|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-720 |
0e+00 |
|
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: 953.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 116 QPYEWISYKEVADKAEYVGSALLQKGYKPSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAEL 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 196 SLVFVDKsdkvdlmlesvenkltpglktiiimdpfdsdvvergkkcGVEIMSMKALEDLGRANRRKPKPPSPGDLAVICF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 276 TSGTTGNPKGALITHQNVVSDCSAFVKVTENVVAPSPDDILISFLPLAHMFERVVEktlrlnssdihisylplahmyeql 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVE------------------------ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 356 mlCVMLCHGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKIFG--QANTTMKRWILDFASKRKEAELRSGIIR 433
Cdd:cd05927 178 --ALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVR 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 434 NNSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCC 513
Cdd:cd05927 256 ASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 514 LIKLVDVEEMNYLAA--KGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQG 591
Cdd:cd05927 336 EVKLVDVPEMNYDAKdpNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQG 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 592 EYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAIVIPDVETLSSWAKKK-GFSGSHADLCRNKDVKKAILDDMVRLGKE 670
Cdd:cd05927 416 EYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKE 495
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1788937591 671 AGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRPELRKYFRSQIDELYS 720
Cdd:cd05927 496 NGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-722 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 694.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 86 YDDVTTLYETFQRGIQVSNNGPCLGSR-KPDQ---PYEWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWV 161
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIPKG--ACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 162 IIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVdKSDKVDLMLESVENklTPGLKTIIIMDPFDSDVVERGKKC 241
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 242 GVEIMSMKALEDLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTEnvvapspddilisFLP 321
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK-------------FYP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 322 lahmfervvektlrlnsSDIHISYLPLAHMYEQLMLCVMLCHGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFD 401
Cdd:PLN02736 262 -----------------SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 402 KIFG--QANTTMKRWILDFASKRKEAELRSGiiRNNS-LWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAALGC 478
Cdd:PLN02736 325 GITNavKESGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 479 QFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLIKLVDVEEMNYLAAKG---EGEICVKGSNVFKGYLKDPAKTAEA 555
Cdd:PLN02736 403 RVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 556 LDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAIVIPDVETLS 635
Cdd:PLN02736 483 IDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 636 SWAKKKGFSGSH-ADLCRNKDVKKAILDDMVRLGKEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRPELRKYFRSQ 714
Cdd:PLN02736 563 AWAASEGIKYEDlKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKA 642
|
....*...
gi 1788937591 715 IDELYSTI 722
Cdd:PLN02736 643 ISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-720 |
6.75e-176 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 516.19 E-value: 6.75e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 86 YDDVTTLYETFQRGIQVSNNGPCLgSRKPDQPYEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQ 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVKP--GDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 166 GCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVDKSDKVDLMLESVENklTPGLKTIIIMDPfdsdvveRGKKCGVEI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLDP-------RGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 246 MSMKALEDLGRANR------RKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVtenvVAPSPDDILISF 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 320 LPLAHMFERVVEktlrlnssdihisylplahmyeqlmlCVMLCHGAKIGFfQGDIRLLMDDLKMLQPTIFPVVPRLLNRM 399
Cdd:COG1022 231 LPLAHVFERTVS--------------------------YYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 400 FDKIFGQAN--TTMKRWILDFA---SKRKEAELRSGiiRNNSLW--------DKIIFHKIQASLGGKVRLMVTGAAPVSA 466
Cdd:COG1022 284 YAGIQAKAEeaGGLKRKLFRWAlavGRRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 467 TVLTFLRAaLGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLIKLVDveemnylaakgEGEICVKGSNVFKGYL 546
Cdd:COG1022 362 ELARFFRA-LGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYY 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 547 KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESlQAFLIAI 626
Cdd:COG1022 430 KNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAAL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 627 VIPDVETLSSWAKKKGFS-GSHADLCRNKDVKKAILDDMVRLgkEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRP 705
Cdd:COG1022 509 IVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRK 586
|
650
....*....|....*
gi 1788937591 706 ELRKYFRSQIDELYS 720
Cdd:COG1022 587 VILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-707 |
3.88e-163 |
|
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: 477.86 E-value: 3.88e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 116 QPYEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAEL 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEP--GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 196 SLVFVDKsdkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkppsPGDLAVICF 275
Cdd:cd05907 79 KALFVED----------------------------------------------------------------PDDLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 276 TSGTTGNPKGALITHQNVVSDCSAFVKVtenvVAPSPDDILISFLPLAHMFERVVektlrlnssdihISYLPLahmyeql 355
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRA------------GLYVPL------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 356 mlcvmlCHGAKIGFFQgDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKIFGQANTTMKRWILDFASkrkeaelrsgiirnn 435
Cdd:cd05907 152 ------LAGARIYFAS-SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV--------------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 436 slwdkiifhkiqaslGGKVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLI 515
Cdd:cd05907 210 ---------------GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEV 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 516 KLVDveemnylaakgEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIA 595
Cdd:cd05907 274 RIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNIS 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 596 PEKIENIYQRSEPVAQVFVHGESlQAFLIAIVIPDVETLSSWAKKKGFSGSH-ADLCRNKDVKKAILDDMVRLGkeAGLK 674
Cdd:cd05907 343 PEPIENALKASPLISQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGIAYTDvAELAANPAVRAEIEAAVEAAN--ARLS 419
|
570 580 590
....*....|....*....|....*....|...
gi 1788937591 675 PFEQVKGITLHSELFTVENGLLTPTLKSKRPEL 707
Cdd:cd05907 420 RYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
77-723 |
8.62e-159 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 474.33 E-value: 8.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 77 DSDEPLSFFYDDVTTLYETFQRGIQVSNNGPClgsrkpdQPYEWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQN 156
Cdd:PLN02861 41 DIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKV-------GPYVWLTYKEVYDAAIRIGSAIRSRGVNPG--DRCGIYGSN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 157 RPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVDKSdKVDLMLeSVENKLTPGLKTIIIMDPFDSDVVE 236
Cdd:PLN02861 112 CPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES-KISSIL-SCLPKCSSNLKTIVSFGDVSSEQKE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 237 RGKKCGVEIMSMKALEDLGRANRRKPkPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSA---FVKVTENVVApspd 313
Cdd:PLN02861 190 EAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLStdhLLKVTDRVAT---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 314 dilisflplahmfervvektlrlnSSDIHISYLPLAHMYEQLMLCVMLCHGAKIGFFQGDIRLLMDDLKMLQPTIFPVVP 393
Cdd:PLN02861 265 ------------------------EEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 394 RLLNRMFDKIFG--QANTTMKRWILDFASKRKEAELRSGIIRNNS--LWDKIIFHKIQASLGGKVRLMVTGAAPVSATVL 469
Cdd:PLN02861 321 RVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 470 TFLRAALGCQFYEGYGQTECTAGCSLTVPGDWT-AGHVGAPMPCCLIKLVDVEEMNY--LAAKGEGEICVKGSNVFKGYL 546
Cdd:PLN02861 401 EFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 547 KDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAI 626
Cdd:PLN02861 481 KRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 627 VIPDVETLSSWAKKKGFSGSHADLCRNKDVKKAILDDMVRLGKEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRPE 706
Cdd:PLN02861 560 VVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQ 639
|
650
....*....|....*..
gi 1788937591 707 LRKYFRSQIDELYSTIK 723
Cdd:PLN02861 640 LLKYYKDCIDQLYSEAK 656
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-723 |
9.10e-158 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 472.20 E-value: 9.10e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 87 DDVTTLYETFQRGIQVSNNGPCLGSR-----KPDQpYEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWV 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 162 IIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVDKSdKVDLMLESVENKlTPGLKTIIIMDPFDSDVVERGKKC 241
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK-KISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 242 GVEIMSMKALEDLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENV-VAPSPDDILISFL 320
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSAnAALTVKDVYLSYL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 321 PLAHMFERVVEKtlrlnssdihisylplahmyeqlmlCVMLcHGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMF 400
Cdd:PLN02614 277 PLAHIFDRVIEE-------------------------CFIQ-HGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 401 DKIFGQANTT--MKRWILDFASKRKEAELRSGI--IRNNSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAAL 476
Cdd:PLN02614 331 SGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 477 GCQFYEGYGQTECTAGCSLTVPGDW-TAGHVGAPMPCCLIKLVDVEEMNY--LAAKGEGEICVKGSNVFKGYLKDPAKTA 553
Cdd:PLN02614 411 CCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTK 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 554 EALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAIVIPDVET 633
Cdd:PLN02614 491 EVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQI 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 634 LSSWAKKKGFSGSHADLCRNKDVKKAILDDMVRLGKEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRPELRKYFRS 713
Cdd:PLN02614 570 LERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQS 649
|
650
....*....|
gi 1788937591 714 QIDELYSTIK 723
Cdd:PLN02614 650 VIDEMYKTTN 659
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-722 |
2.84e-154 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 462.75 E-value: 2.84e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 88 DVTTLYETFQRGIQVSNNGPCLGSRKPDQ----PYEWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVII 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAEPG--SRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 164 EQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVdKSDKVDLMLESvENKLTPGLKTIIIMDPFDSDVVERGKKCGV 243
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFV-QDKKIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 244 EIMSMKALEDLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNV---VSDCSAFVKVTENVVapSPDDILISFL 320
Cdd:PLN02430 196 KTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVatfVRGVDLFMEQFEDKM--THDDVYLSFL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 321 PLAHMFERVVEKtlrlnssdihisylplaHMYEQlmlcvmlchGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMF 400
Cdd:PLN02430 274 PLAHILDRMIEE-----------------YFFRK---------GASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 401 DKIFG--QANTTMKRWILDFASKRKEAELRSGIIRNNS--LWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAAL 476
Cdd:PLN02430 328 EGIQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 477 GCQFYEGYGQTECTAGCSLTVPGDWTA-GHVGAPMPCCLIKLVDVEEMNY--LAAKGEGEICVKGSNVFKGYLKDPAKTA 553
Cdd:PLN02430 408 CAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 554 EALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAIVIPDVET 633
Cdd:PLN02430 488 EVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEEN 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 634 LSSWAKKKGFSGSHADLCRNKDVKKAILDDMVRLGKEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRPELRKYFRS 713
Cdd:PLN02430 567 TNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQV 646
|
....*....
gi 1788937591 714 QIDELYSTI 722
Cdd:PLN02430 647 EIDEMYRKL 655
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-704 |
4.43e-152 |
|
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: 451.67 E-value: 4.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 117 PYEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELS 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKP--GDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 197 LVFVDksdkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkpPSPGDLAVICFT 276
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 277 SGTTGNPKGALITHQNVVSDCSAFVKVTENVVapSPDDILISFLPLAHMFERVVEktlrlnssdihisylplahmyeqlM 356
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPELL--GPDDRYLAYLPLAHIFELAAE------------------------N 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 357 LCVMlcHGAKIGFfqGDIRLLMD--------DLKMLQPTIFPVVPRLLNRMFDKIFGQANT--TMKRWILDFASKRKEAE 426
Cdd:cd17639 151 VCLY--RGGTIGY--GSPRTLTDkskrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKA 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 LRSGIirNNSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHV 506
Cdd:cd17639 227 LKEGP--GTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 507 GAPMPCCLIKLVDVEEMNYLAAKGE--GEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKH 584
Cdd:cd17639 304 GPPLPCCEIKLVDWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKD 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 585 IFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAIVIPDVETLSSWAKKKGFSGSH-ADLCRNKDVKKAILDD 663
Cdd:cd17639 384 LVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSEwEELCEDKKLQKAVLKS 463
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1788937591 664 MVRLGKEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKR 704
Cdd:cd17639 464 LAETARAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-720 |
3.69e-135 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 414.51 E-value: 3.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 62 VEVEGTDG-ARRSAilDSDEPLSFFYDDVTTLYETFQRGIQVSNNGPCLGSRK---------PDQ---------PYEWIS 122
Cdd:PLN02387 31 VDVGGEPGyAIRNA--RFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 123 YKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVDK 202
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 203 SDKVDLMleSVENKLTPGLKTIIIMDPFDSDVVERGKKCGVEIMSMKALEDLGRANRRKPKPPSPGDLAVICFTSGTTGN 282
Cdd:PLN02387 187 KQLKKLI--DISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 283 PKGALITHQNVVSDCSAFVKVTenvvapsPDdilisflplahmfervvektlrLNSSDIHISYLPLAHMYEQLMLCVMLC 362
Cdd:PLN02387 265 PKGVMMTHGNIVATVAGVMTVV-------PK----------------------LGKNDVYLAYLPLAHILELAAESVMAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 363 HGAKIGFfqGDIRLLMD-----------DLKMLQPTIFPVVPRLLNRMFDKIFGQANTT--MKRWILDFASKRKEAELR- 428
Cdd:PLN02387 316 VGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEg 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 429 -----SGIIRnnSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTA 503
Cdd:PLN02387 394 swfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 504 GHVGAPMPCCLIKLVDVEEMNYLAAKG---EGEICVKGSNVFKGYLKDPAKTAEA--LDKDG--WLHTGDIGKWLPNGTL 576
Cdd:PLN02387 472 GRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 577 KIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAIVIPDVETLSSWAKKKGFS-GSHADLCRNKD 655
Cdd:PLN02387 552 EIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEE 631
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 656 VKKAILDDMVRLGKEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRPELRKYFRSQIDELYS 720
Cdd:PLN02387 632 AVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
112-589 |
1.77e-123 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 374.73 E-value: 1.77e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQP------YEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEA 185
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALGVGK--GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 186 ITYIINKAELSLVFVDKSDKVDLMLESVENKLTPGLKTIIIMDPFDsdvvergkkcgvEIMSMKALEDLGRANRRKPKPP 265
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVL------------KEEPLPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENVVAPSPDDILISFLPLAHMFERVVEktlrlnssdihisy 345
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLG-------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 lplahmyeqlmLCVMLCHGAKIGFFQGDIRL----LMDDLKMLQPTIFPVVPRLLNRMFDkifgqanttmkrwildfaSK 421
Cdd:pfam00501 219 -----------LLGPLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------------------AG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 422 RKEAELRSGiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDW 501
Cdd:pfam00501 270 APKRALLSS-----------------------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDE 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 ---TAGHVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKI 578
Cdd:pfam00501 327 dlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEI 406
|
490
....*....|.
gi 1788937591 579 IDRKKHIFKLA 589
Cdd:pfam00501 407 VGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
60-719 |
1.99e-98 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 318.84 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 60 QSVEVEGTDGARRSAIL----DSDEPL-----SFFYDDvtTLYETFQRGIQVSNNGPCLGSRK---------PDQ----- 116
Cdd:PTZ00216 32 QNVPVPGTETENASAIYriagVTDEEHerlrnEWYYGP--NFLQRLERICKERGDRRALAYRPvervekevvKDAdgker 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 117 PYE--------WISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITY 188
Cdd:PTZ00216 110 TMEvthfnetrYITYAELWERIVNFGRGLAELGLTK--GSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 189 IINKAELSLVfVDKSDKVDLMLESVENKLTPGLkTIIIMDPFDSDVvergKKCGVEIMSMKALEDLGRANRRKPKPPSPG 268
Cdd:PTZ00216 188 ALRETECKAI-VCNGKNVPNLLRLMKSGGMPNT-TIIYLDSLPASV----DTEGCRLVAWTDVVAKGHSAGSHHPLNIPE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 ---DLAVICFTSGTTGNPKGALITHQNVVSDCSAFV-KVTENVVAPSPDDILISFLPLAHMFERVVEKtlrlnssdihis 344
Cdd:PTZ00216 262 nndDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTN------------ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 345 ylplahmyeqlmlcVMLCHGAKIGFfqGDIRLLMD-------DLKMLQPTIFPVVPRLlnrmFDKI----------FGqa 407
Cdd:PTZ00216 330 --------------IFLARGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG-- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 408 ntTMKRWILDFASKRKEAELRSGiiRNNSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQT 487
Cdd:PTZ00216 388 --SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 488 EcTAGC-SLTVPGDWTAGHVGAPMPCCLIKLVDVEEMNYlAAKGE--GEICVKGSNVFKGYLKDPAKTAEALDKDGWLHT 564
Cdd:PTZ00216 463 E-TVCCgGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 565 GDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQ----VFVHgeSLQAFLIAIVIPDVETLSSWAKK 640
Cdd:PTZ00216 541 GDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKE 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788937591 641 KGFSGSHADLCRNKDVKKAILDDMVRLGKEAGLKPFEQVKGITLHSELFTVENGLLTPTLKSKRPELRKYFRSQIDELY 719
Cdd:PTZ00216 619 HGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-705 |
3.15e-89 |
|
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: 287.33 E-value: 3.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 116 QPYEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAEL 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA--GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 196 SLVFVdksdkvdlmlesvENkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkppSPGDLAVICF 275
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 276 TSGTTGNPKGALITHQNVVSDCSAFVKvtenVVAPSPDDILISFLPLAHMFERVVEKTlrlnssdihisylplahmyeqL 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSD----IVPPQPGDRFLSILPIWHSYERSAEYF---------------------I 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 356 MLCVMLCHGAKigffqgdIRLLMDDLKMLQPTIFPVVPRLlnrmfdkifgqanttmkrWIldfaskrkeaELRSGI---I 432
Cdd:cd17640 151 FACGCSQAYTS-------IRTLKDDLKRVKPHYIVSVPRL------------------WE----------SLYSGIqkqV 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 433 RNNSLWDKIIFHKiqASLGGKVRLMVTGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPC 512
Cdd:cd17640 196 SKSSPIKQFLFLF--FLSGGIFKFGISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPG 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 513 CLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGE 592
Cdd:cd17640 273 TEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGE 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 593 YIAPEKIENIYQRSEPVAQVFVHGESlQAFLIAIVIPDVETLSSWAKKKG--FSGSHADLCRNKDVKKAILDD-MVRLGK 669
Cdd:cd17640 353 NVEPQPIEEALMRSPFIEQIMVVGQD-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYKNEiKDEISN 431
|
570 580 590
....*....|....*....|....*....|....*.
gi 1788937591 670 EAGLKPFEQVKGITLHSELFTvENGLLTPTLKSKRP 705
Cdd:cd17640 432 RPGFKSFEQIAPFALLEEPFI-ENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-711 |
1.40e-79 |
|
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: 263.17 E-value: 1.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 118 YEWISYKEVADKAEYVGSALLQKGYKPSPDqyFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSL 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 198 VFVDKSDKVDLMLESVenkltPGLKTIIIMDPFDSDVVERGKKcgvEIMSMKALEDlgranrRKPkPPSPGDLAVICFTS 277
Cdd:cd05932 82 LFVGKLDDWKAMAPGV-----PEGLISISLPPPSAANCQYQWD---DLIAQHPPLE------ERP-TRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 278 GTTGNPKGALITHQNVVSDCSAFVkvteNVVAPSPDDILISFLPLAHMFERVvektlrlnssdihisYLPLAHMYEQLML 357
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLSYLPLAHVTERV---------------FVEGGSLYGGVLV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 358 cvmlchgakigFFQGDIRLLMDDLKMLQPTIFPVVPRLLnrmfdkifgqanTTMKRWILDFASKRKEAELRSGIIRNnsl 437
Cdd:cd05932 208 -----------AFAESLDTFVEDVQRARPTLFFSVPRLW------------TKFQQGVQDKIPQQKLNLLLKIPVVN--- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 438 wdKIIFHKIQASLG-GKVRLMVTGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLIK 516
Cdd:cd05932 262 --SLVKRKVLKGLGlDQCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 517 LVDveemnylaakgEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 596
Cdd:cd05932 339 ISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAP 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 597 EKIENIYQRSEPVAQVFVHGESLQAfLIAIVIpdvetLSSWAKKKGFSGSHADLCRNkdvKKAILDDMvrlgkEAGLKPF 676
Cdd:cd05932 408 APIENKLAEHDRVEMVCVIGSGLPA-PLALVV-----LSEEARLRADAFARAELEAS---LRAHLARV-----NSTLDSH 473
|
570 580 590
....*....|....*....|....*....|....*
gi 1788937591 677 EQVKGITLHSELFTVENGLLTPTLKSKRPELRKYF 711
Cdd:cd05932 474 EQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-719 |
2.50e-73 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 249.20 E-value: 2.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 113 KPDQPYEWISYKEVADKAEYVGSALLQKGYkpspDQY--FGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYII 190
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 191 NKAELSLVFVDKSDKVDLMLEsVENKLtPGLKTIIIM-DPFDSdvvergKKCGVeiMSMKALEDLGR-----ANRRKPKP 264
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAIIQYkEPLKE------KEPNL--YSWDEFMELGRsipdeQLDAIISS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 265 PSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENVVAPSPDDILISFLPLAHmfervvektlrlnssdihis 344
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSH-------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 345 ylPLAHMYEqlmLCVMLCHGAKIGFFQGDIR--LLMDDLKMLQPTIFPVVPRLLNRMFDKI--FGQANTTMKRWILDFAs 420
Cdd:cd05933 207 --IAAQILD---IWLPIKVGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 421 KRKEAE-------LRSGIIRNNSLWDKIIFHKIQASLG-GKVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAG 492
Cdd:cd05933 281 KGVGLEtnlklmgGESPSPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 493 CSLTVPGDWTAGHVGAPMPCCLIKLVDVEemnylaAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLP 572
Cdd:cd05933 360 HTISNPQAYRLLSCGKALPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 573 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEP-VAQVFVHGESLQaFLIAIV----IPDVET------LSS----W 637
Cdd:cd05933 434 DGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLtlkcEVNPETgepldeLTEeaieF 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 638 AKKkgfSGSHA----DLCRNKD--VKKAILDDMVRLGKEAGLKPFEQVKGITLHSElFTVENGLLTPTLKSKRPELRKYF 711
Cdd:cd05933 513 CRK---LGSQAtrvsEIAGGKDpkVYEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKY 588
|
....*...
gi 1788937591 712 RSQIDELY 719
Cdd:cd05933 589 KDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
112-641 |
2.28e-67 |
|
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: 228.93 E-value: 2.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQP-----YEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAI 186
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVGP--GDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 187 TYIINKAELSLVFVdksdkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkpps 266
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 pgdlAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVtenvVAPSPDDILISFLPLAHMFervvektlrlnssdihisyl 346
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVF-------------------- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plahmyeQLMLCVM--LCHGAKI----GFfqgDIRLLMDDLKMLQPTIFPVVPRLLNRMFDkifgqanttmkrwildfAS 420
Cdd:COG0318 155 -------GLTVGLLapLLAGATLvllpRF---DPERVLELIERERVTVLFGVPTMLARLLR-----------------HP 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 421 KRKEAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGD 500
Cdd:COG0318 208 EFARYDLSS------------------------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDP 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 WTA--GHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKI 578
Cdd:COG0318 264 GERrpGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYI 341
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788937591 579 IDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLI--AIVIPDVETLSSWAKKK 641
Cdd:COG0318 342 VGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
121-704 |
2.59e-66 |
|
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: 229.23 E-value: 2.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRG--DVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKSDKVDLMLESVENklTPGLKTIIIMDPFDSDVVERGKkcgveIMSMKALEDLGRA-NRRKPK-------PPSPGDLAV 272
Cdd:cd17641 90 EDEEQVDKLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 273 ICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENvvapSPDDILISFLPLAHMFERVVektlrlnssdihisylplahMY 352
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQMY--------------------SV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 353 EQLMLCVMLCHgakigfFQGDIRLLMDDLKMLQPTIFPVVPRLLN--------RMFDKifGQANTTMKRWILDFASKRKE 424
Cdd:cd17641 219 GQALVCGFIVN------FPEEPETMMEDLREIGPTFVLLPPRVWEgiaadvraRMMDA--TPFKRFMFELGMKLGLRALD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 AELRSgiiRNNSLW--------DKIIFHKIQASLG-GKVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCSL 495
Cdd:cd17641 291 RGKRG---RPVSLWlrlaswlaDALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 496 TVPGDWTAGHVGAPMPCCLIKLVDVeemnylaakgeGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGT 575
Cdd:cd17641 367 HRDGDVDPDTVGVPFPGTEVRIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGH 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 576 LKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESlQAFLIAIVIPDVETLSSWAKKKGFS-GSHADLCRNK 654
Cdd:cd17641 436 LVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRP 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1788937591 655 DVKKAILDDMVRLGKEagLKPFEQV-KGITLHSELfTVENGLLTPTLKSKR 704
Cdd:cd17641 515 EVYELIRKEVEKVNAS--LPEAQRIrRFLLLYKEL-DADDGELTRTRKVRR 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
118-697 |
2.19e-63 |
|
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: 221.95 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 118 YEWISYKEVADKAEYVGSALlQKGYKPSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSL 197
Cdd:cd17632 65 FETITYAELWERVGAVAAAH-DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 198 VFVDkSDKVDLMLESVENKLTPGlkTIIIMDPFDSDVVER-----------GKKCGVEIMSMKALEDLG-RANRRKPKPP 265
Cdd:cd17632 144 LAVS-AEHLDLAVEAVLEGGTPP--RLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDlPPAPLFRPEP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVVSdcsAFVKVTENVVAPSPDDILISFLPLAHMFERVVektlrlnssdihisy 345
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLVAT---FWLKVSSIQDIRPPASITLNFMPMSHIAGRIS--------------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 lplahmyeqlmLCVMLCHGAkIGFFQG--DIRLLMDDLKMLQPTIFPVVPRLlnrmFDKIFGQANTTMKRWILDFA---- 419
Cdd:cd17632 283 -----------LYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRV----CDMLFQRYQAELDRRSVAGAdaet 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 420 -SKRKEAELRsgiirnnslwdkiifhkiQASLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCSLTvp 498
Cdd:cd17632 347 lAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL-- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 499 gdwtAGHVGAPmPCCLIKLVDVEEMNYLAAKG---EGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGT 575
Cdd:cd17632 405 ----DGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 576 LKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLIAIVIPDVETLSswakkkgfSGSHADLcrnkd 655
Cdd:cd17632 480 LVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALA--------GEDTARL----- 546
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1788937591 656 vKKAILDDMVRLGKEAGLKPFEQVKGITLHSELFTVENGLLT 697
Cdd:cd17632 547 -RAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-704 |
6.63e-61 |
|
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: 211.92 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVgsALLQKGYKPSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd05914 8 LTYKDLADNIAKF--ALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKSDkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkppspgDLAVICFTSGTT 280
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 281 GNPKGALITHQNVVSDCsAFVKVTENVvapSPDDILISFLPLAHMFervvektlrlnssdihisylPLahMYEQLMLCVM 360
Cdd:cd05914 102 GNSKGVMLTYRNIVSNV-DGVKEVVLL---GKGDKILSILPLHHIY--------------------PL--TFTLLLPLLN 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 361 lchGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKIFGQANTTMKRWILdfaskrkeaeLRSGIIRNNSLWDK 440
Cdd:cd05914 156 ---GAHVVFLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK----------FKLAKKINNRKIRK 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 441 IIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPmpcclIKLVDV 520
Cdd:cd05914 223 LAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 521 EEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIE 600
Cdd:cd05914 297 RIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIE 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 601 NIYQRSEPVAQ--VFV-HGEslqafLIAIVIPDVETLSSWAKKkgfsgshadlcrNKDVKKAILDDmVRLGKEAGLKPFE 677
Cdd:cd05914 377 AKINNMPFVLEslVVVqEKK-----LVALAYIDPDFLDVKALK------------QRNIIDAIKWE-VRDKVNQKVPNYK 438
|
570 580
....*....|....*....|....*..
gi 1788937591 678 QVKGITLHSELFTVengllTPTLKSKR 704
Cdd:cd05914 439 KISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-641 |
2.14e-60 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 206.37 E-value: 2.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLPLAHMFervvektlrlnssdihisylPL 348
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIG--------------------GL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHMYeqlmlcVMLCHGAKI----GFFQGDIRLLMDDLKmlqPTIFPVVPRLLNRMFDkifgqanttmkrwildfASKRKE 424
Cdd:cd04433 57 FGLL------GALLAGGTVvllpKFDPEAALELIEREK---VTILLGVPTLLARLLK-----------------APESAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 AELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWT-- 502
Cdd:cd04433 111 YDLSS------------------------LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArk 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 503 AGHVGAPMPCCLIKLVDVEEmNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRK 582
Cdd:cd04433 167 PGSVGRPVPGVEVRIVDPDG-GELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRL 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788937591 583 KHIFKlAQGEYIAPEKIENIYQRSEPVAQVFVHG---ESLQAFLIAIVIP------DVETLSSWAKKK 641
Cdd:cd04433 245 KDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
112-635 |
5.98e-57 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 201.25 E-value: 5.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQPY-----EWISYKEVADKAEYVGSALLQKGYKPSpDQyFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAI 186
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQPG-DR-VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 187 TYIINKAelslvfvdksdkvdlmlesvenkltpGLKTIIIMDPFdSDVVERGKKcgveimsmkaledlgranRRKPKPPS 266
Cdd:cd05936 89 EHILNDS--------------------------GAKALIVAVSF-TDLLAAGAP------------------LGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENVVapSPDDILISFLPLAHMFERVVektlrlnssdihisyl 346
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL--EGDDVVLAALPLFHVFGLTV---------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plahmyeQLMLCVMLchGAKIGFFQG-DIRLLMDDLKMLQPTIFPVVPRLLNRMFDkifgqanttmkrwildfASKRKEA 425
Cdd:cd05936 186 -------ALLLPLAL--GATIVLIPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 426 ELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCSLTvpGDWT 502
Cdd:cd05936 240 DFSS------------------------LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspvVAVNPLD--GPRK 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 503 AGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 582
Cdd:cd05936 294 PGSIGIPLPGTEVKIVD-DDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRK 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 583 KHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFliaIVIPDVETLS 635
Cdd:cd05936 372 KDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpySGEAVKAF---VVLKEGASLT 427
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-616 |
2.02e-56 |
|
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: 200.13 E-value: 2.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpDQyFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKG-DV-VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKsDKVDLMLESVenKLTPGLKTIIIMDPFDSDVVERGK----KCGVEImsmkaledlgrANRRKPKPPSPGDLAVICFT 276
Cdd:cd05911 89 DP-DGLEKVKEAA--KELGPKDKIIVLDDKPDGVLSIEDllspTLGEED-----------EDLPPPLKDGKDDTAAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 277 SGTTGNPKGALITHQNVVSDCSafvkvtenvvapspddilISFLPLAHMFErvvektlrlnSSDIHISYLPLAHMYEQLM 356
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLIANLS------------------QVQTFLYGNDG----------SNDVILGFLPLYHIYGLFT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 357 LCVMLCHGAK-IGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFdkifgqanttmKRWILDFASkrkeaeLRSgiirnn 435
Cdd:cd05911 207 TLASLLNGATvIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALA-----------KSPLLDKYD------LSS------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 436 slwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCL 514
Cdd:cd05911 264 ------------------LRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVE 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 515 IKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 594
Cdd:cd05911 326 AKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQV 404
|
490 500
....*....|....*....|..
gi 1788937591 595 APEKIENIYQRSEPVAQVFVHG 616
Cdd:cd05911 405 APAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
110-641 |
1.55e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 192.81 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 110 GSRKPDQPY-----EWISYKEVADKAEYVGSALLQKGYKPSpDQyFGIFAQNRPEWVIieqGCYAYSM---VVVPLYDTL 181
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIGKG-DR-VAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 182 GNEAITYIINKAELSLVFVdksdkVDLMLESVE--NKLTPGLKTIIIMDPFDSDVVERGkkcgveimsMKALED-LGRAN 258
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFLGVDYsaTTRLPALEHVVICETEEDDPHTEK---------MKTFTDfLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 259 RRKPKPP-SPGDLAVICFTSGTTGNPKGALITHQNVVS---DCSAFVKVTEnvvapspDDILISFLPLAHMFervvektl 334
Cdd:PRK07656 156 PAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSnaaDWAEYLGLTE-------GDRYLAANPFFHVF-------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 335 rlnssdihisylplahMYEQLML-CVMlcHGAKI----GFfqgDIRLLMDDLKMLQPTIFPVVPrllnrmfdkifgqant 409
Cdd:PRK07656 221 ----------------GYKAGVNaPLM--RGATIlplpVF---DPDEVFRLIETERITVLPGPP---------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 410 TMKRWILDFAsKRKEAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTE 488
Cdd:PRK07656 264 TMYNSLLQHP-DRSAEDLSS------------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSE 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 489 CTAGCSLTVPGD---WTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTG 565
Cdd:PRK07656 319 ASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 566 DIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLIAIVIPDV--ETLSS 636
Cdd:PRK07656 398 DLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAYVVLKPGAELteEELIA 476
|
....*
gi 1788937591 637 WAKKK 641
Cdd:PRK07656 477 YCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
86-617 |
2.21e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 189.63 E-value: 2.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 86 YDDVTTLYETFQRGIQVSnngpclgsrkPDQP-YEW----ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEW 160
Cdd:PRK06187 2 QDYPLTIGRILRHGARKH----------PDKEaVYFdgrrTTYAELDERVNRLANALRALGVKK--GDRVAVFDWNSHEY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 161 VIieqgCY-AYSM---VVVPLYDTLGNEAITYIINKAELSLVFVDkSDKVDLmLESVENKLtPGLKTIIIMDpfDSDVVE 236
Cdd:PRK06187 70 LE----AYfAVPKigaVLHPINIRLKPEEIAYILNDAEDRVVLVD-SEFVPL-LAAILPQL-PTVRTVIVEG--DGPAAP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 237 RGKKCGveimsmkALEDL--GRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSD---CSAFVKVTenvvaps 311
Cdd:PRK06187 141 LAPEVG-------EYEELlaAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLS------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 312 PDDILISFLPLAHMFErvvektlrlnssdIHISYLPLAHmyeqlmlcvmlchGAKI---GFFqgDIRLLMDDLKMLQPTI 388
Cdd:PRK06187 207 RDDVYLVIVPMFHVHA-------------WGLPYLALMA-------------GAKQvipRRF--DPENLLDLIETERVTF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 389 FPVVPRLLNRMFdkifgQANTTMKRWIldfaskrkeaelrsgiirnNSLwdkiifhkiqaslggkvRLMVTGAAPVSATV 468
Cdd:PRK06187 259 FFAVPTIWQMLL-----KAPRAYFVDF-------------------SSL-----------------RLVIYGGAALPPAL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 469 LTFLRAALGCQFYEGYGQTECT-AGCSLT----VPGDWT-AGHVGAPMPCCLIKLVDvEEMNYLAAKGE--GEICVKGSN 540
Cdd:PRK06187 298 LREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGevGEIIVRGPW 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788937591 541 VFKGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFVHGE 617
Cdd:PRK06187 377 LMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAEVAVIGV 451
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
269-641 |
1.60e-40 |
|
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: 154.37 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENvvapSPDDILISFLPLAHMFERVVE--KTLRLNSSdihisyl 346
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRW----TEDDVLLHVLPLHHVHGLVNAllCPLFAGAS------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plahmyeqlmlCVMLchgakiGFF---QGDIRLLMDDLkmlqpTIFPVVPRllnrMFDKIFGQANTTmkrwILDFASKRK 423
Cdd:cd05941 159 -----------VEFL------PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAH----FTDPQFARA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 424 EAElrsgiirnnslwdkiifhkiqaslgGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCSLTVP--GDW 501
Cdd:cd05941 209 AAA-------------------------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGER 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 TAGHVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 581
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGR 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1788937591 582 KK-HIFKlAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAF---LIAIVIP-------DVETLSSWAKKK 641
Cdd:cd05941 342 SSvDIIK-SGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
111-616 |
1.22e-38 |
|
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: 148.91 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 111 SRKPDQP-YEW----ISYKEVADKAEYVGSALLQKGYKPSpDQyFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEA 185
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVAKG-DR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 186 ITYIINKAELSLVFvdksdkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkpp 265
Cdd:cd17631 84 VAYILADSGAKVLF------------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 spGDLAVICFTSGTTGNPKGALITHQNVvsdcsafvkvTENVVApspddILISFlplahmfervvektlRLNSSDIHISY 345
Cdd:cd17631 98 --DDLALLMYTSGTTGRPKGAMLTHRNL----------LWNAVN-----ALAAL---------------DLGPDDVLLVV 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 LPLAHMYEQLMLCVM-LCHGAKI----GFfqgDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKifGQANTTmkrwilDFAS 420
Cdd:cd17631 146 APLFHIGGLGVFTLPtLLRGGTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 421 krkeaelrsgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCSLTVPGD 500
Cdd:cd17631 215 ---------------------------------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPED 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 W--TAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKI 578
Cdd:cd17631 261 HrrKLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYI 338
|
490 500 510
....*....|....*....|....*....|....*...
gi 1788937591 579 IDRKKHIFKlAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:cd17631 339 VDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIG 375
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
212-602 |
5.93e-38 |
|
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: 148.15 E-value: 5.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 212 SVENKLTPGLKTIIIMD--PFDSDVVERGKKCGVEIMsmkaledlgranrrKPKPP-SPGDLAVICFTSGTTGNPKGALI 288
Cdd:cd05904 113 ELAEKLASLALPVVLLDsaEFDSLSFSDLLFEADEAE--------------PPVVViKQDDVAALLYSSGTTGRSKGVML 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 289 THQNVVSDCSAFVKVTENvvAPSPDDILISFLPLAHMFErvvektlrLNSsdihisylplahmyeqlMLCVMLCHGAKI- 367
Cdd:cd05904 179 THRNLIAMVAQFVAGEGS--NSDSEDVFLCVLPMFHIYG--------LSS-----------------FALGLLRLGATVv 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 368 ---GFfqgDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKifgqanttmkrwildfaSKRKEAELRSgiirnnslwdkiifh 444
Cdd:cd05904 232 vmpRF---DLEELLAAIERYKVTHLPVVPPIVLALVKS-----------------PIVDKYDLSS--------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 445 kiqaslggkVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLTVPGDWTAGHVG-----APMPCclIKLV 518
Cdd:cd05904 277 ---------LRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 519 DVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 598
Cdd:cd05904 346 DPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAE 424
|
....
gi 1788937591 599 IENI 602
Cdd:cd05904 425 LEAL 428
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-720 |
9.15e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 150.64 E-value: 9.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 233 DVVERGKKCGVEIMSmkaLEDLGRANRR--KPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVsdcsafvkvteNVVAP 310
Cdd:PTZ00342 270 DLKEKAKKLGISIIL---FDDMTKNKTTnyKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLY-----------NTVVP 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 311 SPD-DILISFLPlahmfervvektlrlnssDIHISYLPLAHMYEQLMLCVMLCHGAKIGFFQGDIRLLMDDLKMLQPTIF 389
Cdd:PTZ00342 336 LCKhSIFKKYNP------------------KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNIL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 390 PVVPRLLNRMFDKIFGQAN--TTMKRWILdfaskRKEAELRSGiiRNNSLWDKI---IFH---KIQASLGGKVRLMVTGA 461
Cdd:PTZ00342 398 AGVPKVFNRIYTNIMTEINnlPPLKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGG 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 462 APVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPM-PCCLIKLVDVEEMNYLAAKGEGEICVKGSN 540
Cdd:PTZ00342 471 GKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDS 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 541 VFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQ 620
Cdd:PTZ00342 551 IFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSM 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 621 AFLIAIVIPDVETLSSWAK-----------KKGFSGSHADLCRNKDV-KKAILDDMVRLGKEAGLKPFEQVKGITLHSEL 688
Cdd:PTZ00342 631 DGPLAIISVDKYLLFKCLKddnmlestginEKNYLEKLTDETINNNIyVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKV 710
|
490 500 510
....*....|....*....|....*....|....*
gi 1788937591 689 FTVENgLLTPTLKSKRPELRK---YFRSQIDELYS 720
Cdd:PTZ00342 711 WDTNN-YLTPTFKVKRFYVFKdyaFFIDQVKKIYK 744
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
180-644 |
3.51e-37 |
|
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: 145.94 E-value: 3.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 180 TLGNEAITYIINKAEL-----SLVFVDKSDKVDLM----------LESVENKLTPGLKTIIimdpfdsdvvergkKCGVE 244
Cdd:cd05909 64 TAGLRELRACIKLAGIktvltSKQFIEKLKLHHLFdveydarivyLEDLRAKISKADKCKA--------------FLAGK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 245 IMSMKALEDLGRANRrkpkppSPGDLAVICFTSGTTGNPKGALITHQNVVSDcsafVKVTENVVAPSPDDILISFLPLAH 324
Cdd:cd05909 130 FPPKWLLRIFGVAPV------QPDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 325 MFERVVEKTLRLNSSdIHISYLPLAHMYEQLmlcVMLCHGAKIGFFQGDIRLLMDDLKMLQPTifpvvprllnrmfdkif 404
Cdd:cd05909 200 SFGLTGCLWLPLLSG-IKVVFHPNPLDYKKI---PELIYDKKATILLGTPTFLRGYARAAHPE----------------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 405 gqanttmkrwilDFASkrkeaelrsgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGY 484
Cdd:cd05909 259 ------------DFSS---------------------------------LRLVVAGAEKLKDTLRQEFQEKFGIRILEGY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 485 GQTECTAGCSLTVPG-DWTAGHVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLH 563
Cdd:cd05909 294 GTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 564 TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEP----VAQVFV----HGESLQAFLIAIViPDVETLS 635
Cdd:cd05909 373 TGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEILPedneVAVVSVpdgrKGEKIVLLTTTTD-TDPSSLN 450
|
....*....
gi 1788937591 636 SWAKKKGFS 644
Cdd:cd05909 451 DILKNAGIS 459
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
115-641 |
1.42e-35 |
|
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: 141.30 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 115 DQPYEWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVI-----IEQGCyaysmVVVPLYDTLGNEAITYI 189
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKG--DRVAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 190 INKAELSLVFVDKsdkvDLMLESVENKLTPGLKTI-IIMDPFDSDVVERGKKCGVEimsmkaleDLGRANRRKPKPPSPG 268
Cdd:cd05926 82 LADLGSKLVLTPK----GELGPASRAASKLGLAILeLALDVGVLIRAPSAESLSNL--------LADKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSdcSAfvkvtenvvapspddilisflplahmfeRVVEKTLRLNSSDIHISYLPL 348
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAA--SA----------------------------TNITNTYKLTPDDRTLVVMPL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHMYEQLmlCVMLC---HGAKI----GFfqgDIRLLMDDLKMLQPTIFPVVPrllnrmfdkifgqantTMKRWILDFASK 421
Cdd:cd05926 200 FHVHGLV--ASLLStlaAGGSVvlppRF---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 422 RKEAELrsgiirnnslwdkiifhkiqaslgGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT--VPG 499
Cdd:cd05926 259 NPESPP------------------------PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 500 DWTAGHVGAPMPcclIKLVDV-EEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKI 578
Cdd:cd05926 315 PRKPGSVGKPVG---VEVRILdEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFL 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 579 IDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQ--VF-----VHGESLQAfliAIVI-----PDVETLSSWAKKK 641
Cdd:cd05926 392 TGRIKELINRG-GEKISPLEVDGVLLSHPAVLEavAFgvpdeKYGEEVAA---AVVLregasVTEEELRAFCRKH 462
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
121-635 |
6.63e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 134.73 E-value: 6.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSPdqYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGD--RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DksdkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkppspgdLAVICFTSGTT 280
Cdd:cd05934 82 D--------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 281 GNPKGALITHQNVVSDCSAFvkvtenvvapspddilisflplAHMFervvektlRLNSSDIHISYLPLAHMYEQLM-LCV 359
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYS----------------------ARRF--------GLGEDDVYLTVLPLFHINAQAVsVLA 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 360 MLCHGAKI--------GFFQGDIRllmddlkMLQPTIF---PVVPRLLnrmfdkifgqanttMKRWILDfasKRKEAELR 428
Cdd:cd05934 144 ALSVGATLvllprfsaSRFWSDVR-------RYGATVTnylGAMLSYL--------------LAQPPSP---DDRAHRLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 429 sgiirnnslwdkiifhkiqaslggkvrlmVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGA 508
Cdd:cd05934 200 -----------------------------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGR 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 509 PMPCCLIKLVDvEEMNYLAAKGEGEICVK---GSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 585
Cdd:cd05934 251 PAPGYEVRIVD-DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDM 328
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 586 FKlAQGEYIAPEKIENIYQRSEPVAQVFVHG----ESLQAFLIAIVIPDVETLS 635
Cdd:cd05934 329 IR-RRGENISSAEVERAILRHPAVREAAVVAvpdeVGEDEVKAVVVLRPGETLD 381
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-641 |
1.15e-33 |
|
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: 132.40 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDcSAFV----KVTEnvvapspDDILISFLPLAHMFERVVektlrlnssdih 342
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIgerlGLTE-------QDRLCIPVPLFHCFGSVL------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 343 isylplahmyeQLMLCVMlcHGAKIGFfqgdIRLLMDDLKMLQ-------------PTIFPvvpRLLNR-MFDKifgqan 408
Cdd:cd05917 61 -----------GVLACLT--HGATMVF----PSPSFDPLAVLEaiekekctalhgvPTMFI---AELEHpDFDK------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 409 ttmkrwiLDFASkrkeaeLRSGIIrnnslwdkiifhkiqaslggkvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQT 487
Cdd:cd05917 115 -------FDLSS------LRTGIM---------------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMT 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 488 ECTAGCSLTVPGD---WTAGHVGAPMPCCLIKLVDvEEMNYLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALDKDGWLH 563
Cdd:cd05917 155 ETSPVSTQTRTDDsieKRVNTVGRIMPHTEAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLH 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 564 TGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLI--AIVIPDVETL 634
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIRlkEGAELTEEDI 312
|
....*..
gi 1788937591 635 SSWAKKK 641
Cdd:cd05917 313 KAYCKGK 319
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
151-641 |
3.50e-33 |
|
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: 132.96 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 151 GIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVDKS-DKVDLMLESVENKLTPGLktiiimdp 229
Cdd:TIGR01923 28 ALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLlEEKDFQADSLDRIEAAGR-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 230 fdsdvvergkkCGVEIMSMKALEDLgranrrkpkppspgdlAVICFTSGTTGNPKGALITHQNvvsdcsafvkvtenvva 309
Cdd:TIGR01923 100 -----------YETSLSASFNMDQI----------------ATLMFTSGTTGKPKAVPHTFRN----------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 310 pspddilisflplaHMFERV-VEKTLRLNSSDIHISYLPLAHMYEQLMLCVMLCHGAKIGFFQGDIRLLmDDLKMLQPTI 388
Cdd:TIGR01923 136 --------------HYASAVgSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 389 FPVVPRLLNRMFDKifGQANTTMKRWILdfaskrkeaelrsgiirnnslwdkiifhkiqaslggkvrlmvtGAAPVSATV 468
Cdd:TIGR01923 201 ISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPAPL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 469 LTFLRAaLGCQFYEGYGQTE-CTAGCSLTVPGDWTAGHVGAPMPCCLIKL-VDVEEmnylaakGEGEICVKGSNVFKGYL 546
Cdd:TIGR01923 236 IEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 547 kDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESL 619
Cdd:TIGR01923 308 -YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQVP 385
|
490 500
....*....|....*....|..
gi 1788937591 620 QAFLIAIVIPDVETLSSWAKKK 641
Cdd:TIGR01923 386 VAYIVSESDISQAKLIAYLTEK 407
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-616 |
9.29e-32 |
|
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: 130.06 E-value: 9.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 111 SRKPDQPYEWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYII 190
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVKP--GDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 191 NKAELSLVFVDKSdkvdlmLESVENKLTPGLKTI---IIMDPFDSDVVERGKkcGVEimsmkALEDL-GRANRRKPKPPS 266
Cdd:cd12119 94 NHAEDRVVFVDRD------FLPLLEAIAPRLPTVehvVVMTDDAAMPEPAGV--GVL-----AYEELlAAESPEYDWPDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 P-GDLAVICFTSGTTGNPKGALITHQNVVSdcSAFVKVTENVVAPSPDDiliSFLPLAHMFervvektlrlnssdiHISY 345
Cdd:cd12119 161 DeNTAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESD---VVLPVVPMF---------------HVNA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 LPLAHMyeqlmlCVMLchGAKI----GFFQGDIRL-LMDDLKmlqPTIFPVVPrllnrmfdkifgqantTMkrWILDFAS 420
Cdd:cd12119 221 WGLPYA------AAMV--GAKLvlpgPYLDPASLAeLIEREG---VTFAAGVP----------------TV--WQGLLDH 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 421 krkeaelrsgiirnnslwdkiiFHKIQASLGGKVRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCSLTVPG 499
Cdd:cd12119 272 ----------------------LEANGRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 500 DWTAGHV----------GAPMPCCLIKLVDvEEMNYLAAKGE--GEICVKGSNVFKGYLKDPAkTAEALDKDGWLHTGDI 567
Cdd:cd12119 328 EHSNLSEdeqlalrakqGRPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDV 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1788937591 568 GKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:cd12119 406 ATIDEDGYLTITDRSKDVIKSG-GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
121-602 |
1.56e-31 |
|
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: 129.57 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKS--DKVdlmlESVENKLtPGLKTIIIMDpfdSDVVERGKKCgveIMSMKALEDLGRANRRKPKPPS---PGDLAVICF 275
Cdd:cd17642 123 SKKglQKV----LNVQKKL-KIIKTIIILD---SKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 276 TSGTTGNPKGALITHQNVvsdCSAFVKVTENVV--APSPDDILISFLPLAHMFERVVekTLRLNSSDIHISYLPlaHMYE 353
Cdd:cd17642 192 SSGSTGLPKGVQLTHKNI---VARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFT--TLGYLICGFRVVLMY--KFEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 354 QLMLCVMlchgakigffqGDIRLLMddlKMLQPTIFPVVPRllNRMFDKifgqanttmkrwildfaskrkeaelrsgiir 433
Cdd:cd17642 265 ELFLRSL-----------QDYKVQS---ALLVPTLFAFFAK--STLVDK------------------------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 434 nnslWDKIIFHKIqaslggkvrlmVTGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCSLTVPGDWTAGHVGAPMPC 512
Cdd:cd17642 298 ----YDLSNLHEI-----------ASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 513 CLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 592
Cdd:cd17642 363 FYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGY 441
|
490
....*....|
gi 1788937591 593 YIAPEKIENI 602
Cdd:cd17642 442 QVPPAELESI 451
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
77-616 |
3.67e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 128.74 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 77 DSDEPLSffyddVTTLYETFQRGIQVSNNGPCLGSRKPDQPYewiSYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQN 156
Cdd:PRK12583 10 GGDKPLL-----TQTIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQPG--DRVGIWAPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 157 RPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV----DKSDKVDLMLESVENKLT-----------PGL 221
Cdd:PRK12583 80 CAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICadafKTSDYHAMLQELLPGLAEgqpgalacerlPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 222 KTIIIMDPFDS-------DVVERGkkcgvEIMSMKALEDLGRANRRkpkppspGDLAVICFTSGTTGNPKGALITHQNVV 294
Cdd:PRK12583 160 RGVVSLAPAPPpgflawhELQARG-----ETVSREALAERQASLDR-------DDPINIQYTSGTTGFPKGATLSHHNIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 295 SDCsafvkvtenvvapspddilisflplahmfeRVVEKTLRLNSSDIHISYLPLAHMYeQLMLCVMLC--HGAKIgFFQG 372
Cdd:PRK12583 228 NNG------------------------------YFVAESLGLTEHDRLCVPVPLYHCF-GMVLANLGCmtVGACL-VYPN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 373 DirlLMDDLKMLQ-------------PTIFpvVPRLLNRMFDKifgqanttmkrwiLDFASkrkeaeLRSGIIrnnslwd 439
Cdd:PRK12583 276 E---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS------LRTGIM------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 440 kiifhkiqaslggkvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCSLTVPGD---WTAGHVGAPMPCCLI 515
Cdd:PRK12583 325 --------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVETVGRTQPHLEV 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 516 KLVDVEemNYLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 594
Cdd:PRK12583 385 KVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENI 461
|
570 580
....*....|....*....|..
gi 1788937591 595 APEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK12583 462 YPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-635 |
7.18e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 127.96 E-value: 7.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 254 LGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDcsafvkvtenvvapspddilisFLPLAHMFERVVEKt 333
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAN----------------------MLQCRALMGSNLNE- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 334 lrlnSSDIHISYLPLAHMYEQLMLC-VMLCHGAKigffqgdiRLLMDDlkmlqPTIFPVVPRLLNRMFDKIFGQANTTmk 412
Cdd:PRK05677 250 ----GCEILIAPLPLYHIYAFTFHCmAMMLIGNH--------NILISN-----PRDLPAMVKELGKWKFSGFVGLNTL-- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 413 rwildFASkrkeaelrsgiIRNNSLWDKIIFHKIQASLGGkvrlmvtGAAPVSATVLTFlRAALGCQFYEGYGQTECTAG 492
Cdd:PRK05677 311 -----FVA-----------LCNNEAFRKLDFSALKLTLSG-------GMALQLATAERW-KEVTGCAICEGYGMTETSPV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 493 CSLTVPGDWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLP 572
Cdd:PRK05677 367 VSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQE 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 573 NGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFliaIVIPDVETLS 635
Cdd:PRK05677 446 DGYMRIVDRKKDMI-LVSGFNVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETLT 511
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-602 |
7.92e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 127.56 E-value: 7.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 113 KPDQPYEWiSYKEVADKAEYVGSALLQKGYKPSPDQYFGIfaqnrPEW---VIIEQGCYAYSMVVVPLYDTLGNEAITYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPGDRVAFQL-----PGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 190 INKAElSLVF-----VDKSDKVDLMLeSVENKLtPGLKTIIIMDpfdsdvvergkKCGVEIMSMKALEDLGRANRRKPKP 264
Cdd:PRK06087 117 LNKCQ-AKMFfaptlFKQTRPVDLIL-PLQNQL-PQLQQIVGVD-----------KLAPATSSLSLSQIIADYEPLTTAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 265 PSPGD-LAVICFTSGTTGNPKGALITHQNvvsdcsafvkvtenvvapspddILISflplahmfERVVEKTLRLNSSDIHI 343
Cdd:PRK06087 183 TTHGDeLAAVLFTSGTEGLPKGVMLTHNN----------------------ILAS--------ERAYCARLNLTWQDVFM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 SYLPLAHmyeqlmlcvmlchgaKIGFFQGDIR-LLMDDLKMLQPTIFPVVP-RLLNRmfdkifgQANTTM---KRWILDF 418
Cdd:PRK06087 233 MPAPLGH---------------ATGFLHGVTApFLIGARSVLLDIFTPDAClALLEQ-------QRCTCMlgaTPFIYDL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 419 --ASKRKEAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AG 492
Cdd:PRK06087 291 lnLLEKQPADLSA------------------------LRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 493 CSLTVPGDWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLP 572
Cdd:PRK06087 344 VNLDDPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDE 422
|
490 500 510
....*....|....*....|....*....|
gi 1788937591 573 NGTLKIIDRKKHIFkLAQGEYIAPEKIENI 602
Cdd:PRK06087 423 AGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
246-625 |
2.05e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 126.48 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 246 MSMKALEDLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDcsaFVKVTENVVAPSPDDilisflplahm 325
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVAN---MLQVRACLSQLGPDG----------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 326 fervveKTLRLNSSDIHISYLPLAHMYEQLM--LCVMLchgakigffQGDIRLLMDDlkmlqptifpvvPRLLNRMFDKi 403
Cdd:PRK12492 251 ------QPLMKEGQEVMIAPLPLYHIYAFTAncMCMMV---------SGNHNVLITN------------PRDIPGFIKE- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 404 fgqanttMKRWILdfaskrkeaelrSGIIRNNSLWDKIIFHKIQASLGGKvRLMVT---GAAPVSATVLTFlRAALGCQF 480
Cdd:PRK12492 303 -------LGKWRF------------SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTI 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 481 YEGYGQTECTAGCSLTVPGDWTA-GHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKD 559
Cdd:PRK12492 362 VEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAE 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788937591 560 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLIA 625
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
254-585 |
5.49e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 125.50 E-value: 5.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 254 LGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCS---AFVKVtenvVAPSPddilisflplahmfERVv 330
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPG----LGDGP--------------ERV- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 331 ektlrlnssdihISYLPLAHMYeQLMLCV---MLCHGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLlnrmFDKIfgqa 407
Cdd:PRK05605 266 ------------LAALPMFHAY-GLTLCLtlaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI---- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 408 nttmkrwildfaskRKEAELRsGIirnnslwdkiifhkiqaSLGGkVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYG 485
Cdd:PRK05605 325 --------------AEAAEER-GV-----------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 486 QTECT---AGCSLTvpGDWTAGHVGAPMPCCLIKLVDVEEMNYLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALdKDGW 561
Cdd:PRK05605 370 LTETSpiiVGNPMS--DDRRPGYVGVPFPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGW 446
|
330 340
....*....|....*....|....
gi 1788937591 562 LHTGDIGKWLPNGTLKIIDRKKHI 585
Cdd:PRK05605 447 FRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
269-625 |
2.15e-29 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 123.63 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSdcsafvkvteNVVAPSPddiliSFLPLAHMFERVVektlrlnssdihISYLPL 348
Cdd:PRK08974 207 DLAFLQYTGGTTGVAKGAMLTHRNMLA----------NLEQAKA-----AYGPLLHPGKELV------------VTALPL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHMYEQLMLCVMLCHgakigffQGDIRLLMDDlkmlqPTIFP-VVPRLLNRMFDKIFGqANTTMKRWIldfaskrkeael 427
Cdd:PRK08974 260 YHIFALTVNCLLFIE-------LGGQNLLITN-----PRDIPgFVKELKKYPFTAITG-VNTLFNALL------------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 rsgiirNNSLwdkiiFHKIQASlggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCSLTVPGdwTAG 504
Cdd:PRK08974 315 ------NNEE-----FQELDFS---SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 505 HVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKH 584
Cdd:PRK08974 379 SIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKD 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1788937591 585 IFkLAQGEYIAPEKIENIYQRSEPVAQVF-------VHGESLQAFLIA 625
Cdd:PRK08974 457 MI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-654 |
2.50e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 123.38 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 114 PDQPYEWiSYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEqgcYAYS-----MVVV-PLYDTlgNEaIT 187
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKG--DRVGIWAPNVPEWVLTQ---FATAkigaiLVTInPAYRL--SE-LE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 188 YIINKAELS-LVFVDK---SDKVDlMLESVENKLT------------PGLKTIIIMDPfdsdvverGKKCGV----EIMS 247
Cdd:PRK08315 109 YALNQSGCKaLIAADGfkdSDYVA-MLYELAPELAtcepgqlqsarlPELRRVIFLGD--------EKHPGMlnfdELLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 248 MKALEDLGRANRRKPKPpSPGDLAVICFTSGTTGNPKGALITHQNVVSDcsAFVkVTENVvAPSPDDILISFLPLAHMFE 327
Cdd:PRK08315 180 LGRAVDDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNN--GYF-IGEAM-KLTEEDRLCIPVPLYHCFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 328 RVvektlrlnssdihisylplahmyeqlmLCVMLC--HGAKI-----GFfqgdirllmDDLKMLQ-------------PT 387
Cdd:PRK08315 255 MV---------------------------LGNLACvtHGATMvypgeGF---------DPLATLAaveeerctalygvPT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 388 IFpvVPRLLNRMFDKifgqanttmkrwiLDFASkrkeaeLRSGIirnnslwdkiifhkiqasLGGK---VRLM------- 457
Cdd:PRK08315 299 MF--IAELDHPDFAR-------------FDLSS------LRTGI------------------MAGSpcpIEVMkrvidkm 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 458 ----VTGAapvsatvltflraalgcqfyegYGQTECTAGCSLTVPGD------WTaghVGAPMPCCLIKLVDVEEMNYLA 527
Cdd:PRK08315 340 hmseVTIA----------------------YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPETGETVP 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 528 AKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSE 607
Cdd:PRK08315 395 RGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHP 473
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 608 PVAQVFVHGeslqafliaivIPDV---ETLSSWAK-KKGFSGSHADL---CRNK 654
Cdd:PRK08315 474 KIQDVQVVG-----------VPDEkygEEVCAWIIlRPGATLTEEDVrdfCRGK 516
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-616 |
2.08e-28 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 116.83 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSAF---VKVTEnvvapspDDILISFLPLAHMFErvvektlrlnssdihisy 345
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWadcADLTE-------DDRYLIINPFFHTFG------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 lplahmYEQLMLcVMLCHGAKI---GFFqgDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKifgqanttmkrwildfaSKR 422
Cdd:cd17638 56 ------YKAGIV-ACLLTGATVvpvAVF--DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGR 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 KEAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGcSLTVPGD- 500
Cdd:cd17638 110 KKFDLSS------------------------LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDd 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 --WTAGHVGAPMPCCLIKLVDveemnylaakgEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKI 578
Cdd:cd17638 165 aeTVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRI 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 1788937591 579 IDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:cd17638 234 TDRLKDMY-IVGGFNVYPAEVEGALAEHPGVAQVAVIG 270
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
267-641 |
2.40e-28 |
|
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: 118.78 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSdcsaFVKVTENVVAPSPDDILISFLPLAHmfervvektlrlnssDIHIsyl 346
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSF---------------DVSV--- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plahmyeqLMLCVMLCHGAKI----GFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRmfdkifgqanttmkrwILDFASKR 422
Cdd:cd05930 150 --------WEIFGALLAGATLvvlpEEVRKDPEALADLLAEEGITVLHLTPSLLRL----------------LLQELELA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 KEAELRsgiirnnslwdkiifhkiqaslggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTV--PGD 500
Cdd:cd05930 206 ALPSLR--------------------------LVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRvpPDD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 WTAGHV--GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLP 572
Cdd:cd05930 260 EEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLP 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788937591 573 NGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFV---HGESLQAFLIAIVIP------DVETLSSWAKKK 641
Cdd:cd05930 339 DGNLEFLGRIDDQVKIR-GYRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPdeggelDEEELRAHLAER 415
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
266-600 |
4.36e-28 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 119.31 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVVSdcsafvKVTENVVAPSPDdilisflplahmfervvektLRLNSSDIHISY 345
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVT------SVAQQVDGENPN--------------------LYFHSDDVILCV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 LPLAHMYEqlMLCVMLCH---GAKIGFFQG-DIRLLMDDLKMLQPTIFPVVPRLL-----NRMFDKifgqanttmkrwiL 416
Cdd:PLN02246 231 LPMFHIYS--LNSVLLCGlrvGAAILIMPKfEIGALLELIQRHKVTIAPFVPPIVlaiakSPVVEK-------------Y 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 417 DFASkrkeaelrsgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCSL 495
Cdd:PLN02246 296 DLSS---------------------------------IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 496 TV-------PGDWTAGHVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIG 568
Cdd:PLN02246 341 AMclafakePFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIG 420
|
330 340 350
....*....|....*....|....*....|..
gi 1788937591 569 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 600
Cdd:PLN02246 421 YIDDDDELFIVDRLKELIKY-KGFQVAPAELE 451
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
255-624 |
1.07e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 118.20 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 255 GRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDC--------SAFVKvtenvvAPSPDD-ILISFLPLAHM 325
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK------KPRPDQlNFVCALPLYHI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 326 FervvektlrlnssdihisylplahmyeQLMLCVMLchGAKIGffqG---------DIRLLMDDLKMLQPTIFPVVPRLL 396
Cdd:PRK07059 265 F---------------------------ALTVCGLL--GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 397 NRMFdkifgqanttmkrwildfaskrkeaelrsgiirNNSLWDKIIFHKIQASLGGkvrlmvtGAApVSATVLTFLRAAL 476
Cdd:PRK07059 313 NALL---------------------------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMT 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 477 GCQFYEGYG--QTECTAGCSLTVPGDWTaGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAE 554
Cdd:PRK07059 352 GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAK 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788937591 555 ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQrSEP----VAQVFVH----GESLQAFLI 624
Cdd:PRK07059 430 VMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSGFNVYPNEIEEVVA-SHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
121-641 |
2.47e-27 |
|
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: 115.48 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIieqgcyaysmvvvplydtlgneAITYIInKAELSLVFV 200
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPG--DVVPLLSDRSLEMLV----------------------AILAIL-KAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DK---SDKVDLMLESVEnkltpglKTIIIMdpfdsdvvergkkcgveimsmkaledlgranrrkpkPPSPGDLAVICFTS 277
Cdd:cd17653 78 DAklpSARIQAILRTSG-------ATLLLT------------------------------------TDSPDDLAYIIFTS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 278 GTTGNPKGALITHQNVVsdcsafvkvteNVVAPSPDdilisflplahmfervvekTLRLNSSDIHISYLPLAHMYEQLML 357
Cdd:cd17653 115 GSTGIPKGVMVPHRGVL-----------NYVSQPPA-------------------RLDVGPGSRVAQVLSIAFDACIGEI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 358 CVMLCHGAKIGF------FQGDIRLLmdDLKMLQPTIFPVVPRllnRMFDKIfgqanttmkrwildfaskrkeaelrsgi 431
Cdd:cd17653 165 FSTLCNGGTLVLadpsdpFAHVARTV--DALMSTPSILSTLSP---QDFPNL---------------------------- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 432 irnnslwdKIIFhkiqasLGGKvrlmvtgaaPVSATVLTflRAALGCQFYEGYGQTECTAGCSLT--VPGDWTagHVGAP 509
Cdd:cd17653 212 --------KTIF------LGGE---------AVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKP 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 510 MPCCLIKLVDVEEMNYLAAKgEGEICVKGSNVFKGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKK 583
Cdd:cd17653 265 IPNSTCYILDADLQPVPEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGRED 343
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 584 HIFKLaQGEYIAPEKIENIYQRSEPVAQ---VFVHGEslqaFLIAIVIP---DVETLSSWAKKK 641
Cdd:cd17653 344 NQVKV-RGFRINLEEIEEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
264-614 |
3.41e-27 |
|
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: 114.67 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 264 PPSPGDLAVICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLPLAHmfervvektlrlnssDIHI 343
Cdd:TIGR01733 116 PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLV----NLLAWLARRYGLDPDDRVLQFASLSF---------------DASV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 SYLPLAhmyeqlmlcvmLCHGAkigffqgdiRLLMDDLKMLQPTifpvvPRLLNRMFDkifgQANTTMkrWILdfaskrk 423
Cdd:TIGR01733 177 EEIFGA-----------LLAGA---------TLVVPPEDEERDD-----AALLAALIA----EHPVTV--LNL------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 424 eaelrsgiirNNSLWDKIIFHKIQASLGgkVRLMVTGA-APVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT-VPGDW 501
Cdd:TIGR01733 219 ----------TPSLLALLAAALPPALAS--LRLVILGGeALTPALVDRWRARGPGARLINLYGPTETTVWSTATlVDPDD 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 TAGHV----GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAE--------ALDKDGWLHTGDIGK 569
Cdd:TIGR01733 287 APRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVR 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1788937591 570 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV 614
Cdd:TIGR01733 366 YLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
254-612 |
3.68e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 116.51 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 254 LGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSD---CSAFVKVTENVvaPSPDDILISFLPLAHMFervv 330
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKL--EEGCEVVITALPLYHIF---- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 331 ekTLRLNSsdihisylpLAHMyeQLMLCVMLCHGAKigffqgDIRLLMDDLKMLQPTIFPVVPRLLNRMFdkifgqantt 410
Cdd:PRK08751 268 --ALTANG---------LVFM--KIGGCNHLISNPR------DMPGFVKELKKTRFTAFTGVNTLFNGLL---------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 411 mkrwildfaskrkeaelrsgiirNNSLWDKIIFHKIQASLGGkvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECT 490
Cdd:PRK08751 319 -----------------------NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETS 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 491 -AGCSLTVPGDWTAGHVGAPMPCCLIKLVDveEMNYLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIG 568
Cdd:PRK08751 368 pAACINPLTLKEYNGSIGLPIPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIA 445
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1788937591 569 KWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQV 612
Cdd:PRK08751 446 RMDEQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAMMPGVLEV 488
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
263-581 |
9.42e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.95 E-value: 9.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 263 KPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDcsafVKVTENVVAPSPDDILISFLPLAHMFERVVekTLrlnssdih 342
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSFGLTV--TL-------- 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 343 isYLPLahmyeqLMLCVMLCH-----GAKIGffqgdirllmddlKML---QPTIfpvvprllnrMFdkifgqANTTMkrw 414
Cdd:PRK08633 843 --WLPL------LEGIKVVYHpdptdALGIA-------------KLVakhRATI----------LL------GTPTF--- 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 415 ildfaskrkeaeLRSgIIRNNSLwDKIIFhkiqASLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCS 494
Cdd:PRK08633 883 ------------LRL-YLRNKKL-HPLMF----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVAS 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 495 LTVP-----GDWT-----AGHVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEAL---DKDGW 561
Cdd:PRK08633 941 VNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGW 1020
|
330 340
....*....|....*....|
gi 1788937591 562 LHTGDIGKWLPNGTLKIIDR 581
Cdd:PRK08633 1021 YVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
255-617 |
1.16e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 113.93 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 255 GRANRRKPKPPsPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFvkvtENVVAPSPDDILISFLPLAHMFERV--VEK 332
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHVHGLVlgVLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 333 TLRLNSSDIHI-SYLPLAHMYEqlmlcvmLCHGAkigffqgdirllmddlkmlqpTIFPVVPrllnrmfdkifgqantTM 411
Cdd:PRK07787 191 PLRIGNRFVHTgRPTPEAYAQA-------LSEGG---------------------TLYFGVP----------------TV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 412 krwildfaskrkeaelrsgiirnnslWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA 491
Cdd:PRK07787 227 --------------------------WSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 492 GCSLTVPGDWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGE--GEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGK 569
Cdd:PRK07787 281 TLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAV 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 570 WLPNGTLKIIDR------KKHIFKLAQGEyiapekIENIYQRSEPVAQVFVHGE 617
Cdd:PRK07787 360 VDPDGMHRIVGRestdliKSGGYRIGAGE------IETALLGHPGVREAAVVGV 407
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-602 |
3.03e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 113.54 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSD-CSAFVKVTenvvapspddilisflplAHMFERVVekTLRLnssdihisyLP 347
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVG------------------PEMIGQVV--TLGL---------IP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 348 LAHMYEQLMLC--VMLCHGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLlnrmfdkifgqanttmkrwILDFASkrkea 425
Cdd:PLN02330 236 FFHIYGITGICcaTLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPI-------------------ILNLVK----- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 426 elrsgiirnNSLWDKIIFHKIqaslggKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagCSLTVPGDWTAG 504
Cdd:PLN02330 292 ---------NPIVEEFDLSKL------KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CITLTHGDPEKG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 505 H-------VGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLK 577
Cdd:PLN02330 355 HgiakknsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIF 434
|
330 340
....*....|....*....|....*
gi 1788937591 578 IIDRKKHIFKLaQGEYIAPEKIENI 602
Cdd:PLN02330 435 IVDRIKELIKY-KGFQVAPAELEAI 458
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-602 |
4.38e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 113.28 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspdqyfG----IFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELS 196
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKK------GdrvaIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 197 LVF-----------VDKSDKVDLMLESvenklTPGLKTIIIMDPFDSDVVERGkkcgveimsMKALEDL--GRANRRKPK 263
Cdd:COG0365 114 VLItadgglrggkvIDLKEKVDEALEE-----LPSLEHVIVVGRTGADVPMEG---------DLDWDELlaAASAEFEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 264 PPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKvteNVVAPSPDDILisflplahmfervvektlrLNSSDI-- 341
Cdd:COG0365 180 PTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVF-------------------WCTADIgw 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 342 --HISYL---PLAH-----MYEqlmlcvmlchgAKIGFFQGDiRL--LMDDLKmlqPTIFPVVPRLLnRMfdkifgqant 409
Cdd:COG0365 238 atGHSYIvygPLLNgatvvLYE-----------GRPDFPDPG-RLweLIEKYG---VTVFFTAPTAI-RA---------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 410 tMKRWILDFASKRKeaeLRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC 489
Cdd:COG0365 292 -LMKAGDEPLKKYD---LSS------------------------LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 490 TAGCSLTVPGDWT-AGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSN--VFKGYLKDPAKTAEAL--DKDGWLHT 564
Cdd:COG0365 344 GGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRT 422
|
490 500 510
....*....|....*....|....*....|....*...
gi 1788937591 565 GDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 602
Cdd:COG0365 423 GDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESA 459
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
111-616 |
4.56e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 112.77 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 111 SRKPDQP-YEW----ISYKEVADKAEYVGSALLQKGykPSPDQYFGIFAQNRPE-WVIIEQGCYAySMVVVPLYDTLGNE 184
Cdd:PRK06188 23 KRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALG--LGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 185 AITYIINKAELSLVFVDKSDKVDLMLESVENklTPGLKTIIIMDPFDSdvvergkkcGVEImsmkaledLGRANRRKPKP 264
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPAPFVERALALLAR--VPSLKHVLTLGPVPD---------GVDL--------LAAAAKFGPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 265 PS----PGDLAVICFTSGTTGNPKGALITHQNVVsdcsafvkvTENVVAPS----PDDIliSFLPLAhmfervvektlrl 336
Cdd:PRK06188 161 LVaaalPPDIAGLAYTGGTTGKPKGVMGTHRSIA---------TMAQIQLAewewPADP--RFLMCT------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 337 nssdihisylPLAHMYEQLMLCVMLCHGAKI---GFfqgDIRLLMDDLKMLQPTIFPVVPrllnrmfdkifgqantTMKR 413
Cdd:PRK06188 217 ----------PLSHAGGAFFLPTLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVP----------------TMIY 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 414 WILDFASKRKeAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGC 493
Cdd:PRK06188 268 ALLDHPDLRT-RDLSS------------------------LETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 494 SLTVPGDWTAGHV------GAPMPCCLIKLVDvEEMNYLAAkGE-GEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGD 566
Cdd:PRK06188 323 TYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGD 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1788937591 567 IGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK06188 400 VAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
122-644 |
6.52e-26 |
|
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: 111.32 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 122 SYKEVADKAEYVGSALLQKGYKPSPDQYFGIfaQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELslvfvd 201
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQL--PNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 202 ksdkvdlmlesvenkltpglKTIIIMDPFdsdvvergkkcgveimsmkaledlgranRRKPKPPSPGDLAVICFTSGTTG 281
Cdd:cd05903 75 --------------------KVFVVPERF----------------------------RQFDPAAMPDAVALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 282 NPKGALITHQNVVSDCSAFVkvtENVVAPSPDDILISfLPLAHmfervvektlrlnssdiHISYLplahmyeqlmlcvml 361
Cdd:cd05903 107 EPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAH-----------------QTGFV--------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 362 cHGAKIGFFQGDIRLLMDDLkmlQPTifpVVPRLLNRmfDKI-FGQANTTMKRWILDfASKRKEAELRSgiirnnslwdk 440
Cdd:cd05903 151 -YGFTLPLLLGAPVVLQDIW---DPD---KALALMRE--HGVtFMMGATPFLTDLLN-AVEEAGEPLSR----------- 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 441 iifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGD-WTAGHV-GAPMPCCLIKLV 518
Cdd:cd05903 210 -------------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPeDRRLYTdGRPLPGVEIKVV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 519 DvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEK 598
Cdd:cd05903 277 D-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLE 353
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 599 IENIYQRSEPVAQVFV-------HGESLQAFLI--AIVIPDVETLSSWAKKKGFS 644
Cdd:cd05903 354 VEDLLLGHPGVIEAAVvalpderLGERACAVVVtkSGALLTFDELVAYLDRQGVA 408
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-601 |
8.73e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 111.38 E-value: 8.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 173 VVVPLYDTLGNEAITYIINKAELSLVFVDksdkvdlmlESVENKLTPGLktiiiMDPFDSDVVERGkkcgveimsmkalE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLAD---------AGAADRLRDAL-----PASPDPGTVLDA-------------D 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 253 DLGRANRRKPK-PPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENvvapSPDDILISFLPLAHMFervve 331
Cdd:cd05922 101 GIRAARASAPAhEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI----TADDRALTVLPLSYDY----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 332 KTLRLNSSdihisylplahmyeqlmlcvmLCHGAKIgFFQGDIRL---LMDDLKMLQPTIFPVVP---RLLNRM-FDKIf 404
Cdd:cd05922 172 GLSVLNTH---------------------LLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPstyAMLTRLgFDPA- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 405 gqanttmkrwildfaskrKEAELRsgiirnnslwdkiifhkIQASLGGKVRlmvtgaapvSATVLTFLRAALGCQFYEGY 484
Cdd:cd05922 229 ------------------KLPSLR-----------------YLTQAGGRLP---------QETIARLRELLPGAQVYVMY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 485 GQTECTAGCSlTVPGDWTA---GHVGAPMPCCLIKLVDVEEMnyLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALDKDG 560
Cdd:cd05922 265 GQTEATRRMT-YLPPERILekpGSIGLAIPGGEFEILDDDGT--PTPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGG 341
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1788937591 561 WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 601
Cdd:cd05922 342 VLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-616 |
1.61e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 111.11 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 119 EWISYKEVADKAEYVGSALLQK-GYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLydtlgNEAITyiinKAELSL 197
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKG--ERIAILSQNSLEYIVLLFAIAKVECIAVPL-----NIRLT----ENELIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 198 VFVDKsdkvdlmlesvenkltpGLKTIIIMDPFDSDVVERGKKCGVE-IMSMKALEDLGRANRRKPKPPSPGDLAVICFT 276
Cdd:PRK06839 95 QLKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 277 SGTTGNPKGALITHQNVvsdcsaFVKVTENVVApspddilisflplahmfervvektLRLNSSDIHISYLPLAHMyeqlm 356
Cdd:PRK06839 158 SGTTGKPKGAVLTQENM------FWNALNNTFA------------------------IDLTMHDRSIVLLPLFHI----- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 357 lcvmlchgAKIGFFQgdirllmddlkmlQPTIFP----VVPRLLN-----RMFDK-----IFGQAntTMKRWILDfASKR 422
Cdd:PRK06839 203 --------GGIGLFA-------------FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 KEAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCSLTVPGDW- 501
Cdd:PRK06839 259 ETTNLQS------------------------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDAr 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 -TAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIID 580
Cdd:PRK06839 314 rKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVG 391
|
490 500 510
....*....|....*....|....*....|....*.
gi 1788937591 581 RKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK06839 392 RKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
122-616 |
2.27e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 110.79 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 122 SYKEVADKAEYVGSALLQKGYKPSpDQyFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVD 201
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKG-DR-VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 202 kSDKVDLmLESVENKLTpglktiiiMDPFDSDVVERGKKCGveiMSMKALEDLGRANRRKPKPPSP--GDLAVICFTSGT 279
Cdd:PRK08316 116 -PALAPT-AEAALALLP--------VDTLILSLVLGGREAP---GGWLDFADWAEAGSVAEPDVELadDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 280 TGNPKGALITHQNVVSD-CSAFVkvtenvvapspddilisflplahmfervvekTLRLNSSDIHISYLPLAH---MYEQL 355
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEyVSCIV-------------------------------AGDMSADDIPLHALPLYHcaqLDVFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 356 MLCVMLchGAKIGFFQG-DIRLLMDDLKMLQPTIF---PVVprllnrmfdkifgqanttmkrWIL-----DFAsKRKEAE 426
Cdd:PRK08316 232 GPYLYV--GATNVILDApDPELILRTIEAERITSFfapPTV---------------------WISllrhpDFD-TRDLSS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 LRSGIIrnnslwdkiifhkiqaslggkvrlmvtGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLTVPGDwTAGH 505
Cdd:PRK08316 288 LRKGYY---------------------------GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 506 VG-APMPCCLI--KLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 582
Cdd:PRK08316 340 PGsAGRPVLNVetRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRK 417
|
490 500 510
....*....|....*....|....*....|....
gi 1788937591 583 KHIFKLAqGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK08316 418 KDMIKTG-GENVASREVEEALYTHPAVAEVAVIG 450
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
264-583 |
3.03e-25 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 110.35 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 264 PPSPGDLAVICFTSGTTGNPKGALITHQNVVS------DCSAFvkvtenvvapSPDDILISFLPLAHMFERVVEktlrln 337
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSnaltlvDYWRF----------TPDDVLIHALPIFHTHGLFVA------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 338 ssdIHISylplahmyeqlmlcvmLCHGAKIGFFQG-DIRLLMDdlKMLQPTIFPVVPRLLNRMFdkifgqanttmkrwil 416
Cdd:PRK07514 216 ---TNVA----------------LLAGASMIFLPKfDPDAVLA--LMPRATVMMGVPTFYTRLL---------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 417 dfASKRKEAELRSGIirnnslwdkiifhkiqaslggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT 496
Cdd:PRK07514 259 --QEPRLTREAAAHM-----------------------RLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 497 VPGDWTAGHVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTL 576
Cdd:PRK07514 314 YDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYV 393
|
....*..
gi 1788937591 577 KIIDRKK 583
Cdd:PRK07514 394 HIVGRGK 400
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
114-583 |
7.71e-25 |
|
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: 109.29 E-value: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 114 PDQPYEWISYKEVADKAEYVGSALLQKGYKPsPDQYFGIFAQNRpEWVIIEQGCYAYSMVVVPLydtlgNEAITY-IINK 192
Cdd:cd05906 33 ADGSEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL-----TVPPTYdEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 193 AELSLVFVDKsdkvdlMLES----VENKLTPGLKTIIIMDPFDSDVVErgkkcgveimsmkALEDLGRANRRKPKPPS-P 267
Cdd:cd05906 106 RLRKLRHIWQ------LLGSpvvlTDAELVAEFAGLETLSGLPGIRVL-------------SIEELLDTAADHDLPQSrP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 268 GDLAVICFTSGTTGNPKGALITHQNVVSDCSAfvKVTENVVAPspDDILISFLPLAHMfERVVEKTLR---LNSSDIHIs 344
Cdd:cd05906 167 DDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDHV-GGLVELHLRavyLGCQQVHV- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 345 ylPLAHMyeqlmlcvmlchgakigffqgdirlLMDDLKMLqptifpvvpRLLNRMfdkifgQANTTmkrWILDFA-SKRK 423
Cdd:cd05906 241 --PTEEI-------------------------LADPLRWL---------DLIDRY------RVTIT---WAPNFAfALLN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 424 EAELRsgiiRNNSLWDkiifhkiqasLGGKVRLMVTGAAPVSATVLTFLR--AALGCQ---FYEGYGQTECTAGCSLTVP 498
Cdd:cd05906 276 DLLEE----IEDGTWD----------LSSLRYLVNAGEAVVAKTIRRLLRllEPYGLPpdaIRPAFGMTETCSGVIYSRS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 499 ---GDWTAGH----VGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGkWL 571
Cdd:cd05906 342 fptYDHSQALefvsLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FL 419
|
490
....*....|..
gi 1788937591 572 PNGTLKIIDRKK 583
Cdd:cd05906 420 DNGNLTITGRTK 431
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
269-617 |
7.92e-25 |
|
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: 107.82 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALIT---HQNVVSDCSAFVKVTENvvapspdDILISFLPlahMFervvektlrlnssdiHISY 345
Cdd:cd05912 78 DIATIMYTSGTTGKPKGVQQTfgnHWWSAIGSALNLGLTED-------DNWLCALP---LF---------------HISG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 LPLahMYEQLML-CVMLCHGAkigfFqgDIRLLMDDLKMLQPTIFPVVPRLLNRMFdKIFGQAnttmkrwildfaskrke 424
Cdd:cd05912 133 LSI--LMRSVIYgMTVYLVDK----F--DAEQVLHLINSGKVTIISVVPTMLQRLL-EILGEG----------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 aelrsgiiRNNSLwdkiifhkiqaslggkvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCSLTVPGDWTA- 503
Cdd:cd05912 187 --------YPNNL-----------------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 504 --GHVGAPMPCCLIKLVDVEEmnylAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDR 581
Cdd:cd05912 240 kiGSAGKPLFPVELKIEDDGQ----PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDR 314
|
330 340 350
....*....|....*....|....*....|....*.
gi 1788937591 582 KKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHGE 617
Cdd:cd05912 315 RSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGVVGI 349
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-720 |
1.03e-24 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 110.71 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 89 VTTLYETFQRGIQVSNNGPCLGSRKPDQPYEWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCY 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 169 AYSMVVVPLYDTlgNEAITYIINKAELSLVFVDKSDkVDLMLESVENKLtpglKTIIIMDPF-DSDVVERGKKCGVEIMS 247
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNS-VAAILTCRSRKL----ETVVYTHSFyDEDDHAVARDLNITLIP 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 248 MKALEDLGRAnRRKPKPPSPGDLAVICFTSGTT-----GNPKGALITHQNVVSDCSAFVKVTenvVAPSP--DDILISFL 320
Cdd:PTZ00297 577 YEFVEQKGRL-CPVPLKEHVTTDTVFTYVVDNTtsasgDGLAVVRVTHADVLRDISTLVMTG---VLPSSfkKHLMVHFT 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 321 PLAHMFERVvektlrlnssdihisylplahmyeqlmlCV--MLCHGAKIGffQGDIRLLMDDLKMLQPTIFPVVPRLlnr 398
Cdd:PTZ00297 653 PFAMLFNRV----------------------------FVlgLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--- 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 399 mfdkiFGQANTTMKR----------WILDfaskrKEAELRSGII----RNNSLWDKIIFHKIQASLGGKVRLMVTGAAPV 464
Cdd:PTZ00297 700 -----FSTSRLQLSRanerysavysWLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 465 SATvltflraalgcqfyegYGQTECTAGCSltvpgdwtaghvgapMPCcliklvdVEEMNYLAAkgEGEICVKGS----- 539
Cdd:PTZ00297 770 STS----------------FSLLEHISVCY---------------VPC-------LREVFFLPS--EGVFCVDGTpapsl 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 540 NVFKGYLKDPAKTAE----ALDKDGWL-HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYQRSEPVAQVF 613
Cdd:PTZ00297 810 QVDLEPFDEPSDGAGigqlVLAKKGEPrRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIF 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 614 VHGESLQAfLIAIVIPDVETLS-SWAKKKGFS---GSHADLCRNKDVKKA---ILDDMVRLGKEAGLKPFEQVKGITLHS 686
Cdd:PTZ00297 890 LYADPSRP-IIAIVSPNRDTVEfEWRQSHCMGeggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHP 968
|
650 660 670
....*....|....*....|....*....|....
gi 1788937591 687 ELFTVENGLLTPTLKSKRPELRKYFRSQIDELYS 720
Cdd:PTZ00297 969 HAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-602 |
2.48e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 108.01 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 262 PKPP-SPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENVVAPSpddilisflplahmfervvektlrlNSSD 340
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYP-------------------------GSDN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 341 IHISYLPLAHMYeQLMLCVM--LCHGAKI----GFFQGDIRLLMDDLKMlqpTIFPVVPRLLNRMFDKIFGQANTTMKrw 414
Cdd:PLN02574 246 VYLAALPMFHIY-GLSLFVVglLSLGSTIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 415 ildfaskrkeaelrsgiirnnslwdkiifhkiqaslggKVRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA-- 491
Cdd:PLN02574 320 --------------------------------------SLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvg 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 492 --GCSLTVPGDWTAghVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGK 569
Cdd:PLN02574 362 trGFNTEKLSKYSS--VGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAY 439
|
330 340 350
....*....|....*....|....*....|...
gi 1788937591 570 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 602
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAV 471
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
269-624 |
4.31e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 107.04 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENVVapSPDDILISFLPLAHMFervvektlrlnssdihisylpl 348
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCK--EGEEVVLGVLPFFHVY---------------------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 aHMYEQLMLCVMlcHGAKIGFF-QGDIRLLMDDLKMLQPTIFPVVPRLLNRMFDkifgqanttmkrwildfASKRKEAEL 427
Cdd:PRK06710 263 -GMTAVMNLSIM--QGYKMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALLN-----------------SPLLKEYDI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 RSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT------VPGDw 501
Cdd:PRK06710 323 SS------------------------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNflwekrVPGS- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 taghVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDR 581
Cdd:PRK06710 378 ----IGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDR 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1788937591 582 KKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLI 624
Cdd:PRK06710 453 KKDMI-VASGFNVYPREVEEVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-672 |
4.42e-24 |
|
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: 107.13 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 107 PCLGSRKPDQPYEWISYKEVADKAEYVGSALLQKGYkpSPDQYFGIFAQNRPEWVIIEQGCY---AYSMVVVPLYDTLGN 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGL--SAERPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 184 E--AITYIINKAELSLVFVDKSDKVDLMLESVenkLTPGLKTIIIMDPFDSdvveRGKKCGVEIMSMKALEDLGRANRRK 261
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVSRNAVAG----RGAISFAELAATPPTAAVDAAFAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 262 pkppSPGDLAVICFTSGTTGNPKGALITHQNVVSDcSAFVKVTENVVAPSPDdILISFLPLAHMF--ERVVEKTLRlNSS 339
Cdd:cd05921 163 ----GPDTVAKFLFTSGSTGLPKAVINTQRMLCAN-QAMLEQTYPFFGEEPP-VLVDWLPWNHTFggNHNFNLVLY-NGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 340 DIHISY-LPLAHMYEQLMlcvmlchgakigffqgdirllmDDLKMLQPTIFPVVPrllnrmfdkifgqanttmKRWILDF 418
Cdd:cd05921 236 TLYIDDgKPMPGGFEETL----------------------RNLREISPTVYFNVP------------------AGWEMLV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 419 ASKRKEAELRsgiirnnslwdkiifhkiqASLGGKVRLMVTGAAPVSATVLTFLRAaLGCQ-------FYEGYGQTECTA 491
Cdd:cd05921 276 AALEKDEALR-------------------RRFFKRLKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATETAP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 492 GCSLTVPGDWTAGHVGAPMPCCLIKLVDVEemnylaakGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWL 571
Cdd:cd05921 336 TATFTHWPTERSGLIGLPAPGTELKLVPSG--------GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 572 ----PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYQRSEPVAQVFVHGESlQAFLIAIVIPDVETLSSWAKKKgfSG 645
Cdd:cd05921 408 dpddPAKGLVFDGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACRRLVGLQ--EA 484
|
570 580
....*....|....*....|....*..
gi 1788937591 646 SHADLCRNKDVKKAILDDMVRLGKEAG 672
Cdd:cd05921 485 SDAEVLRHAKVRAAFRDRLAALNGEAT 511
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
266-636 |
4.61e-24 |
|
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: 106.47 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENvvapSPDDILISFLplAHMFervvektlrlnssDIHIsy 345
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGL----TSESRVLQFA--SYTF-------------DVSI-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 lplahmYEQLMlcvMLCHGAKIGffqgdI---RLLMDDLkmlqptifpvvPRLLNRMfdkifgQANTtmkrwildfaskr 422
Cdd:cd05918 163 ------LEIFT---TLAAGGCLC-----IpseEDRLNDL-----------AGFINRL------RVTW------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 keAELRSGIIRnnslwdkiIFHKIQASLggkVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCSLT-VPGDW 501
Cdd:cd05918 199 --AFLTPSVAR--------LLDPEDVPS---LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSpVVPST 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 TAGHVGAPMPCCLIkLVDVEEMNYLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALDKD-GWLH------------TGDI 567
Cdd:cd05918 264 DPRNIGRPLGATCW-VVDPDNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDL 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 568 GKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEP-----VAQVFVH-GESLQAFLIAIVIPDVETLSS 636
Cdd:cd05918 343 VRYNPDGSLEYVGRKDTQVKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSSGS 416
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
47-672 |
1.10e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 106.12 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 47 RPKALKPPcdlsmqSVEVE-GTDGARrsaILDSDEPLSffyDDVTTLYETFQRGIQVSNNGPCLGSRKPDQPYEWISYKE 125
Cdd:PRK08180 7 RPVAFAPP------AVEVErRADGTI---YLRSAEPLG---DYPRRLTDRLVHWAQEAPDRVFLAERGADGGWRRLTYAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 126 VADKAEYVGSALLQKGYkpSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPL---YdtlgneaityiinkaelSLVFVDK 202
Cdd:PRK08180 75 ALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaY-----------------SLVSQDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 203 SDkvdlmLESVENKLTPGL----------KTIIIMDPFDSDVV-ERGKKCGVEIMSMKALEDL--GRANRRKPKPPSPGD 269
Cdd:PRK08180 136 GK-----LRHVLELLTPGLvfaddgaafaRALAAVVPADVEVVaVRGAVPGRAATPFAALLATppTAAVDAAHAAVGPDT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 270 LAVICFTSGTTGNPKGALITHQNVVS------DCSAFVKVTENVvapspddiLISFLPLAHMFErvvektlrlNSSDIHI 343
Cdd:PRK08180 211 IAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPPV--------LVDWLPWNHTFG---------GNHNLGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 sylplahmyeqlmlcvMLCHGAKI---------GFFQGDIRllmdDLKMLQPTIFPVVPR----LLNRMfdkifgqantt 410
Cdd:PRK08180 274 ----------------VLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemLVPAL----------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 411 mkrwildfaskRKEAELRsgiirnnslwdkiifhkiqASLGGKVRLMVTGAAPVSATVLTFL----RAALGCQ--FYEGY 484
Cdd:PRK08180 323 -----------ERDAALR-------------------RRFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGL 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 485 GQTEcTAGCSL--TVPGDwTAGHVGAPMPCCLIKLVDVEemnylaakGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWL 562
Cdd:PRK08180 373 GMTE-TAPSATftTGPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYY 442
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 563 HTGDIGKWL----PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYQRSEPVAQVFVHGESlQAFLIAIVIPDVETLSS 636
Cdd:PRK08180 443 RSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITGHD-RDEIGLLVFPNLDACRR 521
|
650 660 670
....*....|....*....|....*....|....*.
gi 1788937591 637 WAKKKGfSGSHADLCRNKDVKKAILDDMVRLGKEAG 672
Cdd:PRK08180 522 LAGLLA-DASLAEVLAHPAVRAAFRERLARLNAQAT 556
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-616 |
4.84e-23 |
|
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: 100.81 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNvvsdcsafvkvtenvvapspddILISFLPLAHmfervvekTLRLNSSDIHISYLPL 348
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN----------------------LIAANLQLIH--------AMGLTEADVYLNMLPL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AH-MYEQLMLCVMLCHGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKIfgqanttmkrwildfasKRKEAEL 427
Cdd:cd17637 51 FHiAGLNLALATFHAGGANVVMEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAA-----------------EKSGVDL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 RSgiIRNnslwdkiifhkiqaslggkvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCSLTVPGDWTAGHV 506
Cdd:cd17637 114 SS--LRH-----------------------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSA 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 507 GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KH 584
Cdd:cd17637 165 GRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKE 242
|
330 340 350
....*....|....*....|....*....|..
gi 1788937591 585 IFKlAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:cd17637 243 LIK-PGGENVYPAEVEKVILEHPAIAEVCVIG 273
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
112-614 |
7.70e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 102.91 E-value: 7.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQPY-----EWISYKEVADKAEYVGSALLQKGYKPSpDQyFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAI 186
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVKRG-DR-VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 187 TYIINKAELSLVFVDkSDKVDLmLESVENKLTPgLKTIIIMDPFDSDVVERGkkcgVEIMSMKALedlgrANRRKPKPPS 266
Cdd:PRK06155 111 EHILRNSGARLLVVE-AALLAA-LEAADPGDLP-LPAVWLLDAPASVSVPAG----WSTAPLPPL-----DAPAPAAAVQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHqnvvsdcsafvkvtenvvapspddilisflplAHMF--ERVVEKTLRLNSSDIHIS 344
Cdd:PRK06155 179 PGDTAAILYTSGTTGPSKGVCCPH--------------------------------AQFYwwGRNSAEDLEIGADDVLYT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 345 YLPLAHMYEQLMLCVMLCHGAKI---------GFFqgdirllmDDLKMLQPTIFPVVPRLLNrmfdkifgqanttmkrwI 415
Cdd:PRK06155 227 TLPLFHTNALNAFFQALLAGATYvleprfsasGFW--------PAVRRHGATVTYLLGAMVS-----------------I 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 416 LDfaSKRKEAELRSgiirnnslwdkiifHKIQASLGGKVrlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCSL 495
Cdd:PRK06155 282 LL--SQPARESDRA--------------HRVRVALGPGV----------PAALHAAFRERFGVDLLDGYGSTETNFVIAV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 496 TVPGDwTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVF---KGYLKDPAKTAEALdKDGWLHTGDIGKWLP 572
Cdd:PRK06155 336 THGSQ-RPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDA 412
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1788937591 573 NGTLKIIDRKKHIFKlAQGEYIAPEKIENIYQRSEPVAQVFV 614
Cdd:PRK06155 413 DGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAV 453
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-641 |
8.20e-23 |
|
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: 102.41 E-value: 8.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 111 SRKPDQPY-----EWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVI----IEQGCYAYsmvvVPLYDTL 181
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVGP--DTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 182 GNEAITYIINKAELSLVFVDKsdKVDlmlesvenKLTPGLKTIIIMDpfDSDVVERGKkcgveimsmkalEDLGRANRrk 261
Cdd:cd17655 82 PEERIQYILEDSGADILLTQS--HLQ--------PPIAFIGLIDLLD--EDTIYHEES------------ENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 262 pkppsPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVtenVVAPSPDDILIsFLPLAhmFERVVEKtlrlnssdi 341
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKV---IYQGEHLRVAL-FASIS--FDASVTE--------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 342 hisylplahMYEQLMLCVMLChgakigffqgdirllmddlkmlqptIFPVVPRLLNRMFDKIFGQANTTmkrwildfASK 421
Cdd:cd17655 196 ---------IFASLLSGNTLY-------------------------IVRKETVLDGQALTQYIRQNRIT--------IID 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 422 RKEAELRsgiirnnslwdkiIFHKIQASLGGKVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCS--LTV 497
Cdd:cd17655 234 LTPAHLK-------------LLDAADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 498 PGDWTAGHV--GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWL------HTGDIGK 569
Cdd:cd17655 301 PETDQQVSVpiGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLAR 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788937591 570 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQ--VFVH-GESLQAFLIAIVIPD----VETLSSWAKKK 641
Cdd:cd17655 380 WLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSEkelpVAQLREFLARE 457
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
113-637 |
8.68e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 102.93 E-value: 8.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 113 KPDQPY-----EWISYKEVADKAEYVGSALLQKGYKpspdqyFG----IFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGN 183
Cdd:PRK07786 30 QPDAPAlrflgNTTTWRELDDRVAALAGALSRRGVG------FGdrvlILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 184 EAITYIINKAELSLVFVDKsdkvdlMLESVE---NKLTPGLKTIIIM-DPFDSDVVergkkcgveimsmkALEDLGRANr 259
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEA------ALAPVAtavRDIVPLLSTVVVAgGSSDDSVL--------------GYEDLLAEA- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 260 rkPKPPSPGDL-----AVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTEnvvAPSPDDILISFLPLAHMfervvektl 334
Cdd:PRK07786 163 --GPAHAPVDIpndspALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVGVPLFHI--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 335 rlnssdihisyLPLAHMYEQLMLcvmlchGAKIgffqgdirllmddlkmlqpTIFPVvprllnRMFDKifGQanttmkrw 414
Cdd:PRK07786 229 -----------AGIGSMLPGLLL------GAPT-------------------VIYPL------GAFDP--GQ-------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 415 ILDFAskrkEAELRSGIIRNNSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT-AG 492
Cdd:PRK07786 257 LLDVL----EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSpVT 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 493 CSLTvpGD---WTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDkDGWLHTGDIGK 569
Cdd:PRK07786 333 CMLL--GEdaiRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVR 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788937591 570 WLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAF---LIAIVIPD-------VETLSSW 637
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEF 485
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-642 |
1.31e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.44 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGR--GDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKS-DKVDL--MLESVENKLtPGLKTIIIMDPFDSDVVERgkkcgveIMSMKALE---DLGR--ANRRkpkpPSPGDLAV 272
Cdd:PRK13295 134 PKTfRGFDHaaMARRLRPEL-PALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGPDDVTQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 273 ICFTSGTTGNPKGALITHQNVVSdcsafvkvteNVVapspddilisflPLAhmfERvvektLRLNSSDIHISYLPLAH-- 350
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMA----------NIV------------PYA---ER-----LGLGADDVILMASPMAHqt 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 351 --MYeQLMLCVMLchGAKIgffqgdirllmddlkMLQPTIFPVvprllnRMFDKI------FGQANTTmkrWILDFASKR 422
Cdd:PRK13295 252 gfMY-GLMMPVML--GATA---------------VLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 KEAELRSgiirnnslwdkiifhkiqASLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCSLTVPGD-- 500
Cdd:PRK13295 305 KESGRPV------------------SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpd 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 -WTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEalDKDGWLHTGDIGKWLPNGTLKII 579
Cdd:PRK13295 362 eRASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRIS 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788937591 580 DRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG---ESLQAFLIAIVIP------DVETLSSWAKKKG 642
Cdd:PRK13295 439 GRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAypdERLGERACAFVVPrpgqslDFEEMVEFLKAQK 509
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
267-633 |
1.32e-22 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 101.55 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSdcsaFVKVTENVVAPSPDDILISFLPLahmfervvektlrlnSSDihisyl 346
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPF---------------SFD------ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plahmyeqlmLCVM-----LCHGAKIGFF----QGDIRLLMDDLKMLQPTIFPVVPRLLNR-MFDKIFGQANTTMKRWIL 416
Cdd:cd05945 151 ----------LSVMdlypaLASGATLVPVprdaTADPKQLFRFLAEHGITVWVSTPSFAAMcLLSPTFTPESLPSLRHFL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 417 dFAskrkeaelrsgiirnnslwdkiifhkiqaslggkvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT 496
Cdd:cd05945 221 -FC----------------------------------------GEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 497 -VPGDWTAGH----VGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKD---GWLHTGDIG 568
Cdd:cd05945 260 eVTPEVLDGYdrlpIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLV 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788937591 569 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV----HGESLQAfLIAIVIPDVET 633
Cdd:cd05945 339 RLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
173-583 |
1.36e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 102.73 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 173 VVVPLYDTLGNEAITYIINKAELSLVF-------VDKSDKVDLMLESVenkltPGLKTIIIMDPfdSDVVERGKKCGVEI 245
Cdd:PRK07529 108 IANPINPLLEPEQIAELLRAAGAKVLVtlgpfpgTDIWQKVAEVLAAL-----PELRTVVEVDL--ARYLPGPKRLAVPL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 246 MSMKA---LEDLGRANRRKP-------KPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDC---SAFVKVTenvvapsP 312
Cdd:PRK07529 181 IRRKAharILDFDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLG-------P 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 313 DDILISFLPLAHMFERVVektlrlnssdihisylplahmyeQLMLcvMLCHGAKIGF-----FQGDirLLMDDLKML--- 384
Cdd:PRK07529 254 GDTVFCGLPLFHVNALLV-----------------------TGLA--PLARGAHVVLatpqgYRGP--GVIANFWKIver 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 385 -QPTIFPVVPRLLNRMFDKIFGQANTTmkrwildfaskrkeaelrsgiirnnslwdkiifhkiqaSLggkvRLMVTGAAP 463
Cdd:PRK07529 307 yRINFLSGVPTVYAALLQVPVDGHDIS--------------------------------------SL----RYALCGAAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 464 VSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVP-GDWTAGHVGAPMPCCLIKLVDVEEM-NYL--AAKGE-GEICVKG 538
Cdd:PRK07529 345 LPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAG 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1788937591 539 SNVFKGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 583
Cdd:PRK07529 425 PNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-624 |
1.62e-22 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 101.02 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPlydtlgneaITYIINKAELSLVFV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVP---------INPMLKERELEYILN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKsdkvdlmlesvenkltpGLKTIIIMDPFDsdvvergkkcgveimsmkaledlgranrrkpkppspgDLAVICFTSGTT 280
Cdd:cd05935 71 DS-----------------GAKVAVVGSELD-------------------------------------DLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 281 GNPKGALITHQNVVSDCSAFVKVTeNVvapSPDDILISFLPLAHMfervvektlrlnssdihisylplAHMYEQLMLCVM 360
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWT-GL---TPSDVILACLPLFHV-----------------------TGFVGSLNTAVY 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 361 LchGAKIGFF-QGDIRLLMDDLKMLQPTIFPVVPRLLNRMFdkifgqanttmkrwildfaskrkeaelrsgiirnNSLwd 439
Cdd:cd05935 150 V--GGTYVLMaRWDRETALELIEKYKVTFWTNIPTMLVDLL----------------------------------ATP-- 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 440 kiifhKIQASLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLIKLVD 519
Cdd:cd05935 192 -----EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVID 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 520 VEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 596
Cdd:cd05935 267 IETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWP 345
|
490 500 510
....*....|....*....|....*....|....*
gi 1788937591 597 EKIENIYQRSEPVAQVFV-------HGESLQAFLI 624
Cdd:cd05935 346 AEVEAKLYKHPAI*EVCVisvpderVGEEVKAFIV 380
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-654 |
1.65e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 101.61 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 120 WISYKEVADKAEYVGSALLQKGYkpSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVF 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 200 VDKSdkvdlmlesvenkltpglktiiimdpFD-SDVVERGKKcgveimSMKALedlgranrrkpKPPSPGDLAVICFTSG 278
Cdd:cd12118 107 VDRE--------------------------FEyEDLLAEGDP------DFEWI-----------PPADEWDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 279 TTGNPKGALITHQnvvsdcSAFVKVTENVVApspddilisflplahmfervvektLRLNSSDIHISYLPLAHmyeqlmlC 358
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILE------------------------WEMKQHPVYLWTLPMFH-------C 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 359 VMLCHGAKIGFFQG--------DIRLLMDDLKMLQPTIFPVVPRLLNrmfdkifgqanttmkrwildfaskrkeaelrsg 430
Cdd:cd12118 187 NGWCFPWTVAAVGGtnvclrkvDAKAIYDLIEKHKVTHFCGAPTVLN--------------------------------- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 431 IIRNNSlwdkiifHKIQASLGGKVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG----CSL-----TVPGDW 501
Cdd:cd12118 234 MLANAP-------PSDARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEE 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 TAG---HVGAPMPCCL-IKLVDVEEMNYLAAKGE--GEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGT 575
Cdd:cd12118 304 RARlkaRQGVRYVGLEeVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGY 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 576 LKIIDRKKHIFkLAQGEYIAPEKIENIyqrsepvaqVFVHGESLQAFLIAivIPD---VETLSSWAK-KKGFSGSHADL- 650
Cdd:cd12118 383 IEIKDRSKDII-ISGGENISSVEVEGV---------LYKHPAVLEAAVVA--RPDekwGEVPCAFVElKEGAKVTEEEIi 450
|
....*.
gi 1788937591 651 --CRNK 654
Cdd:cd12118 451 afCREH 456
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
112-600 |
1.90e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 101.42 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQP--------YEWiSYKEVaDKAEYVGSALLQKgYKPSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGN 183
Cdd:PRK09088 7 LQPQRLaavdlalgRRW-TYAEL-DALVGRLAAVLRR-RGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 184 EAITYIINKAELSLVFVDksdkvdlmlesvenkltpglktiiimdpfdsDVVERGKKCGVEIMSMKALEDLGRANRRKPK 263
Cdd:PRK09088 84 SELDALLQDAEPRLLLGD-------------------------------DAVAAGRTDVEDLAAFIASADALEPADTPSI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 264 PPSpgDLAVICFTSGTTGNPKGALITHQNVVSDCSAFvKVTENVVAPSpddiliSFLPLAHMFervvektlrlnssdiHI 343
Cdd:PRK09088 133 PPE--RVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-GVLGRVDAHS------SFLCDAPMF---------------HI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 SYLpLAHMYEQLMlcvmlcHGAKIGFFQGdirllmddlkmLQPTifpvvpRLLNRMFDKIFGqanttmkrwILDFASKRK 423
Cdd:PRK09088 189 IGL-ITSVRPVLA------VGGSILVSNG-----------FEPK------RTLGRLGDPALG---------ITHYFCVPQ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 424 EAELrsgiIRNNSLWDkiifhkiqASLGGKVRLMVTGAAP-VSATVLTFLraALGCQFYEGYGQTEctAGCSLTVPGDWT 502
Cdd:PRK09088 236 MAQA----FRAQPGFD--------AAALRHLTALFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCD 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 503 -----AGHVGAPMPCCLIKLVDVEEmNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLK 577
Cdd:PRK09088 300 virakAGAAGIPTPTVQTRVVDDQG-NDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFW 378
|
490 500
....*....|....*....|...
gi 1788937591 578 IIDRKKHIFkLAQGEYIAPEKIE 600
Cdd:PRK09088 379 VVDRKKDMF-ISGGENVYPAEIE 400
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
121-641 |
7.22e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 99.65 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKK--GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DksdkvdlmlesvenkltpglktiiimDPFDSDVVErgkkcgveIMSMKaLEDLGRANRRKPKPPSPGDL---AVICFTS 277
Cdd:PRK03640 106 D--------------------------DDFEAKLIP--------GISVK-FAELMNGPKEEAEIQEEFDLdevATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 278 GTTGNPKGALITHQN----VVSdcSAF-VKVTENvvapspDDILISfLPLahmfervvektlrlnssdIHISYLPLahMY 352
Cdd:PRK03640 151 GTTGKPKGVIQTYGNhwwsAVG--SALnLGLTED------DCWLAA-VPI------------------FHISGLSI--LM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 353 EQLML-CVMLCH----GAKIgffqgdIRLLMDDlkmlQPTIFPVVPRLLNRMFDKIfGQANTtmkrwildfaskrkeael 427
Cdd:PRK03640 202 RSVIYgMRVVLVekfdAEKI------NKLLQTG----GVTIISVVSTMLQRLLERL-GEGTY------------------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 rsgiirNNSLwdkiifhkiqaslggkvRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCSLTVPGDWTA---G 504
Cdd:PRK03640 253 ------PSSF-----------------RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 505 HVGAPMPCCLIKLVDveEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKH 584
Cdd:PRK03640 308 SAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSD 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 585 IFkLAQGEYIAPEKIENIYQRSEPVAQVFVHGESLQ-------AFLIAIVIPDVETLSSWAKKK 641
Cdd:PRK03640 385 LI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
122-709 |
9.92e-22 |
|
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: 98.56 E-value: 9.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 122 SYKEVADKAEYVGSAL----LQKGykpspdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSL 197
Cdd:cd05972 2 SFRELKRESAKAANVLaklgLRKG------DRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 198 VFVDKSDkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkppspgdLAVICFTS 277
Cdd:cd05972 76 IVTDAED-----------------------------------------------------------------PALIYFTS 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 278 GTTGNPKGALITHQnvvsdcsafvkvtenvvapspddilisfLPLAHMfeRVVEKTLRLNSSDIHIS-------YLPLAH 350
Cdd:cd05972 91 GTTGLPKGVLHTHS----------------------------YPLGHI--PTAAYWLGLRPDDIHWNiadpgwaKGAWSS 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 351 MYEQLML--CVMLCHGAKIgffqgDIRLLMDDLKMLQPTIFPVVPrllnrmfdkifgqanTTMKRWI-LDFASKRKEAel 427
Cdd:cd05972 141 FFGPWLLgaTVFVYEGPRF-----DAERILELLERYGVTSFCGPP---------------TAYRMLIkQDLSSYKFSH-- 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 rsgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVG 507
Cdd:cd05972 199 --------------------------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMG 252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 508 APMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNV--FKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 585
Cdd:cd05972 253 RPTPGYDVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDI 330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 586 FKlAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLIaivipdvetlsswaKKKGFSGShadlcrnkdvkK 658
Cdd:cd05972 331 IK-SSGYRIGPFEVESALLEHPAVAEAAVvgspdpvRGEVVKAFVV--------------LTSGYEPS-----------E 384
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1788937591 659 AILDDMVRLGKEAgLKPFEQVKGITLHSELftvengLLTPTLKSKRPELRK 709
Cdd:cd05972 385 ELAEELQGHVKKV-LAPYKYPREIEFVEEL------PKTISGKIRRVELRD 428
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-636 |
1.06e-21 |
|
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: 99.12 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGykPSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARG--LRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKsdkvdlmlesvenkltpglktiiimdpfDSDVVERGKKCGVEIMSMKALEDLGRANRR----KPKPPSPGDLAVICFT 276
Cdd:cd05923 107 AV----------------------------DAQVMDAIFQSGVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 277 SGTTGNPKGALITHQNVVSDCSAFVKVTEnvvapspddilisflplahmfervvektLRLNSSDIHISYLPLAHMyeqlm 356
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAESRVLFMSTQAG----------------------------LRHGRHNVVLGLMPLYHV----- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 357 lcvmlchgakIGFFQgdirLLMDDLkMLQPTIFPVvprllnRMFDKifGQAnttmKRWIldfaskrkEAELRSGIIRNNS 436
Cdd:cd05923 206 ----------IGFFA----VLVAAL-ALDGTYVVV------EEFDP--ADA----LKLI--------EQERVTSLFATPT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 437 LWDKIIFHKIQASLGGK-VRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCSLTVPgDWTAGHVGAPMPCCLI 515
Cdd:cd05923 251 HLDALAAAAEFAGLKLSsLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 516 KLVDV-EEMNYLAAKG-EGEICVK--GSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 591
Cdd:cd05923 328 RIVRIgGSPDEALANGeEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGG 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1788937591 592 EYIAPEKIENIYQRSEPVAQVFVHG---ESLQAFLIAIVIPDVETLSS 636
Cdd:cd05923 406 ENIHPSEIERVLSRHPGVTEVVVIGvadERWGQSVTACVVPREGTLSA 453
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
119-609 |
3.40e-21 |
|
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: 98.08 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 119 EWISYKEVADKAEYVGSALLQKGykpSPDQYFGIFAQNRPEWVIIEQGC-YAySMVVVPLYDTLGNEA---ITYIINKAE 194
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGClYA-GAIAVPLPPPTPGRHaerLAAILADAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 195 LSLVFVDKS--DKVDLMLESVENKLTPglkTIIIMDPFDSDVvergkkcgveimsmkaledlgrANRRKPKPPSPGDLAV 272
Cdd:cd05931 99 PRVVLTTAAalAAVRAFAASRPAAGTP---RLLVVDLLPDTS----------------------AADWPPPSPDPDDIAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 273 ICFTSGTTGNPKGALITHQNVVSDCSAFVKVTEnvvaPSPDDILISFLPLAHmfervvektlrlnssDIHISYLPLAHMY 352
Cdd:cd05931 154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG----LDPGDVVVSWLPLYH---------------DMGLIGGLLTPLY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 353 EQLmLCVMLchgAKIGFFQGDIRLLmddlkmlqptifpvvpRLLNRmfdkifGQANTT-MKRWILDFASKRKEAELRSGI 431
Cdd:cd05931 215 SGG-PSVLM---SPAAFLRRPLRWL----------------RLISR------YRATISaAPNFAYDLCVRRVRDEDLEGL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 432 irnnslwDkiifhkiqasLGgKVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECTAGCSLTVPG------ 499
Cdd:cd05931 269 -------D----------LS-SWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATLFVSGGPPGtgpvvl 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 500 ----DWTAGHV----------------GAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAE----- 554
Cdd:cd05931 331 rvdrDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgal 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1788937591 555 -ALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPV 609
Cdd:cd05931 411 aATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-609 |
5.73e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 97.37 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 220 GLKTIIIMDPFDSDV---VERGkkcgveiMSMKALEDLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSD 296
Cdd:PRK07768 108 GAKAVVVGEPFLAAApvlEEKG-------IRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 297 CSAfvkvtenvvapspddilisflplahMFERV---VEKtlrlnssDIHISYLPLAH-MYEQLMLCVMLCHGAkigffqg 372
Cdd:PRK07768 181 AEA-------------------------MFVAAefdVET-------DVMVSWLPLFHdMGMVGFLTVPMYFGA------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 373 dirllmdDLKMLQPTIFPVVPRLLNRMFDKIfgQANTTMKRwilDFA----SKRkeaeLRSgiirnnslwdkiifhkiQA 448
Cdd:PRK07768 222 -------ELVKVTPMDFLRDPLLWAELISKY--RGTMTAAP---NFAyallARR----LRR-----------------QA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 449 SLG----GKVRLMVTGAAPVS-ATVLTFLRA---------ALGCqfyeGYGQTECTAGCSLTVPGD-------------- 500
Cdd:PRK07768 269 KPGafdlSSLRFALNGAEPIDpADVEDLLDAgarfglrpeAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaa 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 ------WTAGHV------GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLkDPAKTAEALDKDGWLHTGDIG 568
Cdd:PRK07768 345 lrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLG 422
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1788937591 569 KWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPV 609
Cdd:PRK07768 423 YLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIERAAARVEGV 462
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-641 |
1.78e-20 |
|
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: 95.35 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKP----------SPDQYFGIFAqnrpewvIIEQGCyAYsmvvVPLYDTLGNEAITYII 190
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGPgdvvgvlaerSPELVVALLA-------VLKAGA-AY----VPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 191 NKAELSLVFVDKSDKVDLmlesvenkltPGLKTIIIMDPFDSDVVERGKKCgveimsmkaledlgranrrkpkPPSPGDL 270
Cdd:cd12117 91 ADAGAKVLLTDRSLAGRA----------GGLEVAVVIDEALDAGPAGNPAV----------------------PVSPDDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 271 AVICFTSGTTGNPKGALITHQNVVSdcsaFVKVTeNVVAPSPDDILISFLPLAhmFErvvektlrlnssdihisylplAH 350
Cdd:cd12117 139 AYVMYTSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLA--FD---------------------AS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 351 MYEqlmLCVMLCHGAKIgffqgdirLLMDDLKMLQPTifpvvprllnRMFDKIFGQANTTMkrWildfaskrkeaeLRSG 430
Cdd:cd12117 191 TFE---IWGALLNGARL--------VLAPKGTLLDPD----------ALGALIAEEGVTVL--W------------LTAA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 431 IIrnNSLWDKIIfhkiqASLGGkVRLMVTGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCSLTVPGDWTAGHV- 506
Cdd:cd12117 236 LF--NQLADEDP-----ECFAG-LRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIp 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 507 -GAPMPCCLIKLVDveEMNYLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKI 578
Cdd:cd12117 308 iGRPIANTRVYVLD--EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEF 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 579 IDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV------HGE-SLQAFLIAIVIPDVETLSSWAKKK 641
Cdd:cd12117 386 LGRIDDQVKI-RGFRIELGEIEAALRAHPGVREAVVvvredaGGDkRLVAYVVAEGALDAAELRAFLRER 454
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-576 |
1.87e-20 |
|
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: 96.85 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 86 YDDVTTLYETFQRgiQVSnngpclgsRKPDQP-----YEWISYKEVADKAEYVGSALLQKGYKP----------SPDQYF 150
Cdd:COG1020 472 YPADATLHELFEA--QAA--------RTPDAVavvfgDQSLTYAELNARANRLAHHLRALGVGPgdlvgvclerSLEMVV 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 151 GIFAqnrpewvIIEQGCyAYsmvvVPLYDTLGNEAITYIINKAELSLVfvdksdkvdlmlesvenkLTpglktiiimdpf 230
Cdd:COG1020 542 ALLA-------VLKAGA-AY----VPLDPAYPAERLAYMLEDAGARLV------------------LT------------ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 231 DSDVVERGKKCGVEIMSMKALEDLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSdcsaFVKVTENVVAP 310
Cdd:COG1020 580 QSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGL 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 311 SPDDILISFLPLAhmFervvektlrlnssDihisylplAHMYEqlmLCVMLCHGAKIGFFQGDIRL----LMDDLKMLQP 386
Cdd:COG1020 656 GPGDRVLQFASLS--F-------------D--------ASVWE---IFGALLSGATLVLAPPEARRdpaaLAELLARHRV 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 387 TIFPVVPRLLNRMFDkifgqanttmkrwildfASKRKEAELRsgiirnnslwdkiifhkiqaslggkvRLMVTGAAPVSA 466
Cdd:COG1020 710 TVLNLTPSLLRALLD-----------------AAPEALPSLR--------------------------LVLVGGEALPPE 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 467 TVLTFLRAALGCQFYEGYGQTECTAGCSLTV--PGDWTAGHV--GAPMPCCLIKLVDvEEMNyLAAKG-EGEICVKGSNV 541
Cdd:COG1020 747 LVRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQ-PVPVGvPGELYIGGAGL 824
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1788937591 542 FKGYLKDPAKTAEA-----LDKDG--WLHTGDIGKWLPNGTL 576
Cdd:COG1020 825 ARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-630 |
2.21e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 95.05 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 119 EWISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGP--GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 199 fvdksdkvdlmlesvenkLTpglktiiimdpfDSDVVERGKKCGVEIMsmKALEDLGRANRRKPKPPSPGDLAVICFTSG 278
Cdd:cd12116 89 ------------------LT------------DDALPDRLPAGLPVLL--LALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 279 TTGNPKGALITHQNVVSdcsaFVKVTENVVAPSPDDILISFLPLAhmFervvektlrlnssDIHIsylplahmyeqLMLC 358
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--F-------------DISL-----------LELL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 359 VMLCHGAKIGFFQGDIRllMDDLKMLQ------PTIFpvvprllnrmfdkifgQANTTMKRWILDfaskrkeaelrSGii 432
Cdd:cd12116 187 LPLLAGARVVIAPRETQ--RDPEALARlieahsITVM----------------QATPATWRMLLD-----------AG-- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 433 rnnslWDKiifhkiQASLggkvRLMVTGAA--PVSATVLTflraALGCQFYEGYGQTECT--AGCSLTVPGDwTAGHVGA 508
Cdd:cd12116 236 -----WQG------RAGL----TALCGGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 509 PMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDR 581
Cdd:cd12116 296 PLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGR 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1788937591 582 KKHIFKLaQGEYIAPEKIENIYQRSEPVAQ--VFVHGESLQAFLIAIVIPD 630
Cdd:cd12116 375 ADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-639 |
2.33e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 95.41 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQPYEW-----ISYKEVADKAEYVGSALLQK-GYKPSpDQyFGIFAQNRPEWVIieqGCYAYSM---VVVPLYDTLG 182
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLQQEcGVRKG-DR-VLLYMQNSPQFVI---AYYAILRanaVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 183 NEAITYIINKAELSLVFVdKSDKVDLMLESVEnklTPGLKTIII-----MDPFDSDV------VERGKKCGVEIMSMKAL 251
Cdd:PRK08314 97 EEELAHYVTDSGARVAIV-GSELAPKVAPAVG---NLRLRHVIVaqysdYLPAEPEIavpawlRAEPPLQALAPGGVVAW 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 252 EDLGRANRRkPKP--PSPGDLAVICFTSGTTGNPKGALITHQNVVSdcsafvkvteNVVAPS------PDDILISFLPLA 323
Cdd:PRK08314 173 KEALAAGLA-PPPhtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMA----------NAVGSVlwsnstPESVVLAVLPLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 324 HmfervvektlrlnssdihisylpLAHMyeQLMLCVMLCHGAKIgffqgdirLLMddlkmlqptifP-----VVPRLLNR 398
Cdd:PRK08314 242 H-----------------------VTGM--VHSMNAPIYAGATV--------VLM-----------PrwdreAAARLIER 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 399 mFDKIFGQANTTMkrwILDF-ASKR-KEAELRSgiirnnslwdkiifhkiQASLGGkvrlmvtGAAPVSATVLTFLRAAL 476
Cdd:PRK08314 278 -YRVTHWTNIPTM---VVDFlASPGlAERDLSS-----------------LRYIGG-------GGAAMPEAVAERLKELT 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 477 GCQFYEGYGQTEcTAGCSLTVPGDwtaghvgAPMPCCL--------IKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKD 548
Cdd:PRK08314 330 GLDYVEGYGLTE-TMAQTHSNPPD-------RPKLQCLgiptfgvdARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 549 PAKTAEA---LDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYQRSEPVAQVFV-------HGES 618
Cdd:PRK08314 402 PEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGET 480
|
570 580
....*....|....*....|....*
gi 1788937591 619 LQAFLI----AIVIPDVETLSSWAK 639
Cdd:PRK08314 481 VKAVVVlrpeARGKTTEEEIIAWAR 505
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-617 |
5.41e-20 |
|
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: 92.16 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENvvapSPDDILISFLPLAHMFERVVEKTLRLnSSDIHISYL 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLF----DPDDVLLCGLPLFHVNGSVVTLLTPL-ASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 -PLAHMYEQLMlcvmlchgakigffqGDIRLLMDDLKmlqPTIFPVVPRLLNrmfdkifgqanTTMKRWIldfaskrkEA 425
Cdd:cd05944 76 gPAGYRNPGLF---------------DNFWKLVERYR---ITSLSTVPTVYA-----------ALLQVPV--------NA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 426 ELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVP-GDWTAG 504
Cdd:cd05944 119 DISS------------------------LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 505 HVGAPMPCCLIKLVDVE-EMNYL--AAKGE-GEICVKGSNVFKGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIID 580
Cdd:cd05944 175 SVGLRLPYARVRIKVLDgVGRLLrdCAPDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITG 253
|
330 340 350
....*....|....*....|....*....|....*..
gi 1788937591 581 RKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHGE 617
Cdd:cd05944 254 RAKDLI-IRGGHNIDPALIEEALLRHPAVAFAGAVGQ 289
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
119-624 |
1.96e-19 |
|
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: 91.72 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 119 EWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLV 198
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKG--DRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 199 FVDKSDkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkppspgDLAVICFTSG 278
Cdd:cd05971 83 VTDGSD----------------------------------------------------------------DPALIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 279 TTGNPKGALITHQnvvsdcsafvkvtenvvapspddILISFLPlahmferVVEKTLRLNSSDIHISYLPlahmyeqlmlc 358
Cdd:cd05971 99 TTGPPKGALHAHR-----------------------VLLGHLP-------GVQFPFNLFPRDGDLYWTP----------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 359 vmlchgAKIGFFQGdirlLMDdlkMLQPTIFPVVPRLLNRM--FDKifGQANTTMKRWILDFASKRKEAeLRsgIIRnns 436
Cdd:cd05971 138 ------ADWAWIGG----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR--- 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 437 lwdkiiFHKIQASLGG-KVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCSLTVPGDwtAGHVGAPMPC 512
Cdd:cd05971 197 ------QQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPG 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 513 CLIKLVDvEEMNYLAAKGEGEICVK--GSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 590
Cdd:cd05971 269 HRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS- 345
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1788937591 591 GEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLI 624
Cdd:cd05971 346 GYRIGPAEIEECLLKHPAVLMAAVvgipdpiRGEIVKAFVV 386
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
173-635 |
1.97e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 92.44 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 173 VVVPLYDTLGNEAITYIINKAELSLVFVdkSDKVDLMLESVENKLTPGLKTIIIMDPFDSDVVergkkcGVeiMSMKALE 252
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVT--SAQFYPMYRQIQQEDATPLRHICLTRVALPADD------GV--SSFTQLK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 253 DLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVsdcsaFVKV-TENVVAPSPDDILISFLPlahmfervve 331
Cdd:PRK08008 158 AQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR-----FAGYySAWQCALRDDDVYLTVMP---------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 332 ktlrlnssDIHISYLPLAHMyeqlmlcVMLCHGAKIGF--------FQGDIRL----------LMDDLKMLQPtifpVVP 393
Cdd:PRK08008 223 --------AFHIDCQCTAAM-------AAFSAGATFVLlekysaraFWGQVCKyratitecipMMIRTLMVQP----PSA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 394 -----RLLNRMFdkifgqanttmkrwILDFASKRKEA-ELRSGiirnnslwdkiifhkiqaslggkVRLMVTgaapvsat 467
Cdd:PRK08008 284 ndrqhCLREVMF--------------YLNLSDQEKDAfEERFG-----------------------VRLLTS-------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 468 vltflraalgcqfyegYGQTECTAGCSLTVPGD---WTAghVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKG---SNV 541
Cdd:PRK08008 319 ----------------YGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 542 FKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFVHG----- 616
Cdd:PRK08008 380 FKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGikdsi 458
|
490 500
....*....|....*....|.
gi 1788937591 617 --ESLQAFliaIVIPDVETLS 635
Cdd:PRK08008 459 rdEAIKAF---VVLNEGETLS 476
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
47-697 |
9.81e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 90.49 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 47 RPKALKPPcdlsmqSVEVEG-TDGarrSAILDSDEPLSffyDDVTTLYETFQRGIQVSNNGPCLGSRKPDQ-PYEWISYK 124
Cdd:PRK12582 17 RPLNWKPP------DISVERrADG---SIVIKSRHPLG---PYPRSIPHLLAKWAAEAPDRPWLAQREPGHgQWRKVTYG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 125 EVADKAEYVGSALLQKGYkpSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPL---YDTLGNE--AITYIINKAELSLVF 199
Cdd:PRK12582 85 EAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 200 VDKSDKVDLMLESVE---------NKLTPGLKTIiimdPFDsDVVERGKKCGVEimsmKALEDLGranrrkpkppsPGDL 270
Cdd:PRK12582 163 AQSGAPFARALAALDlldvtvvhvTGPGEGIASI----AFA-DLAATPPTAAVA----AAIAAIT-----------PDTV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 271 AVICFTSGTTGNPKGALITHQNVvsdCSAFVKVtENVVAPSPDD---ILISFLPLAHMFE-RVVEKTLRLNSSDIHISY- 345
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRMM---CANIAMQ-EQLRPREPDPpppVSLDWMPWNHTMGgNANFNGLLWGGGTLYIDDg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 LPLAHMYEQlmlcvmlchgakigffqgDIRllmdDLKMLQPTIFPVVPRLLNRMFDKIfgqanttmkrwildfaskRKEA 425
Cdd:PRK12582 299 KPLPGMFEE------------------TIR----NLREISPTVYGNVPAGYAMLAEAM------------------EKDD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 426 ELRSGIIRNnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGCSLTVpg 499
Cdd:PRK12582 339 ALRRSFFKN-------------------LRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAPTTTGT-- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 500 DWTA---GHVGAPMPCCLIKLVDVEEmNYlaakgegEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWL----P 572
Cdd:PRK12582 397 HWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddP 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 573 NGTLKIIDRKKHIFKLAQGEYIAPEKIE-NIYQRSEPVAQ-VFVHGESlQAFLIAIVIPDVETLSSWAKKKGfsGSHADL 650
Cdd:PRK12582 469 EKGLIFDGRVAEDFKLSTGTWVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDV 545
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1788937591 651 CRNKDVKKAILDDMVRLGKEAGlKPFEQVKGITLHSELFTVENGLLT 697
Cdd:PRK12582 546 VKHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
112-616 |
2.59e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 88.79 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQPY-----EWISYKEVADKAEYVGSALlqKGYKPSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAI 186
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRILQAAGML--HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 187 TYIINKAELSLVFVDKsdkvdlmlesvENKLTPGLKT-IIIMDPFDSDVVERGKKCGVEIMSMKaledlgranrrkpkPP 265
Cdd:PRK06145 92 AYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA--------------AV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVvsdcsaFVKVTENVVA--PSPDDILISFLPLAHmfervvektlrLNSSDihi 343
Cdd:PRK06145 147 APTDLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHVIAlgLTASERLLVVGPLYH-----------VGAFD--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 syLP-LAHMYEQLMLCVMLchgakigffQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFdkifgqanTTMKRWILDFASKR 422
Cdd:PRK06145 207 --LPgIAVLWVGGTLRIHR---------EFDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 keaelrsgiirnnslWdkiifhkiqaSLGGkvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWT 502
Cdd:PRK06145 268 ---------------W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREI 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 503 A--GHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIID 580
Cdd:PRK06145 316 EkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTD 393
|
490 500 510
....*....|....*....|....*....|....*..
gi 1788937591 581 RKKHIFkLAQGEYIAPEKIEN-IYQRSEpVAQVFVHG 616
Cdd:PRK06145 394 RKKDMI-ISGGENIASSEVERvIYELPE-VAEAAVIG 428
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
266-722 |
3.64e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 88.70 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAfvKVTenVVAPSPDDILISFLPLahmfervvektlrlnssdIHISY 345
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLA--KIA--IVGYGEDDVYLHTAPL------------------CHIGG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 LPLAhmyeQLMLCVMLCHGAKIGFfqgDIRLLMDDLKMLQPTIFPVVPRLL------NRMfdKIFGQANTTMKRwILDFA 419
Cdd:PLN02860 228 LSSA----LAMLMVGACHVLLPKF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRK-ILNGG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 420 SKrkeaelrsgiirnnslwdkiifhkIQASLGGKVRLMVTGAAPVSA-------TVLTFLRaalgcqFYEGYGQTECTAG 492
Cdd:PLN02860 298 GS------------------------LSSRLLPDAKKLFPNAKLFSAygmteacSSLTFMT------LHDPTLESPKQTL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 493 CSLTVPGDWTAGH-----VGAPMPCCLIKLVDVEEMNylaakgEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDI 567
Cdd:PLN02860 348 QTVNQTKSSSVHQpqgvcVGKPAPHVELKIGLDESSR------VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 568 GKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYQRSEPVAQVFVHGeSLQAFLIAIVIPDVETLSSWakkKGFSGSH 647
Cdd:PLN02860 422 GWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGW---IWSDNEK 496
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 648 ADLCRNKDVKKAILDDMVRlgkEAGLKPFEQVKGITLHSELFTvenglLTPTLKSKRPELRKYFRSQIDELYSTI 722
Cdd:PLN02860 497 ENAKKNLTLSSETLRHHCR---EKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-641 |
9.55e-18 |
|
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: 85.08 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSdcSAfvkvtenvvapspdDILISFLPLahmfervvektlrlNSSDIHISYLPL 348
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--------------AGLHSRLGF--------------GGGDSWLLSLPL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHM--YEQLMLCVMLchGAKIGFFQGDiRLLMDDLKMLQPTIFPVVPRLLNRMFDKifGQANTTMKRwildfaskrkeae 426
Cdd:cd17630 51 YHVggLAILVRSLLA--GAELVLLERN-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 lrsgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHV 506
Cdd:cd17630 113 ---------------------------LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 507 GAPMPCCLIKLVDveemnylaakgEGEICVKGSNVFKGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 586
Cdd:cd17630 165 GVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI 231
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788937591 587 kLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLIAIVIPDVETLSSWAKKK 641
Cdd:cd17630 232 -ISGGENIQPEEIEAALAAHPAVRDAFVvgvpdeeLGQRPVAVIVGRGPADPAELRAWLKDK 292
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
264-600 |
1.25e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 87.02 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 264 PPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTenvVAPSPDDILISFLPlahMFervvektlrlnssdihi 343
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA---VVGGEDSVFLSFLP---EF----------------- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 sylplahmyeqlmlcvmlchgakigFFQGDirllmdDLKMLQPTIF--PVVprLLNRmFDkifgqANTTMkrwildfask 421
Cdd:PRK06178 262 -------------------------WIAGE------NFGLLFPLFSgaTLV--LLAR-WD-----AVAFM---------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 422 rkEAELRSGIIRNNSLWDkiifhkiqaslgGKVRLMVTGAapVSATVLTFL--------------------RAALGCQFY 481
Cdd:PRK06178 293 --AAVERYRVTRTVMLVD------------NAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALTGSVLA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 482 EG-YGQTEcTAGCSltvpgDWTAG-------------HVGAPMPCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLK 547
Cdd:PRK06178 357 EAaWGMTE-THTCD-----TFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWN 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1788937591 548 DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 600
Cdd:PRK06178 431 KPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVE 481
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-629 |
2.39e-17 |
|
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: 85.88 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKR--EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 dkSDKVDLMLESVENKLTPGLKTIIIMDPFDSDVVErgkkcgveimsmKALEDL--GRANRRKPKPPSPGDLAVICFTSG 278
Cdd:cd05959 108 --SGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 279 TTGNPKGALITHQNVVSDCSAFVKvteNVVAPSPDDILISFLPLAHMFErvvektlrLNSSdihiSYLPLAhmyeqlmlc 358
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG--------LGNS----LTFPLS--------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 359 vmlchgakigffQGDIRLLM----------DDLKMLQPTIFPVVPRLLNRMFdkifgqANTTMKRWilDFASkrkeaelr 428
Cdd:cd05959 230 ------------VGATTVLMperptpaavfKRIRRYRPTVFFGVPTLYAAML------AAPNLPSR--DLSS-------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 429 sgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGA 508
Cdd:cd05959 282 -------------------------LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGK 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 509 PMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKl 588
Cdd:cd05959 337 PVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK- 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1788937591 589 AQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLI---AIVIP 629
Cdd:cd05959 414 VSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTkpkAFVVL 457
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
269-625 |
6.18e-17 |
|
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: 84.05 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKvteNVVAPSPDDILISflpLAHMFervveKTLRLNSSDIhisyLPL 348
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMF-----FGYGLGNSLW----FPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHmyeqlmlcvmlchGAKIGFFQG--DIRLLMDDLKMLQPTIFPVVPRLlnrmfdkifgqanttmkrwildFASKRKEAE 426
Cdd:cd05919 157 AV-------------GASAVLNPGwpTAERVLATLARFRPTVLYGVPTF----------------------YANLLDSCA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 LRSGIIRNnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHV 506
Cdd:cd05919 202 GSPDALRS-------------------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGST 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 507 GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 586
Cdd:cd05919 263 GRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDML 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1788937591 587 KLAqGEYIAPEKIENIYQRSEPVAQVFV------HGES-LQAFLIA 625
Cdd:cd05919 341 KVG-GQWVSPVEVESLIIQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
255-630 |
8.65e-17 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 85.02 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 255 GRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSafvKVTEnVVAPSPDDILISFLPLAHMFervvektl 334
Cdd:PRK06814 780 GRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRA---QVAA-RIDFSPEDKVFNALPVFHSF-------- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 335 rlnssdihisylplaHMYEQLMLcvMLCHGAKIGFFQgdirllmddlkmlQPTIFPVVPRLlnrmfdkIFgQANTTmkrw 414
Cdd:PRK06814 848 ---------------GLTGGLVL--PLLSGVKVFLYP-------------SPLHYRIIPEL-------IY-DTNAT---- 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 415 ILdFASKrkeaELRSGIIRNNSLWDkiiFHKIqaslggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCS 494
Cdd:PRK06814 886 IL-FGTD----TFLNGYARYAHPYD---FRSL--------RYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIA 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 495 LTVPGDWTAGHVGAPMPCCLIKLVDVEEMNylaaKGeGEICVKGSNVFKGYLK-DPAKTAEALdKDGWLHTGDIGKWLPN 573
Cdd:PRK06814 950 LNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEE 1023
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1788937591 574 GTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPvaqvfvhgESLQAfliAIVIPD 630
Cdd:PRK06814 1024 GFITIKGRAKRFAKIA-GEMISLAAVEELAAELWP--------DALHA---AVSIPD 1068
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
447-629 |
1.65e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.53 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 447 QASLGGKVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCSLTVPGD-WT------AGHVGAPMPCCLIKLVD 519
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLAD 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 520 VEEMNYLA-------AKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 592
Cdd:PLN03102 374 VDVKNKETqesvprdGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGE 451
|
170 180 190
....*....|....*....|....*....|....*..
gi 1788937591 593 YIAPEKIENIyqrsepvaqVFVHGESLQAFLIAIVIP 629
Cdd:PLN03102 452 NISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
264-630 |
2.11e-16 |
|
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: 82.78 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 264 PPSPGDLAVICFTSGTTGNPKGALITHQNVVSdcsaFVKVTENVVAPSPDDILISFLPLAhmFERVVEKTLrlnssdihi 343
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIF--------- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 SYLplahmyeqlmlcvmlCHGAKIGFFQGDIRllMDDLKMLqptifpvvpRLLNRM-FDKIFgqANTTMKRWILdfaskr 422
Cdd:cd17651 197 STL---------------CAGATLVLPPEEVR--TDPPALA---------AWLDEQrISRVF--LPTVALRALA------ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 kEAELRSGiirnnslwdkiifhkiqaSLGGKVRLMVTGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCSLTVPGD 500
Cdd:cd17651 243 -EHGRPLG------------------VRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 ---WTA-GHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWL------HTGDIGKW 570
Cdd:cd17651 304 paaWPApPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARW 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788937591 571 LPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQ--VFVHGE-SLQAFLIAIVIPD 630
Cdd:cd17651 383 LPDGELEFLGRADDQVKI-RGFRIELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGD 444
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-630 |
2.20e-16 |
|
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: 82.13 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTEnvvapspddilISFLPLAHMfeRVVEKTLRLNSSDihisyl 346
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYE-----------LDSFPVRLL--QMASFSFDVFAGD------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plahmyeqlmLCVMLCHGakigffqGDIRLLMDDLKMLQPTIFpvvpRLLNRMFDKIFgQANTTMKRWILDFASKRKE-- 424
Cdd:cd17650 153 ----------FARSLLNG-------GTLVICPDEVKLDPAALY----DLILKSRITLM-ESTPALIRPVMAYVYRNGLdl 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 AELRSGIIRNNSLWDKIiFHKIQASLGGKVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcslTVPgdwtag 504
Cdd:cd17650 211 SAMRLLIVGSDGCKAQD-FKTLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP------ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 505 hVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKI 578
Cdd:cd17650 272 -IGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVEL 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 579 IDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV---HGESLQAFLIAIVIPD 630
Cdd:cd17650 350 LGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-635 |
2.71e-16 |
|
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: 82.50 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKP-------SPdqyfgifaqNRPEWVIIeqgCYAYSMV-VVPLYdTL----GNEaITY 188
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPgdrvvvqLP---------NVAEFVIV---FFALFRAgAIPVF-ALpahrRAE-ISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 189 IINKAELS-LVFVDKSDKVDL--MLESVeNKLTPGLKTIIIMDPFDSDVvergkkcgveimsmkALEDLGRANRRKPKP- 264
Cdd:COG1021 117 FAEQSEAVaYIIPDRHRGFDYraLAREL-QAEVPSLRHVLVVGDAGEFT---------------SLDALLAAPADLSEPr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 265 PSPGDLAVICFTSGTTGNPKgaLI--THqnvvsdcsafvkvtenvvapspDDILISFlplahmfERVVEkTLRLNSSDIH 342
Cdd:COG1021 181 PDPDDVAFFQLSGGTTGLPK--LIprTH----------------------DDYLYSV-------RASAE-ICGLDADTVY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 343 ISYLPLAHMYeqlmlcVMLCHGAkIGFFQGDIRLLM-DDLKmlqP-TIFP-----------VVPRLLNRMfdkifgqant 409
Cdd:COG1021 229 LAALPAAHNF------PLSSPGV-LGVLYAGGTVVLaPDPS---PdTAFPlierervtvtaLVPPLALLW---------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 410 tmkrwiLDFASKRKeAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE- 488
Cdd:COG1021 289 ------LDAAERSR-YDLSS------------------------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEg 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 489 ---CTagcSLTVPGDWTAGHVGAPM-PCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHT 564
Cdd:COG1021 338 lvnYT---RLDDPEEVILTTQGRPIsPDDEVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRT 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788937591 565 GDIGKWLPNGTLKIIDRKK-HIFKlaQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFliaiVIPDVETLS 635
Cdd:COG1021 414 GDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENLLLAHPAVHDAAVvampdeyLGERSCAF----VVPRGEPLT 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-630 |
4.02e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.47 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYkpSPDQYFGIFAQNRPEWVI----IEQGCYAYsmvvVPLYDTLGNEAITYIINKAELS 196
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGV--GPEVRVAIAAERSFELVVallaVLKAGGAY----VPLDPNYPAERLAYMLEDSGAA 2102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 197 LVFVDKSDKVDLMLesvenkltPGlktiiimdpfdsdvvergkkcGVEIMSMKALEDLGRANRRKPKPP-SPGDLAVICF 275
Cdd:PRK12316 2103 LLLTQRHLLERLPL--------PA---------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIY 2153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 276 TSGTTGNPKGALITHQNVVSDCSAfvkvtenvvapspddilisflplahmfervVEKTLRLNSSDIHISYLPLAH--MYE 353
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVAHCQA------------------------------AGERYELSPADCELQFMSFSFdgAHE 2203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 354 QLMlcVMLCHGAkigffqgdiRLLMDDLKMLQPtifpvvprllNRMFDKIFGQANTtmkrwILDFASkrkeaelrsgiir 433
Cdd:PRK12316 2204 QWF--HPLLNGA---------RVLIRDDELWDP----------EQLYDEMERHGVT-----ILDFPP------------- 2244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 434 nnSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLTFLRAALGCQF-YEGYGQTECTagcslTVPGDWTAGHV------ 506
Cdd:PRK12316 2245 --VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYlFNGYGPTEAV-----VTPLLWKCRPQdpcgaa 2317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 507 GAPMPCCLIKL---VDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTL 576
Cdd:PRK12316 2318 YVPIGRALGNRrayILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVV 2397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1788937591 577 KIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV---HGESLQAfLIAIVIPD 630
Cdd:PRK12316 2398 EYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
453-600 |
4.12e-16 |
|
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: 81.77 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 453 KVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCSLTVPG-DWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGE 531
Cdd:cd05970 302 SLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCEAGEE 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 532 GEICVKGSN-----VFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIE 600
Cdd:cd05970 380 GEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVE 451
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
269-629 |
4.55e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 81.86 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTEnvvaPSPDDILISFLPLAHmfervvektlrlnssdihisylpl 348
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYR----LSPRDATVAVMPLYH------------------------ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHMYEQLMLCVMLCHGAKI----GFFQGdiRLLMDDLKMLQPTIFPVVPrllnrmfdkifgqantTMKRWILDFA----S 420
Cdd:PRK05852 229 GHGLIAALLATLASGGAVLlparGRFSA--HTFWDDIKAVGATWYTAVP----------------TIHQILLERAatepS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 421 KRKEAELRsgIIRNNSlwdkiifhkiqaslggkvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT---------- 490
Cdd:PRK05852 291 GRKPAALR--FIRSCS-------------------------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqieg 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 491 AGCSLTvPGDWT--AGHVGAPMpcclIKLVDVEEMNyLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIG 568
Cdd:PRK05852 344 IGQTEN-PVVSTglVGRSTGAQ----IRIVGSDGLP-LPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLG 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 569 KWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFVHGESLQAF---LIAIVIP 629
Cdd:PRK05852 417 SLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-611 |
1.43e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 80.52 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 259 RRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLPLAHMFERVVEktlrlns 338
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSFGLTVG------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 339 sdihisylplahmyeqlmLCVMLCHGAKIGFFQgdirllmddlkmlQPTIFPVVPRLL-NRMFDKIFGQAnTTMKRWI-- 415
Cdd:PRK08043 425 ------------------LFTPLLTGAEVFLYP-------------SPLHYRIVPELVyDRNCTVLFGTS-TFLGNYArf 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 416 ---LDFAskrkeaelrsgiirnnslwdkiifhkiqaslggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG 492
Cdd:PRK08043 473 anpYDFA---------------------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPV 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 493 CSLTVPGDWTAGHVGAPMPCCLIKLVDVEEMnylaAKGeGEICVKGSNVFKGYLK--DP-------AKTAEALDKDGWLH 563
Cdd:PRK08043 520 VSINVPMAAKPGTVGRILPGMDARLLSVPGI----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYD 594
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1788937591 564 TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQ 611
Cdd:PRK08043 595 TGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-602 |
1.65e-15 |
|
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: 78.46 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQnvvsdcsAFVKVTENVvapspddilisflpLAHMFERVVEktlrlnssDIHISYLPL 348
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANK-------TFFAVPDIL--------------QKEGLNWVVG--------DVTYLPLPA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHMYEQLMLCVMLCHGAKIGFFQGDIRL--LMDDLKMLQPTIFPVVPrllnrmfdkifgqanTTMKRWILDFASKRKEAE 426
Cdd:cd17635 53 THIGGLWWILTCLIHGGLCVTGGENTTYksLFKILTTNAVTTTCLVP---------------TLLSKLVSELKSANATVP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 lrsgiirnnslwdkiifhkiqaslggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWT-AGH 505
Cdd:cd17635 118 --------------------------SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 506 VGAPMPCCLIKLVDVEEMNYLAAkGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 585
Cdd:cd17635 172 VGRPYPGVDVYLAATDGIAGPSA-SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSES 249
|
330
....*....|....*..
gi 1788937591 586 FKLAqGEYIAPEKIENI 602
Cdd:cd17635 250 INCG-GVKIAPDEVERI 265
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-630 |
4.04e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 79.02 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRG--DRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKS-DKVDL--MLESVENKLTPGLKTIIIMDPFDSDVVERGKKCGVEIMSMKALEDLGRAnrrkPKPPSPGDLAVICFT- 276
Cdd:PRK06164 114 WPGfKGIDFaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGALLFTt 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 277 SGTTGNPK------GALITHQNVVSDcsafvkvtenVVAPSPDDILISFLPLAHMFErvvektlrLNSSdihisylplah 350
Cdd:PRK06164 190 SGTTSGPKlvlhrqATLLRHARAIAR----------AYGYDPGAVLLAALPFCGVFG--------FSTL----------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 351 myeqlmlcvmlchgakIGFFQGDIRLLMDDLkmlqptiF--PVVPRLL-----------NRMFDKIFGQANTTMkrwilD 417
Cdd:PRK06164 241 ----------------LGALAGGAPLVCEPV-------FdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----D 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 418 FASKRkeaelRSGIirnnslwdkiifhkiqASLggkvrlmvtgaAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCSL-T 496
Cdd:PRK06164 293 FPSAR-----LFGF----------------ASF-----------APALGELAALARAR-GVPLTGLYGSSEVQALVALqP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 497 VPGDWTAGHV--GAPM-PCCLIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPN 573
Cdd:PRK06164 340 ATDPVSVRIEggGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGD 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1788937591 574 GTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFVHGESL--QAFLIAIVIPD 630
Cdd:PRK06164 420 GQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRdgKTVPVAFVIPT 477
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
115-609 |
5.22e-15 |
|
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: 78.30 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 115 DQPYEWISYKEVADKAEYVGSALLQKGYKPSPDQYFGIfaQNRPEWVIIEQGCYAYSMVVVPlydtlgneaityiinkae 194
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQI--THNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 195 lslVFVDKSDKVDLMLESVENKLTpglktiiimDPFdsdvvergkkcgvEIMSMKALEDLgranrrkpkppsPGDLAVIC 274
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLK---------NPY-------------LITEEEVLCEL------------ADELAFIQ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 275 FTSGTTGNPKGALITHQNVVSDCSAFVKVTENvvapSPDDILISFLPLAHmfervvektlRLNSSDIHISYLpLAHMYEQ 354
Cdd:cd05908 113 FSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTH----------DMGLIAFHLAPL-IAGMNQY 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 355 LMlcvmlchgakigffqgdirllmddlkmlqPT-IFPVVPRLLNRMFDKifGQANTTMKRwilDFASKRKEAELRSGIIR 433
Cdd:cd05908 178 LM-----------------------------PTrLFIRRPILWLKKASE--HKATIVSSP---NFGYKYFLKTLKPEKAN 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 434 NnslWDKiifhkiqaslgGKVRLMVTGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCSL------------ 495
Cdd:cd05908 224 D---WDL-----------SSIRMILNGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitl 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 496 ----------------TVPGDWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKD 559
Cdd:cd05908 290 grrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD 368
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1788937591 560 GWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPV 609
Cdd:cd05908 369 GWLKTGDLG-FIRNGRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-633 |
7.19e-15 |
|
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: 77.73 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLPLAHMFErVVEktlrlnssdIHisyL 346
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE---------IW---G 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 PLAHmyeqlmlcvmlchGAKIGFFQGDIRLLMDDLkmlqptifpvvPRLLNRMFDKIFGQANTTMKRWIldfaskrkEAE 426
Cdd:cd17643 155 ALLH-------------GGRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 LRsgiirnnslwdkiiFHKIQASLggkvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCSLTV--PGDW 501
Cdd:cd17643 203 DR--------------DGRDPLAL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRPldAADL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 ---TAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAE-------ALDKDGWLHTGDIGKWL 571
Cdd:cd17643 265 paaAASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRL 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 572 PNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV---HGESLQAFLIAIVIPDVET 633
Cdd:cd17643 344 PDGELEYLGRADEQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
483-616 |
1.02e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 75.80 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 483 GYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLIKLVDvEEMNYLAAkGE-GEICVKGSNVFKGYLKDPAKTAEALdKDGW 561
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 562 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVIG 272
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
264-630 |
1.07e-14 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 77.32 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 264 PPSPGDLAVICFTSGTTGNPKGALITHQNVVsdcsafvkvteNVVAPSPDDIlisflPLAHMfERVVEKTLRlnSSDIHI 343
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIV-----------NRLLWMQDEY-----PLGPG-DRVLQKTPL--SFDVSV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 sylplahmYEQLmlcVMLCHGAKIgffqgdirllmddlkmlqptifpVVPR--------LLNRMFDKifgQANTTMkrwi 415
Cdd:cd17646 195 --------WELF---WPLVAGARL-----------------------VVARpgghrdpaYLAALIRE---HGVTTC---- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 416 lDFASKRKEAELRSGiirnnslwdkiifhkiQASLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSL 495
Cdd:cd17646 234 -HFVPSMLRVFLAEP----------------AAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTH 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 496 -TVPGDWTAGHV--GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLH------TGD 566
Cdd:cd17646 297 wPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGD 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788937591 567 IGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV---HGESLQAFLIAIVIPD 630
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
447-614 |
1.29e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 77.29 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 447 QASLGGKVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEcTAGCSlTV---PGDWTA----------GHVGAPMPcc 513
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTE-TYGPA-TVcawQPEWDAlplderaqlkARQGVRYP-- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 514 L---IKLVDVEEMNYLAAKGE--GEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 588
Cdd:PRK08162 366 LqegVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-I 443
|
170 180
....*....|....*....|....*.
gi 1788937591 589 AQGEYIAPEKIENIYQRSEPVAQVFV 614
Cdd:PRK08162 444 SGGENISSIEVEDVLYRHPAVLVAAV 469
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
119-616 |
2.40e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 76.36 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 119 EWISYKEVADKAEYVGSALlQKGYKPSPDQYFGIFAQNRPEW--VIIEQGCYAysMVVVPLYDTLGNEAITYIINKAELS 196
Cdd:PRK05620 37 EQTTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHleVLFAVACMG--AVFNPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 197 LVFVDKSDKVDL--MLESvenklTPGLKTIIIMDPFDSDVVERGKKCGVEIMSMKALEDlGRANRRkPKPPSPGDLAV-I 273
Cdd:PRK05620 114 VIVADPRLAEQLgeILKE-----CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDETTAAaI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 274 CFTSGTTGNPKGALITHQNVvsdcsafvkvtenvvapspddilisFLplahmfervveKTLRLNSSDihisYLPLAHMyE 353
Cdd:PRK05620 187 CYSTGTTGAPKGVVYSHRSL-------------------------YL-----------QSLSLRTTD----SLAVTHG-E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 354 QLMLCVMLCH----GAKIGFFQGDIRLLMDDLKMLQPTIFPVVprllnrmfdkifgqaNTTMKRwildfaskrkeaeLRS 429
Cdd:PRK05620 226 SFLCCVPIYHvlswGVPLAAFMSGTPLVFPGPDLSAPTLAKII---------------ATAMPR-------------VAH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 430 GIirnNSLWDKIIFHKIQ-----ASLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAG 504
Cdd:PRK05620 278 GV---PTLWIQLMVHYLKnpperMSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 505 HVGAP-------MPCCL-IKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKT----------------AEALDKDG 560
Cdd:PRK05620 351 EARWAyrvsqgrFPASLeYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADG 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1788937591 561 WLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK05620 431 WLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-631 |
4.95e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 76.35 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 55 CDLSMQSVEvegtdgARRSAILDSDEPLSFFYDDvtTLYETFQRGIQVSNNGPCLGSRKpdqpyEWISYKEVADKAEYVG 134
Cdd:PRK12467 485 GELPLLDAE------ERARELVRWNAPATEYAPD--CVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANRLA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 135 SALLQKGYkpSPDQYFGIFAQNRPEWVI----IEQGCYAYsmvvVPLYDTLGNEAITYIINKAELSLVFVDkSDKVDLMl 210
Cdd:PRK12467 552 HVLIAAGV--GPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVRLLLTQ-SHLLAQL- 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 211 esvenKLTPGLKTIIIMDPFDsdvvergkkcgveimsmkalEDLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITH 290
Cdd:PRK12467 624 -----PVPAGLRSLCLDEPAD--------------------LLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISH 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 291 QNVVSdcsaFVKVTENVVAPSPDDILISFLPLAhmfervvektlrlnsSDIHIsylplahmyeqLMLCVMLCHGAKIgff 370
Cdd:PRK12467 679 GALAN----YVCVIAERLQLAADDSMLMVSTFA---------------FDLGV-----------TELFGALASGATL--- 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 371 qgdirLLMDDLKMLQPTIFpvvprllnrmFDKIFGQANTtmkrwILDFASkrkeaelrsgiirnnSLWDKIIFHKIQASL 450
Cdd:PRK12467 726 -----HLLPPDCARDAEAF----------AALMADQGVT-----VLKIVP---------------SHLQALLQASRVALP 770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 451 GGKVRLMVTGAA-PVSATVLTFlRAALGCQFYEGYGQTECTAGCSL----TVPGDWTAGHVGAPMPCCLIKLVDvEEMNY 525
Cdd:PRK12467 771 RPQRALVCGGEAlQVDLLARVR-ALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANLGLYILD-HYLNP 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 526 LAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 598
Cdd:PRK12467 849 VPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGE 927
|
570 580 590
....*....|....*....|....*....|....*
gi 1788937591 599 IENIYQRSEPVAQVFV--HGESLQAFLIAIVIPDV 631
Cdd:PRK12467 928 IEARLLAQPGVREAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-630 |
1.68e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 73.46 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRP--GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKSDkvDLMLESVENKLTPGLKTIIIMDPFdsdvvergkkcgveimsmkaledlgranrrKPKPPSPGDLAVICFTSGTT 280
Cdd:cd12114 91 DGPD--AQLDVAVFDVLILDLDALAAPAPP------------------------------PPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 281 GNPKGALITHQ---NVVSDCSAFVKVTenvvapsPDDILISFLPLAHmfervvektlRLNSSDIhisYLPLAHmyeqlml 357
Cdd:cd12114 139 GTPKGVMISHRaalNTILDINRRFAVG-------PDDRVLALSSLSF----------DLSVYDI---FGALSA------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 358 cvmlchGAKIGFFQGDIR----LLMDDLKMLQPTIFPVVPRLLNRMFDkifgqanttmkrwildfaskrkeaELRSGIIR 433
Cdd:cd12114 192 ------GATLVLPDEARRrdpaHWAELIERHGVTLWNSVPALLEMLLD------------------------VLEAAQAL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 434 NNSL--------WdkiifhkIQASLGGKVRLMVTGAAPVSatvltflraaLGcqfyegyGQTEcTAGCSL-----TVPGD 500
Cdd:cd12114 242 LPSLrlvllsgdW-------IPLDLPARLRALAPDARLIS----------LG-------GATE-ASIWSIyhpidEVPPD 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 WTAGHVGAPMPCCLIKLVDveemnylaAKGE-------GEICVKGSNVFKGYLKDPAKTAEAL--DKDG--WLHTGDIGK 569
Cdd:cd12114 297 WRSIPYGRPLANQRYRVLD--------PRGRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGR 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788937591 570 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQ--VFVHGESLQAFLIAIVIPD 630
Cdd:cd12114 369 YRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
446-614 |
2.01e-13 |
|
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: 72.99 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 446 IQASLGG---KVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLIKLVDVEE 522
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 523 mnylAAKGEGEICVKGSN-----VFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPE 597
Cdd:cd05974 271 ----APATEGEVALDLGDtrpvgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISPF 344
|
170
....*....|....*..
gi 1788937591 598 KIENIYQRSEPVAQVFV 614
Cdd:cd05974 345 ELESVLIEHPAVAEAAV 361
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
460-614 |
4.11e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.21 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 460 GAA-PVSatvLTFLRAALGCQFYEGYGQTECTAgcslTV---PGDWTAGhVGAPMPCCLIKLVDveemnylaakgeGEIC 535
Cdd:PRK09029 249 GAAiPVE---LTEQAEQQGIRCWCGYGLTEMAS----TVcakRADGLAG-VGSPLPGREVKLVD------------GEIW 308
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788937591 536 VKGSNVFKGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV 614
Cdd:PRK09029 309 LRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
517-623 |
1.03e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.41 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 517 LVDVEEMNYLAAKGE--GEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 594
Cdd:PLN02479 386 VVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENI 463
|
90 100 110
....*....|....*....|....*....|....*.
gi 1788937591 595 APEKIENIYQRSEPVAQVFV-------HGESLQAFL 623
Cdd:PLN02479 464 SSLEVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-641 |
1.26e-12 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 70.54 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVtenVVAPSPDDILIsFLPLAhmFERVVEKtlrlnssdihisyl 346
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKE---YGITSSDRVLQ-FASIA--FDVAAEE-------------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plahmyeqlmLCVMLCHGAKIgffqgdirllmddlkMLQPtifpvvprllNRMFDKI--FGQANTTMKRWILDFASkrke 424
Cdd:cd17644 165 ----------IYVTLLSGATL---------------VLRP----------EEMRSSLedFVQYIQQWQLTVLSLPP---- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 aelrsgiirnnSLWDKIIFHKIQASLGG--KVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCSLTVPGD 500
Cdd:cd17644 206 -----------AYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 WTAGH-----VGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLH--------TGDI 567
Cdd:cd17644 275 LTERNitsvpIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 568 GKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV---HGESLQAFLIAIVIP------DVETLSSWA 638
Cdd:cd17644 354 ARYLPDGNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPhyeespSTVELRQFL 432
|
...
gi 1788937591 639 KKK 641
Cdd:cd17644 433 KAK 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
458-624 |
1.43e-12 |
|
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: 70.57 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 458 VTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVK 537
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 538 GSNV-----FKGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQV 612
Cdd:cd05928 376 VKPIrpfglFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 1788937591 613 FV-------HGESLQAFLI 624
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-602 |
3.58e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.46 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVtenvVAPSPDDILISFLPLAHMFErvvektlrLNSSDIH--IS 344
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAYG--------FNSCTLFplLS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 345 YLPLAHMYEQLMlcvmlchgAKigffqgDIRLLMDDLKMlqpTIFPVVPRLLNrmfdkifgqanttmkrWILDfASKRKE 424
Cdd:PRK06334 250 GVPVVFAYNPLY--------PK------KIVEMIDEAKV---TFLGSTPVFFD----------------YILK-TAKKQE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 AELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTAGCSL-TVPGDWT 502
Cdd:PRK06334 296 SCLPS------------------------LRFVVIGGDAFKDSLYQeALKTFPHIQLRQGYGTTECSPVITInTVNSPKH 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 503 AGHVGAPMPCCLIKLVDvEEMNYLAAKGE-GEICVKGSNVFKGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIID 580
Cdd:PRK06334 352 ESCVGMPIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKG 430
|
330 340
....*....|....*....|..
gi 1788937591 581 RKKHIFKLAqGEYIAPEKIENI 602
Cdd:PRK06334 431 RLSRFVKIG-AEMVSLEALESI 451
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
121-633 |
3.60e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 69.32 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKgYKPSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:PRK07867 29 TSWREHIRGSAARAAALRAR-LDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 DKSDKVdlMLESVEnkltPGLKTIIIMDPFDSDVVergkkcgveimsmkaleDLGRANRRKPKPPSPGDLAVICFTSGTT 280
Cdd:PRK07867 108 ESAHAE--LLDGLD----PGVRVINVDSPAWADEL-----------------AAHRDAEPPFRVADPDDLFMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 281 GNPKGALITHqnvvsdcsafvkvtENVVAPSPddilisflPLAHMFErvvektlrLNSSDIHISYLPLAHMyEQLM--LC 358
Cdd:PRK07867 165 GDPKAVRCTH--------------RKVASAGV--------MLAQRFG--------LGPDDVCYVSMPLFHS-NAVMagWA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 359 VMLCHGAKI---------GFfqgdirllMDDLKMLQPTIFPVVPRLLNrmfdkifgqanttmkrWILDFASKRKEAElrs 429
Cdd:PRK07867 214 VALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGKPLS----------------YVLATPERPDDAD--- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 430 giirnNSLwdKIIFhkiqaslGGKvrlmvtGAAPVSATvltfLRAALGCQFYEGYGQTEctAGCSLTVPGDWTAGHVGAP 509
Cdd:PRK07867 267 -----NPL--RIVY-------GNE------GAPGDIAR----FARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 510 MPCclIKLVDVE--------------EMNYLAAKGEgEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGT 575
Cdd:PRK07867 321 PPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGY 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1788937591 576 LKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFVHGeslqafliaivIPDVET 633
Cdd:PRK07867 397 AYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPDPVV 442
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
455-625 |
5.53e-12 |
|
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: 68.51 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 455 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE----CTAgcsLTVPGDWTAGHVGAPM-PCCLIKLVDvEEMNYLAAK 529
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 530 GEGEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRSEPV 609
Cdd:cd05920 334 EEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRHPAV 412
|
170 180
....*....|....*....|...
gi 1788937591 610 AQVFV-------HGESLQAFLIA 625
Cdd:cd05920 413 HDAAVvampdelLGERSCAFVVL 435
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-616 |
1.09e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 67.79 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQPY-------EWISYKEVADKAEYVGSALLQKGYKPSpDQYfGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNE 184
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLKRG-DHV-AIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 185 AITYIINKAElSLVFVDKSDKVDLMLEsvENKLTPGLKTIIIMDPFDSdvvergkkcgveimsMKALEDLGRANRRKPKP 264
Cdd:PRK13391 87 EAAYIVDDSG-ARALITSAAKLDVARA--LLKQCPGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 265 PSP----GDLavICFTSGTTGNPKGalithqnvvsdcsafvkvtenVVAPSPDDILISFLPLAHMFERVVektlRLNSSD 340
Cdd:PRK13391 149 PIAdeslGTD--MLYSSGTTGRPKG---------------------IKRPLPEQPPDTPLPLTAFLQRLW----GFRSDM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 341 IHISYLPLAHMYEQLMlcVMLCHGAkigffqGDIRLLMDD------LKMLQP---TIFPVVPRllnrMFDKIFGQANTTM 411
Cdd:PRK13391 202 VYLSPAPLYHSAPQRA--VMLVIRL------GGTVIVMEHfdaeqyLALIEEygvTHTQLVPT----MFSRMLKLPEEVR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 412 KRWilDFASkrkeaelrsgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTA 491
Cdd:PRK13391 270 DKY--DLSS---------------------------------LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 492 GCSLTVPGDWTA--GHVGAPMpccLIKLVDVEEMNYLAAKGE-GEICVKGSNVFKgYLKDPAKTAEALDKDG-WLHTGDI 567
Cdd:PRK13391 314 GFTACDSEEWLAhpGTVGRAM---FGDLHILDDDGAELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDI 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1788937591 568 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK13391 390 GYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
245-613 |
1.41e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 67.62 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 245 IMSMKALEDLGRANRRKPKPP---SPGDLAVICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLP 321
Cdd:PRK09274 148 LWGGTTLATLLRDGAAAPFPMadlAPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGIEPGEIDLPTFP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 322 LahmfervvektlrlnssdihisylplahmyeqlmlcvMLCHGAKIGffqgdirllmddLKMLQPTIFPVVPRLLN--RM 399
Cdd:PRK09274 224 L-------------------------------------FALFGPALG------------MTSVIPDMDPTRPATVDpaKL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 400 FDKIFGQANTTMkrwildFASKrkeaelrsgiirnnSLWDKIIFHKIQ--ASLGGkVRLMVTGAAPVSATVLTFLRAAL- 476
Cdd:PRK09274 255 FAAIERYGVTNL------FGSP--------------ALLERLGRYGEAngIKLPS-LRRVISAGAPVPIAVIERFRAMLp 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 477 -GCQFYEGYGQTECTAGCS------LTVPGDWT---AGH-VGAPMPCCLIKLVDV--------EEMNYLAAKGEGEICVK 537
Cdd:PRK09274 314 pDAEILTPYGATEALPISSiesreiLFATRAATdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 538 GSNVFKGYLKDPAKTAEA--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniyqrSEPVAQV 612
Cdd:PRK09274 394 GPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERI 461
|
.
gi 1788937591 613 F 613
Cdd:PRK09274 462 F 462
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-600 |
1.48e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 67.60 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPL-YDTLGNEaITYIINKAELSLVF 199
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGP--GDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 200 VDKS--DKVDLMLESvenklTPGLKTIIIMDPFDSDVVERGkkcGVEIMSMKALEDLGRAnrrkPKPPSPGDLAVICfTS 277
Cdd:PRK07798 106 YEREfaPRVAEVLPR-----LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-TG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 278 GTTGNPKGALITHQNV-VSDCSAFVKVTENVVApSPDDILisflplahmfERVVEKT-LRLnssdihisylplahmyeqL 355
Cdd:PRK07798 173 GTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIE-DEEELA----------KRAAAGPgMRR------------------F 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 356 MLCVMLcHGAK-----IGFFQGdirllmddlkmlQPTIFPVVPRL-------------LNRMFdkIFGQAnttMKRWILD 417
Cdd:PRK07798 224 PAPPLM-HGAGqwaafAALFSG------------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 418 FASKRKEAELRSgiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLT 496
Cdd:PRK07798 286 ALEARGPYDLSS------------------------LFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSGT 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 497 VPGDwtAGHVGAP--MPCCLIKLVDvEEMNYLAAkGEGEICV--KGSNVFKGYLKDPAKTAEAL-DKDG--WLHTGDIGK 569
Cdd:PRK07798 342 VAKG--AVHTGGPrfTIGPRTVVLD-EDGNPVEP-GSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRAR 417
|
490 500 510
....*....|....*....|....*....|.
gi 1788937591 570 WLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 600
Cdd:PRK07798 418 VEADGTITLLGRGSVCINTG-GEKVFPEEVE 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-640 |
3.49e-11 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 66.04 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCS---AFVKVTENvvapspddilisflplahmfervvektlrlNSSDIHI 343
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEwhrPYFGVTPA------------------------------DKSLVYA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 344 SYLPLAHMYEqlmLCVMLCHGAKIGFFQGDIRLLMDDLkmlqptifpvvprllNRMFDkifgQANTTMKRWILDFASKRK 423
Cdd:cd17645 153 SFSFDASAWE---IFPHLTAGAALHVVPSERRLDLDAL---------------NDYFN----QEGITISFLPTGAAEQFM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 424 EAElrsgiirNNSLwdkiifhkiqaslggkvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCSLTVPGDWTA 503
Cdd:cd17645 211 QLD-------NQSL-----------------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 504 GHVGAPMPCCLIKLVDVEEMNYLAAKG-EGEICVKGSNVFKGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTL 576
Cdd:cd17645 260 ANIPIGKPIDNTRVYILDEALQLQPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNI 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1788937591 577 KIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLIAIVIPDVETLSSWAKK 640
Cdd:cd17645 340 EFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
521-616 |
3.62e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 66.22 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 521 EEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 600
Cdd:PRK07470 356 DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIE 433
|
90
....*....|....*.
gi 1788937591 601 NIYQRSEPVAQVFVHG 616
Cdd:PRK07470 434 EKLLTHPAVSEVAVLG 449
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
251-616 |
7.10e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 65.33 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 251 LEDL--GRANRRKPKPPSPGdlAVICFTSGTTGNPKGALITHqnvvsdcsafvkvtenvvaPSPddilisFLPLAHMFER 328
Cdd:PRK07788 190 LDDLiaGSSTAPLPKPPKPG--GIVILTSGTTGTPKGAPRPE-------------------PSP------LAPLAGLLSR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 329 VvekTLRLNSSDIHISylPLAHMYEQLMLCVMLCHGAKIGF---FqgDIRLLMDDLKMLQPTIFPVVPRLLNRMFDkifg 405
Cdd:PRK07788 243 V---PFRAGETTLLPA--PMFHATGWAHLTLAMALGSTVVLrrrF--DPEATLEDIAKHKATALVVVPVMLSRILD---- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 406 qanttmkrwILDFASKRKEAelrsgiirnNSLwdKIIFhkiqaslggkvrlmVTGAApVSATVLTFLRAALGCQFYEGYG 485
Cdd:PRK07788 312 ---------LGPEVLAKYDT---------SSL--KIIF--------------VSGSA-LSPELATRALEAFGPVLYNLYG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 486 QTECtAGCSLTVPGDWTA--GHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAealdKDGWLH 563
Cdd:PRK07788 357 STEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLS 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1788937591 564 TGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-641 |
7.65e-11 |
|
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: 65.08 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCSAfvkvTENVVAPSPDDILISFLPLahmfervvektlrlnSSDIhisyl 346
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA----TAERYGLTPGDRELQFASF---------------NFDG----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 plAHmyEQLMlcVMLCHGAkigffqgdiRLLMDDLKMLQPtifpvvPRLLNRMFDK----IFGQANTTMKRWILDFASKr 422
Cdd:cd17649 149 --AH--EQLL--PPLICGA---------CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 keaelrsgiirnnslwdkiifhkiQASLGGKVRLMVTGAAPVSATvltFLRAALGCQ--FYEGYGQTECTAGCSLTV--P 498
Cdd:cd17649 207 ------------------------GDGRPPSLRLYIFGGEALSPE---LLRRWLKAPvrLFNAYGPTEATVTPLVWKceA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 499 GDWTAGH---VGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEAL--DKDG-----WLHTGDIG 568
Cdd:cd17649 260 GAARAGAsmpIGRPLGGRSAYILD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 569 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFVHGES--LQAFLIAIVIP--------DVETLSSWA 638
Cdd:cd17649 339 RWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLraaaaqpeLRAQLRTAL 417
|
...
gi 1788937591 639 KKK 641
Cdd:cd17649 418 RAS 420
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
266-641 |
8.73e-11 |
|
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: 64.58 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVtenvVAPSPDDILISFLPLahmfervvektlrlnSSDIHISY 345
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA----FDVGPGSRVLQFASP---------------SFDASVWE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 LPLAhmyeqlmlcvmLCHGAkigffqgdiRLLMDDLKMLQPtifpvvprllnrmfdkifGQanttmkrwildfaskrkea 425
Cdd:cd17652 152 LLMA-----------LLAGA---------TLVLAPAEELLP------------------GE------------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 426 ELRsGIIRnnslwDKIIFHKIQ----------ASLGGKVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAGCSL 495
Cdd:cd17652 175 PLA-DLLR-----EHRITHVTLppaalaalppDDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 496 TVP-GDWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKD------GWLH-TGDI 567
Cdd:cd17652 246 AGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 568 GKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQ--VFVHGESL-QAFLIAIVI------PDVETLSSWA 638
Cdd:cd17652 325 ARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHL 403
|
...
gi 1788937591 639 KKK 641
Cdd:cd17652 404 AER 406
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
269-629 |
8.99e-11 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 64.81 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKvteNVVAPSPDDILISFLPLAHMFERvvektlrlnssdihisylpl 348
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGL-------------------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 ahmyeQLMLCVMLCHGAKIGFFQGDI-RLLMDDLKMLQPTIFPVVPrllnrmfdkifgqantTMKRWILdfASKRKEAEL 427
Cdd:cd05958 155 -----GGVLLFPFGVGASGVLLEEATpDLLLSAIARYKPTVLFTAP----------------TAYRAML--AHPDAAGPD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 RSGiirnnslwdkiifhkiqaslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVG 507
Cdd:cd05958 212 LSS-----------------------LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 508 APMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNvfkGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 587
Cdd:cd05958 269 KPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1788937591 588 LAqGEYIAPEKIENIYQRSEPVAQVFVHGESLQAFLI---AIVIP 629
Cdd:cd05958 345 SG-GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVvvkAFVVL 388
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
250-612 |
1.78e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.02 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 250 ALEDL---GRANRRKPKPPSP-GDLAVICFTSGTTGNPKGALITHQNVVSDCSAfvkVTENVVAPSPDDILISFLPLAHm 325
Cdd:PRK05851 130 TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYH- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 326 fervvektlrlnssDIHISYLplahmyeqlmLCVMLChGAKIgffqgdirllmddlkMLQPT-IFPVVP-RLLNRMFDKi 403
Cdd:PRK05851 206 --------------DMGLAFL----------LTAALA-GAPL---------------WLAPTtAFSASPfRWLSWLSDS- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 404 fgQANTTMK-----RWILDFASKRKEAELrsgiirnnslwdkiifhkiqaslgGKVRLMVTGAAPVSATVLT-FLRAALG 477
Cdd:PRK05851 245 --RATLTAApnfayNLIGKYARRVSDVDL------------------------GALRVALNGGEPVDCDGFErFATAMAP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 478 CQFYEG-----YGQTECTagCSLTVP---------------GDWTAGH--VGAPMPCCLIKLVDVEEMNYLAAKGEGEIC 535
Cdd:PRK05851 299 FGFDAGaaapsYGLAEST--CAVTVPvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIE 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788937591 536 VKGSNVFKGYLKDPaktaeALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyqrsepVAQV 612
Cdd:PRK05851 377 IRGASMMSGYLGQA-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
111-602 |
5.16e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.46 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 111 SRKPDQPYEWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYII 190
Cdd:PRK06018 30 TRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLG--DRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 191 NKAELSLVFVDKSdkVDLMLESVENKLtPGLKTIIIMDpfDSDVVERGKkcgveIMSMKALEDL--GRANRRKPKPPSPG 268
Cdd:PRK06018 108 NHAEDRVVITDLT--FVPILEKIADKL-PSVERYVVLT--DAAHMPQTT-----LKNAVAYEEWiaEADGDFAWKTFDEN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQ-NVVSdcsAFVKVTENVVAPSPDDILISFLPLAHMfervvektlrlNSSDIHISylp 347
Cdd:PRK06018 178 TAAGMCYTSGTTGDPKGVLYSHRsNVLH---ALMANNGDALGTSAADTMLPVVPLFHA-----------NSWGIAFS--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 348 lahmyEQLMLCVMLCHGAKIGffQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFDKifgqanttmkrwildfaSKRKEAEL 427
Cdd:PRK06018 241 -----APSMGTKLVMPGAKLD--GASVYELLDTEKVTFTAGVPTVWLMLLQYMEK-----------------EGLKLPHL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 RSGIIrnnslwdkiifhkiqaslGGkvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECTAGCSL--------TV 497
Cdd:PRK06018 297 KMVVC------------------GG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSPLGTLaalkppfsKL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 498 PGDWTAGHV---GAPMPCCLIKLVDvEEMNYLAAKGE--GEICVKGSNVFKGYLKdpaKTAEALDKDGWLHTGDIGKWLP 572
Cdd:PRK06018 347 PGDARLDVLqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDA 422
|
490 500 510
....*....|....*....|....*....|
gi 1788937591 573 NGTLKIIDRKKHIFKlAQGEYIAPEKIENI 602
Cdd:PRK06018 423 YGYMRITDRSKDVIK-SGGEWISSIDLENL 451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
267-636 |
5.17e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.44 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLPLAhmFERVVEKTlrlnssdihisYL 346
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFS--FDGSHEGL-----------YH 4755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 PLahmyeqlmlcvmlCHGAkigffqgdiRLLMDDLKMLQPTifpvvpRLLNRMfdkifGQANTTMkrwiLDFASkrkeae 426
Cdd:PRK12316 4756 PL-------------INGA---------SVVIRDDSLWDPE------RLYAEI-----HEHRVTV----LVFPP------ 4792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 lrsgiirnnSLWDKIIFHKIQASLGGKVRLMVTG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAGCSL-TVPGDWTA 503
Cdd:PRK12316 4793 ---------VYLQQLAEHAERDGEPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTVLLwKARDGDAC 4862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 504 G----HVGAPMPCCLIKLVDVEeMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLP 572
Cdd:PRK12316 4863 GaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRA 4941
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788937591 573 NGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFVHGE--SLQAFLIAIVIPDVETLSS 636
Cdd:PRK12316 4942 DGVIDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVIAQegAVGKQLVGYVVPQDPALAD 5006
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
250-629 |
7.63e-10 |
|
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: 62.01 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 250 ALEDLGRANRRKPKPPSPgDLA---VICFTSGTTGNPKGALITHQNVvsdcsafvkvtenvvaPSPDDILISFLPLAHMF 326
Cdd:cd05929 105 GLEDYEAAEGGSPETPIE-DEAagwKMLYSGGTTGRPKGIKRGLPGG----------------PPDNDTLMAAALGFGPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 327 ERVVektlrlnssdihisYLPLAHMYeqlmlcvmlcHGAKIGFFQGDIRL-----LM---DDLKMLQP------TIFPVV 392
Cdd:cd05929 168 ADSV--------------YLSPAPLY----------HAAPFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 393 PRLLNRMFdKIFGQAnttmkRWILDFASKrkeaelrsgiirnnslwdKIIFHkiqaslggkvrlmvtGAAPVSATVLTFL 472
Cdd:cd05929 224 PTMFVRLL-KLPEAV-----RNAYDLSSL------------------KRVIH---------------AAAPCPPWVKEQW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 473 RAALGCQFYEGYGQTECTAGCSLTvPGDWTA--GHVGAPMPCCLiKLVDvEEMNYLAAKGEGEICVKGSNVFKgYLKDPA 550
Cdd:cd05929 265 IDWGGPIIWEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGKV-HILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 551 KTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG---ESLQAFLIAIV 627
Cdd:cd05929 341 KTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVV 419
|
..
gi 1788937591 628 IP 629
Cdd:cd05929 420 QP 421
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-630 |
2.45e-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: 60.02 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPspDQYFGIFAQNRPEWV-----IIEQGCyAYsmvvVPLYDTLGNEAITYIINKAEL 195
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGP--ESRVGVCLERTPDLVvallaVLKAGA-AY----VPLDPAYPPERLRFILEDAQA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 196 SLVFVDksdkvdlmlesvenkltpglktiiimdpfdsdvvergkkcgveimsmkaledlgranrrkpkppsPGDLAVICF 275
Cdd:cd12115 98 RLVLTD-----------------------------------------------------------------PDDLAYVIY 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 276 TSGTTGNPKGALITHQNVVsdcsAFVKVTENVVapSPDDilisflpLAhmfervveKTLRLNSSDIHISylplahMYEql 355
Cdd:cd12115 113 TSGSTGRPKGVAIEHRNAA----AFLQWAAAAF--SAEE-------LA--------GVLASTSICFDLS------VFE-- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 356 mLCVMLCHGAKIGFFQGDIRLLmDDLKMLQPTIFPVVPRLLnrmfdkifgqanttmkrwildfaskrkEAELRsgiirnn 435
Cdd:cd12115 164 -LFGPLATGGKVVLADNVLALP-DLPAAAEVTLINTVPSAA---------------------------AELLR------- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 436 slwdkiifhkiQASLGGKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCSLTVPGDWTAGHVGAPMPC 512
Cdd:cd12115 208 -----------HDALPASVRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLAN 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 513 CLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIF 586
Cdd:cd12115 277 TQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQV 355
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1788937591 587 KLaQGEYIAPEKIENIYQRSEPVAQ--VFVHGESL-QAFLIAIVIPD 630
Cdd:cd12115 356 KV-RGFRIELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
481-632 |
3.53e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 59.92 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 481 YEGYGQTEctaGCSLTV--PGDWTA--GHVGAPMpCCLIKLVDvEEMNYLAAKGEGEICVK-GSNVFKgYLKDPAKTAEA 555
Cdd:PRK08276 291 HEYYASSE---GGGVTVitSEDWLAhpGSVGKAV-LGEVRILD-EDGNELPPGEIGTVYFEmDGYPFE-YHNDPEKTAAA 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788937591 556 LDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHGeslqafliaivIPDVE 632
Cdd:PRK08276 365 RNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
506-629 |
4.12e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 59.52 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 506 VGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEAL-DKDGW--LHTGDIGKwLPNGTLKIIDRK 582
Cdd:PRK04813 320 IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLLFYQGRI 397
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1788937591 583 KHIFKLAqGEYIAPEKIENIYQRSEPVAQVFV----HGESLQAfLIAIVIP 629
Cdd:PRK04813 398 DFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVP 446
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
455-630 |
4.33e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 59.62 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 455 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE----------------CTAGCSLTvPGD--WTAGHVGAPMPcclik 516
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnytrlddsderifTTQGRPMS-PDDevWVADADGNPLP----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 517 lvdveemnylaaKGE-GEICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----G 591
Cdd:PRK10946 377 ------------QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgG 439
|
170 180 190
....*....|....*....|....*....|....*....
gi 1788937591 592 EYIAPEKIENIYQRsepvaqvfvHGESLQAFLIAivIPD 630
Cdd:PRK10946 440 EKIAAEEIENLLLR---------HPAVIHAALVS--MED 467
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
122-684 |
5.20e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 59.33 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 122 SYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFVD 201
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPG--DRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 202 KSdkvdlMLESVEnKLTPGLKTI---IIMDpfDSDVVERGKkcgveiMSMKALEDLGRANRRKPKPPS--PGDLAVICFT 276
Cdd:PRK07008 119 LT-----FLPLVD-ALAPQCPNVkgwVAMT--DAAHLPAGS------TPLLCYETLVGAQDGDYDWPRfdENQASSLCYT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 277 SGTTGNPKGALITHQNVVsdCSAFVKVTENVVAPSPDDiliSFLPLAHMFervvektlrlnssdiHISYLPLAHMyeqlm 356
Cdd:PRK07008 185 SGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARD---AVLPVVPMF---------------HVNAWGLPYS----- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 357 lCVMLchGAKIgffqgdirllmddlkmlqptIFPvvprllnrmfdkifGQAnttmkrwiLDFASKRK--EAELRSGIIRN 434
Cdd:PRK07008 240 -APLT--GAKL--------------------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 435 NSLWDKIIFHKIQASLG-GKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCSLT-----VPGD----- 500
Cdd:PRK07008 275 PTVWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkl 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 501 -WTAGHV--GAPMpccliKLVDVE--EMNYlAAKGEGEICVKGSNVFKGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGT 575
Cdd:PRK07008 355 lEKQGRViyGVDM-----KIVGDDgrELPW-DGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGF 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 576 LKIIDRKKHIFKlAQGEYIAPEKIENIyqrsePVAQVFVHgeslQAFLIAIVIP--DVETLSSWAKKKGFSGSHADLCRN 653
Cdd:PRK07008 425 MQITDRSKDVIK-SGGEWISSIDIENV-----AVAHPAVA----EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAF 494
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1788937591 654 KDVKKA---ILDDMVRL--------GKEAGLKPFEQVKGITL 684
Cdd:PRK07008 495 YEGKVAkwwIPDDVVFVdaiphtatGKLQKLKLREQFRDYVL 536
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
455-632 |
7.25e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.94 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 455 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCSLTVPGDWTA--GHVGAPMPCCLIKLVDvEEMNYLAAKGEG 532
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 533 EICVK--GSNVFKgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVA 610
Cdd:PRK12406 352 EIYSRiaGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVH 428
|
170 180
....*....|....*....|..
gi 1788937591 611 QVFVHGeslqafliaivIPDVE 632
Cdd:PRK12406 429 DCAVFG-----------IPDAE 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-639 |
1.14e-08 |
|
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: 58.13 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTENvvapSPDDILISFLPLAHmfervvektlrlNSSDIhisylpl 348
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGA----LPSDVLYTCLPLYH------------STALI------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 ahmyeqLMLCVMLCHGAKIGF---FQGdiRLLMDDLKMLQPTIFPVVPRLLnrmfdkifgqanttmkRWILdfASKRKEA 425
Cdd:cd05940 139 ------VGWSACLASGATLVIrkkFSA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 426 ELRsgiirnnslwdkiifHKIQASLGGKVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGcSLTVPG-DWTA 503
Cdd:cd05940 193 ERK---------------HKVRMIFGNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSG-FINFFGkPGAI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 504 GHVGA----PMPCCLIKlVDVEEMNYL---------AAKGE-----GEICVKGSnvFKGYLkDPAKTAEAL------DKD 559
Cdd:cd05940 247 GRNPSllrkVAPLALVK-YDLESGEPIrdaegrcikVPRGEpglliSRINPLEP--FDGYT-DPAATEKKIlrdvfkKGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 560 GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFVHGESL-----QAFLIAIVIPDVE-- 632
Cdd:cd05940 323 AWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNEef 401
|
....*..
gi 1788937591 633 TLSSWAK 639
Cdd:cd05940 402 DLSALAA 408
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-613 |
1.28e-08 |
|
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: 57.86 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 265 PSPGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTEnvvaPSPDDILISFLPLAHMFervvektlrlnssdihis 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG----IRPGEVDLATFPLFALF------------------ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 345 ylplahmyeqlmlcvmlchGAKIGffqgdirllmddLKMLQPTIFPVVPrllnrmfdkifGQANttmKRWILDFASKRKE 424
Cdd:cd05910 140 -------------------GPALG------------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 aelrSGIIRNNSLWDKIIFHKIQASLG-GKVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCS------L 495
Cdd:cd05910 175 ----SIVFGSPALLERVARYCAQHGITlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 496 TVPGDWTAGH----VGAPMPCCLIKLVDVEEMNY--------LAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDG--- 560
Cdd:cd05910 251 ATTTAATSGGagtcVGRPIPGVRVRIIEIDDEPIaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNseg 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 561 -WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIapekieniyqrSEPVAQVF 613
Cdd:cd05910 331 fWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLY-----------TEPVERVF 373
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
507-600 |
1.90e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.71 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 507 GAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAkTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIF 586
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI 464
|
90
....*....|....
gi 1788937591 587 kLAQGEYIAPEKIE 600
Cdd:PRK09192 465 -IINGRNIWPQDIE 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
265-634 |
2.22e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.86 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 265 PSPGDLAVICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLPLAhmFERVVEKtlrlnssdihis 344
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWE------------ 1776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 345 ylplahmyeqlmLCVMLCHGAkigffqgdiRLLMDDlkmlqptifPVVPRLLNRMFDKIFGQANTTmkrwiLDFASkrke 424
Cdd:PRK12467 1777 ------------LFWPLINGA---------RLVIAP---------PGAHRDPEQLIQLIERQQVTT-----LHFVP---- 1817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 425 aelrsgiirnnSLWDKIIFHKIQASLGGKVRLMVTG--AAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CSLT 496
Cdd:PRK12467 1818 -----------SMLQQLLQMDEQVEHPLSLRRVVCGgeALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRK 1884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 497 VPGDWTAGHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEAL------DKDGWLH-TGDIGK 569
Cdd:PRK12467 1885 DLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLAR 1963
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788937591 570 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQ--VFVHGESLQAFLIAIVIPDVETL 634
Cdd:PRK12467 1964 YRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGL 2029
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
448-624 |
2.25e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 57.14 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 448 ASLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctagCSLTVPGDWTAGHV------GAPMPCCLIKLVDvE 521
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTE----LGMVLANHHALEHPvhagsaGRAMPGWRVAVLD-D 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 522 EMNYLAAKGEGEICVKGSNV----FKGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPE 597
Cdd:cd05973 276 DGDELGPGEPGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPF 350
|
170 180 190
....*....|....*....|....*....|....
gi 1788937591 598 KIENIYQRSEPVAQVFV-------HGESLQAFLI 624
Cdd:cd05973 351 DVESALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
273-666 |
2.75e-08 |
|
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: 56.26 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 273 ICFTSGTTGNPKGALITHQNVVsdcsAFVKVTENVVAPSPDDILISFLPLAHmfervvekTLRLNSSdihISYLPLAhmy 352
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSH--------SLFLYGA---ISALYLG--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 353 eqlmlcvmlchGAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLnrmfdkifgqanttmkrwildfaskrkEAELRSGII 432
Cdd:cd17633 67 -----------GTFIGQRKFNPKSWIRKINQYNATVIYLVPTML---------------------------QALARTLEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 433 RNnslwdkiifhkiqaslggKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMP 511
Cdd:cd17633 109 ES------------------KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 512 CCLIKLVDVEEmnylaaKGEGEICVKGSNVFKGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 591
Cdd:cd17633 171 NVEIEIRNADG------GEIGKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGG 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 592 EYIAPEKIENIYQRSEPVAQVFVHGES------LQAFLIAIVIPDVETLSSWAKKKgfsgshadLCRNKDVKKAI-LDDM 664
Cdd:cd17633 239 INIFPTEIESVLKAIPGIEEAIVVGIPdarfgeIAVALYSGDKLTYKQLKRFLKQK--------LSRYEIPKKIIfVDSL 310
|
..
gi 1788937591 665 VR 666
Cdd:cd17633 311 PY 312
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
266-641 |
3.41e-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: 56.64 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 266 SPGDLAVICFTSGTTGNPKGALITHQNVVSDCsafVKVTENVVAPSPDDILISFLPlAHMFErvvektlrlnssdihisy 345
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR---TSLSERYFGRDNGDEAVLFFS-NYVFD------------------ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 346 lplaHMYEQLMLCVMlcHGAKIGFFQGDIRLlmDDlkmlqptifpvvprllNRMFDKIFGQANTtmkrWILDFASKRKEA 425
Cdd:cd17648 150 ----FFVEQMTLALL--NGQKLVVPPDEMRF--DP----------------DRFYAYINREKVT----YLSGTPSVLQQY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 426 ELRsgiiRNNSLwdkiifhkiqaslggkVRLMVTGAApVSATVLTFLRAALGCQFYEGYGQTEC--TAGCSLTVPGDWTA 503
Cdd:cd17648 202 DLA----RLPHL----------------KRVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 504 GHVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAE-------------ALDKDGWLH-TGDIGK 569
Cdd:cd17648 261 KSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 570 WLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV--------HGESLQAFLIAIVIPDVETLS-----S 636
Cdd:cd17648 340 WLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHVPesdllS 418
|
....*
gi 1788937591 637 WAKKK 641
Cdd:cd17648 419 FLRAK 423
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
477-635 |
5.98e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 55.80 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 477 GCQFYEGYGQTEctAGCSLTVPGDWTAGHVGAPMPCCLIklVDVE-----------EMNYLAAKGE--GEICVK-GSNVF 542
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAPGVAI--YNPEtltecavarfdAHGALLNADEaiGELVNTaGAGFF 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 543 KGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFVHG----ES 618
Cdd:PRK13388 364 EGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRV 441
|
170
....*....|....*..
gi 1788937591 619 LQAFLIAIVIPDVETLS 635
Cdd:PRK13388 442 GDQVMAALVLRDGATFD 458
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-611 |
1.12e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALlQKGYKPSpDQYFGIFAQNrPEWVIIEQGCYAYSMVVVPLYDTLGN-----EAITYIINKAEL 195
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL-QARASFG-DRAVLLFPSG-PDYVAAFFGCLYAGVIAVPAYPPESArrhhqERLLSIIADAEP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 196 SLVFVDkSDKVDLMLEsVENKLTPGLKTIIIMDPFDSDVVERGkkcgveimsmkaledlgranrRKPKPPsPGDLAVICF 275
Cdd:PRK05691 118 RLLLTV-ADLRDSLLQ-MEELAAANAPELLCVDTLDPALAEAW---------------------QEPALQ-PDDIAFLQY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 276 TSGTTGNPKGALITHQNVVSdcsafvkvtenvvapspDDILISflplaHMFervvekTLRLNSSDIHISYLPLAHmyeql 355
Cdd:PRK05691 174 TSGSTALPKGVQVSHGNLVA-----------------NEQLIR-----HGF------GIDLNPDDVIVSWLPLYH----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 356 mlcvmlchgaKIGFFQGdirllmddlkMLQPtIFPVVPRLLnrMFDKIFGQANTtmkRWIL-------------DFA--- 419
Cdd:PRK05691 221 ----------DMGLIGG----------LLQP-IFSGVPCVL--MSPAYFLERPL---RWLEaiseyggtisggpDFAyrl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 420 -SKR-KEAELRSgiiRNNSLWdkiifhkiqaslggkvRLMVTGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT- 490
Cdd:PRK05691 275 cSERvSESALER---LDLSRW----------------RVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATl 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 491 --AGC-------SLTVPGDWTAGHV-----GAPMPCC-------LIKLVDVEEMNYLAAKGEGEICVKGSNVFKGYLKDP 549
Cdd:PRK05691 336 fvSGGrrgqgipALELDAEALARNRaepgtGSVLMSCgrsqpghAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNP 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788937591 550 AKTAEA-LDKDG--WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQ 611
Cdd:PRK05691 416 EASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
454-612 |
1.14e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.01 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 454 VRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCSLTVPGDWT---AGHVGAPMPCCLIKLVDVEEMNYLAA 528
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 529 KGE-----GEICVKGSNVFKGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIy 603
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI- 443
|
....*....
gi 1788937591 604 qrSEPVAQV 612
Cdd:PRK05857 444 --AEGVSGV 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
454-625 |
1.76e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 454 VRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTE---------CTAGCSLTVPgdwtaghVGAPMPCCLIKLVDvEEM 523
Cdd:PRK05691 1390 LRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTEtainvthwqCQAEDGERSP-------IGRPLGNVLCRVLD-AEL 1461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 524 NYLAAKGEGEICVKGSNVFKGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 596
Cdd:PRK05691 1462 NLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEP 1540
|
170 180 190
....*....|....*....|....*....|.
gi 1788937591 597 EKIENIYQRSEPVAQ--VFVHGESLQAFLIA 625
Cdd:PRK05691 1541 EEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
1.80e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.50 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCyAYSMVVVPLYDT-LGNEAITYIINKAELSLVF 199
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKG--DVVALLMENRPEYLAAWLGL-AKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 200 VDkSDKVDLmLESVENKLTPGlKTIIIMDPFDSDVVErgkkcgveimsmkALEDLGRANRRKPKPPSP-------GDLAV 272
Cdd:PRK08279 140 VG-EELVEA-FEEARADLARP-PRLWVAGGDTLDDPE-------------GYEDLAAAAAGAPTTNPAsrsgvtaKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1788937591 273 ICFTSGTTGNPKGALITHQNVVSDCSAFVKVTenvvAPSPDDILISFLPLAH 324
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLL----RLTPDDVLYCCLPLYH 251
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
113-294 |
9.00e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.20 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 113 KPDQPYEWISYKEVADKAEYVGSALLQKGYKPSpDQYFgIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINK 192
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKG-DRVF-IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 193 AELSLVFVDKSdkvdlMLESVENKLTPGLKTIIIMDpfdsDVVERGKKCgveiMSMKALedLGRANRRKPKPP-SPGDLA 271
Cdd:PRK04319 144 SEAKVLITTPA-----LLERKPADDLPSLKHVLLVG----EDVEEGPGT----LDFNAL--MEQASDEFDIEWtDREDGA 208
|
170 180
....*....|....*....|...
gi 1788937591 272 VICFTSGTTGNPKGALITHQNVV 294
Cdd:PRK04319 209 ILHYTSGSTGKPKGVLHVHNAML 231
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
264-325 |
1.55e-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: 51.52 E-value: 1.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788937591 264 PPSPGDLAVICFTSGTTGNPKGALITHQNVVSdCSAFVKVTeNVVApspDDILISFLPLAHM 325
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLC-GVTA---DDVIYITLPLYHS 196
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-632 |
1.59e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 112 RKPDQPY-----EWISYKEVADKAEYVGSALLQKGYkpSPDQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAI 186
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERGV--GPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 187 TYIINKAelslvfvdksdKVDLMLESVENKLTPGLKTIIIMdpfdsdvVERGKkcgveimsmkalEDLGRANrrKPKPPS 266
Cdd:PRK12316 3147 AYMLEDS-----------GAQLLLSQSHLRLPLAQGVQVLD-------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVvsdcSAFVKVTENVVAPSPDDILISFLPLAhmFERVVEKTlrlnssdihisYL 346
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRHSAL----SNHLCWMQQAYGLGVGDRVLQFTTFS--FDVFVEEL-----------FW 3257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 PLAHmyeqlmlcvmlchGAKIgfFQGDIRLLMDdlkmlqptifpvvPRLLNRMFDKifGQANTTMKRWildfaskrkeae 426
Cdd:PRK12316 3258 PLMS-------------GARV--VLAGPEDWRD-------------PALLVELINS--EGVDVLHAYP------------ 3295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 lrsgiirnnSLWDKIIFHKIQASLGGKVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGH- 505
Cdd:PRK12316 3296 ---------SMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQ---QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAv 3363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 506 -VGAPMPCCLIKLVDVEeMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKI 578
Cdd:PRK12316 3364 pIGRPIANRACYILDGS-LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEY 3442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 579 IDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAfLIAIVIPDVE 632
Cdd:PRK12316 3443 IGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
269-632 |
2.44e-06 |
|
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: 50.55 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVsdcsafvkvteNVVAPSPDDILISFlplahmFERVvektLRLNSSDIHISYLPL 348
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNMV-----------NLLHFEREKTNINF------SDKV----LQFATCSFDVCYQEI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 349 AHMyeqlmlcvmLCHGAKIGFFQGDIRLLMDDLKML------QPTIFPVVprLLNRMFDKifgqanttmKRWILDFASKR 422
Cdd:cd17656 188 FST---------LLSGGTLYIIREETKRDVEQLFDLvkrhniEVVFLPVA--FLKFIFSE---------REFINRFPTCV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 423 KeaelrsgiirnnslwdkiifHKIQAslgGKvRLMVTGaapvsaTVLTFLRAAlGCQFYEGYGQTECTAGCSLTV-PGDW 501
Cdd:cd17656 248 K--------------------HIITA---GE-QLVITN------EFKEMLHEH-NVHLHNHYGPSETHVVTTYTInPEAE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 502 TAGH--VGAPMPCCLIKLVDVEEMnyLAAKGE-GEICVKGSNVFKGYLKDPAKTAEALDKDGW------LHTGDIGKWLP 572
Cdd:cd17656 297 IPELppIGKPISNTWIYILDQEQQ--LQPQGIvGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLP 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1788937591 573 NGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQ--VFVHGESL-QAFLIAIVIPDVE 632
Cdd:cd17656 375 DGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
253-324 |
3.57e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 50.33 E-value: 3.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788937591 253 DLGRANRRKPKPPSPGDLAVICFTSGTTGNPKGALITHQNVVSDC----SAFVKVTENVvaPSPDDILISFLPLAH 324
Cdd:PRK05850 145 DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYH 218
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
114-616 |
1.20e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 48.47 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 114 PDQPY-------EWISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPE-----WVIIEQGCYAysmvvvplydtl 181
Cdd:PRK13390 11 PDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLRTG--DVVALLSDNSPEalvvlWAALRSGLYI------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 182 gnEAITYIINKAELSLVFVDKsdkvdlmlesvenkltpGLKTIIIMDPFDSDVVERGKKC------GVEIMSMKALED-L 254
Cdd:PRK13390 77 --TAINHHLTAPEADYIVGDS-----------------GARVLVASAALDGLAAKVGADLplrlsfGGEIDGFGSFEAaL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 255 GRANRRKPKPPSPgdlAVICFTSGTTGNPKGalithqnVVSDcsafvkVTENVVaPSPDDILISflplahmferVVEKTL 334
Cdd:PRK13390 138 AGAGPRLTEQPCG---AVMLYSSGTTGFPKG-------IQPD------LPGRDV-DAPGDPIVA----------IARAFY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 335 RLNSSDIHISYLPLAHMyEQLMLCVMLcH---GAKIGFFQGDIRLLMDDLKMLQPTIFPVVPRLLNRMFdkifgqanttm 411
Cdd:PRK13390 191 DISESDIYYSSAPIYHA-APLRWCSMV-HalgGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL----------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 412 krwildfaskRKEAELRSgiirnnsLWDKiifhkiqaslgGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTA 491
Cdd:PRK13390 258 ----------KLDADVRT-------RYDV-----------SSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AH 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 492 GCSLTVPGDWTA--GHVGAPMPCCLiKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKDG--WLHTGDI 567
Cdd:PRK13390 309 GMTFIDSPDWLAhpGSVGRSVLGDL-HICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDL 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1788937591 568 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFVHG 616
Cdd:PRK13390 387 GSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVAVIG 434
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-290 |
2.26e-05 |
|
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: 47.87 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpDQyFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLVFV 200
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 201 D----KSDKVDLMLESVEnkltpglKTIIIMDPFDSDVVERGKKCGVeimSMKALEDLGRANRRKPKPP-----SPGDLA 271
Cdd:cd05968 170 AdgftRRGREVNLKEEAD-------KACAQCPTVEKVVVVRHLGNDF---TPAKGRDLSYDEEKETAGDgaertESEDPL 239
|
170
....*....|....*....
gi 1788937591 272 VICFTSGTTGNPKGALITH 290
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVH 258
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
443-641 |
3.39e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 47.08 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 443 FHKIQASLGGKVRLMVTGA---AP-VSATVLTFLRAalgcQFYEGYGQTECTAGCSLtVPGDWTAGHVGAPMPCCLIKLV 518
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAkweAEaKEKIKNIFPYA----KLYEFYGASELSFVTAL-VDEESERRPNSVGRPFHNVQVR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 519 DVEEMNYLAAKGE-GEICVKGSNVFKGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 597
Cdd:PRK07638 320 ICNEAGEEVQKGEiGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPE 397
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1788937591 598 KIENIYQRSEPVAQVFVHG---ESLQAFLIAIVI--PDVETLSSWAKKK 641
Cdd:PRK07638 398 EIESVLHEHPAVDEIVVIGvpdSYWGEKPVAIIKgsATKQQLKSFCLQR 446
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
267-625 |
4.92e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.08 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 267 PGDLAVICFTSGTTGNPKGALITHQNVVSDCSAFVKVTEnvvaPSPDDILISFLPLAhmFERVVEKtlrlnssdihiSYL 346
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYE----LDANDRVLLFMSFS--FDGAQER-----------FLW 3298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 347 PLahmyeqlmlcvmlCHGAKIGFFQGDIRllmDDLKMLQptifpvvprLLNRmfdkifgQANTtmkrwILDFASKRKEAE 426
Cdd:PRK12467 3299 TL-------------ICGGCLVVRDNDLW---DPEELWQ---------AIHA-------HRIS-----IACFPPAYLQQF 3341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 427 LRsgiirnnslwdkiiFHKIQAslGGKVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCSL-TVPGDWTAG 504
Cdd:PRK12467 3342 AE--------------DAGGAD--CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCE 3405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 505 H----VGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPN 573
Cdd:PRK12467 3406 ApyapIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRAD 3484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1788937591 574 GTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFV------HGESLQAFLIA 625
Cdd:PRK12467 3485 GVIEYLGRIDHQVKI-RGFRIELGEIEARLLQHPSVREAVVlardgaGGKQLVAYVVP 3541
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
261-294 |
7.18e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.58 E-value: 7.18e-05
10 20 30
....*....|....*....|....*....|....*
gi 1788937591 261 KPKPPS-PGDLAVICFTSGTTGNPKGALITHQNVV 294
Cdd:PRK10252 590 APLQLSqPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
532-615 |
1.97e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 45.04 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 532 GEICVKGSNVFKGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQR 605
Cdd:PRK10252 803 GDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQA 881
|
90
....*....|
gi 1788937591 606 SEPVAQVFVH 615
Cdd:PRK10252 882 LPDVEQAVTH 891
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
530-616 |
2.95e-04 |
|
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: 43.91 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 530 GEGEICVKGsNVFKGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYQRS 606
Cdd:cd05924 213 GVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEALKSH 290
|
90
....*....|
gi 1788937591 607 EPVAQVFVHG 616
Cdd:cd05924 291 PAVYDVLVVG 300
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
518-623 |
5.18e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 43.19 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 518 VDVEEMNYLAAKGEGE----ICVKGSNVFKGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 593
Cdd:cd05915 343 LRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEW 421
|
90 100 110
....*....|....*....|....*....|....*..
gi 1788937591 594 IAPEKIENIYQRSEPVAQVFV-------HGESLQAFL 623
Cdd:cd05915 422 ISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
121-290 |
6.71e-04 |
|
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: 42.95 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYKPSpdQYFGIFAQNRPEWVIIEQGCYAYSMVVVPLYDTLGNEAITYIINKAELSLV-- 198
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKG--DRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLit 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 199 ---FVDKSDKVDL--MLESVENKLTPGLKTIIIMDPFDSDVverGKKCGVEIMSMKALEDlgRANRRKPKPPSPGDLAVI 273
Cdd:cd17634 163 adgGVRAGRSVPLkkNVDDALNPNVTSVEHVIVLKRTGSDI---DWQEGRDLWWRDLIAK--ASPEHQPEAMNAEDPLFI 237
|
170
....*....|....*..
gi 1788937591 274 CFTSGTTGNPKGALITH 290
Cdd:cd17634 238 LYTSGTTGKPKGVLHTT 254
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
269-299 |
6.87e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 42.72 E-value: 6.87e-04
10 20 30
....*....|....*....|....*....|.
gi 1788937591 269 DLAVICFTSGTTGNPKGALITHQNVVSDCSA 299
Cdd:PRK07824 36 DVALVVATSGTTGTPKGAMLTAAALTASADA 66
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
481-624 |
9.30e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 42.44 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 481 YEGYGQTEctAGCSLTV-PGDWTAG--HVGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYlkDPAKTAEAld 557
Cdd:PRK13382 341 YNNYNATE--AGMIATAtPADLRAApdTAGRPAEGTEIRILD-QDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDF-- 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 558 KDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYQRSEPVAQVFV-------HGESLQAFLI 624
Cdd:PRK13382 414 HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDVAEAAVigvddeqYGQRLAAFVV 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-637 |
1.28e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 42.64 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 121 ISYKEVADKAEYVGSALLQKGYkpSPDQYFGIFAQNRPEWVI----IEQGCYAYsmvvVPLYDTLGNEAITYIINKAELS 196
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGV--GPDVLVGVAMERSIEMVVallaILKAGGAY----VPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 197 LVFVDKSDKVDLmlesvenKLTPGLKTIIIMDPfdsdvvergkkcgveimsmkALEDLGRANRRKPKPPSPGDLAVICFT 276
Cdd:PRK12316 611 LLLSQSHLGRKL-------PLAAGVQVLDLDRP--------------------AAWLEGYSEENPGTELNPENLAYVIYT 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 277 SGTTGNPKGALITHQNVVSDCSAF-----VKVTENVVAPSPDDILIS----FLPLAHmfervvEKTLRLNSSDIHISYLP 347
Cdd:PRK12316 664 SGSTGKPKGAGNRHRALSNRLCWMqqaygLGVGDTVLQKTPFSFDVSvwefFWPLMS------GARLVVAAPGDHRDPAK 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 348 LAHMYEQlmlcvmlcHGakigffqgdirllMDDLKMlqptifpvVPRLLNRMFDKIFGQANTTMKRWILdfaskrkeael 427
Cdd:PRK12316 738 LVELINR--------EG-------------VDTLHF--------VPSMLQAFLQDEDVASCTSLRRIVC----------- 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 428 rSGiirnnslwdkiifhkiqASLGGKVRLMVTGAAPVsatvltflraalgCQFYEGYGQTECTAG--CSLTVPGDWTAGH 505
Cdd:PRK12316 778 -SG-----------------EALPADAQEQVFAKLPQ-------------AGLYNLYGPTEAAIDvtHWTCVEEGGDSVP 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 506 VGAPMPCCLIKLVDVEeMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKII 579
Cdd:PRK12316 827 IGRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYA 905
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788937591 580 DRKKHIFKLaQGEYIAPEKIENIYQRSEPVAQVFVHGESLQAfLIAIVIPD------VETLSSW 637
Cdd:PRK12316 906 GRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAH 967
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
484-625 |
2.25e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788937591 484 YGQTECTAGCSL-TVPGDWTAGH---VGAPMPCCLIKLVDvEEMNYLAAKGEGEICVKGSNVFKGYLKDPAKTAEALDKD 559
Cdd:PRK05691 4016 YGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPH 4094
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788937591 560 GW-------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYQRSEPV------AQVFVHGESLQAFLIA 625
Cdd:PRK05691 4095 PFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI-RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
251-324 |
7.27e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 39.33 E-value: 7.27e-03
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gi 1788937591 251 LEDLGRANRRKPKPPSPGDL-AVICF--TSGTTGNPKGALITHQNVVSdCSAFVKVTENVvapSPDDILISFLPLAH 324
Cdd:cd05939 84 LDPLLTQSSTEPPSQDDVNFrDKLFYiyTSGTTGLPKAAVIVHSRYYR-IAAGAYYAFGM---RPEDVVYDCLPLYH 156
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