqqssgFLFHRWDSMfagdAAEARQAVEQRIAGigrGDTACIIYTSGTGG 195
Cdd:PRK12316 2107 QRHLLERlPLPAGVAR--------------------LPLDRDAEW----ADYPDTAPAVQLAG---ENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 196 APRGVMQHHGAIL--CNVAGAAeiliedFGIADDERFLSFLPLSHAYEHTgGQFLPISVGAQIYYAEG----LEKLASNI 269
Cdd:PRK12316 2160 LPKGVAVSHGALVahCQAAGER------YELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDelwdPEQLYDEM 2232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 270 EETRPTIMVVVPRLFEVLrtrimkqvqkqgglaeklmntaLEVGERraAGKPkfgdglrdalvgrllkPKIRQR-FGGri 348
Cdd:PRK12316 2233 ERHGVTILDFPPVYLQQL----------------------AEHAER--DGRP----------------PAVRVYcFGG-- 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 349 KAMVSGGAPLN----PEVGIFfesmgltmlQGYGQTEA---------GPVISCN-------RPAAGIAMHSVGPAMRGVD 408
Cdd:PRK12316 2271 EAVPAASLRLAwealRPVYLF---------NGYGPTEAvvtpllwkcRPQDPCGaayvpigRALGNRRAYILDADLNLLA 2341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 409 IRIAedGEILVRGELVMQGYWHNEAET-ERTIKDGWLH-------TGDI------GHVDDKGRIvitdrkkDMIVNDKGD 474
Cdd:PRK12316 2342 PGMA--GELYLGGEGLARGYLNRPGLTaERFVPDPFSAsgerlyrTGDLaryradGVVEYLGRI-------DHQVKIRGF 2412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 475 NVAPQKVEGMLTLQPEIGQAMV---AGDKKPYIVGLIVPD--AEWTLEWCREQGKQ 525
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAVVvaqDGASGKQLVAYVVPDdaAEDLLAELRAWLAA 2468
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
10-482 |
1.25e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 64.37 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 10 NLVELFLKRAAEKGD------LPFLGARiGGSWQTISWNEaaeqvclLAENLRALGLR------DGDRVCLVSENRPEWC 77
Cdd:PRK07769 22 NLVRHVERWAKVRGDklayrfLDFSTER-DGVARDLTWSQ-------FGARNRAVGARlqqvtkPGDRVAILAPQNLDYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 78 IADLAIMASGCITVPTYITN----TERDHAhILDNSGAKAVIVSTE------KLLRPLHGALQASGIAdhVIGIDDlhrq 147
Cdd:PRK07769 94 IAFFGALYAGRIAVPLFDPAepghVGRLHA-VLDDCTPSAILTTTDsaegvrKFFRARPAKERPRVIA--VDAVPD---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 148 qssgflfhrwdsmfagDAAEARQAVEqriagIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGaaeiLIEDFGIADD 227
Cdd:PRK07769 167 ----------------EVGATWVPPE-----ANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQ----VIDALEGQEG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 228 ERFLSFLPLSHAYehtgGQ---FLPISVGAQIyyaegleklasnieetrpTIMVvvPRLFeVLRT-RIMKQVQKQGGLAE 303
Cdd:PRK07769 222 DRGVSWLPFFHDM----GLitvLLPALLGHYI------------------TFMS--PAAF-VRRPgRWIRELARKPGGTG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 304 KLM----NTALEVGERRaaGKPKFGDGLRDAlvgrllkpkirqrfgGRIKAMVSGGAPLNP-EVGIFFESMGLTMLQ--- 375
Cdd:PRK07769 277 GTFsaapNFAFEHAAAR--GLPKDGEPPLDL---------------SNVKGLLNGSEPVSPaSMRKFNEAFAPYGLPpta 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 376 ---GYGQTEA------------GPVISCNR---------------PAAgIAMHSVGPAMRG-----VDIRIAED------ 414
Cdd:PRK07769 340 ikpSYGMAEAtlfvsttpmdeePTVIYVDRdelnagrfvevpadaPNA-VAQVSAGKVGVSewaviVDPETASElpdgqi 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 GEILVRGELVMQGYWHNEAETERTIK------------------DGWLHTGDIGhVDDKGRIVITDRKKDMIVNDkGDNV 476
Cdd:PRK07769 419 GEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshaegapddALWVRTGDYG-VYFDGELYITGRVKDLVIID-GRNH 496
|
....*.
gi 2786869514 477 APQKVE 482
Cdd:PRK07769 497 YPQDLE 502
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
13-511 |
2.30e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 63.12 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 13 ELFLKRAAEKGdlpfLGARIGGswQTISWNE----AAEQVCLLaenlraLGLRDGDR---VCLVSENRPEWCIADLAIMA 85
Cdd:PRK13388 7 QLLRDRAGDDT----IAVRYGD--RTWTWREvlaeAAARAAAL------IALADPDRplhVGVLLGNTPEMLFWLAAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 86 SGCITVPtyITNTERDHAHILDNSGAKAVIVSTEKLLRPLHGALQASGiaDHVIGIDDlhrqqssgflfHRWDSMFAGdA 165
Cdd:PRK13388 75 GGYVLVG--LNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLDLPG--VRVLDVDT-----------PAYAELVAA-A 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 166 AEARQAVEqriagIGRGDTACIIYTSGTGGAPRGVMQHHGailcNVAGAAEILIEDFG-IADDERFLSfLPLSHAYEHTG 244
Cdd:PRK13388 139 GALTPHRE-----VDAMDPFMLIFTSGTTGAPKAVRCSHG----RLAFAGRALTERFGlTRDDVCYVS-MPLFHSNAVMA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 245 GQFLPISVGAqiyyaegleklasnieetrptiMVVVPRLFEVlrTRIMKQVQKQGGlaeKLMNTaleVGERRA-----AG 319
Cdd:PRK13388 209 GWAPAVASGA----------------------AVALPAKFSA--SGFLDDVRRYGA---TYFNY---VGKPLAyilatPE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 320 KPKFGDG-LRDALvGRLLKPKIRQRFGGRikamvsggaplnpevgiffesMGLTMLQGYGQTEAGPVI---------SCN 389
Cdd:PRK13388 259 RPDDADNpLRVAF-GNEASPRDIAEFSRR---------------------FGCQVEDGYGSSEGAVIVvrepgtppgSIG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 390 RPAAGIAM---HSVGPAMRGvdiRIAEDGEIL----VRGELV-------MQGYWHNEAETERTIKDGWLHTGDIGHVDDK 455
Cdd:PRK13388 317 RGAPGVAIynpETLTECAVA---RFDAHGALLnadeAIGELVntagagfFEGYYNNPEATAERMRHGMYWSGDLAYRDAD 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 456 GRIVITDRKKDMIVNDkGDNVAPQKVEGMLTLQPEIGQAMVAGdkkpyivgliVPD 511
Cdd:PRK13388 394 GWIYFAGRTADWMRVD-GENLSAAPIERILLRHPAINRVAVYA----------VPD 438
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
42-513 |
3.67e-10 |
|
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: 62.44 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 42 NEAAEQVcllAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITvPTYITNTERDH-AHILDNSGAKAVIVStek 120
Cdd:cd05939 10 NEYSNKV---ANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVET-ALINSNLRLESlLHCITVSKAKALIFN--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 121 LLRPLHgaLQASgiadhvigiDDLHRQQSSGFlfhrwdsmfagdaaearqaveqriagigrGDTACIIYTSGTGGAPRGV 200
Cdd:cd05939 83 LLDPLL--TQSS---------TEPPSQDDVNF-----------------------------RDKLFYIYTSGTTGLPKAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 201 MQHHGAILCNVAGAAEIliedFGIADDERFLSFLPLshaYeHTGGQFLpiSVGAQIYYAEGL---EKL-ASNI----EET 272
Cdd:cd05939 123 VIVHSRYYRIAAGAYYA----FGMRPEDVVYDCLPL---Y-HSAGGIM--GVGQALLHGSTVvirKKFsASNFwddcVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 273 RPTImvvvprlfevlrtrimkqVQKQGGLAEKLMNTALEVGERRAAGKPKFGDGLRdalvgrllkPKIRQRFGGRIKAmv 352
Cdd:cd05939 193 NCTI------------------VQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLR---------PQIWEQFVRRFGI-- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 353 sggaplnPEVGIFfesmgltmlqgYGQTEAGPVISC--NRPAAGIAMHSVGPAMRGVD-IRIAEDGEILVR--------- 420
Cdd:cd05939 244 -------PQIGEF-----------YGATEGNSSLVNidNHVGACGFNSRILPSVYPIRlIKVDEDTGELIRdsdglcipc 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 421 -----GELVMQ-----------GYWhNEAETERTI-KDGWLH------TGDIGHVDDKGRIVITDRKKDMIvNDKGDNVA 477
Cdd:cd05939 306 qpgepGLLVGKiiqndplrrfdGYV-NEGATNKKIaRDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTF-RWKGENVS 383
|
490 500 510
....*....|....*....|....*....|....*.
gi 2786869514 478 PQKVEGMltLQPEIGQAMVAgdkkpyIVGLIVPDAE 513
Cdd:cd05939 384 TTEVEGI--LSNVLGLEDVV------VYGVEVPGVE 411
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
37-513 |
1.35e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 60.41 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 stekllrplhgalqasgiadhvigiddlhrqqssgflfhrwdsmfagdaaearqaveqriagiGRGDTACIIYTSGTGGA 196
Cdd:cd12115 103 ---------------------------------------------------------------DPDDLAYVIYTSGSTGR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 197 PRGV-MQHHGAI-LCNVAGAaeilieDFGIADDERFLSFLP----LShAYEhtggQFLPISVGAQIYYAEGLEKLASNIE 270
Cdd:cd12115 120 PKGVaIEHRNAAaFLQWAAA------AFSAEELAGVLASTSicfdLS-VFE----LFGPLATGGKVVLADNVLALPDLPA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 271 ETRPTIMVVVPRLfevlrtriMKQVQKQGGLAEKLMNTALevgerraAGKPKFGDgLRDALVGRLLKPKIRQRFGGRIKA 350
Cdd:cd12115 189 AAEVTLINTVPSA--------AAELLRHDALPASVRVVNL-------AGEPLPRD-LVQRLYARLQVERVVNLYGPSEDT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 MVSGGAPLNPEvgiffesmgltmlqgyGQTEagpvISCNRPAAGIAMHSVGPAMRGVDIRIAedGEILVRGELVMQGYWH 430
Cdd:cd12115 253 TYSTVAPVPPG----------------ASGE----VSIGRPLANTQAYVLDRALQPVPLGVP--GELYIGGAGVARGYLG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 431 NEAET-ERTIKDGWL------HTGDIGHVDDKGRIVITDRKKDMiVNDKGDNVAPQKVEGMLTLQPEIGQAMVA--GDKK 501
Cdd:cd12115 311 RPGLTaERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQ-VKVRGFRIELGEIEAALRSIPGVREAVVVaiGDAA 389
|
490
....*....|....
gi 2786869514 502 P--YIVGLIVPDAE 513
Cdd:cd12115 390 GerRLVAYIVAEPG 403
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-513 |
2.40e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.74 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAkAVIV 116
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGV-QLLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLR--PLHGALQasgiadhVIGIDdlhrqqssgflfhRWDSMFAGDAAEarqAVEQRIAGIgrgDTACIIYTSGTG 194
Cdd:PRK12316 614 SQSHLGRklPLAAGVQ-------VLDLD-------------RPAAWLEGYSEE---NPGTELNPE---NLAYVIYTSGST 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 195 GAPRGVMQHHGAiLCNVAGAAEiliEDFGIADDERFLSFLPLSHAYEHTgGQFLPISVGAQIYYAEG-----LEKLASNI 269
Cdd:PRK12316 668 GKPKGAGNRHRA-LSNRLCWMQ---QAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVAAPgdhrdPAKLVELI 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 270 EETRPTIMVVVPRLFEVLrtrimkqvQKQGGLAEKLMNTALEVGerraagkpkfGDGLRDALVGRLLKPKirqrfggrik 349
Cdd:PRK12316 743 NREGVDTLHFVPSMLQAF--------LQDEDVASCTSLRRIVCS----------GEALPADAQEQVFAKL---------- 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 350 amvsggaplnPEVGIFfesmgltmlQGYGQTEA-------------GPVISCNRPAAGIAMHSVGPAMRGVDIRIAedGE 416
Cdd:PRK12316 795 ----------PQAGLY---------NLYGPTEAaidvthwtcveegGDSVPIGRPIANLACYILDANLEPVPVGVL--GE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 417 ILVRGELVMQGYWHNEAET-ERTIKDGWL------HTGDI------GHVDDKGRIvitdrkkDMIVNDKGDNVAPQKVEG 483
Cdd:PRK12316 854 LYLAGRGLARGYHGRPGLTaERFVPSPFVagermyRTGDLaryradGVIEYAGRI-------DHQVKLRGLRIELGEIEA 926
|
490 500 510
....*....|....*....|....*....|
gi 2786869514 484 MLTLQPEIGQAMVAGDKKPYIVGLIVPDAE 513
Cdd:PRK12316 927 RLLEHPWVREAAVLAVDGKQLVGYVVLESE 956
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
350-515 |
2.65e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 59.29 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 350 AMVSGGAPLNPEVGIFFESMGLTMLQGYGQTE-AGPVISCNRPaagiamhsvgpaMRGVDIRIaEDGEILVRGELVMQGY 428
Cdd:PRK07824 155 AVLVGGGPAPAPVLDAAAAAGINVVRTYGMSEtSGGCVYDGVP------------LDGVRVRV-EDGRIALGGPTLAKGY 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 429 wHNEAETERTIKDGWLHTGDIGHVDDkGRIVITDRkKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMVAGDKKP----YI 504
Cdd:PRK07824 222 -RNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGR-ADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDrlgqRV 298
|
170
....*....|.
gi 2786869514 505 VGLIVPDAEWT 515
Cdd:PRK07824 299 VAAVVGDGGPA 309
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
51-517 |
4.80e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 58.99 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 51 LAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASG--CITV-----PTYItnterdhAHILDNSGAKAVIvsTEKLLR 123
Cdd:PRK06018 52 VSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGaiCHTVnprlfPEQI-------AWIINHAEDRVVI--TDLTFV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 124 PLhgalqASGIADH-------VIGIDDLHRQQSS---GFLFHRWDSMFAGDAAearqaveqriAGIGRGDTAC-IIYTSG 192
Cdd:PRK06018 123 PI-----LEKIADKlpsveryVVLTDAAHMPQTTlknAVAYEEWIAEADGDFA----------WKTFDENTAAgMCYTSG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 193 TGGAPRGVMQHHGAilcNVAGAAEILIED-FGIADDERFLSFLPLSHAyEHTGGQFLPISVGAQIYYAEGLEKLASniee 271
Cdd:PRK06018 188 TTGDPKGVLYSHRS---NVLHALMANNGDaLGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLVMPGAKLDGAS---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 272 trptimvvvprLFEVLRTrimkqvqkqgglaEKLMNTAlevgerraaGKPKFGDGLRDALVGRLLK-PKIrqrfggriKA 350
Cdd:PRK06018 260 -----------VYELLDT-------------EKVTFTA---------GVPTVWLMLLQYMEKEGLKlPHL--------KM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 351 MVSGGAPLnPEVGI-FFESMGLTMLQGYGQTEAGPV--ISCNRP----AAGIAMHSV----GPAMRGVDIRIAED----- 414
Cdd:PRK06018 299 VVCGGSAM-PRSMIkAFEDMGVEVRHAWGMTEMSPLgtLAALKPpfskLPGDARLDVlqkqGYPPFGVEMKITDDagkel 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 -------GEILVRGELVMQGYWhnEAETERTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLTL 487
Cdd:PRK06018 378 pwdgktfGRLKVRGPAVAAAYY--RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVI-KSGGEWISSIDLENLAVG 454
|
490 500 510
....*....|....*....|....*....|....*.
gi 2786869514 488 QPEIGQAMVAG------DKKPYIVGLIVPDAEWTLE 517
Cdd:PRK06018 455 HPKVAEAAVIGvyhpkwDERPLLIVQLKPGETATRE 490
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
331-522 |
1.32e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 57.35 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 331 LVGRLLKpkIRQRFGgriKAMVSGgAPLNPEVGIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMhsvGPAMRGVDIR 410
Cdd:PRK08308 203 ILGRLLP--GTFQFH---AVMTSG-TPLPEAWFYKLRERTTYMMQQYGCSEAGCVSICPDMKSHLDL---GNPLPHVSVS 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 411 IAED----GEILVRgelvmqgywhneaetertIKDGWLHTGDIGHVDDKGRIVITDRKKDMIvNDKGDNVAPQKVEGMLT 486
Cdd:PRK08308 274 AGSDenapEEIVVK------------------MGDKEIFTKDLGYKSERGTLHFMGRMDDVI-NVSGLNVYPIEVEDVML 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2786869514 487 LQPEIGQAMVAGDKKPY---IVGLIVpDAEWTL------EWCREQ 522
Cdd:PRK08308 335 RLPGVQEAVVYRGKDPVageRVKAKV-ISHEEIdpvqlrEWCIQH 378
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
42-537 |
1.52e-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: 57.48 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 42 NEAAEQvclLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIVSTEkl 121
Cdd:cd17656 20 NERSNQ---LARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRH-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 122 lrpLHGALQASGIADHVIgiddlhrqqssgflfhrWDSMFAGDAAEARQAVEQRiagigrgDTACIIYTSGTGGAPRGVM 201
Cdd:cd17656 95 ---LKSKLSFNKSTILLE-----------------DPSISQEDTSNIDYINNSD-------DLLYIIYTSGTTGKPKGVQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 202 QHHGAILCNVAGAAEILIEDFGiaddERFLSFLPLSH--AYEHTggqFLPISVGAQIYYAEgleklasniEETRPTimvv 279
Cdd:cd17656 148 LEHKNMVNLLHFEREKTNINFS----DKVLQFATCSFdvCYQEI---FSTLLSGGTLYIIR---------EETKRD---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 280 VPRLFEVLRTRIMKQVQKQGGLAEKLMNtalevgERRAagKPKFGDGLrdalvgrllkpkirqrfggriKAMVSGGAPL- 358
Cdd:cd17656 208 VEQLFDLVKRHNIEVVFLPVAFLKFIFS------EREF--INRFPTCV---------------------KHIITAGEQLv 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 359 -NPEVGIFFESMGLTMLQGYGQTEAGPVISCN-RPAAGIA-MHSVGPAMRGVDIRIAED----------GEILVRGELVM 425
Cdd:cd17656 259 iTNEFKEMLHEHNVHLHNHYGPSETHVVTTYTiNPEAEIPeLPPIGKPISNTWIYILDQeqqlqpqgivGELYISGASVA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 426 QGYW-HNEAETERTIKDGW------LHTGDIGHVDDKGRIVITDRKKDMiVNDKGDNVAPQKVEGMLTLQPEIGQAMV-- 496
Cdd:cd17656 339 RGYLnRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQ-VKIRGYRIELGEIEAQLLNHPGVSEAVVld 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2786869514 497 ----AGDKkpYIVGLIVPDAEWTLEWCREqgkqfdcKKVQELPEF 537
Cdd:cd17656 418 kaddKGEK--YLCAYFVMEQELNISQLRE-------YLAKQLPEY 453
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
183-595 |
1.58e-08 |
|
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: 57.17 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAilcnVAGAAEILIEDFGIADDERFLSFlpLSHAYE-HTGGQFLPISVGAQIYYA-- 259
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHRA----LSTSALAHGRALGLTSESRVLQF--ASYTFDvSILEIFTTLAAGGCLCIPse 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 260 -EGLEKLASNIEETRPTIMVVVPRlfevlrtrimkqvqkqgglaeklmntalevgerraagkpkfgdglrdalVGRLLKP 338
Cdd:cd05918 181 eDRLNDLAGFINRLRVTWAFLTPS-------------------------------------------------VARLLDP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 339 K----IRQrfggrikaMVSGGAPLNPEVgIFFESMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRG----VDIR 410
Cdd:cd05918 212 EdvpsLRT--------LVLGGEALTQSD-VDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAtcwvVDPD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 411 -------IAEDGEILVRGELVMQGYWHNEAETERT-IKD-GWLH------------TGDIGHVDDKGRIVITDRKKDMI- 468
Cdd:cd05918 283 nhdrlvpIGAVGELLIEGPILARGYLNDPEKTAAAfIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVk 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 469 VNdkGDNVAPQKVEGMLTLQ-PEIGQAMVA------GDKKPYIVGLIVPDAEwtlewcREQGKQFDCKKVQELPEFRNAV 541
Cdd:cd05918 363 IR--GQRVELGEIEHHLRQSlPGAKEVVVEvvkpkdGSSSPQLVAFVVLDGS------SSGSGDGDSLFLEPSDEFRALV 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 542 RAAVDRVNKDL------SVVEKVRQFafadePftieneeMTPSMKIRRHKIKErYAERLD 595
Cdd:cd05918 435 AELRSKLRQRLpsymvpSVFLPLSHL-----P-------LTASGKIDRRALRE-LAESLS 481
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
16-208 |
2.09e-08 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 57.28 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 16 LKRAAEKGDLPFLGARIGGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMA-----SGC-- 88
Cdd:cd05943 76 LLRHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASigaiwSSCsp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 89 -------------------ITVPTYITNTER-DH----AHILDN--SGAKAVIVSTEkllrplhgalqasgIADHVIGId 142
Cdd:cd05943 156 dfgvpgvldrfgqiepkvlFAVDAYTYNGKRhDVrekvAELVKGlpSLLAVVVVPYT--------------VAAGQPDL- 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 143 dlhrqqSSGFLFHRWDSmFAGDAAEARQAVEQriagIGRGDTACIIYTSGTGGAPRGVMQHHGAIL 208
Cdd:cd05943 221 ------SKIAKALTLED-FLATGAAGELEFEP----LPFDHPLYILYSSGTTGLPKCIVHGAGGTL 275
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
15-498 |
2.33e-08 |
|
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: 56.67 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 15 FLKRAAekgdlPFLGARIGGSWQtISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTY 94
Cdd:cd05915 7 LFGRKE-----VVSRLHTGEVHR-TTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 95 ITNTERDHAHILDNSGAKAVIVSTEKLlrplhgalqasGIADHVIGI-DDLHRQQSSGFLFHRWDSMFAGDAAEARQave 173
Cdd:cd05915 81 PRLSPKEIAYILNHAEDKVLLFDPNLL-----------PLVEAIRGElKTVQHFVVMDEKAPEGYLAYEEALGEEAD--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 174 qrIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAeiLIEDFGIADDERFLSFLPLSHAyehtggqflpiSVG 253
Cdd:cd05915 147 --PVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAAS--LVDGTALSEKDVVLPVVPMFHV-----------NAW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 254 AQIYYAEGLEKLASNIEETRPTimvvvprlfEVLRTRIMKQvqkqgglaeKLMNTAlevgerraaGKPKFGDGLRDAlvg 333
Cdd:cd05915 212 CLPYAATLVGAKQVLPGPRLDP---------ASLVELFDGE---------GVTFTA---------GVPTVWLALADY--- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 334 rllKPKIRQRFGGRIKAMVSGGAPlnPEVGIFFESMG-LTMLQGYGQTEA-GPVISCN--------------RPAAGIAM 397
Cdd:cd05915 262 ---LESTGHRLKTLRRLVVGGSAA--PRSLIARFERMgVEVRQGYGLTETsPVVVQNFvkshleslseeeklTLKAKTGL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 398 HSVGPAMRGVD---IRIAEDGE----ILVRGELVMQGYWHNEAETE-RTIKDGWLHTGDIGHVDDKGRIVITDRKKDMIV 469
Cdd:cd05915 337 PIPLVRLRVADeegRPVPKDGKalgeVQLKGPWITGGYYGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIK 416
|
490 500
....*....|....*....|....*....
gi 2786869514 470 NDkGDNVAPQKVEGMLTLQPEIGQAMVAG 498
Cdd:cd05915 417 SG-GEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
183-513 |
5.62e-08 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 55.48 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAILCNVAGaaeiLIEDFGIA--DDERFLSFlpLSHAYEHTGGQFLPISVGAQ---IY 257
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS----LSERYFGRdnGDEAVLFF--SNYVFDFFVEQMTLALLNGQklvVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 258 YAEGL---EKLASNIEETRPTIMVVVP---RLFEVLRTRIMKQVqkqgglaeklmntaLEVGERRAAgkPKFGdglrdal 331
Cdd:cd17648 169 PDEMRfdpDRFYAYINREKVTYLSGTPsvlQQYDLARLPHLKRV--------------DAAGEEFTA--PVFE------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 332 vgrllkpKIRQRFGGRIkamvsggaplnpevgiffesmgltmLQGYGQTEAGpVISCNR--------------PAAGIAM 397
Cdd:cd17648 226 -------KLRSRFAGLI-------------------------INAYGPTETT-VTNHKRffpgdqrfdkslgrPVRNTKC 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 398 HSVGPAMRGVDIRIAedGEILVRGELVMQGYWHNEA-----------ETERTIKDG----WLHTGDI------GHVDDKG 456
Cdd:cd17648 273 YVLNDAMKRVPVGAV--GELYLGGDGVARGYLNRPEltaerflpnpfQTEQERARGrnarLYKTGDLvrwlpsGELEYLG 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 457 RivitdrkKDMIVNDKGDNVAPQKVEGMLTLQPEIGQAMV---------AGDKKPYIVGLIVPDAE 513
Cdd:cd17648 351 R-------NDFQVKIRGQRIEPGEVEAALASYPGVRECAVvakedasqaQSRIQKYLVGYYLPEPG 409
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
182-522 |
7.67e-08 |
|
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: 54.95 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 182 GDTACIIYTSGTGGAPRGVM-QHHGaiLCNVAGAaeiLIEDFGIADDERFLSFLPLS---HAYEHTGGqflpISVGAQIY 257
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVvTHRG--LANLAAA---QIAAFDVGPGSRVLQFASPSfdaSVWELLMA----LLAGATLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 258 YAEGleklasniEETRPTimvvvPRLFEVLRT-RIMKQVQKQGGLAeklmntALEVGerraagkpkfgdglrDALVGRLL 336
Cdd:cd17652 164 LAPA--------EELLPG-----EPLADLLREhRITHVTLPPAALA------ALPPD---------------DLPDLRTL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 337 kpkirqrfggrikamVSGGAPLNPEVGIFFeSMGLTMLQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDIRIAED-- 414
Cdd:cd17652 210 ---------------VVAGEACPAELVDRW-APGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDArl 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 415 --------GEILVRGELVMQGYWHNEAET-ERTIKD------GWLH-TGDIGHVDDKGRIVITDRKKDMiVNDKGDNVAP 478
Cdd:cd17652 274 rpvppgvpGELYIAGAGLARGYLNRPGLTaERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQ-VKIRGFRIEL 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2786869514 479 QKVEGMLTLQPEIGQAMV------AGDKK--PYIVGLI--VPDAEWTLEWCREQ 522
Cdd:cd17652 353 GEVEAALTEHPGVAEAVVvvrddrPGDKRlvAYVVPAPgaAPTAAELRAHLAER 406
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
182-482 |
1.11e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.77 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 182 GDTACIIYTSGTGGAPRGVMQHHGAILCNVAGAAEILIEDfgiADDERFLSFLPLshaYEHTGGQFLPISV--GAQIYYA 259
Cdd:PRK05851 152 GGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLD---AATDVGCSWLPL---YHDMGLAFLLTAAlaGAPLWLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 260 EGLEKLASN------IEETRPTiMVVVPrlfevlrtrimkqvqkqgglaeklmNTALE-VGerraagkpKFGDGLRDALV 332
Cdd:PRK05851 226 PTTAFSASPfrwlswLSDSRAT-LTAAP-------------------------NFAYNlIG--------KYARRVSDVDL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 333 GRLlkpkirqRFGgrikamVSGGAPLNPE-VGIFFESM---GL---TMLQGYGQTEAGPVISCNRPAAGIAMHSV----- 400
Cdd:PRK05851 272 GAL-------RVA------LNGGEPVDCDgFERFATAMapfGFdagAAAPSYGLAESTCAVTVPVPGIGLRVDEVttddg 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 401 ---------GPAMRGVDIRIA-----------EDGEILVRGELVMQGYWhNEAETERtikDGWLHTGDIGHVDDKGrIVI 460
Cdd:PRK05851 339 sgarrhavlGNPIPGMEVRISpgdgaagvagrEIGEIEIRGASMMSGYL-GQAPIDP---DDWFPTGDLGYLVDGG-LVV 413
|
330 340
....*....|....*....|..
gi 2786869514 461 TDRKKDMIVNdKGDNVAPQKVE 482
Cdd:PRK05851 414 CGRAKELITV-AGRNIFPTEIE 434
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
37-260 |
1.40e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 54.67 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAKAVIV 116
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 117 STEKLLRplhgalqasgiadhVIGIDDLhrqqssgflfhrwdSMFAGDAAEARQAVeqRIAGIGR-GDTACIIYTSGTGG 195
Cdd:PRK10252 562 TADQLPR--------------FADVPDL--------------TSLCYNAPLAPQGA--APLQLSQpHHTAYIIFTSGSTG 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786869514 196 APRGVMQHHGAILCNVagaaEILIEDFGIADDERFLSFLPLS---HAYEHtggqFLPISVGAQIYYAE 260
Cdd:PRK10252 612 RPKGVMVGQTAIVNRL----LWMQNHYPLTADDVVLQKTPCSfdvSVWEF----FWPFIAGAKLVMAE 671
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
37-531 |
1.79e-06 |
|
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: 50.75 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRA-LGLRDGDRVCLVSENRPEWCIADLAIMASGCIT--VPTYItnteRDHA--HILDNSGA 111
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVafLNTNI----RSKSllHCFRCCGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 112 KAVIVSTEKL--LRPLHGALQASGI-------ADHVIGIDDLHRQQssgflfhrwdsmfagDAAEARQAVEQRIAGIGRG 182
Cdd:cd05938 80 KVLVVAPELQeaVEEVLPALRADGVsvwylshTSNTEGVISLLDKV---------------DAASDEPVPASLRAHVTIK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 183 DTACIIYTSGTGGAPRGVMQHHGAIL--CNVAGAaeiliedFGIADDERFLSFLPLshaYeHTGGQFLPIS----VGAQI 256
Cdd:cd05938 145 SPALYIYTSGTTGLPKAARISHLRVLqcSGFLSL-------CGVTADDVIYITLPL---Y-HSSGFLLGIGgcieLGATC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 257 YYAEGLEklASNI-EETRPTIMVVVPRLFEVLRTrimkqvqkqgglaekLMNTALEVGERRAAGKPKFGDGLRDALVGRL 335
Cdd:cd05938 214 VLKPKFS--ASQFwDDCRKHNVTVIQYIGELLRY---------------LCNQPQSPNDRDHKVRLAIGNGLRADVWREF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 336 LkpkirQRFGG-RIK---AMVSG-----------GAplnpeVG--IFFESMGLTM-LQGYGQTEAGPViscnRPAAGIAM 397
Cdd:cd05938 277 L-----RRFGPiRIRefyGSTEGnigffnytgkiGA-----VGrvSYLYKLLFPFeLIKFDVEKEEPV----RDAQGFCI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 398 HsvgpamrgvdiriAEDGEIlvrGELVMQ--------GYWHNEAETERTI-------KDGWLHTGDIGHVDDKGRIVITD 462
Cdd:cd05938 343 P-------------VAKGEP---GLLVAKitqqspflGYAGDKEQTEKKLlrdvfkkGDVYFNTGDLLVQDQQNFLYFHD 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786869514 463 RKKDMIvNDKGDNVAPQKVEGMLTLQPEIGQAMVagdkkpYivGLIVPDAE-------WTLewcrEQGKQFDCKKV 531
Cdd:cd05938 407 RVGDTF-RWKGENVATTEVADVLGLLDFLQEVNV------Y--GVTVPGHEgrigmaaVKL----KPGHEFDGKKL 469
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
382-482 |
2.39e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.51 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 382 AGPVISCNRPAAGIAMHSVGPAMrGVDIRIAEDGEILVRGELVMQGYWHNEAETERT-------------------IKDG 442
Cdd:PRK12476 398 AVAHVSCGQVARSQWAVIVDPDT-GAELPDGEVGEIWLHGDNIGRGYWGRPEETERTfgaklqsrlaegshadgaaDDGT 476
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2786869514 443 WLHTGDIGHVDDkGRIVITDRKKDMIVNDkGDNVAPQKVE 482
Cdd:PRK12476 477 WLRTGDLGVYLD-GELYITGRIADLIVID-GRNHYPQDIE 514
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
37-208 |
3.32e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 50.18 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCI---TVPTYitnterdhahildnsGAKA 113
Cdd:PRK03584 113 RELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIwssCSPDF---------------GVQG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 114 VI----VSTEKLL---------------RPLHGALQAS--GIAdHVIGIDDLHRQQSSGFL--FHRWDsmfagDAAEARQ 170
Cdd:PRK03584 178 VLdrfgQIEPKVLiavdgyryggkafdrRAKVAELRAAlpSLE-HVVVVPYLGPAAAAAALpgALLWE-----DFLAPAE 251
|
170 180 190
....*....|....*....|....*....|....*...
gi 2786869514 171 AVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAIL 208
Cdd:PRK03584 252 AAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGIL 289
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
37-237 |
5.76e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.12 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 37 QTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGC--ITVPTYItNTERDHAhILDNSGAKAV 114
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHayIPVDVSS-PAERIEM-IIEVAKPSLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 115 IvSTEKLLrplhgaLQASGIadHVIGIDDLHrqqssgflfhrwDSMFAGDAAEARQAVEQRiagigrgDTACIIYTSGTG 194
Cdd:PRK04813 104 I-ATEELP------LEILGI--PVITLDELK------------DIFATGNPYDFDHAVKGD-------DNYYIIFTSGTT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2786869514 195 GAPRGVMQHHGailcNVAGAAEILIEDFGIADDERFLSFLPLS 237
Cdd:PRK04813 156 GKPKGVQISHD----NLVSFTNWMLEDFALPEGPQFLNQAPYS 194
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-281 |
2.49e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 11 LVELFLKRAAEKGDLPFLgaRIGGswQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCIT 90
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPAL--TFAG--QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 91 VP---TYitNTERDHaHILDNSGAkAVIVSTEKLLRPLhGALQAsGIAdhvigiddlhrqqssgflfhRWdSMFAGDAAE 167
Cdd:PRK05691 2266 VPldpEY--PLERLH-YMIEDSGI-GLLLSDRALFEAL-GELPA-GVA--------------------RW-CLEDDAAAL 2318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 168 ARQAVEQRIAGIGRGDTACIIYTSGTGGAPRGVMQHHGAIlcnvAGAAEILIEDFGIADDERFLSFLPLSH--AYEHTgg 245
Cdd:PRK05691 2319 AAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEI----AMHCQAVIERFGMRADDCELHFYSINFdaASERL-- 2392
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2786869514 246 qFLPISVGAQIYY-AEG---LEKLASNIEETRPTIMVVVP 281
Cdd:PRK05691 2393 -LVPLLCGARVVLrAQGqwgAEEICQLIREQQVSILGFTP 2431
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
182-518 |
2.78e-05 |
|
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: 46.69 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 182 GDTACIIYTSGTGGAPRGVMQHHGailcNVAGAAEILIEDFGIADDE-RFLSFLPLSHAYEH--------TGGQFLPISV 252
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHR----NVAHAAHAWRREYELDSFPvRLLQMASFSFDVFAgdfarsllNGGTLVICPD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 253 GAQIYYAEglekLASNIEETRPTIMVVVPRLFEVLrtriMKQVQKQGGLAEKLmnTALEVGErraagkpkfgdglrDALV 332
Cdd:cd17650 169 EVKLDPAA----LYDLILKSRITLMESTPALIRPV----MAYVYRNGLDLSAM--RLLIVGS--------------DGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 333 GRLLKPKIRqRFGGRIKAMVSGGAplnPEVGI---FFEsmgltmlQGYGQTEAGPVISCNRPAAGIAMHSVGPAMRGVDI 409
Cdd:cd17650 225 AQDFKTLAA-RFGQGMRIINSYGV---TEATIdstYYE-------EGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 410 RIAedGEILVRGELVMQGYWHNEAETERTIKDGWL-------HTGDI------GHVDDKGRIvitdrkkDMIVNDKGDNV 476
Cdd:cd17650 294 GVA--GELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLarwradGNVELLGRV-------DHQVKIRGFRI 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2786869514 477 APQKVEGMLTLQPEIGQAMVA--GDKK--PYIVGLIVPDAewTLEW 518
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAvrEDKGgeARLCAYVVAAA--TLNT 408
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
33-205 |
2.17e-04 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 44.09 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCITVPTYITNTERDHAHILDNSGAK 112
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 113 AVIVSTEKLLR----PLHG----ALQASGIADHVI-------------GIDdlhrqqssgflfHRWDSMFAGdaAEARQA 171
Cdd:cd05966 159 LVITADGGYRGgkviPLKEivdeALEKCPSVEKVLvvkrtggevpmteGRD------------LWWHDLMAK--QSPECE 224
|
170 180 190
....*....|....*....|....*....|....
gi 2786869514 172 VEQRIAgigrGDTACIIYTSGTGGAPRGVMQHHG 205
Cdd:cd05966 225 PEWMDS----EDPLFILYTSGSTGKPKGVVHTTG 254
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
185-233 |
5.41e-04 |
|
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: 42.81 E-value: 5.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2786869514 185 ACIIYTSGTGGAPRGVMQHHGAILCNVAGaaeiLIEDFGIADDERFLSF 233
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSLVNLSHG----LIKEYGITSSDRVLQF 153
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
33-203 |
9.06e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 38.97 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 33 GGSWQTISWNEAAEQVCLLAENLRALGLRDGDRVCLVSENRPEWCIADLAIMASGCI-TV------PTYItnTERdhahI 105
Cdd:PRK00174 93 PGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhSVvfggfsAEAL--ADR----I 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786869514 106 LDnSGAKAVIVSTEKLLR----PLHG----ALQASGIADHVI-----GID-DLHRqqssgflfHR---WDSMFAGDAAEA 168
Cdd:PRK00174 167 ID-AGAKLVITADEGVRGgkpiPLKAnvdeALANCPSVEKVIvvrrtGGDvDWVE--------GRdlwWHELVAGASDEC 237
|
170 180 190
....*....|....*....|....*....|....*
gi 2786869514 169 rQAVEqriagIGRGDTACIIYTSGTGGAPRGVmQH 203
Cdd:PRK00174 238 -EPEP-----MDAEDPLFILYTSGSTGKPKGV-LH 265
|
|
| |
