|
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 ... |
116-694 |
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: 962.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 116 QPYEWLSYKQVEEMSECVGSGLIQKGFKAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAEL 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 196 SLVFVDKpekanllldgvenklipglktivlmdsfgsslleqgqkcGVEIISMKALEDLGRANRQKPKPPAPEDIAVICF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 276 TSGTTGNPKGAVITHRNVVSDCSAFVKMTENVFIPTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFFQGDIRLLMDDL 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 356 KALRPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDKLIFHKIQSSLGGRVKLMIT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 434 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAA--KGEGEVCVK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 512 GPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGE 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 592 SLQAFLIAIVVPDAETVGPWARKR-GFEGSFEELCRNKDVRKAILEDMVRLGKDSGLKSFEQVKAISLHPELFTIDNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 970702926 671 TPTMKAKRPDLQNYFRSQINELYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-694 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 710.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 86 YDDVTTLYEGFQRGMRVSNNGACLGSR-KPDQ---PYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWV 161
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 162 IIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVdKPEKANLLLDGVENklIPGLKTIVLMDSFGSSLLEQGQKC 241
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 242 GVEIISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvFIPTpdDTLISFLP 321
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYPS--DVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 322 LAHMFERVVECTMLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEA 399
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 400 ELRSGiiRNNS-LWDKLIFHKIQSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAG 478
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 479 HVGAPMPCSLIKLVDVEEMNYLAAKG---EGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 556 KKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDAETVGPWARKRGFE-GSFEELCRNKDVRKAI 634
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 635 LEDMVRLGKDSGLKSFEQVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELYS 694
Cdd:PLN02736 589 LADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 537.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 86 YDDVTTLYEGFQRGMRVSNNGACLgSRKPDQPYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQ 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 166 GCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDKPEKANLLLDGVENklIPGLKTIVLMDsfgssllEQGQKCGVEI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 246 ISMKALEDLGRANR------QKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKmtenVFIPTPDDTLISF 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLE----RLPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 320 LPLAHMFERVVECTMLCHGAKIGFfQGDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---S 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 395 KRKEAELRSGiiRNNSLW--------DKLIFHKIQSSLGGRVKLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 467 CCLTVAGDWTAGHVGAPMPCSLIKLVDveemnylaakgEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 547 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESlQAFLIAIVVPDAETVGPWARKRG-FEGSFEELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970702926 626 RNKDVRKAILEDMVRLGKdsGLKSFEQVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELYS 694
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-679 |
1.02e-169 |
|
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: 493.65 E-value: 1.02e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 116 QPYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAEL 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 196 SLVFVDKPEkanllldgvenklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkppapeDIAVICF 275
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 276 TSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAHMFERV-VECTMLCHGAKIGFFQgDIRLLMDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLP----ATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 355 LKALRPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdklifhkiqsslGGRVKLMITG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 435 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDveemnylaakgEGEVCVKGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 515 VFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESlQ 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 595 AFLIAIVVPDAETVGPWARKRG-FEGSFEELCRNKDVRKAILEDMVRLGKdsGLKSFEQVKAISLHPELFTIDNGLLTPT 673
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*.
gi 970702926 674 MKAKRP 679
Cdd:cd05907 445 LKLKRP 450
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
77-698 |
1.93e-163 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 485.50 E-value: 1.93e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 77 DSDEPLVYFYDDVTTLYEGFQRGMRVSNNGAClgsrkpdQPYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQN 156
Cdd:PLN02861 41 DIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKV-------GPYVWLTYKEVYDAAIRIGSAIRSRGVN--PGDRCGIYGSN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 157 RPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDKPEKANLLldGVENKLIPGLKTIVLMDSFGSSLLE 236
Cdd:PLN02861 112 CPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 237 QGQKCGVEIISMKALEDLGRANRQKPkPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSA---FVKMTENVFipTPD 313
Cdd:PLN02861 190 EAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLStdhLLKVTDRVA--TEE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 314 DTLISFLPLAHMFERVVECTMLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLlnrmFDRIFG------QANTTLKR 387
Cdd:PLN02861 267 DSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 388 WLLDFASKRKEAELRSGIIRNNS--LWDKLIFHKIQSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA 465
Cdd:PLN02861 343 KLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 466 GCCLTVAGDWT-AGHVGAPMPCSLIKLVDVEEMNY--LAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIG 542
Cdd:PLN02861 423 GCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 543 KWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDAETVGPWARKRGFEGSFE 622
Cdd:PLN02861 502 EWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFK 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970702926 623 ELCRNKDVRKAILEDMVRLGKDSGLKSFEQVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELYSTVKV 698
Cdd:PLN02861 582 SLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
4.38e-161 |
|
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: 473.63 E-value: 4.38e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 117 PYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELS 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 197 LVFVDkpekanllldgvenklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkpPAPEDIAVICFT 276
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 277 SGTTGNPKGAVITHRNVVSDCSAfvkMTENVFI-PTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFfqGDIRLLMD-- 353
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAG---LGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDks 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 354 ------DLKALRPTVFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDKLIFHKIQSSLG 425
Cdd:cd17639 172 krgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 426 GRVKLMITGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGE 505
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 506 --GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPV 583
Cdd:cd17639 329 prGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 584 AQVFVHGESLQAFLIAIVVPDAETVGPWARKRGF-EGSFEELCRNKDVRKAILEDMVRLGKDSGLKSFEQVKAISLHPEL 662
Cdd:cd17639 409 NNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEE 488
|
570
....*....|....*.
gi 970702926 663 FTIDNGLLTPTMKAKR 678
Cdd:cd17639 489 WTPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-696 |
1.03e-154 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 463.13 E-value: 1.03e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 88 DVTTLYEGFQRGMRVSNNGACLGSRKPDQ----PYEWLSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVII 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASG--AEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 164 EQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV-DKPEKANLLLDGVENKLipgLKTIVLMDSFGSSLLEQGQKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDKKIKELLEPDCKSAKR---LKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 243 VEIISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNV---VSDCSAFVKMTENVFipTPDDTLISF 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVatfVRGVDLFMEQFEDKM--THDDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 320 LPLAHMFERVVECTMLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 398 EAELRSGIIRNNS--LWDKLIFHKIQSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 476 TA-GHVGAPMPCSLIKLVDVEEMNY--LAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 553 IDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDAETVGPWARKRGFEGSFEELCRNKDVRK 632
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970702926 633 AILEDMVRLGKDSGLKSFEQVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELYSTV 696
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-697 |
1.18e-153 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 460.64 E-value: 1.18e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 87 DDVTTLYEGFQRGMRVSNNGACLGSR-----KPDQpYEWLSYKQVEEMSECVGSGLIQKGFKAapDQFIGIFAQNRPEWV 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 162 IIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDKPEKANLLldgvenKLIPG----LKTIVLMDSFGSSLLEQ 237
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF------KTCPNsteyMKTVVSFGGVSREQKEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 238 GQKCGVEIISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVFIP-TPDDTL 316
Cdd:PLN02614 193 AETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAlTVKDVY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 317 ISFLPLAHMFERVVECTMLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFAS 394
Cdd:PLN02614 273 LSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 395 KRKEAELRSGI--IRNNSLWDKLIFHKIQSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVA 472
Cdd:PLN02614 353 SYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 473 GDW-TAGHVGAPMPCSLIKLVDVEEMNY--LAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGT 549
Cdd:PLN02614 433 DELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGS 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 550 LKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDAETVGPWARKRGFEGSFEELCRNKD 629
Cdd:PLN02614 512 MKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEK 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970702926 630 VRKAILEDMVRLGKDSGLKSFEQVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELYSTVK 697
Cdd:PLN02614 592 AKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-694 |
3.76e-135 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 413.74 E-value: 3.76e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 62 VEVAGSDG-ARRSAilDSDEPLVYFYDDVTTLYEGFQRGMRVSNNGACLGSRK---------PDQ---------PYEWLS 122
Cdd:PLN02387 31 VDVGGEPGyAIRNA--RFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 123 YKQVEEMSECVGSGLIQKGFKAapDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDK 202
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 203 PEKANLLldGVENKLiPGLKTIVLMDSFGSSL-LEQGQKCGVEIISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTG 281
Cdd:PLN02387 187 KQLKKLI--DISSQL-ETVKRVIYMDDEGVDSdSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 282 NPKGAVITHRNVVSDCSAFvkMTenvFIP--TPDDTLISFLPLAHMFERVVECTMLCHGAKIGFfqGDIRLLMD------ 353
Cdd:PLN02387 264 LPKGVMMTHGNIVATVAGV--MT---VVPklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkik 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 354 -----DLKALRPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELR------SGIIRnnSLWDKLIFHKI 420
Cdd:PLN02387 337 kgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 QSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYL 500
Cdd:PLN02387 415 RAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYL 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 501 AAKG---EGEVCVKGPNVFQGYLKDPAKTAEV--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKI 573
Cdd:PLN02387 495 ISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKV 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 574 ENIYLRSEPVAQVFVHGESLQAFLIAIVVPDAETVGPWARKRGFE-GSFEELCRNKDVRKAILEDMVRLGKDSGLKSFEQ 652
Cdd:PLN02387 575 EAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEI 654
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 970702926 653 VKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELYS 694
Cdd:PLN02387 655 PAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
112-563 |
5.55e-129 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 388.21 E-value: 5.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 112 RKPDQP------YEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEA 185
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALGVG--KGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 186 ITYIINKAELSLVFVDKPEKANLLLDGVENKLIPGLKTIVLMDSFGSSLLeqgqkcgveiisMKALEDLGRANRQKPKPP 265
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVFIPTPDDTLISFLPLAHMFERVVEC-TMLCHGAKIGFF 344
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGDIRL----LMDDLKALRPTVFPVVPRLLNRMFDrifgqaNTTLKRWLLdfaskrkeaelrsgiirnnslwdklifhki 420
Cdd:pfam00501 233 PGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------AGAPKRALL------------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qsslgGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDW---TAGHVGAPMPCSLIKLVDVEEM 497
Cdd:pfam00501 277 -----SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETG 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970702926 498 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
121-693 |
1.88e-106 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 338.87 E-value: 1.88e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVfV 200
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI-V 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DKPEKANLLLDGVENKLIPGLkTIVLMDSFGSSLleqgQKCGVEIISMKALEDLGRANRQKPKPPAPE---DIAVICFTS 277
Cdd:PTZ00216 199 CNGKNVPNLLRLMKSGGMPNT-TIIYLDSLPASV----DTEGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 278 GTTGNPKGAVITHRNVVSDCSAFV-KMTENVFIPTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFfqGDIRLLMD--- 353
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 354 ----DLKALRPTVFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEAELRSGiiRNNSLWDKLIFHK 419
Cdd:PTZ00216 352 rphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 IQSSLGGRVKLMITGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCCLTV--AGDWTAGHVGAPMPCSLIKLVDVEEM 497
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCGGIqrTGDLEPNAVGQLLKGVEMKLLDTEEY 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 498 NYlAAKGE--GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN 575
Cdd:PTZ00216 499 KH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 576 IYLRSEPVAQ----VFVHgeSLQAFLIAIVVPDAETVGPWARKRGFEGSFEELCRNKDVRKAILEDMVRLGKDSGLKSFE 651
Cdd:PTZ00216 578 LYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFE 655
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 970702926 652 QVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELY 693
Cdd:PTZ00216 656 IVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
4.24e-94 |
|
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: 299.66 E-value: 4.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 116 QPYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAEL 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 196 SLVFVdkpekanllldgvENklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkppAPEDIAVICF 275
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 276 TSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFfqGDIRLLMDDL 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVP----PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 356 KALRPTVFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDKLIFHKIQSslGGRVKLMI 432
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 433 TGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKG 512
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 513 PNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGES 592
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 593 lQAFLIAIVVPDAETVGPWARKRG--FEGSFEELCRNKDVRKAI-LEDMVRLGKDSGLKSFEQVKAISLHPELFtIDNGL 669
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 970702926 670 LTPTMKAKRP 679
Cdd:cd17640 457 MTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
118-678 |
5.67e-78 |
|
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: 258.55 E-value: 5.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 118 YEWLSYKQVEEMSECVGSGLiqKGFKAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSL 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAAL--RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 198 VFVDKPEKANLLLDGVENKLIpglkTIVLMDSFGSSLLEQGQkcgvEIISMKALEdlgranrQKPKPPAPEDIAVICFTS 277
Cdd:cd05932 82 LFVGKLDDWKAMAPGVPEGLI----SISLPPPSAANCQYQWD----DLIAQHPPL-------EERPTRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 278 GTTGNPKGAVITHRNVVSDCSAFVkmteNVFIPTPDDTLISFLPLAHMFERV-VECTMLCHGAKIgFFQGDIRLLMDDLK 356
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 357 ALRPTVFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRKEAELRsgIIRNNSLWDKLIFHKIQSSLG-GRVKLMITGA 435
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGVQ---------------DKIPQQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 436 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDveemnylaakgEGEVCVKGPNV 515
Cdd:cd05932 285 APVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 516 FQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQA 595
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 596 fLIAIVVPDAEtvgpwARKRGFEGSFEELCRNkdvRKAILEDMvrlgkDSGLKSFEQVKAISLHPELFTIDNGLLTPTMK 675
Cdd:cd05932 433 -PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTLK 498
|
...
gi 970702926 676 AKR 678
Cdd:cd05932 499 IKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
112-615 |
1.74e-75 |
|
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: 250.11 E-value: 1.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 112 RKPDQP-----YEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAI 186
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 187 TYIINKAELSLVFVdkpekanllldgvenklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkppa 266
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 pediAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAHMFERVVEC-TMLCHGAKI---- 341
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG----LTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLvllp 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 342 GFfqgDIRLLMDDLKALRPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdklifhkiq 421
Cdd:COG0318 175 RF---DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------ 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 422 sslggrVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTA--GHVGAPMPCSLIKLVDvEEMNY 499
Cdd:COG0318 217 ------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 500 LAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLR 579
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 970702926 580 SEPVAQVFV-------HGESLQAFLI--AIVVPDAETVGPWARKR 615
Cdd:COG0318 368 HPGVAEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-678 |
7.62e-71 |
|
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: 241.17 E-value: 7.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 122 SYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIE---QGCFAYSMvviPLYDTLGTEAITYIINKAELSLV 198
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAElaaQAIGALSL---GIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 199 FVDKPEKANLLLDGVENklIPGLKTIVLMDSFGSSLLEQGQkcgveIISMKALEDLGRA-NRQKPK-------PPAPEDI 270
Cdd:cd17641 88 IAEDEEQVDKLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 271 AVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENvfipTPDDTLISFLPLAHMFERV--VECTMLChGAKIGFFQgDI 348
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQMysVGQALVC-GFIVNFPE-EP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 349 RLLMDDLKALRPTVFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDKLIF 417
Cdd:cd17641 235 ETMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 418 HKIQSSLG-GRVKLMITGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVee 496
Cdd:cd17641 315 RPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 mnylaakgeGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENi 576
Cdd:cd17641 392 ---------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIEN- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 577 YLRSEPV---AQVFVHGeslQAFLIAIVVPDAETVGPWARKRGFE-GSFEELCRNKDVRKAILEDMVRLGKDsgLKSFEQ 652
Cdd:cd17641 462 KLKFSPYiaeAVVLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQR 536
|
570 580
....*....|....*....|....*.
gi 970702926 653 VKAISLHPELFTIDNGLLTPTMKAKR 678
Cdd:cd17641 537 IRRFLLLYKELDADDGELTRTRKVRR 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
144-671 |
5.56e-69 |
|
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: 236.58 E-value: 5.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 144 AAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDK---PEKANLLLDGvenkliPG 220
Cdd:cd17632 90 VRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAehlDLAVEAVLEG------GT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 221 LKTIVLMD----------SFGSS---LLEQGqkCGVEIISMKALEDLGrANRQKPKPPAPED--IAVICFTSGTTGNPKG 285
Cdd:cd17632 164 PPRLVVFDhrpevdahraALESArerLAAVG--IPVTTLTLIAVRGRD-LPPAPLFRPEPDDdpLALLIYTSGSTGTPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 286 AVITHRNVVSdcsAFVKMTENVFIPTPDDTLISFLPLAHMFERVVECTMLCHGAkIGFFQG--DIRLLMDDLKALRPTVF 363
Cdd:cd17632 241 AMYTERLVAT---FWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 364 PVVPRLLNRMFDRIfgQAntTLKRWLLDFA-----SKRKEAELRsgiirnnslwdklifhkiQSSLGGRVKLMITGAAPV 438
Cdd:cd17632 317 FLVPRVCDMLFQRY--QA--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 439 SATVLTFLRAALGCQFYEGYGQTEctAGcclTVAGDwtaGHVGAPmPCSLIKLVDVEEMNYLAAKG---EGEVCVKGPNV 515
Cdd:cd17632 375 SAEMKAFMESLLDLDLHDGYGSTE--AG---AVILD---GVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 516 FQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQA 595
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERA 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970702926 596 FLIAIVVP--DAETVGPWARKRGfegsfeelcrnkdvrkAILEDMVRLGKDSGLKSFEQVKAISLHPELFTIDNGLLT 671
Cdd:cd17632 526 YLLAVVVPtqDALAGEDTARLRA----------------ALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
4.89e-68 |
|
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: 234.17 E-value: 4.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 113 KPDQPYEWLSYKQVEEMSECVGSGLIQKGFkaapDQF--IGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYII 190
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 191 NKAELSLVFVDKPEKANLLLDgVENKLiPGLKTIVlmdSFGSSLLEQGQKcgveIISMKALEDLGR-----ANRQKPKPP 265
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAII---QYKEPLKEKEPN----LYSWDEFMELGRsipdeQLDAIISSQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVFIPTPDDTLISFLPLAHMFERVVEC-TMLCHGAKIGFF 344
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGDIR--LLMDDLKALRPTVFPVVPRLLNRMFDRI--FGQANTTLKRWLLDFAsKRKEAE-------LRSGIIRNNSLWD 413
Cdd:cd05933 228 QPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRLAK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 414 KLIFHKIQSSLG-GRVKLMITGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLV 492
Cdd:cd05933 307 KLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 493 DVEemnylaAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEK 572
Cdd:cd05933 386 NPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 573 IENIYLRSEP-VAQVFVHGESLQaFLIAIVV----PDAETVGP----------WARKRGFEGS-FEELCRNKD--VRKAI 634
Cdd:cd05933 460 IEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkceVNPETGEPldelteeaieFCRKLGSQATrVSEIAGGKDpkVYEAI 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 970702926 635 LEDMVRLGKDSgLKSFEQVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQINELY 693
Cdd:cd05933 539 EEGIKRVNKKA-ISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-615 |
9.21e-67 |
|
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: 222.93 E-value: 9.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFFQG-D 347
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKfD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 348 IRLLMDDLKALRPTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdklifhkiqsslggr 427
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAP-----------------ESAGYDLSS------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 428 VKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWT--AGHVGAPMPCSLIKLVDVEEmNYLAAKGE 505
Cdd:cd04433 116 LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPGEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 506 GEVCVKGPNVFQGYLKDPAKTAEVlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQ 585
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAE 272
|
330 340 350
....*....|....*....|....*....|....*....
gi 970702926 586 VFVHG---ESLQAFLIAIVVP------DAETVGPWARKR 615
Cdd:cd04433 273 AAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-590 |
5.59e-65 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 222.86 E-value: 5.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DKPEKANLLLDGvenKLIPGLKTIVLMDSFGSSLLEQGQ----KCGVEIismkaledlgrANRQKPKPPAPEDIAVICFT 276
Cdd:cd05911 89 DPDGLEKVKEAA---KELGPKDKIIVLDDKPDGVLSIEDllspTLGEED-----------EDLPPPLKDGKDDTAAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 277 SGTTGNPKGAVITHRNVVSDCSaFVKMTENVFIPtPDDTLISFLPLAHMFERVVECTMLCHGAK-IGFFQGDIRLLMDDL 355
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLIANLS-QVQTFLYGNDG-SNDVILGFLPLYHIYGLFTTLASLLNGATvIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 356 KALRPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDKlifHKIQSslggrVKLMITGA 435
Cdd:cd05911 233 EKYKITFLYLVPPIAAALA---------------------------------KSPLLDK---YDLSS-----LRVILSGG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 436 APVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPN 514
Cdd:cd05911 272 APLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQ 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970702926 515 VFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHG 590
Cdd:cd05911 352 VMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
112-615 |
8.15e-63 |
|
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: 216.66 E-value: 8.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 112 RKPDQPY-----EWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLyDTLGTEai 186
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPL-NPLYTP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 187 tyiinkaelslvfvdkPEKANLLLDGvenklipGLKTIVLMDSFgSSLLEQGQKcgveiismkaledlgranRQKPKPPA 266
Cdd:cd05936 86 ----------------RELEHILNDS-------GAKALIVAVSF-TDLLAAGAP------------------LGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAfVKMTENVFIpTPDDTLISFLPLAHMFERVVECT-MLCHGAKIGFFQ 345
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWLEDLL-EGDDVVLAALPLFHVFGLTVALLlPLALGATIVLIP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 346 G-DIRLLMDDLKALRPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiirnnslwdklifhkiqssl 424
Cdd:cd05936 202 RfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS--------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 ggrVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAK 503
Cdd:cd05936 244 ---LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELPPG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 504 GEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPV 583
Cdd:cd05936 320 EVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAV 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 970702926 584 AQVFV-------HGESLQAFliaIVVPDAETVGP-----WARKR 615
Cdd:cd05936 398 AEAAVvgvpdpySGEAVKAF---VVLKEGASLTEeeiiaFCREQ 438
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
9.74e-63 |
|
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: 216.15 E-value: 9.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQV----EEMSECVGSGLIQKGFKaapdqfIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELS 196
Cdd:cd05914 8 LTYKDLadniAKFALLLKINGVGTGDR------VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 197 LVFVDKPEkanllldgvenklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkppapeDIAVICFT 276
Cdd:cd05914 82 AIFVSDED----------------------------------------------------------------DVALINYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 277 SGTTGNPKGAVITHRNVVSDCsAFVKMTENVfipTPDDTLISFLPLAHMFERVVECTM-LCHGAKIGFFQGDIRLLMDDL 355
Cdd:cd05914 98 SGTTGNSKGVMLTYRNIVSNV-DGVKEVVLL---GKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 356 KALRPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLdfaskrkeaeLRSGIIRNNSLWDKLIFHKIQSSLGGRVKLMITGA 435
Cdd:cd05914 174 AFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK----------FKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 436 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPmpcslIKLVDVEEMNYLAAKGEGEVCVKGPNV 515
Cdd:cd05914 244 AKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 516 FQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVA--QVFV-HGEs 592
Cdd:cd05914 318 MKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVqEKK- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 593 lqafLIAIVVPDAEtvgpwarkrgFEGSFEELCRNKdvRKAILEDmVRLGKDSGLKSFEQVKAISLHPELFTidnglLTP 672
Cdd:cd05914 397 ----LVALAYIDPD----------FLDVKALKQRNI--IDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE-----KTP 454
|
....*.
gi 970702926 673 TMKAKR 678
Cdd:cd05914 455 KGKIKR 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
110-615 |
1.04e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 217.46 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 110 GSRKPDQPY-----EWLSYKQVEEMSECVGSGLIQKGFKAApDQfIGIFAQNRPEWVIieqGCFAYSM---VVIPLYDTL 181
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIGKG-DR-VAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 182 GTEAITYIINKAELSLVFVdkpekANLLL--DGVENKLIPGLKTIVLMDSfgssllEQGQKCGVEIISMKALedLGRANR 259
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFLgvDYSATTRLPALEHVVICET------EEDDPHTEKMKTFTDF--LAAGDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 260 QKPKPP-APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAHMFERVVEC-TMLCH 337
Cdd:PRK07656 157 AERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLG----LTEGDRYLAANPFFHVFGYKAGVnAPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 338 GAKI----GFfqgDIRLLMDDLKALRPTVFPVVPrllnrmfdrifgqantTLKRWLLDFAsKRKEAELRSgiirnnslwd 413
Cdd:PRK07656 233 GATIlplpVF---DPDEVFRLIETERITVLPGPP----------------TMYNSLLQHP-DRSAEDLSS---------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 414 klifhkiqsslggrVKLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLTVAGD---WTAGHVGAPMPCSLI 489
Cdd:PRK07656 283 --------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVEN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 490 KLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:PRK07656 349 KIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVY 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 970702926 570 PEKIENIYLRSEPVAQVFV-------HGESLQAFliaiVVP------DAETVGPWARKR 615
Cdd:PRK07656 427 PAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
122-615 |
8.55e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 201.57 E-value: 8.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 122 SYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIieqgC-FAYSM---VVIPLYDTLGTEAITYIINKAELSL 197
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLE----AyFAVPKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 198 VFVDK---PEKANLLldgvenKLIPGLKTIVLMDSFGSSLleqgqkCGVEIISmkaLEDLgrANRQKPKPPAPE----DI 270
Cdd:PRK06187 107 VLVDSefvPLLAAIL------PQLPTVRTVIVEGDGPAAP------LAPEVGE---YEEL--LAAASDTFDFPDidenDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 271 AVICFTSGTTGNPKGAVITHRNVVSD---CSAFVKMTenvfiptPDDTLISFLPLAHMFERVVECTMLCHGAKI---GFF 344
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLS-------RDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 qgDIRLLMDDLKALRPTVFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrkeaelrsgiirnnslwdklifhkiqssl 424
Cdd:PRK06187 243 --DPENLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF----------------------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 gGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLT----VAGDWT-AGHVGAPMPCSLIKLVDvEEMN 498
Cdd:PRK06187 281 -SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLPGQWTkRRSAGRPLPGVEARIVD-DDGD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 499 YLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEVLDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:PRK06187 359 ELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 970702926 577 YLRSEPVAQVFV-------HGESLQAFliaIVVPDAETVGP-----WARKR 615
Cdd:PRK06187 437 LYGHPAVAEVAVigvpdekWGERPVAV---VVLKPGATLDAkelraFLRGR 484
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
269-615 |
4.44e-43 |
|
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: 161.30 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENvfipTPDDTLISFLPLAHMFERVVE--CTMLCHGAKI--GFF 344
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRW----TEDDVLLHVLPLHHVHGLVNAllCPLFAGASVEflPKF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGDIRLLMDDLKALrpTVFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdklifhkiqssl 424
Cdd:cd05941 166 DPKEVAISRLMPSI--TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA------------------------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 gGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTV--AGDWTAGHVGAPMPCSLIKLVDVEEMNYLAA 502
Cdd:cd05941 212 -ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNplDGERRPGTVGMPLPGVQARIVDEETGEPLPR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 503 KGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIENIYLRSE 581
Cdd:cd05941 289 GEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHP 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 970702926 582 PVAQVFVHGESLQAF---LIAIVVP-------DAETVGPWARKR 615
Cdd:cd05941 368 GVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
121-582 |
7.29e-43 |
|
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: 162.40 E-value: 7.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGL----IQKGfkaapdQFIGIFAQNRPEWVIIeqgCFAYSM--VVIPLYDTLGTEA-ITYIINKA 193
Cdd:cd05904 33 LTYAELERRVRRLAAGLakrgGRKG------DVVLLLSPNSIEFPVA---FLAVLSlgAVVTTANPLSTPAeIAKQVKDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 194 ELSLVFVDKPekanllldgVENKLIPGLKTIVLMDS--FGSSLLEQGQKCGveiismkaledlGRANRQKPKPPaPEDIA 271
Cdd:cd05904 104 GAKLAFTTAE---------LAEKLASLALPVVLLDSaeFDSLSFSDLLFEA------------DEAEPPVVVIK-QDDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 272 VICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVfiPTPDDTLISFLPLAHMFE-RVVECTMLCHGAKI----GFfqg 346
Cdd:cd05904 162 ALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFHIYGlSSFALGLLRLGATVvvmpRF--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 DIRLLMDDLKALRPTVFPVVPRLLNRMfdrifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdklifhkiqSSLgg 426
Cdd:cd05904 237 DLEELLAAIERYKVTHLPVVPPIVLAL---------------------------VKSPIVDKYDL----------SSL-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 427 rvKLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAG---CCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAA 502
Cdd:cd05904 278 --RQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 503 KGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIyLRSEP 582
Cdd:cd05904 356 NQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL-LLSHP 433
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
111-604 |
2.46e-41 |
|
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: 156.23 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 111 SRKPDQP-YEW----LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEA 185
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVA--KGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 186 ITYIINKAELSLVFvdkpekanllldgvenklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkpp 265
Cdd:cd17631 84 VAYILADSGAKVLF------------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 apEDIAVICFTSGTTGNPKGAVITHRNVvsdcsAFVKMTENVFIP-TPDDTLISFLPLAHMFERVVECTM-LCHGAKI-- 341
Cdd:cd17631 98 --DDLALLMYTSGTTGRPKGAMLTHRNL-----LWNAVNALAALDlGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvi 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 342 --GFfqgDIRLLMDDLKALRPTVFPVVPRLLNRMFDRifGQANTTlkrwllDFASKRKeaelrsgiirnnslwdklifhk 419
Cdd:cd17631 171 lrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSSLRA---------------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 iqsslggrvklMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTVAGDW--TAGHVGAPMPCSLIKLVDvEEM 497
Cdd:cd17631 218 -----------VIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDG 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 498 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIY 577
Cdd:cd17631 285 REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVL 362
|
490 500 510
....*....|....*....|....*....|....
gi 970702926 578 LRSEPVAQVFV-------HGESlqafLIAIVVPD 604
Cdd:cd17631 363 YEHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-694 |
1.34e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 156.03 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 233 SLLEQGQKCGVEIISmkaLEDLGRANRQ--KPKPPAPEDIAVICFTSGTTGNPKGAVITHRNV------VSDCSAFVKMt 304
Cdd:PTZ00342 270 DLKEKAKKLGISIIL---FDDMTKNKTTnyKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKKY- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 305 envfiptPDDTLISFLPLAHMFERVVECTMLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFGQAN-- 382
Cdd:PTZ00342 346 -------NPKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnl 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 383 TTLKRWLLdfaskRKEAELRSGiiRNNSLWDKL---IFH---KIQSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYE 456
Cdd:PTZ00342 419 PPLKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 457 GYGQTECTAGCCLTVAGDWTAGHVGAPM-PCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGW 535
Cdd:PTZ00342 492 GYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGY 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 536 LHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDAETVGPWARKR 615
Cdd:PTZ00342 572 FKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDD 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 616 GF-------EGSFEELCRNKDVRKAILEDMVR-----LGKDSGLKSFEQVKAISLHPELFTIDNgLLTPTMKAKR----P 679
Cdd:PTZ00342 652 NMlestginEKNYLEKLTDETINNNIYVDYVKgkmleVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRfyvfK 730
|
490
....*....|....*
gi 970702926 680 DLqNYFRSQINELYS 694
Cdd:PTZ00342 731 DY-AFFIDQVKKIYK 744
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
254-643 |
1.51e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 150.92 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 254 LGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCS---AFVKMtenvfIPTPDDTLISFLPLAHMFERVV 330
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPG-----LGDGPERVLAALPMFHAYGLTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 331 ECT--MLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiIRN 408
Cdd:PRK05605 280 CLTlaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE-----------------AAEERGVDLSG--VRN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 409 NslwdklifhkiqsslggrvklmITGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLTVAGDWTAGHVGAPMP 485
Cdd:PRK05605 341 A----------------------FSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFP 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 486 CSLIKLVDVEEMNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 564
Cdd:PRK05605 397 DTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITG 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 565 GEYIAPEKIENIYLRSEPVAQVFVHG-------ESLQAfliAIVVPDAETVGP-----WARK--------RGFEgSFEEL 624
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEDAAVVGlpredgsEEVVA---AVVLEPGAALDPeglraYCREhltrykvpRRFY-HVDEL 550
|
410 420
....*....|....*....|..
gi 970702926 625 CRN---KDVRKAILEDMVRLGK 643
Cdd:PRK05605 551 PRDqlgKVRRREVREELLEKLG 572
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
246-599 |
2.06e-38 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 150.20 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 246 ISMKALEDLGRaNRQKPKPP-APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAfVKMTENVFIPTPDDTLISFLPLAH 324
Cdd:PRK08974 184 ISFRSALHKGR-RMQYVKPElVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-AKAAYGPLLHPGKELVVTALPLYH 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 325 MFERVVECTMLCHgakigffQGDIRLLMD---DLKALrptvfpvVPRLLNRMFDRIFGqANTTLKRWLldfaskrkeael 401
Cdd:PRK08974 262 IFALTVNCLLFIE-------LGGQNLLITnprDIPGF-------VKELKKYPFTAITG-VNTLFNALL------------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 402 rsgiirNNSLWDKLIFhkiqSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLTVAGdwTAG 478
Cdd:PRK08974 315 ------NNEEFQELDF----SSL----KLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 479 HVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:PRK08974 379 SIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKD 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 970702926 559 IFkLAQGEYIAPEKIENIYLRSEPVAQVF-------VHGESLQAFLIA 599
Cdd:PRK08974 457 MI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-607 |
3.35e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 149.91 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 254 LGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSD---CSAFvkMTENvfIPTPDDTLISFLPLAHMFERVV 330
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRAL--MGSN--LNEGCEILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 331 EC--TMLChgakigffqGDIRLLMDDlkalrptvfpvvPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRN 408
Cdd:PRK05677 269 HCmaMMLI---------GNHNILISN------------PRDLPAMV--------KELGKWKF------------SGFVGL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 409 NSLWDKLI----FHKIQSSlggRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPM 484
Cdd:PRK05677 308 NTLFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 485 PCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 564
Cdd:PRK05677 385 PSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVS 462
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 970702926 565 GEYIAPEKIENIYLRSEPVAQVfvhgeslqaflIAIVVPDAET 607
Cdd:PRK05677 463 GFNVYPNELEDVLAALPGVLQC-----------AAIGVPDEKS 494
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-578 |
6.45e-38 |
|
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: 148.44 E-value: 6.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 122 SYKQVEEMSECVGSGLIQKGFKAapDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVD 201
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 202 KPEKANLLldGVENKLiPGLKTIVLMDSFGSSlleQGQKCGVEIISMkalEDLGRANRQKPKPPA---PEDIAVICFTSG 278
Cdd:cd17642 124 KKGLQKVL--NVQKKL-KIIKTIIILDSKEDY---KGYQCLYTFITQ---NLPPGFNEYDFKPPSfdrDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 279 TTGNPKGAVITHRNVvsdCSAFVKMTENVFI--PTPDDTLISFLPLAHMFERVVECTMLCHGAKIGF-FQGDIRLLMDDL 355
Cdd:cd17642 195 STGLPKGVQLTHKNI---VARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 356 KALRPTVFPVVPRLLnrmfdrIFGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdklifhkiqSSLggrvKLMITGA 435
Cdd:cd17642 272 QDYKVQSALLVPTLF------AFFAKSTLVDKYDL-------------------------------SNL----HEIASGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 436 APVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPN 514
Cdd:cd17642 311 APLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPM 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970702926 515 VFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYL 578
Cdd:cd17642 391 IMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILL 453
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
115-615 |
4.25e-37 |
|
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: 145.53 E-value: 4.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 115 DQPYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVI-----IEQGCfaysmVVIPLYDTLGTEAITYI 189
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIK--KGDRVAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 190 INKAELSLVFVDKPEkanlLLDGVENKLIPGLKTIVL-MDSFGSSLLEQGQKCGVEiismkaleDLGRANRQKPKPPAPE 268
Cdd:cd05926 82 LADLGSKLVLTPKGE----LGPASRAASKLGLAILELaLDVGVLIRAPSAESLSNL--------LADKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVSDcsafVKMTENVFIPTPDDTLISFLPLAHMFERVVEC-TMLCHGAKI----GF 343
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLlSTLAAGGSVvlppRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 344 fqgDIRLLMDDLKALRPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnslwDKLIFhkIQSS 423
Cdd:cd05926 226 ---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP-----------PKLRF--IRSC 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 424 lggrvklmitgAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT--VAGDWTAGHVGAPmpcSLIKLVDV-EEMNYL 500
Cdd:cd05926 274 -----------SASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKP---VGVEVRILdEDGEIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 501 AAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRS 580
Cdd:cd05926 340 PPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSH 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 970702926 581 EPVAQ--VF-----VHGESLQAFliaiVVP------DAETVGPWARKR 615
Cdd:cd05926 419 PAVLEavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
180-576 |
4.55e-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: 145.17 E-value: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 180 TLGTEAITYIINKAELSLVFVDKP--EKANLL-------------LDGVENKLIPGLKTIVLMdsfgsslleqgqkcGVE 244
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFL--------------AGK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 245 IISMKALEDLGRANRQkpkppaPEDIAVICFTSGTTGNPKGAVITHRNVVSDcsafVKMTENVFIPTPDDTLISFLPLAH 324
Cdd:cd05909 130 FPPKWLLRIFGVAPVQ------PDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 325 MFERVVeCTM--LCHGAKIGFfqgdirllmddlkALRPTVFPVVPRLLNRMFDRIFGqANTTLKRWLLDFASKRKEAELR 402
Cdd:cd05909 200 SFGLTG-CLWlpLLSGIKVVF-------------HPNPLDYKKIPELIYDKKATILL-GTPTFLRGYARAAHPEDFSSLR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 403 sgiirnnslwdklifhkiqsslggrvkLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA-GCCLTVAGDWTAGHVG 481
Cdd:cd05909 265 ---------------------------LVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPvISVNTPQSPNKEGTVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 482 APMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 561
Cdd:cd05909 318 RPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAK 396
|
410
....*....|....*
gi 970702926 562 LAqGEYIAPEKIENI 576
Cdd:cd05909 397 IA-GEMVSLEAIEDI 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-628 |
1.08e-36 |
|
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: 140.88 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDcSAFVKMTENVfipTPDDTLISFLPLAHMFERVVEcTMLC--HGAKIGF- 343
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIGERLGL---TEQDRLCIPVPLFHCFGSVLG-VLACltHGATMVFp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 344 ---FqgDIRLLMDDLKALRPTVFPVVPRllnrMFDRIFGQAnttlKRWLLDFASkrkeaeLRSGIIrnnslwdklifhki 420
Cdd:cd05917 76 spsF--DPLAVLEAIEKEKCTALHGVPT----MFIAELEHP----DFDKFDLSS------LRTGIM-------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qsslggrvklmitGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTVAGD---WTAGHVGAPMPCSLIKLVDvEE 496
Cdd:cd05917 126 -------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHTEAKIVD-PE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 MNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:cd05917 192 GGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEE 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 576 IYLRSEPVAQVFVHGeslqafliaivVPDA---ETVGPWAR-KRGFEGSFEEL---CRNK 628
Cdd:cd05917 271 FLHTHPKVSDVQVVG-----------VPDErygEEVCAWIRlKEGAELTEEDIkayCKGK 319
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-668 |
8.60e-36 |
|
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: 140.66 E-value: 8.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 123 YKQVEEMSECVGSGLIQKGfkaapdQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDk 202
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 203 pekanllldgvenklipglktivlmdsfgsSLLEqgqKCGVEIISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTGN 282
Cdd:TIGR01923 79 ------------------------------SLLE---EKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 283 PKGAVITHRNVvsdcSAFVKMTENVFIPTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFFQGDIRLLmDDLKALRPTV 362
Cdd:TIGR01923 126 PKAVPHTFRNH----YASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 363 FPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdklifhkiqsslggrvklmitGAAPVSATV 442
Cdd:TIGR01923 201 ISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPAPL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 443 LTFLRAaLGCQFYEGYGQTE-CTAGCCLTVAGDWTAGHVGAPMPCSLIKL-VDVEEmnylaakGEGEVCVKGPNVFQGYL 520
Cdd:TIGR01923 236 IEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 521 kDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHGeslqafliai 600
Cdd:TIGR01923 308 -YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVVP---------- 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970702926 601 vVPDAEtvgpW-ARKRGFegsfeeLCRNKDVRKAILEDMV--RLGKdsglksFEQVKAISLHPELFTIDNG 668
Cdd:TIGR01923 376 -KPDAE----WgQVPVAY------IVSESDISQAKLIAYLteKLAK------YKVPIAFEKLDELPYNASG 429
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
246-599 |
6.84e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 139.96 E-value: 6.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 246 ISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSD------CSAFVKMTENVFIPTPDDTLISF 319
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 320 LPLAHMFERVVECtmLCHgakigFFQGDIRLLMDDlkalrptvfpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkea 399
Cdd:PRK12492 265 LPLYHIYAFTANC--MCM-----MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 400 elrSGIIRNNSLWDKLIFHKIQSSLG-GRVKLMITGA-APVSATVLTFlRAALGCQFYEGYGQTECTAGCCLTVAGDWTA 477
Cdd:PRK12492 309 ---SALLGLNTLFVALMDHPGFKDLDfSALKLTNSGGtALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELAR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 478 -GHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK12492 385 lGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRK 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 970702926 557 KHIFkLAQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFLIA 599
Cdd:PRK12492 464 KDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-615 |
1.17e-34 |
|
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: 134.55 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVSdcsAFVKMTENVFIpTPDDTLISFLPLAHMFERVVECTM-LCHGAKI---GFF 344
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR---AAAAWADCADL-TEDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 qgDIRLLMDDLKALRPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdklifhkiqSSL 424
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 ggrvKLMITGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLTVAGDWT--AGHVGAPMPCSLIKLVDveemnyla 501
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVATMCRPGDDAEtvATTCGRACPGFEVRIAD-------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 502 akgEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 581
Cdd:cd17638 186 ---DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHP 261
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 970702926 582 PVAQVFV-------HGESLQAFLIA--IVVPDAETVGPWARKR 615
Cdd:cd17638 262 GVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-590 |
5.50e-34 |
|
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: 136.61 E-value: 5.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 111 SRKPDQPYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYII 190
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVK--PGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 191 NKAELSLVFVDkpekANL--LLDGVENKLiPGLKTIVLMDSFGSSLLEQGqkcgVEIISMKALedLGRANRQKPKPPAPE 268
Cdd:cd12119 94 NHAEDRVVFVD----RDFlpLLEAIAPRL-PTVEHVVVMTDDAAMPEPAG----VGVLAYEEL--LAAESPEYDWPDFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 -DIAVICFTSGTTGNPKGAVITHRNVVSDCSAfvkmtenvfIPTPDDTLIS----FLPLAHMFErvVE-------CTMLc 336
Cdd:cd12119 163 nTAAAICYTSGTTGNPKGVVYSHRSLVLHAMA---------ALLTDGLGLSesdvVLPVVPMFH--VNawglpyaAAMV- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 337 hGAKI----GFFQGDirLLMDDLKALRPTVFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRKeaelrsgiirnnslw 412
Cdd:cd12119 231 -GAKLvlpgPYLDPA--SLAELIEREGVTFAAGVPTVWQGLLDH--------LEANGRDLSSLRR--------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 413 dklifhkiqsslggrvkLMITGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLTVAGDWTAGHV----------G 481
Cdd:cd12119 285 -----------------VVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 482 APMPCSLIKLVDvEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEvLDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd12119 346 RPVPGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDV 423
|
490 500 510
....*....|....*....|....*....|.
gi 970702926 560 FKLAqGEYIAPEKIENIYLRSEPVAQVFVHG 590
Cdd:cd12119 424 IKSG-GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
254-613 |
8.49e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 136.55 E-value: 8.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 254 LGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSD---CSAFVKMTENvfIPTPDDTLISFLPLAHMFE--- 327
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGK--LEEGCEVVITALPLYHIFAlta 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 328 ------RVVECTMLCHGAKigffqgDIRLLMDDLKALRPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeael 401
Cdd:PRK08751 272 nglvfmKIGGCNHLISNPR------DMPGFVKELKKTRFTAFTGVNTLFNGLL--------------------------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 402 rsgiirNNSLWDKLIFHKIQSSLGGrvklmitGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT-VAGDWTAGHV 480
Cdd:PRK08751 319 ------NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 481 GAPMPCSLIKLVDveEMNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK08751 385 GLPIPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDM 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970702926 560 FkLAQGEYIAPEKIENIYLRSEPVAQVFVHG----ESLQAFLIAIVVPD----AETVGPWAR 613
Cdd:PRK08751 463 I-LVSGFNVYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDpaltAEDVKAHAR 523
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
255-598 |
1.90e-33 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 135.53 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 255 GRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDC--------SAFVKmtenvfiPTPDDTLISF--LPLAH 324
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYH 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 325 MFERVVeCTMLchGAKIGffqG---------DIRLLMDDLKALRPTVFPVVPRLLNRMFdrifgqanttlkrwlldfask 395
Cdd:PRK07059 264 IFALTV-CGLL--GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 396 rkeaelrsgiirNNSLWDKLIFHKIQSSLGGrvklmitGAApVSATVLTFLRAALGCQFYEGYG--QTECTAGCCLTVAG 473
Cdd:PRK07059 317 ------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDAT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 474 DWTaGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PRK07059 377 EFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIV 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 970702926 554 DRKKHIFkLAQGEYIAPEKIENIyLRSEP----VAQVFVH----GESLQAFLI 598
Cdd:PRK07059 455 DRKKDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-615 |
2.69e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 132.80 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVkmteNVFIPTPDDTLISFLPLAHMFERVVECT-MLCHGAKI------ 341
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSA----RRFGLGEDDVYLTVLPLFHINAQAVSVLaALSVGATLvllprf 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 342 --GFFQGDIRllmddlkALRPTVF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdkli 416
Cdd:cd05934 158 saSRFWSDVR-------RYGATVTnylGAMLSYLLAQPPSPDDRAH---------------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 417 fhkiqsslggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTVAGDWTA--GHVGAPMPCSLIKLVDv 494
Cdd:cd05934 197 ------------RLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTE--TIVGVIGPRDEPRrpGSIGRPAPGYEVRIVD- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 495 EEMNYLAAKGEGEVCVK---GPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPE 571
Cdd:cd05934 262 DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSA 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 970702926 572 KIENIYLRSEPVAQVFVHG----ESLQAFLIAIVVPDAETVGP-----WARKR 615
Cdd:cd05934 340 EVERAILRHPAVREAAVVAvpdeVGEDEVKAVVVLRPGETLDPeelfaFCEGQ 392
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-628 |
8.67e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 133.78 E-value: 8.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 114 PDQPYEWlSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEqgcFAYS-----MVVI-PLYDTlgtEAIT 187
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIE--KGDRVGIWAPNVPEWVLTQ---FATAkigaiLVTInPAYRL---SELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 188 YIINKAELS-LVFVDK--------------PEKANLLLDGVENKLIPGLKTIVLMDsfgsslleQGQKCGveIISMKALE 252
Cdd:PRK08315 109 YALNQSGCKaLIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLG--------DEKHPG--MLNFDELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 253 DLGRAnRQKPKPPA------PEDIAVICFTSGTTGNPKGAVITHRNVVSDcSAFVKMTENVfipTPDDTLISFLPLAHMF 326
Cdd:PRK08315 179 ALGRA-VDDAELAArqatldPDDPINIQYTSGTTGFPKGATLTHRNILNN-GYFIGEAMKL---TEEDRLCIPVPLYHCF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 327 ErVVECTMLC--HGAKI-----GFfqgdirllmDDLKALR-------------PTVFpvVPRLLNRMFDRifgqanttlk 386
Cdd:PRK08315 254 G-MVLGNLACvtHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR---------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 387 rwlLDFASkrkeaeLRSGIirnnslwdklifhkiqssLGG---------RV-KLM----ITGAapvsatvltflraalgc 452
Cdd:PRK08315 312 ---FDLSS------LRTGI------------------MAGspcpievmkRViDKMhmseVTIA----------------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 453 qfyegYGQTECTAGCCLTVAGD------WTaghVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKT 526
Cdd:PRK08315 348 -----YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKT 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 527 AEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHGeslqafliaivVPDA- 605
Cdd:PRK08315 420 AEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDEk 487
|
570 580
....*....|....*....|....*....
gi 970702926 606 --ETVGPWARKR-GFEGSFEEL---CRNK 628
Cdd:PRK08315 488 ygEEVCAWIILRpGATLTEEDVrdfCRGK 516
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
266-608 |
2.14e-32 |
|
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: 130.73 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVSdcsaFVKMTENVFIPTPDDTLISFLPLAH-MFerVVE-CTMLCHGAKI-- 341
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvv 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 342 --GFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdklifhk 419
Cdd:cd05930 165 lpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLV----------------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 iqsslggrvklmitGAAPVSATVLT-FLRAALGCQFYEGYGQTECTAGCCLTV--AGDWTAGHV--GAPMPCSLIKLVDv 494
Cdd:cd05930 216 --------------GGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYRvpPDDEEDGRVpiGRPIPNTRVYVLD- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 495 EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEV-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 568
Cdd:cd05930 281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRI 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 970702926 569 APEKIENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDAETV 608
Cdd:cd05930 360 ELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGE 402
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-628 |
3.84e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 131.82 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEqgcFAYSMV------VIPLYDTlgtEAITYIINKAE 194
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQ--PGDRVGIWAPNCAEWLLTQ---FATARIgailvnINPAYRA---SELEYALGQSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 195 LSLVFVDK---------------PEKANLLLDGVENKLIPGLKTIVLMD---SFGSSLLEQGQKCGvEIISMKALEDLGR 256
Cdd:PRK12583 118 VRWVICADafktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLApapPPGFLAWHELQARG-ETVSREALAERQA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 257 ANRqkpkppaPEDIAVICFTSGTTGNPKGAVITHRNVVSDcSAFVKMTENVfipTPDDTLISFLPLAHMFERVVeCTMLC 336
Cdd:PRK12583 197 SLD-------RDDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVAESLGL---TEHDRLCVPVPLYHCFGMVL-ANLGC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 337 --HGAKIgFFQGDirlLMDDLKALR-------------PTVFpvVPRLLNRMFDRifgqanttlkrwlLDFASkrkeaeL 401
Cdd:PRK12583 265 mtVGACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS------L 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 402 RSGIIrnnslwdklifhkiqsslggrvklmitGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTVAGD---WTA 477
Cdd:PRK12583 320 RTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 478 GHVGAPMPCSLIKLVDVEemNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK12583 373 ETVGRTQPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRS 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970702926 557 KHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHGeslqafliaivVPD---AETVGPWARKR-GFEGSFEEL---CRNK 628
Cdd:PRK12583 451 KDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDekyGEEIVAWVRLHpGHAASEEELrefCKAR 517
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
265-606 |
8.78e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 129.34 E-value: 8.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 265 PAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFvkmtENVFIPTPDDTLISFLPLAHMfervvectmlcHGAKIGFF 344
Cdd:PRK07787 125 PDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL----AEAWQWTADDVLVHGLPLFHV-----------HGLVLGVL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 qGDIRLLMDDLKALRPTVFPVVPRLLNR--MFdriFGqANTTLKRWLLDFASKRkeaelrsgiirnnslwdklifhkiqs 422
Cdd:PRK07787 190 -GPLRIGNRFVHTGRPTPEAYAQALSEGgtLY---FG-VPTVWSRIAADPEAAR-------------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 423 SLGGrVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAA 502
Cdd:PRK07787 239 ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPH 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 503 KGE--GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLAQGEyiapekIE 574
Cdd:PRK07787 317 DGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------IE 390
|
330 340 350
....*....|....*....|....*....|....*
gi 970702926 575 NIYLRSEPVAQVFVHGE---SLQAFLIAIVVPDAE 606
Cdd:PRK07787 391 TALLGHPGVREAAVVGVpddDLGQRIVAYVVGADD 425
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
266-574 |
1.72e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 129.33 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVK-MTENVFIpTPDDTLISFLPLAHMFErvVECTMLCH---GAKI 341
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLYF-HSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 342 GFFQG-DIRLLMDDLKALRPTVFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdklifhki 420
Cdd:PLN02246 254 LIMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL--------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qSSlggrVKLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAG----CCLTVAGDWTAGHVGApmpCSLI------ 489
Cdd:PLN02246 298 -SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGpvlaMCLAFAKEPFPVKSGS---CGTVvrnael 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 490 KLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:PLN02246 368 KIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVA 446
|
....*
gi 970702926 570 PEKIE 574
Cdd:PLN02246 447 PAELE 451
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
220-588 |
7.19e-31 |
|
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: 125.46 E-value: 7.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 220 GLKTIVLMDSFGSSLLEQGQKCGVEIISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSA 299
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 300 FVKMtenvFIPTPDDTLISFLPLAH------MFervvecTMLCHGAK--------IGFFQGDIRLLMDDLKAlrpTVFPV 365
Cdd:TIGR01733 152 LARR----YGLDPDDRVLQFASLSFdasveeIF------GALLAGATlvvppedeERDDAALLAALIAEHPV---TVLNL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 366 VPRLLNRMfdrifgqanttlkrwlldfaskrkEAELRSGIirnnslwdklifhkiqsslgGRVKLMITGA-APVSATVLT 444
Cdd:TIGR01733 219 TPSLLALL------------------------AAALPPAL--------------------ASLRLVILGGeALTPALVDR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 445 FLRAALGCQFYEGYGQTECTAGC-CLTVAGDWTAGHV----GAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGY 519
Cdd:TIGR01733 255 WRARGPGARLINLYGPTETTVWStATLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGY 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970702926 520 LKDPAKTAEVL--------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFV 588
Cdd:TIGR01733 334 LNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-637 |
1.34e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.14 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLyDTLGTEA-ITYIINKAELSLVF 199
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVK--PGDRVAVQVEKSPEALALYLATLRAGAVFLPL-NTAYTLAeLDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 200 VDkPEKANLLLDGVENKLIPGLKTivlMDSFGS-SLLEQGQKCGveiismKALEDLGRAnrqkpkppaPEDIAVICFTSG 278
Cdd:PRK07514 106 CD-PANFAWLSKIAAAAGAPHVET---LDADGTgSLLEAAAAAP------DDFETVPRG---------ADDLAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 279 TTGNPKGAVITHRNVVS------DCSAFvkmtenvfipTPDDTLISFLPLAH---MFerVVECTMLCHGAKIGFFQgdiR 349
Cdd:PRK07514 167 TTGRSKGAMLSHGNLLSnaltlvDYWRF----------TPDDVLIHALPIFHthgLF--VATNVALLAGASMIFLP---K 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 350 LLMDDLKALRP--TVFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdklifhkiqs 422
Cdd:PRK07514 232 FDPDAVLALMPraTVMMGVPtfytRLLqEPRLTR---------------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 423 SLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctaGCCLT---VAGDWTAGHVGAPMPCSLIKLVDVEEMNY 499
Cdd:PRK07514 266 EAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMNTsnpYDGERRAGTVGFPLPGVSLRVTDPETGAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 500 LAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIfkLAQGEY-IAPEKIENiYL 578
Cdd:PRK07514 343 LPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EI 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 579 RSEP-VAQVFV----H---GESlqafLIAIVVP------DAETV-----GPWAR----KRGFegsF-EELCRN---KdVR 631
Cdd:PRK07514 420 DELPgVVESAVigvpHpdfGEG----VTAVVVPkpgaalDEAAIlaalkGRLARfkqpKRVF---FvDELPRNtmgK-VQ 491
|
....*.
gi 970702926 632 KAILED 637
Cdd:PRK07514 492 KNLLRE 497
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-609 |
2.26e-30 |
|
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: 125.10 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 119 EWLSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 199 FVDkpekanlllDGVENKLIPGLKTIvlmdsfgsslleqgqkcgveiisMKALEDLGRANRQKPKPPAPEDIAVICFTSG 278
Cdd:cd12116 89 LTD---------DALPDRLPAGLPVL-----------------------LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 279 TTGNPKGAVITHRNVVSdcsAFVKMTENvFIPTPDDTLISFLPLAhmFE-RVVECTM-LCHGAKIGFFQGDI----RLLM 352
Cdd:cd12116 137 STGRPKGVVVSHRNLVN---FLHSMRER-LGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 353 DDLKALRPTVFpvvprllnrmfdrifgQANTTLKRWLLDfASKRKEAELRsgiirnnslwdklifhkiqsslggrvklMI 432
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-AGWQGRAGLT----------------------------AL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 433 TGAAPVSATVLTFLrAALGCQFYEGYGQTECTA-GCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVK 511
Cdd:cd12116 246 CGGEALPPDLAARL-LSRVGSLWNLYGPTETTIwSTAARVTAAAGPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 512 GPNVFQGYLKDPAKTAEVLDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVA 584
Cdd:cd12116 324 GDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVA 402
|
490 500
....*....|....*....|....*..
gi 970702926 585 Q--VFVHGESLQAFLIAIVVPDAETVG 609
Cdd:cd12116 403 QaaVVVREDGGDRRLVAYVVLKAGAAP 429
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-610 |
3.92e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 125.63 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 113 KPDQPYEWlSYKQVEEMSECVGSGLIQKGFKAApdqfiGIFAQNRPEW---VIIEQGCFAYSMVVIPLYDTLGTEAITYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 190 INKAELSLVFVDKPEKAN---LLLDGVENKLiPGLKTIVLMDSFGSSLLEQGQKcgvEIISmkALEDLgranrQKPKPPA 266
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQTrpvDLILPLQNQL-PQLQQIVGVDKLAPATSSLSLS---QIIA--DYEPL-----TTAITTH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAHmfervveCTMLCHGAKIGFFQG 346
Cdd:PRK06087 186 GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN----LTWQDVFMMPAPLGH-------ATGFLHGVTAPFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 DIRLLMDDLKALRPTvfpvvpRLLNRmfDRIFGQANTTlkRWLLDFASKRKEAELRSgiirnnslwdklifhkiqSSLgg 426
Cdd:PRK06087 255 ARSVLLDIFTPDACL------ALLEQ--QRCTCMLGAT--PFIYDLLNLLEKQPADL------------------SAL-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 427 rvKLMITGAAPVSATVLtflRAAL--GCQFYEGYGQTECTA------GCCLtvagDWTAGHVGAPMPCSLIKLVDvEEMN 498
Cdd:PRK06087 305 --RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPhavvnlDDPL----SRFMHTDGYAAAGVEIKVVD-EARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 499 YLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYL 578
Cdd:PRK06087 375 TLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
490 500 510
....*....|....*....|....*....|....*
gi 970702926 579 RSEPVAQVFVHG---ESLQAFLIAIVVPDAETVGP 610
Cdd:PRK06087 454 QHPKIHDACVVAmpdERLGERSCAYVVLKAPHHSL 488
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
184-584 |
6.29e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 125.45 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 184 EAITYIINKAELSLVFVDKPE-------KANLLLDGVenkliPGLKTIVLMDS-------FGSSLLEQGQKCGVEIISMK 249
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVDLarylpgpKRLAVPLIRRKAHARILDFD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 250 ALEDLGRANR-QKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAfvkMTENVFIpTPDDTLISFLPLAHMFER 328
Cdd:PRK07529 194 AELARQPGDRlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWL---GALLLGL-GPGDTVFCGLPLFHVNAL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 329 VVEC-TMLCHGAKIGF-----FQGDirLLMDDLKAL----RPTVFPVVPRLLNRMFDRIFGQANTtlkrwlldfaskrke 398
Cdd:PRK07529 270 LVTGlAPLARGAHVVLatpqgYRGP--GVIANFWKIveryRINFLSGVPTVYAALLQVPVDGHDI--------------- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 399 aelrsgiirnnslwdklifhkiqSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT-VAGDWTA 477
Cdd:PRK07529 333 -----------------------SSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNpPDGERRI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 478 GHVGAPMPCSLIKLVDVEEM-NYL--AAKGE-GEVCVKGPNVFQGYLkDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PRK07529 386 GSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLT 464
|
410 420 430
....*....|....*....|....*....|.
gi 970702926 554 DRKKHIFkLAQGEYIAPEKIENIYLRSEPVA 584
Cdd:PRK07529 465 GRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-626 |
1.30e-29 |
|
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: 122.49 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELslvfv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVG--PGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 dkpekanllldgvenklipglKTIVLMDSFgsslleqgqkcgveiismkaledlgranRQKPKPPAPEDIAVICFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERF----------------------------RQFDPAAMPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 281 GNPKGAVITHRNVVSDCSAFVkmtENVFIPTPDDTLISfLPLAHMfervvecTMLCHGAKIGFFQGDIRLLMDDLKALRp 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYA---ERLGLGPGDVFLVA-SPMAHQ-------TGFVYGFTLPLLLGAPVVLQDIWDPDK- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 361 tvfpvVPRLLNRmfDRI-FGQANTTLKRWLLDfASKRKEAELRsgiirnnslwdklifhkiqsslggRVKLMITGAAPVS 439
Cdd:cd05903 174 -----ALALMRE--HGVtFMMGATPFLTDLLN-AVEEAGEPLS------------------------RLRTFVCGGATVP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 440 ATVLTFLRAALGCQFYEGYGQTEC-TAGCCLTVAGDWTAGHV-GAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQ 517
Cdd:cd05903 222 RSLARRAAELLGAKVCSAYGSTECpGAVTSITPAPEDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 518 GYLKDPAKTAEVLDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG---ESLQ 594
Cdd:cd05903 301 GYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLG 378
|
490 500 510
....*....|....*....|....*....|..
gi 970702926 595 AFLIAIVVPdaetvgpwarKRGFEGSFEELCR 626
Cdd:cd05903 379 ERACAVVVT----------KSGALLTFDELVA 400
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
268-591 |
1.49e-29 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 121.68 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 268 EDIAVICFTSGTTGNPKGAVITHRNVVSdcSAfVKMTENVFIpTPDDTLISFLPLAH------MFERVVE-CTMLCHGAk 340
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWW--SA-IGSALNLGL-TEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 341 igfFqgDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdklifhki 420
Cdd:cd05912 152 ---F--DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILL------------------------------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qsslggrvklmitGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCCLTVAGDWTA---GHVGAPMPCSLIKLVDVEEm 497
Cdd:cd05912 197 -------------GGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIEDDGQ- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 498 nylAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:cd05912 261 ---PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
330
....*....|....
gi 970702926 578 LRSEPVAQVFVHGE 591
Cdd:cd05912 336 LSHPAIKEAGVVGI 349
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
111-607 |
1.64e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 123.17 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 111 SRKPDQP-YEW----LSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPE-WVIIEQGCFAySMVVIPLYdTLGTE 184
Cdd:PRK06188 23 KRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALG--LGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALH-PLGSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 185 AI-TYIINKAELSLVFVDK---PEKANLLLDGVenkliPGLKTIVLMDSF--GSSLLEQGQKCGVeiismKALEDlgran 258
Cdd:PRK06188 99 DDhAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPVpdGVDLLAAAAKFGP-----APLVA----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 259 rqkpkPPAPEDIAVICFTSGTTGNPKGAVITHRNVVsdcsafvkmTENVFIPT----PDDtlISFL---PLAHMFERVVE 331
Cdd:PRK06188 164 -----AALPPDIAGLAYTGGTTGKPKGVMGTHRSIA---------TMAQIQLAewewPAD--PRFLmctPLSHAGGAFFL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 332 CTMLCHGAKI---GFfqgDIRLLMDDLKALRPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFASKRKeAELrsgiirn 408
Cdd:PRK06188 228 PTLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDL------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 409 nslwdklifhkiqSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECtaGCCLTV--AGDWTAGHV------ 480
Cdd:PRK06188 281 -------------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEA--PMVITYlrKRDHDPDDPkrltsc 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 481 GAPMPCSLIKLVDvEEMNYLAAkGE-GEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK06188 342 GRPTPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDM 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 970702926 560 FkLAQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQafliAIVVPDAET 607
Cdd:PRK06188 419 I-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVLRPGA 468
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
114-557 |
1.65e-29 |
|
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: 123.55 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 114 PDQPYEWLSYKQVEEMSECVGSGLIQKGFKAaPDQFIGIFAQNRpEWVIIEQGCFAYSMVVIPLydtlgTEAITY-IINK 192
Cdd:cd05906 33 ADGSEEFQSYQDLLEDARRLAAGLRQLGLRP-GDSVILQFDDNE-DFIPAFWACVLAGFVPAPL-----TVPPTYdEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 193 AELSLvfvdkpEKANLLLDgvenklipglKTIVLMDSFG-SSLLEQGQKCGVEIISMKALEDLGRANRQKPKPPA-PEDI 270
Cdd:cd05906 106 RLRKL------RHIWQLLG----------SPVVLTDAELvAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSrPDDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 271 AVICFTSGTTGNPKGAVITHRNVVSDCSAfvKMTENVFipTPDDTLISFLPLAHmferVVECTMlCHGAkigffqgDIRL 350
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGL--TPQDVFLNWVPLDH----VGGLVE-LHLR-------AVYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 351 LMDDLKALRPTVFPVVPRLLnRMFDRIfgQANTTlkrWLLDFA-SKRKEAELRsgiiRNNSLWDklifhkiQSSLggrvK 429
Cdd:cd05906 234 GCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDLLEE----IEDGTWD-------LSSL----R 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 430 LMITGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGCCLTV---AGDWTAGH----VGAPMPCSLIKLVDvEE 496
Cdd:cd05906 293 YLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGVIYSRsfpTYDHSQALefvsLGRPIPGVSMRIVD-DE 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970702926 497 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGkWLPNGTLKIIDRKK 557
Cdd:cd05906 372 GQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
220-588 |
3.60e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 122.40 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 220 GLKTIVLMDSFGSS------LLEQGQKCGVEIISMKALEdlgranrqkpkppapEDIAVICFTSGTTGNPKGAVITHRNV 293
Cdd:PLN02330 145 GLPVIVLGEEKIEGavnwkeLLEAADRAGDTSDNEEILQ---------------TDLCALPFSSGTTGISKGVMLTHRNL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 294 VSD-CSAFV----KMTENVfiptpddTLISFLPLAHMFERVVEC--TMLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVV 366
Cdd:PLN02330 210 VANlCSSLFsvgpEMIGQV-------VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSRFELRTFLNALITQEVSFAPIV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 367 PRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDKLIFHKIqsslggRVKLMITGAAPVSATVLTFL 446
Cdd:PLN02330 283 PPIILNLV---------------------------------KNPIVEEFDLSKL------KLQAIMTAAAPLAPELLTAF 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 447 RAAL-GCQFYEGYGQTECTagcCLTVA-GDWTAGH-------VGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQ 517
Cdd:PLN02330 324 EAKFpGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQ 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970702926 518 GYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFV 588
Cdd:PLN02330 401 GYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
264-608 |
8.82e-29 |
|
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: 119.72 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPEDIAVICFTSGTTGNPKGAVITHRNVVSdcsaFVKMTENVFIPTPDDTLISFLPLA------HMFervvecTMLCH 337
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIAfdacigEIF------STLCN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 338 GAKIgFFQGDIRLLMDDLKALrpTVFPVVPRLLnrmfdrifgqanTTLKRWLLDfaskrkeaelrsgiirnnslwdklif 417
Cdd:cd17653 171 GGTL-VLADPSDPFAHVARTV--DALMSTPSIL------------STLSPQDFP-------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 418 hkiqsslggRVKLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEM 497
Cdd:cd17653 210 ---------NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 498 NYLAAKgEGEVCVKGPNVFQGYLKDPAKTAE----VLDKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:cd17653 279 PVPEGV-VGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLE 356
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 970702926 572 KIENIYLRSEPVAQ---VFVHGEslqaFLIAIVVPdaETV 608
Cdd:cd17653 357 EIEEVVLQSQPEVTqaaAIVVNG----RLVAFVTP--ETV 390
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
2.16e-28 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 122.27 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 89 VTTLYEGFQRGMRVSNNGACLGSRKPDQPYEWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCF 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVR--PGDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 169 AYSMVVIPLYDTLGTeaITYIINKAELSLVFVDKPEKANLLLDGVENklipgLKTIVLMDSFGSSLLEQGQK-CGVEIIS 247
Cdd:PTZ00297 504 LYGFTTLPLVGKGST--MRTLIDEHKIKVVFADRNSVAAILTCRSRK-----LETVVYTHSFYDEDDHAVARdLNITLIP 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 248 MKALEDLGRAnRQKPKPPAPEDIAVICFTSGTT-----GNPKGAVITHRNVVSDCSAFVkMTENVFIPTPDDTLISFLPL 322
Cdd:PTZ00297 577 YEFVEQKGRL-CPVPLKEHVTTDTVFTYVVDNTtsasgDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVHFTPF 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 323 AHMFERVVECTMLCHGAKIGffQGDIRLLMDDLKALRPTVFPVVPRLlnrmfdriFGQANTTLKR----------WLLDf 392
Cdd:PTZ00297 655 AMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 393 askrKEAELRSGII----RNNSLWDKLIFHKIQSSLGGRVKLMITGAAPVSATvltflraalgcqfyegYGQTECTAGCC 468
Cdd:PTZ00297 724 ----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTS----------------FSLLEHISVCY 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 469 ltvagdwtaghvgapMPCsliklvdVEEMNYLAAkgEGEVCVKG---PNVfQGYLK---DPAKTAE----VLDKDGWL-H 537
Cdd:PTZ00297 784 ---------------VPC-------LREVFFLPS--EGVFCVDGtpaPSL-QVDLEpfdEPSDGAGigqlVLAKKGEPrR 838
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 538 TGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAfLIAIVVPDAETVG-PWARKR 615
Cdd:PTZ00297 839 TLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSH 917
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 616 GFE---GSFEELCRNKDVRKA---ILEDMVRLGKDSGLKSFEQVKAISLHPELFTIDNGLLTPTMKAKRPDLQNYFRSQI 689
Cdd:PTZ00297 918 CMGeggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVI 997
|
....*
gi 970702926 690 NELYS 694
Cdd:PTZ00297 998 ERFYS 1002
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
180-605 |
2.23e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 121.95 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 180 TLGTEAITYIINKAELSLV-----FVDKpekanLLLDGVENKLIPGLKTIVLMDsfgssLLEQGQKcgVEIISMKALED- 253
Cdd:PRK08633 698 TASEAALKSAIEQAQIKTVitsrkFLEK-----LKNKGFDLELPENVKVIYLED-----LKAKISK--VDKLTALLAARl 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 254 -----LGRANRQKPKPpapEDIAVICFTSGTTGNPKGAVITHRNVVSDcsafVKMTENVFIPTPDDTLISFLPLAHMFER 328
Cdd:PRK08633 766 lparlLKRLYGPTFKP---DDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSFGL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 329 VVE--------CTMLCH-----GAKIGffqgdirllmddlKALR----------PTVFpvvprllnRMFDRifgqaNTTL 385
Cdd:PRK08633 839 TVTlwlpllegIKVVYHpdptdALGIA-------------KLVAkhratillgtPTFL--------RLYLR-----NKKL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 386 KRwlLDFASKRkeaelrsgiirnnslwdklifhkiqsslggrvkLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA 465
Cdd:PRK08633 893 HP--LMFASLR---------------------------------LVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSP 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 466 GCCLTV-----AGDWT-----AGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVL---DK 532
Cdd:PRK08633 938 VASVNLpdvlaADFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDG 1017
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970702926 533 DGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniylrsEPVAQVFvHGESLQafLIAIVVPDA 605
Cdd:PRK08633 1018 IGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPDE 1080
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-606 |
4.08e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 118.88 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLK--KGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DkPEKANLLLDGVENKlipGLKTIVLMDSFGSSLLEQGqkcgveiisMKALEDLGRANRQKPKPPAP--EDIAVICFTSG 278
Cdd:PRK08316 115 D-PALAPTAEAALALL---PVDTLILSLVLGGREAPGG---------WLDFADWAEAGSVAEPDVELadDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 279 TTGNPKGAVITHRNVVSD---CSAFVKMTenvfiptPDDTLISFLPLAHMFER-VVECTMLCHGAKIGFFQG-DIRLLMD 353
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEyvsCIVAGDMS-------ADDIPLHALPLYHCAQLdVFLGPYLYVGATNVILDApDPELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 354 DLKALRPTVF---PVV-PRLLNR-MFDRIfgqanttlkrwllDFASKRKeaelrsgiirnnslwdklIFHkiqsslggrv 428
Cdd:PRK08316 255 TIEAERITSFfapPTVwISLLRHpDFDTR-------------DLSSLRK------------------GYY---------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 429 klmitGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTVAG-DWTAGHVG-APMPCSLI--KLVDvEEMNYLAAK 503
Cdd:PRK08316 294 -----GASIMPVEVLKELRERLpGLRFYNCYGQTE--IAPLATVLGpEEHLRRPGsAGRPVLNVetRVVD-DDGNDVAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 504 GEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPV 583
Cdd:PRK08316 366 EVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAV 443
|
490 500
....*....|....*....|....*..
gi 970702926 584 AQVFV----HGESLQAfLIAIVVPDAE 606
Cdd:PRK08316 444 AEVAViglpDPKWIEA-VTAVVVPKAG 469
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-582 |
1.16e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 118.02 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 262 PKPP-APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVF-IPTPDDTLISFLPLAHMFERVVECT-MLCHG 338
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYeYPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 339 AKI----GFFQGDIRLLMDDLKAlrpTVFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwdk 414
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 415 lifhkiqsSLggrvKLMITGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTAgccLTVAGDWTA-----GHVGAPMPCSL 488
Cdd:PLN02574 320 --------SL----KQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTA---VGTRGFNTEklskySSVGLLAPNMQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 489 IKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:PLN02574 385 AKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQI 463
|
330
....*....|....
gi 970702926 569 APEKIENIyLRSEP 582
Cdd:PLN02574 464 APADLEAV-LISHP 476
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
108-671 |
1.55e-27 |
|
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: 117.53 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 108 CLGSRKPDQPYEWLSYKQVEEMSECVGSGLIQKGFKAapDQFIGIFAQNRPEWVIIEQGCF---AYSMVVIPLYDTLGTE 184
Cdd:cd05921 13 WLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 185 --AITYIINKAELSLVFVDKPEK-----ANLLLDGVE----NKLIPGLKTIvlmdSFgSSLLEQgqkcgveiismKALED 253
Cdd:cd05921 91 laKLKHLFELLKPGLVFAQDAAPfaralAAIFPLGTPlvvsRNAVAGRGAI----SF-AELAAT-----------PPTAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 254 LGRANRQKpkppAPEDIAVICFTSGTTGNPKGAVITHRNVvsdCSAFVKMTENVFIPTPDD-TLISFLPLAHMFervvec 332
Cdd:cd05921 155 VDAAFAAV----GPDTVAKFLFTSGSTGLPKAVINTQRML---CANQAMLEQTYPFFGEEPpVLVDWLPWNHTF------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 333 tmlchGAKIGF-----------------FQGDIRLLMDDLKALRPTVFPVVPrllnrmfdrifgqanttlKRWLLDFASK 395
Cdd:cd05921 222 -----GGNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVP------------------AGWEMLVAAL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 396 RKEAELRSGIIRnnslwdklifhkiqsslggRVKLMITGAAPVSATVLTFLRAaLGCQ-------FYEGYGQTECTAGCC 468
Cdd:cd05921 279 EKDEALRRRFFK-------------------RLKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATETAPTAT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 469 LTVAGDWTAGHVGAPMPCSLIKLVDVEemnylaakGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWL--- 545
Cdd:cd05921 339 FTHWPTERSGLIGLPAPGTELKLVPSG--------GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpd 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 546 -PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYLRSEPVAQVFVHGESlQAFLIAIVVPDAETVGpwARKRGFEGSFE 622
Cdd:cd05921 411 dPAKGLVFDGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACR--RLVGLQEASDA 487
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 970702926 623 ELCRNKDVRKAILEDMVRLGKDSGLKSFEQVKAISLHpELFTIDNGLLT 671
Cdd:cd05921 488 EVLRHAKVRAAFRDRLAALNGEATGSSSRIARALLLD-EPPSIDKGEIT 535
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
267-646 |
1.93e-27 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 117.67 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVS------DCSAFVKMTENVfiptpddtLISFLPLAHMFERVVECTM-LCHGA 339
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPPV--------LVDWLPWNHTFGGNHNLGIvLYNGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 340 KI---------GFFQGDIRllmdDLKALRPTVFPVVPR----LLNRMfdrifgqanttlkrwlldfaskRKEAELRSgii 406
Cdd:PRK08180 280 TLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemLVPAL----------------------ERDAALRR--- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 407 rnnslwdklifhkiqsSLGGRVKLMITGAAPVSATVLTFL----RAALGCQ--FYEGYGQTEcTAGCCLTVAGDWT-AGH 479
Cdd:PRK08180 331 ----------------RFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGLGMTE-TAPSATFTTGPLSrAGN 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 480 VGAPMPCSLIKLVDVEemnylaakGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWL----PNGTLKIIDR 555
Cdd:PRK08180 394 IGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGR 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 556 KKHIFKLAQGEYIA--PekieniyLRSE------PVAQ-VFVHGESlQAFLIAIVVPDAetvgPWARKR---GFEGSFEE 623
Cdd:PRK08180 466 IAEDFKLSSGTWVSvgP-------LRARavsagaPLVQdVVITGHD-RDEIGLLVFPNL----DACRRLaglLADASLAE 533
|
410 420
....*....|....*....|...
gi 970702926 624 LCRNKDVRKAILEDMVRLGKDSG 646
Cdd:PRK08180 534 VLAHPAVRAAFRERLARLNAQAT 556
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
264-598 |
2.11e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 117.44 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPE-DIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVfiPTPDDTLISFLPLAHMFERVVECTM-LCHGAKI 341
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNC--KEGEEVVLGVLPFFHVYGMTAVMNLsIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 342 GFF-QGDIRLLMDDLKALRPTVFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdklifhki 420
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qsslggrVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAgdW---TAGHVGAPMPCSLIKLVDVEEM 497
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFL--WekrVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 498 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 970702926 578 LRSEPVAQVFV-------HGESLQAFLI 598
Cdd:PRK06710 474 YEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-624 |
4.35e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 116.36 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVK--KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DK---------PEKANLllDGVENKLiPGLKTIVLMDSFGSSLLEQGQKcgveiismkALEDL--GRANRQKPKPPAPED 269
Cdd:COG0365 118 ADgglrggkviDLKEKV--DEALEEL-PSLEHVIVVGRTGADVPMEGDL---------DWDELlaAASAEFEPEPTDADD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 270 IAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKmteNVFIPTPDDTL--------------ISFLPLAHmfervvECTML 335
Cdd:COG0365 186 PLFILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVFwctadigwatghsyIVYGPLLN------GATVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 336 CHGAKIGFFQGDIrlLMDDLKALRPTVFPVVPRLLnRMfdrifgqanttLKRWLLDFASKRkeaelrsgiirnnSLwdkl 415
Cdd:COG0365 257 LYEGRPDFPDPGR--LWELIEKYGVTVFFTAPTAI-RA-----------LMKAGDEPLKKY-------------DL---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 416 ifhkiqSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWT-AGHVGAPMPCSLIKLVDv 494
Cdd:COG0365 306 ------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 495 EEMNYLAAKGEGEVCVKG--PNVFQGYLKDPAKTAEVL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 570
Cdd:COG0365 375 EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGT 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 970702926 571 EKIENIYLRSEPVAQVFV----HGESLQAfLIAIVVPdaetvgpwarKRGFEGSfEEL 624
Cdd:COG0365 454 AEIESALVSHPAVAEAAVvgvpDEIRGQV-VKAFVVL----------KPGVEPS-DEL 499
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
267-609 |
1.03e-26 |
|
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: 114.18 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENvfipTPDDTLISF------LPLAHMFervvecTMLCHGAK 340
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGL----TSESRVLQFasytfdVSILEIF------TTLAAGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 341 IGffqgdI---RLLMDDLkalrptvfpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdkLIF 417
Cdd:cd05918 175 LC-----IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 418 HKIQSSLggrvKLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLT-VAGDWTAGHVGAPMPCSLIkLVDVEE 496
Cdd:cd05918 211 PEDVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSpVVPSTDPRNIGRPLGATCW-VVDPDN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 MNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:cd05918 284 HDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 970702926 563 aQGEYIAPEKIENIYLRSEP-----VAQVFVH-GESLQAFLIAIVVPDAETVG 609
Cdd:cd05918 364 -RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSSG 415
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-590 |
2.88e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.03 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 119 EWLSYKQVEEMSECVGSGLIQKgFKAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLydtlgteaiTYIINKAELSLV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL---------NIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 199 FVDKpekanllldgvenklipGLKTIVLMDSFGSSLLEQGQKCGVE-IISMKALEDLGRANRQKPKPPAPEDIAVICFTS 277
Cdd:PRK06839 96 LKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 278 GTTGNPKGAVITHRNVvsdcsaFVKMTENVFIP--TPDDTLISFLPLAHMfervvectmlchgAKIGFFqgdirllmddl 355
Cdd:PRK06839 159 GTTGKPKGAVLTQENM------FWNALNNTFAIdlTMHDRSIVLLPLFHI-------------GGIGLF----------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 356 kALrPTVFP----VVPRLLN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdklifhkiq 421
Cdd:PRK06839 209 -AF-PTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS------------------ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 422 sslggrVKLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTVAGDW--TAGHVGAPMPCSLIKLVDvEEMNY 499
Cdd:PRK06839 266 ------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 500 LAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 579
Cdd:PRK06839 338 VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINK 415
|
490
....*....|.
gi 970702926 580 SEPVAQVFVHG 590
Cdd:PRK06839 416 LSDVYEVAVVG 426
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-615 |
7.67e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 111.03 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKAApdQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 dkpekanllldgvenklipglktivlmdsfGSSLleqgqkcgveiismkaledlgranrqkpkppapEDIAVICFTSGTT 280
Cdd:cd05935 80 ------------------------------GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 281 GNPKGAVITHRNVVSDCSAFVKMTeNVfipTPDDTLISFLPLAHM--FERVVECTMLCHGAKIGFFQGDIRLLMDDLKAL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWT-GL---TPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 359 RPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASkrkeaelrsgiirnnslwdklifhkiqsslggrVKLMITGAAPV 438
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--------ATPEFKTRDLSS---------------------------------LKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 439 SATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 519 YLKDPAKTAEVLDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVAQVFV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490 500 510
....*....|....*....|....*....|...
gi 970702926 589 HGESLQAFLiaIVVP------DAETVGPWARKR 615
Cdd:cd05935 371 VGEEVKAFI--VLRPeyrgkvTEEDIIEWAREQ 401
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-615 |
7.98e-26 |
|
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: 114.18 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 119 EWLSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQGCF----AYsmvvIPLYDTLGTEAITYIINKAE 194
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALG--VGPGDLVGVCLERSLEMVVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 195 LSLVFVDkpekanllldgvenklipglktivlmdsfgSSLLEQGQKCGVEIISMKALEDLGRANRQKPKPPAPEDIAVIC 274
Cdd:COG1020 574 ARLVLTQ------------------------------SALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 275 FTSGTTGNPKGAVITHRNVVSdcsaFVKMTENVFIPTPDDTLISFLPLAH------MFervvecTMLCHGAKIGFFQGDI 348
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGLGPGDRVLQFASLSFdasvweIF------GALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 349 RLLMDDLKAL----RPTVFPVVPRLLNRMFDRIFgQANTTLKRWLLdfaskrkeaelrsgiirnnslwdklifhkiqssl 424
Cdd:COG1020 694 RRDPAALAELlarhRVTVLNLTPSLLRALLDAAP-EALPSLRLVLV---------------------------------- 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 GGRvklmitgAAPVsATVLTFLRAALGCQFYEGYGQTECTAGCCLTV--AGDWTAGHV--GAPMPCSLIKLVDvEEMNyL 500
Cdd:COG1020 739 GGE-------ALPP-ELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQ-P 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 501 AAKG-EGEVCVKGPNVFQGYLKDPAKTAEV-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:COG1020 809 VPVGvPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGE 887
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 970702926 573 IENIyLRSEP-VAQ--VFVHGESLQA-FLIAIVVPDAETVGPWARKR 615
Cdd:COG1020 888 IEAA-LLQHPgVREavVVAREDAPGDkRLVAYVVPEAGAAAAAALLR 933
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
113-607 |
1.02e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.79 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 113 KPDQPY-----EWLSYKQVEEMSECVGSGLIQKGFKAApDQFIgIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAIT 187
Cdd:PRK07786 30 QPDAPAlrflgNTTTWRELDDRVAALAGALSRRGVGFG-DRVL-ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 188 YIINKAELSLVFVDkPEKANLLLdGVENkLIPGLKTIVLM--DSFGSSLleqgqkcgveiismkALEDLGRANRQkpkPP 265
Cdd:PRK07786 108 FLVSDCGAHVVVTE-AALAPVAT-AVRD-IVPLLSTVVVAggSSDDSVL---------------GYEDLLAEAGP---AH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDI-----AVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfIPTPDDtlISFL--PLAHMFERVVECTMLCHG 338
Cdd:PRK07786 167 APVDIpndspALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSD--VGFVgvPLFHIAGIGSMLPGLLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 339 AKI-----GFFqgDIRLLMDDLKALRPTVFPVVPrllnrmfdrifgqanttlKRWLLDFASKRkeAELRSGIIRNNSlWd 413
Cdd:PRK07786 242 APTviyplGAF--DPGQLLDVLEAEKVTGIFLVP------------------AQWQAVCAEQQ--ARPRDLALRVLS-W- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 414 klifhkiqsslggrvklmitGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLTVAGDWTA--GHVGAPMPCSLIK 490
Cdd:PRK07786 298 --------------------GAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAAR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 491 LVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 570
Cdd:PRK07786 358 VVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYC 434
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 970702926 571 EKIENIYLRSEPVAQVFVHGESLQAF---LIAIVVPDAET 607
Cdd:PRK07786 435 AEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRNDD 474
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-575 |
1.22e-25 |
|
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: 110.61 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 173 VVIPLYDTLGTEAITYIINKAELSLVFVDKpekanllldGVENKLIPGLktIVLMDSfgsslleqgqkcgVEIISMKALE 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADA---------GAADRLRDAL--PASPDP-------------GTVLDADGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 253 DlGRANRQKpKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENvfipTPDDTLISFLPLAHMFERVVEC 332
Cdd:cd05922 104 A-ARASAPA-HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI----TADDRALTVLPLSYDYGLSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 333 TMLCHGAKIgFFQGDIRL---LMDDLKALRPTVFPVVPRLLNrMFDRifgqanttlkrwlLDFAsKRKEAELRsgiirnn 409
Cdd:cd05922 178 THLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTR-------------LGFD-PAKLPSLR------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 410 slwdklifhkiqsslggrvklMIT--GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCClTVAGDWTA---GHVGAPM 484
Cdd:cd05922 235 ---------------------YLTqaGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMT-YLPPERILekpGSIGLAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 485 PCSLIKLVDVEEMnyLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:cd05922 293 PGGEFEILDDDGT--PTPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF 370
|
410
....*....|..
gi 970702926 564 qGEYIAPEKIEN 575
Cdd:cd05922 371 -GNRISPTEIEA 381
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
266-607 |
2.33e-25 |
|
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: 109.64 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVS----DCSAFVKMTENVFIPTPDdtlISF-LPLAHMFervveCTmLCHGAk 340
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVSftnwMLSDFPLGPGDVFLNQAP---FSFdLSVMDLY-----PA-LASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 341 igffqgdirllmddlkalrpTVFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDKLIFHK 419
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 --IQSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCcltVAGDWT----AGH----VGAPMPCSLI 489
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAV---TYIEVTpevlDGYdrlpIGYAKPGAKL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 490 KLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd05945 284 VILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGY 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 970702926 567 YIAPEKIENIYLRSEPVAQVFV----HGESLQAfLIAIVVPDAET 607
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-606 |
2.63e-25 |
|
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: 110.11 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 111 SRKPDQPY-----EWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVI----IEQGCFAYsmvvIPLYDTL 181
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVG--PDTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 182 GTEAITYIINKAELSLVFVDKPEKANLLldgvenklipGLKTIVLMDSfgsslleqgqkcgvEIISMKALEDLGRANRqk 261
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIA----------FIGLIDLLDE--------------DTIYHEESENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 262 pkppaPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFvkmtENVFIPTPDDTLISFLPLAhmFERVVEC--TMLCHGA 339
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVTEifASLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 340 KIGFFQ----GDIRLLMDDLKALRPTVFPVVPRLLNrmfdrifgqanttlkrwLLDFAskrkeaelrsgiirnnslwDKL 415
Cdd:cd17655 205 TLYIVRketvLDGQALTQYIRQNRITIIDLTPAHLK-----------------LLDAA-------------------DDS 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 416 IFHKIqsslggrvKLMITGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCC--LTVAGDWTAGHV--GAPMPCSLI 489
Cdd:cd17655 249 EGLSL--------KHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 490 KLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:cd17655 321 YILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI- 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 970702926 564 QGEYIAPEKIENIYLRSEPVAQ--VFVH-GESLQAFLIAIVVPDAE 606
Cdd:cd17655 399 RGYRIELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSEKE 444
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
121-610 |
5.96e-25 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 109.49 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLiqKGFKAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVfV 200
Cdd:TIGR03098 26 LTYAALSERVLALASGL--RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DKPEKANLLLDGVENklIPGLKTIVLmdsFGSSLLEQGQKCGVEIISMKALEDLGRAnrQKPKPPAPEDIAVICFTSGTT 280
Cdd:TIGR03098 103 TSSERLDLLHPALPG--CHDLRTLII---VGDPAHASEGHPGEEPASWPKLLALGDA--DPPHPVIDSDMAAILYTSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 281 GNPKGAVITHRNVVSDCSAFVKMTENvfipTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFFqgDIRLLMDDLKAL-- 358
Cdd:TIGR03098 176 GRPKGVVLSHRNLVAGAQSVATYLEN----RPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH--DYLLPRDVLKALek 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 359 -RPTVFPVVPRLLNRMFDrifgqanttLKRWLLDFASKRKEAelrsgiirnNSlwdklifhkiqsslGGRvklmitgaap 437
Cdd:TIGR03098 250 hGITGLAAVPPLWAQLAQ---------LDWPESAAPSLRYLT---------NS--------------GGA---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 438 VSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTVAG-DWTAGHVGAPMPCSLIkLVDVEEMNYLAAKGEGEVCVKGPNV 515
Cdd:TIGR03098 288 MPRATLSRLRSFLPnARLFLMYGLTEAFRSTYLPPEEvDRRPDSIGKAIPNAEV-LVLREDGSECAPGEEGELVHRGALV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 516 FQGYLKDPAKTAEVLDK----DGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVA 584
Cdd:TIGR03098 367 AMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVA 445
|
490 500 510
....*....|....*....|....*....|
gi 970702926 585 QVFVHG----ESLQAFLIAIVVPDAETVGP 610
Cdd:TIGR03098 446 EAVAFGvpdpTLGQAIVLVVTPPGGEELDR 475
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
145-574 |
1.41e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 107.97 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 145 APDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDkpekanlllDGVenklipglkti 224
Cdd:PRK09088 45 VDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD---------DAV----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 225 vlmdsfgsslleqgQKCGVEIISMKALEDLGRANRQKPKPPAPED-IAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKM 303
Cdd:PRK09088 105 --------------AAGRTDVEDLAAFIASADALEPADTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 304 TENvfiptpdDTLISFLPLAHMFERVVECT----MLCHGAKI----GFFQGDIRLLMDDLkALRPTVFPVVPRllnrMFD 375
Cdd:PRK09088 171 GRV-------DAHSSFLCDAPMFHIIGLITsvrpVLAVGGSIlvsnGFEPKRTLGRLGDP-ALGITHYFCVPQ----MAQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 376 RIFGQAnttlkrwllDFASkrkeAELRsgiirnnslwdklifhkiqsslggRVKLMITGAAP-VSATVLTFLraALGCQF 454
Cdd:PRK09088 239 AFRAQP---------GFDA----AALR------------------------HLTALFTGGAPhAAEDILGWL--DDGIPM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 455 YEGYGQTEctAGCCLTVAGDWT-----AGHVGAPMPCSLIKLVDVEEmNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEV 529
Cdd:PRK09088 280 VDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQG-NDCPAGVPGELLLRGPNLSPGYWRRPQATARA 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 970702926 530 LDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09088 357 FTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-592 |
2.49e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 106.97 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 123 YKQVEEMSECVGSGLIQKGFKAApdqfigIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDk 202
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKGDRVA------LLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 203 pekanlllDGVENKLIPGLKTIVlmdsfgsSLLEQGQKCGVEIISMKALEDlgranrqkpkppapedIAVICFTSGTTGN 282
Cdd:PRK03640 107 --------DDFEAKLIPGISVKF-------AELMNGPKEEAEIQEEFDLDE----------------VATIMYTSGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 283 PKGAVITHRNVVSdcSAfVKMTENVFIpTPDDTLISFLPLAH------MFERVVE-CTMLCH----GAKIgffqgdIRLL 351
Cdd:PRK03640 156 PKGVIQTYGNHWW--SA-VGSALNLGL-TEDDCWLAAVPIFHisglsiLMRSVIYgMRVVLVekfdAEKI------NKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 352 MDDlkalRPTVFPVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdklifhkiqsslggrvKLM 431
Cdd:PRK03640 226 QTG----GVTIISVVSTMLQRLLERL-GEGTY------------------------PSSF-----------------RCM 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 432 ITGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLTVAGDWTA---GHVGAPM-PCSlIKLVDveEMNYLAAKGEGE 507
Cdd:PRK03640 260 LLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 508 VCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVF 587
Cdd:PRK03640 335 IVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAG 412
|
....*
gi 970702926 588 VHGES 592
Cdd:PRK03640 413 VVGVP 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-598 |
5.27e-24 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 105.50 E-value: 5.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKAApDQFIGIFAqNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKG-DRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DKpekanllldgvenklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkppapEDIAVICFTSGTT 280
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 281 GNPKGAVITHrnvvsdcSAFVKmtenvFIPT--------PDD-------------TLISFL-PLAHMFervveCTMLCHG 338
Cdd:cd05972 94 GLPKGVLHTH-------SYPLG-----HIPTaaywlglrPDDihwniadpgwakgAWSSFFgPWLLGA-----TVFVYEG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 339 AKIgffqgDIRLLMDDLKALRPTVFPVVPrllnrmfdrifgqanTTLKRWLLDFASKRKEAELRSgiirnnslwdklifh 418
Cdd:cd05972 157 PRF-----DAERILELLERYGVTSFCGPP---------------TAYRMLIKQDLSSYKFSHLRL--------------- 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 419 kiqsslggrvklMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMN 498
Cdd:cd05972 202 ------------VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGR 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 499 YLAAKGEGEVCVKGPNV--FQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENI 576
Cdd:cd05972 269 ELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESA 346
|
490 500
....*....|....*....|....*....
gi 970702926 577 YLRSEPVAQVFV-------HGESLQAFLI 598
Cdd:cd05972 347 LLEHPAVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-626 |
6.13e-24 |
|
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: 106.05 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVF- 199
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 200 -VDKPekanllldgvenklipglktiVLMDSFGSslleqgqkcGVEIISMKALEDLGRANRQ----KPKPPAPEDIAVIC 274
Cdd:cd05923 107 aVDAQ---------------------VMDAIFQS---------GVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 275 FTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVFipTPDDTLISFLPLAHMfervvectmlchgakIGFFQgdirLLMDD 354
Cdd:cd05923 157 YTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRH--GRHNVVLGLMPLYHV---------------IGFFA----VLVAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 355 LkALRPTVFPVvprllnRMFDRIFgqanttlkrwlldfASKRKEAELRSGIIRNNSLWDKLIFHKIQSS--LGGRVKLMI 432
Cdd:cd05923 216 L-ALDGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 433 TGAApVSATVLTFLRAALGCQFYEGYGQTECTAGcclTVAGDWTAGHVGAPMPCSLIKLVDV-EEMNYLAAKG-EGEVCV 510
Cdd:cd05923 275 AGAT-MPDAVLERVNQHLPGEKVNIYGTTEAMNS---LYMRDARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 511 K--GPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFV 588
Cdd:cd05923 351 AaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVV 428
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 970702926 589 HG---ESLQAFLIAIVVPDAETVGpwarkrgfEGSFEELCR 626
Cdd:cd05923 429 IGvadERWGQSVTACVVPREGTLS--------ADELDQFCR 461
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-628 |
8.96e-24 |
|
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: 105.46 E-value: 8.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 120 WLSYKQVEEMSECVGSGLIQKGFkaAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVF 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 200 VDKPEKANLLLDGVEnklipglktivlmDSFgsslleqgqkcgveiismkaledlgranrqKPKPPAPE-DIAVICFTSG 278
Cdd:cd12118 107 VDREFEYEDLLAEGD-------------PDF------------------------------EWIPPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 279 TTGNPKGAVITHR----NVVSDCSAFVKMTENVFIPTpddtlisfLPLAHmfervveCTMLCHGAKIGFFQG-------- 346
Cdd:cd12118 144 TTGRPKGVVYHHRgaylNALANILEWEMKQHPVYLWT--------LPMFH-------CNGWCFPWTVAAVGGtnvclrkv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 DIRLLMDDLKALRPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSlwdklifHKIQSSLGG 426
Cdd:cd12118 209 DAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAP-------PSDARPLPH 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 427 RVKLMITGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAGccLTVAGDWTA--------------GHVGAPMPCSL-IKL 491
Cdd:cd12118 249 RVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYG--PATVCAWKPewdelpteerarlkARQGVRYVGLEeVDV 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 492 VDVEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:cd12118 324 LDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENIS 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970702926 570 PEKIENIylrsepvaqVFVHGESLQAFLIAivVPDaETVG--PWAR---KRGFEGSFEEL---CRNK 628
Cdd:cd12118 402 SVEVEGV---------LYKHPAVLEAAVVA--RPD-EKWGevPCAFvelKEGAKVTEEEIiafCREH 456
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
119-583 |
1.18e-23 |
|
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: 105.40 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 119 EWLSYKQVEEMSECVGSGLIQKGfkaAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEA---ITYIINKAEL 195
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 196 SLVFVDKPEKANLLLDGVENKLIPGLKTIVLmDSFGSSLLEQGQkcgveiismkaledlgranrqkPKPPAPEDIAVICF 275
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV-DLLPDTSAADWP----------------------PPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 276 TSGTTGNPKGAVITHRNVVSDCSAFVKmtenVFIPTPDDTLISFLPLAH-----------MFERvVECTMLchgAKIGFF 344
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRR----AYGLDPGDVVVSWLPLYHdmgligglltpLYSG-GPSVLM---SPAAFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGDIRLL--MDDLKAlrptVFPVVPrllNrmfdriFGqanttlkrwlLDFASKRKEAELRSGIirnnslwDkLifhkiqs 422
Cdd:cd05931 229 RRPLRWLrlISRYRA----TISAAP---N------FA----------YDLCVRRVRDEDLEGL-------D-L------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 423 slgGRVKLMITGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLTVAGDWTAGHV------ 480
Cdd:cd05931 271 ---SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDALAGRAvavaad 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 481 ----------GAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEV------LDKDGWLHTGDIGkW 544
Cdd:cd05931 348 dpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLG-F 426
|
490 500 510
....*....|....*....|....*....|....*....
gi 970702926 545 LPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPV 583
Cdd:cd05931 427 LHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
3.33e-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: 101.19 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVSdCSAFVKMTENVfipTPDDTLISFLPLAHMFERVVECTMLCHGAK---IGFFq 345
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIA-ANLQLIHAMGL---TEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 346 gDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdklifhkiqsslg 425
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH----------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 426 grvklmITGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKG 504
Cdd:cd17637 119 ------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAGE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 505 EGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYLRSEP 582
Cdd:cd17637 188 TGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPA 265
|
330 340
....*....|....*....|....
gi 970702926 583 VAQVFVHGeslqafliaivVPDAE 606
Cdd:cd17637 266 IAEVCVIG-----------VPDPK 278
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-685 |
6.88e-23 |
|
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: 100.10 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVSdcSAfvKMTENVFIPTPDDTLISFLPLAHM--FERVVECtmLCHGAKIGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRS--LLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 DiRLLMDDLKALRPTVFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdklifhkiqsslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 427 rVKLMITGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDveemnylaakgEG 506
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 507 EVCVKGPNVFQGYLKDPakTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQV 586
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 587 FVHG---ESLQAFLIAIVVPDAETVgpwarkrgfEGSFEELCRNKdvrkailedmvrlgkdsgLKSFEQVKAISLHPELf 663
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVGRGPAD---------PAELRAWLKDK------------------LARFKLPKRIYPVPEL- 308
|
410 420
....*....|....*....|..
gi 970702926 664 tidngLLTPTMKAKRPDLQNYF 685
Cdd:cd17630 309 -----PRTGGGKVDRRALRAWL 325
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-603 |
1.03e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.82 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAElSLVFV 200
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLG--VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 --------DKPEKANLLLDGvenklIPGLKTIVLM-----DSFGSSLleqgqkCGVEIISMKALEDLGRANRqkpkpPAP 267
Cdd:PRK13295 133 vpktfrgfDHAAMARRLRPE-----LPALRHVVVVggdgaDSFEALL------ITPAWEQEPDAPAILARLR-----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 268 EDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAHMfervvecTMLCHGAKIGFFQGD 347
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG----LGADDVILMASPMAHQ-------TGFMYGLMMPVMLGA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 348 IRLLMDDLKALRptvfpvvprllnrMFDRI------FGQANTTlkrWLLDFASKRKEAELRSgiirnnslwdklifhkiq 421
Cdd:PRK13295 266 TAVLQDIWDPAR-------------AAELIrtegvtFTMASTP---FLTDLTRAVKESGRPV------------------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 422 SSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNY 499
Cdd:PRK13295 312 SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPDERASTTDGCPLPGVEVRVVD-ADGAP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 500 LAAKGEGEVCVKGPNVFQGYLKDPAKTAEvlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLR 579
Cdd:PRK13295 387 LPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYR 463
|
490 500
....*....|....*....|....*..
gi 970702926 580 SEPVAQVFVHG---ESLQAFLIAIVVP 603
Cdd:PRK13295 464 HPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-591 |
1.12e-22 |
|
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: 100.25 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDcsafVKMTENVFIPTPDDTLISFLPLAHMFERVVEC-TMLCHGAKIGF-- 343
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN----AWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLlTPLASGAHVVLag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 344 ---FQGDIrlLMDDLKAL----RPTVFPVVPRLLNRMFDRIFGqanttlkrwlldfaskrkeAELrsgiirnnslwdkli 416
Cdd:cd05944 77 pagYRNPG--LFDNFWKLveryRITSLSTVPTVYAALLQVPVN-------------------ADI--------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 417 fhkiqSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTagCCLTVA---GDWTAGHVGAPMPCSLIKLVD 493
Cdd:cd05944 121 -----SSL----RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT--CLVAVNppdGPKRPGSVGLRLPYARVRIKV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 494 VE-EMNYL--AAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:cd05944 190 LDgVGRLLrdCAPDEvGEICVAGPGVFGGYLYTEGNKNAFVA-DGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNID 267
|
330 340
....*....|....*....|..
gi 970702926 570 PEKIENIYLRSEPVAQVFVHGE 591
Cdd:cd05944 268 PALIEEALLRHPAVAFAGAVGQ 289
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-628 |
1.49e-22 |
|
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: 101.68 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DkPEKANLLLDGVEnKLIPGLKTIVLMDSFGSSLLEqgqkcgveiismKALEDL--GRANRQKPKPPAPEDIAVICFTSG 278
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 279 TTGNPKGAVITHRNVVSDCSAFVKmteNVFIPTPDDTLISFLPLAHMFErvvectmLCHGAKIGFFQGDIRLLM------ 352
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 353 ----DDLKALRPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWdklifhkiQSSLGGRV 428
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAPNL--------PSRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 429 KLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEV 508
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 509 CVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFV 588
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 970702926 589 HGESLQAFLI---AIVVPdaetvgpwarKRGFEGS---FEEL---CRNK 628
Cdd:cd05959 440 VGVEDEDGLTkpkAFVVL----------RPGYEDSealEEELkefVKDR 478
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-616 |
1.87e-22 |
|
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: 101.76 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKAA-------PdqfigifaqNRPEWVIIeqgCFAYSMV-VIPLYdTL----GTEaITY 188
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGdrvvvqlP---------NVAEFVIV---FFALFRAgAIPVF-ALpahrRAE-ISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 189 IINKAELS-LVFVDKPEKANL--LLDGVeNKLIPGLKTIVLMDSFGSSLleqgqkcgveiismkALEDLGRANRQKPKP- 264
Cdd:COG1021 117 FAEQSEAVaYIIPDRHRGFDYraLAREL-QAEVPSLRHVLVVGDAGEFT---------------SLDALLAAPADLSEPr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 265 PAPEDIAVICFTSGTTGNPKgaVI--THR----NVV--SDCSAFvkmtenvfipTPDDTLISFLPLAHMFervvecTMLC 336
Cdd:COG1021 181 PDPDDVAFFQLSGGTTGLPK--LIprTHDdylySVRasAEICGL----------DADTVYLAALPAAHNF------PLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 337 HGAkIGFFQGDIRLLM------DDLKAL----RPTVFPVVPRLLNRMfdrifgqanttlkrwlLDFASKRKeAELrsgii 406
Cdd:COG1021 243 PGV-LGVLYAGGTVVLapdpspDTAFPLiereRVTVTALVPPLALLW----------------LDAAERSR-YDL----- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 407 rnnslwdklifhkiqSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTVAGD---WTAGHVGA 482
Cdd:COG1021 300 ---------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeeVILTTQGR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 483 PMpCSL--IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKK-HI 559
Cdd:COG1021 358 PI-SPDdeVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQI 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970702926 560 FKlaQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFliaiVVPDAETVGP-----WARKRG 616
Cdd:COG1021 436 NR--GGEKIAAEEVENLLLAHPAVHDAAVvampdeyLGERSCAF----VVPRGEPLTLaelrrFLRERG 498
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-615 |
4.30e-22 |
|
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: 100.35 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWV-----IIEQGCfAYsmvvIPLYDTLGTEAITYIINKAEL 195
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG--VGPGDVVGVLAERSPELVvallaVLKAGA-AY----VPLDPELPAERLAFMLADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 196 SLVFVDKPEKANLlldgvenkliPGLKTIVLMDsfgsslleqgqkcgveiismkalEDLGRANRQKPKPPA-PEDIAVIC 274
Cdd:cd12117 96 KVLLTDRSLAGRA----------GGLEVAVVID-----------------------EALDAGPAGNPAVPVsPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 275 FTSGTTGNPKGAVITHRNVVSdcsaFVKMTeNVFIPTPDDTLISFLPL---AHMFERVVEctmLCHGAkigffqgdiRLL 351
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLafdASTFEIWGA---LLNGA---------RLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 352 MDDlkalrptvfPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkEAELrsgiirnnslwdkliFHKI----QSSLGGR 427
Cdd:cd12117 206 LAP---------KGTLLDPDALGALIAEEGVTVL--WL--------TAAL---------------FNQLadedPECFAGL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 428 VKLMITG-AAPVSAtVLTFLRAALGCQFYEGYGQTECT--AGCCLTVAGDWTAGHV--GAPMPCSLIKLVDveEMNYLAA 502
Cdd:cd12117 252 RELLTGGeVVSPPH-VRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD--EDGRPVP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 503 KGE-GEVCVKGPNVFQGYLKDPAKTAEVLDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 575
Cdd:cd12117 329 PGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEA 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 970702926 576 IYLRSEPVAQVFV---HGESLQAFLIAIVVP----DAETVGPWARKR 615
Cdd:cd12117 408 ALRAHPGVREAVVvvrEDAGGDKRLVAYVVAegalDAAELRAFLRER 454
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
111-615 |
5.29e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 100.50 E-value: 5.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 111 SRKPDQP-YEW----LSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQG---CFAYSMVVIPLYDTlg 182
Cdd:PRK06178 44 RERPQRPaIIFyghvITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGilkLGAVHVPVSPLFRE-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 183 teaityiinkAELSLVFVDKPEKANLLLD-------------GVEN-------KLIPGLKTIVLMDSF-GSSLLEQGQkc 241
Cdd:PRK06178 120 ----------HELSYELNDAGAEVLLALDqlapvveqvraetSLRHvivtslaDVLPAEPTLPLPDSLrAPRLAAAGA-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 242 gveIISMKALEDLGRANRQKPkpPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVfipTPDDTLISFLP 321
Cdd:PRK06178 188 ---IDLLPALRACTAPVPLPP--PALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVG---GEDSVFLSFLP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 322 lahMFervvectmlchgakigFFQGDirllmdDLKALRPTVF--PVVprLLNRmfdrifgqanttlkrwlldfaskrkea 399
Cdd:PRK06178 260 ---EF----------------WIAGE------NFGLLFPLFSgaTLV--LLAR--------------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 400 elrsgiirnnslWDKLIF------HKIQSSLG---GRVKLMITGAapVSATVLTFL--------------------RAAL 450
Cdd:PRK06178 286 ------------WDAVAFmaaverYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALT 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 451 GCQFYEG-YGQTEcTAGCCLTVAGDWTAGH--------VGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLK 521
Cdd:PRK06178 352 GSVLAEAaWGMTE-THTCDTFTAGFQDDDFdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 522 DPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHG---ESLQAFLI 598
Cdd:PRK06178 431 KPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVVGrpdPDKGQVPV 508
|
570 580
....*....|....*....|...
gi 970702926 599 AIVVP------DAETVGPWARKR 615
Cdd:PRK06178 509 AFVQLkpgadlTAAALQAWCREN 531
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
268-599 |
1.29e-21 |
|
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: 98.30 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 268 EDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKmteNVFIPTPDDTLISflpLAHMFERVvectMLCHGAKIGFFQGD 347
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFFGY----GLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 348 IRLLMDD----------LKALRPTVFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdklif 417
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 418 hkiqsslggrVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEM 497
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 498 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 970702926 578 LRSEPVAQVFV------HGES-LQAFLIA 599
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
266-598 |
1.63e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 97.89 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRnVVSDCSAFVKMTENVFiPTPDDtlISFLPlahmfervvectmlchgAKIGFFQ 345
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHR-VLLGHLPGVQFPFNLF-PRDGD--LYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 346 GdirlLMDdlkALRPTVFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdkliFHKIQSS 423
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 424 LGG-RVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLTVaGDWTAGHVGAPMPCSLIKLVDvEEMNYL 500
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLviGNCSAL-FPIKPGSMGKPIPGHRVAIVD-DNGTPL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 501 AAKGEGEVCVKGPN--VFQGYLKDPAKTaEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYL 578
Cdd:cd05971 282 PPGEVGEIAVELPDpvAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLL 359
|
330 340
....*....|....*....|....*..
gi 970702926 579 RSEPVAQVFV-------HGESLQAFLI 598
Cdd:cd05971 360 KHPAVLMAAVvgipdpiRGEIVKAFVV 386
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
264-617 |
3.88e-21 |
|
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: 97.41 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPEDIAVICFTSGTTGNPKGAVITHRNVVSdcsaFVKMTENVFIPTPDDTLISFLPLAhmFERVVE--CTMLCHGAKI 341
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQeiFSTLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 342 GFFQGDIRLlmdDLKALRptvfpvvpRLLNRM-FDRIFgqANTTLKRWLLdfaskrkEAELRSGiirnnslwdklifhki 420
Cdd:cd17651 206 VLPPEEVRT---DPPALA--------AWLDEQrISRVF--LPTVALRALA-------EHGRPLG---------------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qsSLGGRVKLMITGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLTVAGD---WTA-GHVGAPMPCSLIKLVDv 494
Cdd:cd17651 250 --VRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 495 EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17651 327 AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRI 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 970702926 569 APEKIENIYLRSEPVAQ--VFVHGE-SLQAFLIAIVVPDAETVGPWARKRGF 617
Cdd:cd17651 406 ELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGDPEAPVDAAELRAA 457
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
213-694 |
5.81e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 97.18 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 213 VENKLIPGLKTIVLMDSFGSSLleqgqkcGVEIISMKALEDLGRANRQKPKPP---APEDIAVICFTSGTTGNPKGAVIT 289
Cdd:PLN02860 121 LQNDRLPSLMWQVFLESPSSSV-------FIFLNSFLTTEMLKQRALGTTELDyawAPDDAVLICFTSGTTGRPKGVTIS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 290 HRNVVSDC---SAFVKMTEnvfiptpDDTLISFLPLAHMFERVVECTMLCHGAKIGFF-QGDIRLLMDDLKALRPTVFPV 365
Cdd:PLN02860 194 HSALIVQSlakIAIVGYGE-------DDVYLHTAPLCHIGGLSSALAMLMVGACHVLLpKFDAKAALQAIKQHNVTSMIT 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 366 VPRLLnrmfdrifgqanttlkrwlldfaskrkeAELRSgIIRNNSLWDklifhkiqsslGGR-VKLMITGAAPVSA---- 440
Cdd:PLN02860 267 VPAMM----------------------------ADLIS-LTRKSMTWK-----------VFPsVRKILNGGGSLSSrllp 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 441 -TVLTFLRAALgcqfYEGYGQTE-C--------------TAGCCLTVAGDWTAGH--------VGAPMPCSLIKLVDVEE 496
Cdd:PLN02860 307 dAKKLFPNAKL----FSAYGMTEaCssltfmtlhdptleSPKQTLQTVNQTKSSSvhqpqgvcVGKPAPHVELKIGLDES 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 MNylaakgEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENI 576
Cdd:PLN02860 383 SR------VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAV 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 577 YLRSEPVAQVFVHGeslqafliaivVPDA---ETVGPWARKR-GFEGSFEELC---RNKDVRKAILEDMVRLGKDSGLKS 649
Cdd:PLN02860 456 LSQHPGVASVVVVG-----------VPDSrltEMVVACVRLRdGWIWSDNEKEnakKNLTLSSETLRHHCREKNLSRFKI 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 970702926 650 feqvkaislhPELFTI--DNGLLTPTMKAKRPDLQNYFRSQINELYS 694
Cdd:PLN02860 525 ----------PKLFVQwrKPFPLTTTGKIRRDEVRREVLSHLQSLPS 561
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
112-610 |
5.91e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.14 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 112 RKPDQPY-----EWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAI 186
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVK--RGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 187 TYIINKAELSLVFVDkpekANLL--LDGVENKLIPgLKTIVLMDSFGSSLLEQGqkcgVEIISMKALedlgrANRQKPKP 264
Cdd:PRK06155 111 EHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAG----WSTAPLPPL-----DAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 265 PAPEDIAVICFTSGTTGNPKGAVITHrnvvsdcSAF----VKMTENVFIpTPDDTLISFLPLAH-----MFERVvectmL 335
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPH-------AQFywwgRNSAEDLEI-GADDVLYTTLPLFHtnalnAFFQA-----L 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 336 CHGAKI---------GFFqgdirllmDDLKALRPTVF----PVVPRLLnrmfdrifgqanttlkrwlldfaSKRKEAELR 402
Cdd:PRK06155 244 LAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARESDR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 403 SgiirnnslwdklifHKIQSSLGGrvklmitgaaPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDwTAGHVGA 482
Cdd:PRK06155 293 A--------------HRVRVALGP----------GVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 483 PMPCSLIKLVDvEEMNYLAAKGEGEVCVKG--PNVF-QGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK06155 348 LAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDA 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 970702926 560 FKlAQGEYIAPEKIENIyLRSEP-VAQVFVH------GESlqAFLIAIVVPDAETVGP 610
Cdd:PRK06155 426 IR-RRGENISSFEVEQV-LLSHPaVAAAAVFpvpselGED--EVMAAVVLRDGTALEP 479
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
268-576 |
6.26e-21 |
|
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: 94.63 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 268 EDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVfipTPDDTLISFLPLAHMFERVVECTMLCHGAKIGFFQGD 347
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNW---VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 348 IRL--LMDDLKALRPTVFPVVPRLLNRMfdrifgqanttlkrwLLDFASKRKEAElrsgiirnnslwdklifhkiqsslg 425
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 426 gRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWT-AGHVGAPMPCSLIKLVDVEEMNYLAAkG 504
Cdd:cd17635 118 -SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970702926 505 EGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
109-671 |
6.83e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 97.42 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 109 LGSRKPDQ-PYEWLSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPL---YDTLGTE 184
Cdd:PRK12582 68 LAQREPGHgQWRKVTYGEAKRAVDALAQALLDLG--LDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 185 --AITYIINKAELSLVFVDKPEK-----ANLLLDGVE----NKLIPGLKTIVLMDSFGSSLLEqgqkcGVEiismKALED 253
Cdd:PRK12582 146 haKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVTvvhvTGPGEGIASIAFADLAATPPTA-----AVA----AAIAA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 254 LGranrqkpkppaPEDIAVICFTSGTTGNPKGAVITHRNVvsdCSAfVKMTENVFIPTPDD---TLISFLPLAHMFervv 330
Cdd:PRK12582 217 IT-----------PDTVAKYLFTSGSTGMPKAVINTQRMM---CAN-IAMQEQLRPREPDPpppVSLDWMPWNHTM---- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 331 ectmlchGAKIGFfQGDIR----LLMDD-----------LKALR---PTVFPVVPRLLNrmfdrifgqanttlkrwLLDF 392
Cdd:PRK12582 278 -------GGNANF-NGLLWgggtLYIDDgkplpgmfeetIRNLReisPTVYGNVPAGYA-----------------MLAE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 393 ASKRKEAELRSgiirnnslwdkliFHKiqsslggRVKLMITGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAG 466
Cdd:PRK12582 333 AMEKDDALRRS-------------FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 467 CCLTVAgdWTA---GHVGAPMPCSLIKLVDVEEmNYlaakgegEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGK 543
Cdd:PRK12582 392 TTTGTH--WDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAAR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 544 WL----PNGTLKIIDRKKHIFKLAQGEYIAPEKieniyLR------SEPVAQ-VFVHGESlQAFLIAIVVPDAETVGPWA 612
Cdd:PRK12582 462 FVdpddPEKGLIFDGRVAEDFKLSTGTWVSVGT-----LRpdavaaCSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLA 535
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 970702926 613 RKRGfeGSFEELCRNKDVRKAILEDMVRLGKDSGLKSfEQVKAISLHPELFTIDNGLLT 671
Cdd:PRK12582 536 GDPD--AAPEDVVKHPAVLAILREGLSAHNAEAGGSS-SRIARALLMTEPPSIDAGEIT 591
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-613 |
1.00e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 96.57 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 112 RKPDQPYEW-----LSYKQVEEMSECVGSGL-----IQKGfkaapDQfIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTL 181
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLqqecgVRKG-----DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 182 GTEAITYIINKAELSLVFVdkpekANLLLDGVEnKLIPGL---KTIVLM----------DSFGSSLLEQGQKCGVEIISM 248
Cdd:PRK08314 96 REEELAHYVTDSGARVAIV-----GSELAPKVA-PAVGNLrlrHVIVAQysdylpaepeIAVPAWLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 249 KALEDlGRANRQKPKP--PAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVkMTENVfipTPDDTLISFLPLAHMf 326
Cdd:PRK08314 170 VAWKE-ALAAGLAPPPhtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSV-LWSNS---TPESVVLAVLPLFHV- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 327 ervvecTMLCHGAKIGFFQGDIRLLMddlkalrptvfpvvPR----LLNRMFDR---IFGQANTTLkrwLLDF-ASKR-K 397
Cdd:PRK08314 244 ------TGMVHSMNAPIYAGATVVLM--------------PRwdreAAARLIERyrvTHWTNIPTM---VVDFlASPGlA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 398 EAELRSgiirnnsLWdklifhkiqsSLGGrvklmitGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG----------- 466
Cdd:PRK08314 301 ERDLSS-------LR----------YIGG-------GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpkl 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 467 CCLTVAgdwTAGhVGApmpcsliKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEV---LDKDGWLHTGDIGK 543
Cdd:PRK08314 357 QCLGIP---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGR 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 544 WLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFliaiVVPDAETVG------- 609
Cdd:PRK08314 426 MDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPEARGktteeei 500
|
....*
gi 970702926 610 -PWAR 613
Cdd:PRK08314 501 iAWAR 505
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-574 |
1.97e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.45 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 220 GLKTIVLMDSFG--SSLLEQGqkcGVEIIsmkALEDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDC 297
Cdd:PRK07768 108 GAKAVVVGEPFLaaAPVLEEK---GIRVL---TVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 298 SAfvkMTENVFIPTPDDTLISFLPLAH-MfervvectmlchgAKIGFFQGDIRLLMDDLKaLRPTVFPVVPRLLNRMFDR 376
Cdd:PRK07768 182 EA---MFVAAEFDVETDVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVK-VTPMDFLRDPLLWAELISK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 377 IFGQ-------ANTTLKRwLLDFASKRKEAELrsgiirnnslwdklifhkiqSSLggrvKLMITGAAPVS-ATVLTFLRA 448
Cdd:PRK07768 245 YRGTmtaapnfAYALLAR-RLRRQAKPGAFDL--------------------SSL----RFALNGAEPIDpADVEDLLDA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 449 ---------ALGCqfyeGYGQTECT-------AGCCLTV-------------AGDWTAGHV------GAPMPCSLIKLVD 493
Cdd:PRK07768 300 garfglrpeAILP----AYGMAEATlavsfspCGAGLVVdevdadllaalrrAVPATKGNTrrlatlGPPLPGLEVRVVD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 494 vEEMNYLAAKGEGEVCVKGPNVFQGYLkDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 573
Cdd:PRK07768 376 -EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDI 452
|
.
gi 970702926 574 E 574
Cdd:PRK07768 453 E 453
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-585 |
5.18e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 94.78 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 259 RQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDTLISFLPLAHMFERVVEC-TMLCH 337
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLfTPLLT 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 338 GAKIGFFQGdirllmddlkalrPTVFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgiirn 408
Cdd:PRK08043 432 GAEVFLYPS-------------PLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA--------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 409 nslwdklifhkiqsslggRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSL 488
Cdd:PRK08043 480 ------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMD 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 489 IKLVDVEEMnylaAKGeGEVCVKGPNVFQGYLK--DP-------AKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK08043 542 ARLLSVPGI----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRF 616
|
330 340
....*....|....*....|....*.
gi 970702926 560 FKLAqGEYIAPEKIENIYLRSEPVAQ 585
Cdd:PRK08043 617 AKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-607 |
5.69e-20 |
|
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: 93.14 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDTLISFLPLAHMFErVVEctM---LCHGAKIgf 343
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE--IwgaLLHGGRL-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 344 fqgdirLLMDDLKALRPTVFPvvpRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwdkliFHKIQSS 423
Cdd:cd17643 163 ------VVVPYEVARSPEDFA---RLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 424 LggrvKLMITGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCLTV-----AGDWTAGHVGAPMPCSLIKLVDvE 495
Cdd:cd17643 212 L----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRPldaadLPAAAASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 496 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--VLDKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANPFGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 970702926 569 APEKIENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDAET 607
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-615 |
6.46e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.80 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFkaAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGL--LPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DKpekanlllDGVENKLIPGLKTIVLMDSFGSSLLEQGQKCGVeiismkaleDLGRANRQKPKPPAPE----DIAVICFT 276
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSV---------HLDAATEPTPATSTPEglrpDDAMIMFT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 277 SGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAHMFERV-VECTMLCHGAKI-----GFFQGdiRL 350
Cdd:PRK05852 185 GGTTGLPKMVPWTHANIASSVRAIITGYR----LSPRDATVAVMPLYHGHGLIaALLATLASGGAVllparGRFSA--HT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 351 LMDDLKALRPTVFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKEAELRsgIIRNNSlwdklifhkiqsslgg 426
Cdd:PRK05852 259 FWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKPAALR--FIRSCS---------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 427 rvklmitgaAPVSATVLTFLRAALGCQFYEGYGQTECTAGCClTVAGDWtAGHVGAP-MPCSLIKLVDVEEMNYLAAKGE 505
Cdd:PRK05852 305 ---------APLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPvVSTGLVGRSTGAQIRIVGSDGL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 506 -------GEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyL 578
Cdd:PRK05852 374 plpagavGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGV-L 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 970702926 579 RSEP---VAQVF-----VHGESLQAFLI--AIVVPDAETVGPWARKR 615
Cdd:PRK05852 451 ASHPnvmEAAVFgvpdqLYGEAVAAVIVprESAPPTAEELVQFCRER 497
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-604 |
1.32e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 68 DGARRS----AILDSDEplvyfYDDVTTLY----EGFQRGMRVSNNGACLGSRKPDQPY-----EWLSYKQVEEMSECVG 134
Cdd:PRK12316 1968 EDAQAAlgelALLDAGE-----RQRILADWdrtpEAYPRGPGVHQRIAEQAARAPEAIAvvfgdQHLSYAELDSRANRLA 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 135 SGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDKPEKANLLLDGve 214
Cdd:PRK12316 2043 HRLRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA-- 2118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 215 nklipglktivlmdsfgsslleqgqkcGVEIISMKALEDLGRANRQKPKPP-APEDIAVICFTSGTTGNPKGAVITHRNV 293
Cdd:PRK12316 2119 ---------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGAL 2171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 294 VSDCSAfvkmTENVFIPTPDDTLISFLPLAhmFERVVECTM--LCHGAkigffqgdiRLLMDDLKALRPtvfpvvprllN 371
Cdd:PRK12316 2172 VAHCQA----AGERYELSPADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDP----------E 2226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 372 RMFDRIFGQANTtlkrwLLDFASkrkeaelrsgiirnnSLWDKLIFHKIQSSLGGRVKLMITGAAPVSATVLTFLRAALG 451
Cdd:PRK12316 2227 QLYDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALR 2286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 452 CQF-YEGYGQTECTA-----GCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAK 525
Cdd:PRK12316 2287 PVYlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGL 2365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 526 TAEVLDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFV---HGESLQA 595
Cdd:PRK12316 2366 TAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ 2444
|
....*....
gi 970702926 596 fLIAIVVPD 604
Cdd:PRK12316 2445 -LVAYVVPD 2452
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
264-610 |
3.22e-19 |
|
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: 91.18 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPEDIAVICFTSGTTGNPKGAVITHRNVVSdcsAFVKMTENvFIPTPDD-----TLISF--------LPLAHMfERVV 330
Cdd:cd17646 134 PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVN---RLLWMQDE-YPLGPGDrvlqkTPLSFdvsvwelfWPLVAG-ARLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 331 ECTMLCHGakigffqgDIRLLMDDLKALRPTVFPVVPRLLnrmfdrifgqanttlkRWLLDFASKRKEAELRsgiirnns 410
Cdd:cd17646 209 VARPGGHR--------DPAYLAALIREHGVTTCHFVPSML----------------RVFLAEPAAGSCASLR-------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 411 lwdklifhkiqsslggRVklmITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TVAGDWTAGHV--GAPMPCS 487
Cdd:cd17646 257 ----------------RV---FCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 488 LIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--VLDKDG----WLHTGDIGKWLPNGTLKIIDRKKHIFK 561
Cdd:cd17646 318 RLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAErfVPDPFGpgsrMYRTGDLARWRPDGALEFLGRSDDQVK 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 970702926 562 LaQGEYIAPEKIENIyLRSEP-VAQVFV---HGESLQAFLIAIVVPDAETVGP 610
Cdd:cd17646 397 I-RGFRVEPGEIEAA-LAAHPaVTHAVVvarAAPAGAARLVGYVVPAAGAAGP 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-605 |
7.28e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.15 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVI----IEQGCFAYsmvvIPLYDTLGTEAITYIINKAELS 196
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 197 LVFVDkpekanllldgvenklipglktivlmdsfgSSLLEQGQKC-GVEIISMKALEDL--GRANRQKPKPPAPEDIAVI 273
Cdd:PRK12467 612 LLLTQ------------------------------SHLLAQLPVPaGLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 274 CFTSGTTGNPKGAVITHRNVVSdcsaFVKMTENVFIPTPDDTLISFLPLAHMFERVVECTMLCHGAKIgffqgdirLLMD 353
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLP 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 354 DLKALRPTVFpvvprllnrmFDRIFGQANTTLKRwlldfaskrkeaelrsgiirNNSLWDKLIFHKIQSSLGGRVKLMIT 433
Cdd:PRK12467 730 PDCARDAEAF----------AALMADQGVTVLKI--------------------VPSHLQALLQASRVALPRPQRALVCG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 434 GAA-PVSATVLTFlRAALGCQFYEGYGQTECTAGC----CLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEV 508
Cdd:PRK12467 780 GEAlQVDLLARVR-ALGPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGEL 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 509 CVKGPNVFQGYLKDPAKTAE--VLDKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSE 581
Cdd:PRK12467 858 YIGGAGLARGYHRRPALTAErfVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQP 936
|
490 500
....*....|....*....|....*.
gi 970702926 582 PVAQVFV--HGESLQAFLIAIVVPDA 605
Cdd:PRK12467 937 GVREAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
173-590 |
8.11e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 90.33 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 173 VVIPLYDTLGTEAITYIINKAELSLVFVDKpekanllldgvENKLIPGLKT-IVLMDSFG---SSLLEQGqkcGVEIISM 248
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAqadSRRLAQG---GLEIPPQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 249 KaledlgranrqkpkPPAPEDIAVICFTSGTTGNPKGAVITHRNVV---SDCSAFVKMTEnvfiptpDDTLISFLPLAHm 325
Cdd:PRK06145 144 A--------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHwksIDHVIALGLTA-------SERLLVVGPLYH- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 326 ferVVECTM-----LCHGAKIGFFQG-DIRLLMDDLKALRPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASKRkea 399
Cdd:PRK06145 202 ---VGAFDLpgiavLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA--- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 400 elrsgiirnnslWdklifhkiqsSLGGrvklmitGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDW--TA 477
Cdd:PRK06145 268 ------------W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 478 GHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK06145 319 GSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKK 396
|
410 420 430
....*....|....*....|....*....|...
gi 970702926 558 HIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG 590
Cdd:PRK06145 397 DMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
138-598 |
1.96e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 88.97 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 138 IQKGFKAApdqfigIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVfVDKPEKANLLLDGVENKL 217
Cdd:PRK08008 59 IRKGDKVA------LHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLL-VTSAQFYPMYRQIQQEDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 218 IPgLKTIVLMDSFGSSllEQGqkcgveIISMKALEDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSdc 297
Cdd:PRK08008 132 TP-LRHICLTRVALPA--DDG------VSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 298 SAFVKMTENVFipTPDDTLISFLPLAHmfervVECTmlCHGAKIGFFQGDIRLLMDDLKA---------LRPTVFPVVPR 368
Cdd:PRK08008 201 AGYYSAWQCAL--RDDDVYLTVMPAFH-----IDCQ--CTAAMAAFSAGATFVLLEKYSArafwgqvckYRATITECIPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 369 LLNrmfdrifgqantTLkrwLLDFASKRKeaelrsgiiRNNSLWDKLIFhkiqsslggrvkLMITgaapvSATVLTFLRA 448
Cdd:PRK08008 272 MIR------------TL---MVQPPSAND---------RQHCLREVMFY------------LNLS-----DQEKDAFEER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 449 aLGCQFYEGYGQTECTAGccltVAGD-------WTAghVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKG---PNVFQG 518
Cdd:PRK08008 311 -FGVRLLTSYGMTETIVG----IIGDrpgdkrrWPS--IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 519 YLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyLRSEP-VAQVFVHG------- 590
Cdd:PRK08008 383 YYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikdsird 460
|
....*...
gi 970702926 591 ESLQAFLI 598
Cdd:PRK08008 461 EAIKAFVV 468
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
168-590 |
1.99e-18 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 89.09 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 168 FAYSM--------VVIPLYDTLGTEAITYIINKAELSLVFVDKpekANLLLDGVEnKLIPGLKTIVLMDSFGSSLLEQGq 239
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIE-KAAPECPSKPKLVWVGDPVPEGW- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 240 kCGVEIISMKALEDLGRanRQKPKPPAPEDIAVICFTSGTTGNPKgavithrnvvsdcsafvkMTENVFIptpddtlisf 319
Cdd:cd05970 160 -IDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK------------------MVEHDFT---------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 320 LPLAHMFErvvecTMLCHGAKigffQGDIRLLMDDL---KAlrptvfpvvprllnrMFDRIFGQANTTLKRWLLDFasKR 396
Cdd:cd05970 209 YPLGHIVT-----AKYWQNVR----EGGLHLTVADTgwgKA---------------VWGKIYGQWIAGAAVFVYDY--DK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 397 KEAELRSGIIRNN---------SLWDKLIFHKIQSSLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTagc 467
Cdd:cd05970 263 FDPKALLEKLSKYgvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETT--- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 468 cLTVAG-DW---TAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCV---KGPNV--FQGYLKDPAKTAEVLdKDGWLHT 538
Cdd:cd05970 340 -LTIATfPWmepKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHT 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 970702926 539 GDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFVHG 590
Cdd:cd05970 417 GDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-607 |
1.50e-17 |
|
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: 85.98 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiptPDDTLISFLPLAHMFERVVE---CTMLCHGAKIGF 343
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYE------LDSFPVRLLQMASFSFDVFAgdfARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 344 FQGDIRL----LMDDLKALRPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEaelrsgiirnnslwdKLIFhk 419
Cdd:cd17650 166 CPDEVKLdpaaLYDLILKSRITLMESTP----------------ALIRPVMAYVYRNGL---------------DLSA-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 iqsslggrVKLMITGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCC---LTVAGDWTAGHV--GAPMPCSLIKLV 492
Cdd:cd17650 213 --------MRLLIVGSDGCKAQDFKTLAARFGqgMRIINSYGVTEATIDSTyyeEGRDPLGDSANVpiGRPLPNTAMYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 493 DvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd17650 285 D-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 970702926 567 YIAPEKIENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDAET 607
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL 406
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
255-605 |
1.74e-17 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 87.33 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 255 GRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDC---SAFVKMTenvfiptPDDTLISFLPLAHMFervve 331
Cdd:PRK06814 780 GRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRaqvAARIDFS-------PEDKVFNALPVFHSF----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 332 ctmlchgakiGFFQGdirLLMDDLKALRPTVFP------VVPRLLnrmFDR----IFGqANTTLKRWL-----LDFASKR 396
Cdd:PRK06814 848 ----------GLTGG---LVLPLLSGVKVFLYPsplhyrIIPELI---YDTnatiLFG-TDTFLNGYAryahpYDFRSLR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 397 keaelrsgiirnnslwdklifhkiqsslggrvkLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWT 476
Cdd:PRK06814 911 ---------------------------------YVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNK 957
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 477 AGHVGAPMPCSLIKLVDVEEMNylaaKGeGEVCVKGPNVFQGYLKdpAKTAEVLD--KDGWLHTGDIGKWLPNGTLKIID 554
Cdd:PRK06814 958 AGTVGRLLPGIEYRLEPVPGID----EG-GRLFVRGPNVMLGYLR--AENPGVLEppADGWYDTGDIVTIDEEGFITIKG 1030
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 970702926 555 RKKHIFKLAqGEYIAPEKIENIYLRSEPvaqvfvhgESLQAfliAIVVPDA 605
Cdd:PRK06814 1031 RAKRFAKIA-GEMISLAAVEELAAELWP--------DALHA---AVSIPDA 1069
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
181-588 |
1.85e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 86.15 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 181 LGTEAITYIINKAELSLVFVDkPEKANLLLDGVEnkLIPGLKTIVLMDsfgssllEQGQKCGVEIISMKALEDL---GRA 257
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIDV-------DDPEYPGGRFIGALDYEAFlasGDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 258 NRQkPKPPAPE-DIAVICFTSGTTGNPKGAVITHR----NVVSDCSAFVKMTENVFIPTpddtlisfLPLAHmfervveC 332
Cdd:PRK08162 172 DFA-WTLPADEwDAIALNYTSGTTGNPKGVVYHHRgaylNALSNILAWGMPKHPVYLWT--------LPMFH-------C 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 333 TMLCH--------GAKIGFFQGDIRLLMDDLKALRPTVF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAEL 401
Cdd:PRK08162 236 NGWCFpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEW 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 402 RSGIirnnslwdklifhkiqsslGGRVKLMITGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLTVAGdWTA-- 477
Cdd:PRK08162 292 RAGI-------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlp 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 478 --------GHVGAPMPC-SLIKLVDVEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLP 546
Cdd:PRK08162 350 lderaqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHP 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 970702926 547 NGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFV 588
Cdd:PRK08162 429 DGYIKIKDRSKDII-ISGGENISSIEVEDVLYRHPAVLVAAV 469
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-615 |
2.36e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 85.95 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 -------DKPEkanlLLDGVENKLIPGLKTIVLMDSFGSSLLEQGQKCGVEIISMKALEDLGRAnrqkPKPPAPEDIAVI 273
Cdd:PRK06164 114 wpgfkgiDFAA----ILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 274 CFT-SGTTGNPK------GAVITHRNVVSDCSAFvkmtenvfipTPDDTLISFLPLAHMFErvveCTMLchgakIGFFQG 346
Cdd:PRK06164 186 LFTtSGTTSGPKlvlhrqATLLRHARAIARAYGY----------DPGAVLLAALPFCGVFG----FSTL-----LGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 DIRLLMDDlkalrptVF--PVVPRLL-----------NRMFDRIFGQANTTLkrwllDFASKRKeaelrsgiirnnslwd 413
Cdd:PRK06164 247 GAPLVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSARL---------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 414 klifhkiqsslggrvkLMITGAAPVSATVLTFLRAAlGCQFYEGYGQTECTA-GCCLTVAGDWTAGHV--GAPM-PCSLI 489
Cdd:PRK06164 299 ----------------FGFASFAPALGELAALARAR-GVPLTGLYGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 490 KLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 569
Cdd:PRK06164 362 RARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVN 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 970702926 570 PEKIENIYLRSEPVAQVFVHGESLQ------AFLIAI--VVPDAETVGPWARKR 615
Cdd:PRK06164 441 PAEIEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
245-587 |
3.14e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 245 IISMKALEDLGRANRQKPKPPA---PEDIAVICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDTLISFLP 321
Cdd:PRK09274 148 LWGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGIEPGEIDLPTFP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 322 LahmfervvectMLCHGAKIGffqgdIRLLMDDLKALRP-TVFPvvprllNRMFDRIFGQANTTLkrwlldFASKrkeae 400
Cdd:PRK09274 224 L-----------FALFGPALG-----MTSVIPDMDPTRPaTVDP------AKLFAAIERYGVTNL------FGSP----- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 401 lrsgiirnnSLWDKLIFHKIQS--SLGGrVKLMITGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC------TAGCCLT 470
Cdd:PRK09274 271 ---------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiESREILF 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 471 VAGDWT---AGH-VGAPMPCSLIKLVDV--------EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--VLDKDG-- 534
Cdd:PRK09274 341 ATRAATdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdv 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 970702926 535 WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniylrSEPVAQVF 587
Cdd:PRK09274 421 WHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIF 462
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-606 |
7.44e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 83.86 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAG--VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DKPekANLLLDGVENKLIPglktivlmdsfgsslleqgqkcgveiismkALEDLGRANRQKPKPPAPEDIAVICFTSGTT 280
Cdd:cd12114 91 DGP--DAQLDVAVFDVLIL------------------------------DLDALAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 281 GNPKGAVITHR---NVVSDcsafvkMTENvFIPTPDDTLISFLPLAH------MFervvecTMLCHGAKIGFFQGDIR-- 349
Cdd:cd12114 139 GTPKGVMISHRaalNTILD------INRR-FAVGPDDRVLALSSLSFdlsvydIF------GALSAGATLVLPDEARRrd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 350 --LLMDDLKALRPTVFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSLwdKLIFHK---IQSSL 424
Cdd:cd12114 206 paHWAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL--RLVLLSgdwIPLDL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 GGRVKLMITGAAPVSatvltflraaLGcqfyegyGQTECTAGCCL----TVAGDWTAGHVGAPMPCSLIKLVDveemnyl 500
Cdd:cd12114 260 PARLRALAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLD------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 501 aAKGE-------GEVCVKGPNVFQGYLKDPAKTAE--VLDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:cd12114 316 -PRGRdcpdwvpGELWIGGRGVALGYLGDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIE 393
|
490 500 510
....*....|....*....|....*....|....*....
gi 970702926 570 PEKIENIYLRSEPVAQ--VFVHGESLQAFLIAIVVPDAE 606
Cdd:cd12114 394 LGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDND 432
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
7.51e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 84.08 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENvfipTPDDTLISFLPLAHMFERVVectmlCHGAKIgfFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEW----KTKDRILSWMPLTHDMGLIA-----FHLAPL--IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 DIRLLMddlkalrPT-VFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDKLIFHKIQSSLG 425
Cdd:cd05908 174 MNQYLM-------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 426 GRVKLMITGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCCLTVAGD------------------------- 474
Cdd:cd05908 228 SSIRMILNGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepevdkkd 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 475 ---WTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGkWLPNGTLK 551
Cdd:cd05908 308 secLTFVEVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLV 385
|
330 340 350
....*....|....*....|....*....|..
gi 970702926 552 IIDRKKHIFkLAQGEYIAPEKIENIYLRSEPV 583
Cdd:cd05908 386 ITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-610 |
1.07e-16 |
|
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: 83.14 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 201 DkpekanllldgvenklipglktivlmdsfgsslleqgqkcgveiismkaledlgranrqkpkppaPEDIAVICFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 281 GNPKGAVITHRNVVsdcsAFVKMTENVFipTPDD-------TLISF-LPLAHMFervveCTmLCHGAKIgffqgdirLLM 352
Cdd:cd12115 118 GRPKGVAIEHRNAA----AFLQWAAAAF--SAEElagvlasTSICFdLSVFELF-----GP-LATGGKV--------VLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 353 DDLKALrptvfpvvprllnrmfdrifgqanttlkrwlLDFASkRKEAELrsgIIRNNSLWDKLIFHkiqSSLGGRVKLMI 432
Cdd:cd12115 178 DNVLAL-------------------------------PDLPA-AAEVTL---INTVPSAAAELLRH---DALPASVRVVN 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 433 TGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVC 509
Cdd:cd12115 220 LAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELY 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 510 VKGPNVFQGYLKDPAKTAEVLDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPV 583
Cdd:cd12115 299 IGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGV 377
|
490 500 510
....*....|....*....|....*....|
gi 970702926 584 AQ--VFVHGESL-QAFLIAIVVPDAETVGP 610
Cdd:cd12115 378 REavVVAIGDAAgERRLVAYIVAEPGAAGL 407
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-610 |
1.66e-16 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 82.42 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAfvkmTENVFIPTPDDTLISFLPLAhmFERVVECTM--LCHGAkigf 343
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA----TAERYGLTPGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 344 fqgdiRLLMDDLKALRPtvfpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASKrkeaelrsgiirnnslwdklifhk 419
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT------------------------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 iQSSLGGRVKLMITGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLTVAGDWTAGH---VGAPMPCSLIKLV 492
Cdd:cd17649 207 -GDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 493 DvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--VLDKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 565
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 970702926 566 EYIAPEKIENIYLRSEPVAQVFVHGES--LQAFLIAIVVPDAETVGP 610
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLRAAAAQP 407
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-607 |
1.74e-16 |
|
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: 82.30 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMtenvFIPTPDDTLISFLPLAhmFERVV-ECTM-LCHGAKIGFF 344
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA----FDVGPGSRVLQFASPS--FDASVwELLMaLLAGATLVLA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGDIRL----LMDDLKALRPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdklifhki 420
Cdd:cd17652 166 PAEELLpgepLADLLREHRITHVTLPPAALAALPPD-------------------------------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qsSLGGRVKLMITGAAPVSATVLtflRAALGCQFYEGYGQTECTAgcCLTVAGDWTAGHV---GAPMPCSLIKLVDvEEM 497
Cdd:cd17652 202 --DLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTV--CATMAGPLPGGGVppiGRPVPGTRVYVLD-ARL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 498 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--VLDKDGWL-----HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 570
Cdd:cd17652 274 RPVPPGVPGELYIAGAGLARGYLNRPGLTAErfVADPFGAPgsrmyRTGDLARWRADGQLEFLGRADDQVKI-RGFRIEL 352
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 970702926 571 EKIENIYLRSEPVAQ--VFVHGESL-QAFLIAIVVPDAET 607
Cdd:cd17652 353 GEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVPAPGA 392
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
147-590 |
2.05e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.91 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 147 DQFIGIFAQNRPEW--VIIEQGCFAysMVVIPLYDTLGTEAITYIINKAELSLVFVD---KPEKANLLLDgvenklIPGL 221
Cdd:PRK05620 64 DQRVGSMMYNCAEHleVLFAVACMG--AVFNPLNKQLMNDQIVHIINHAEDEVIVADprlAEQLGEILKE------CPCV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 222 KTIVLMDSFGSSLLEQGQKCGVEIISMKALEDlGRANrQKPKPPAPEDIAV-ICFTSGTTGNPKGAVITHRNVVSDCSAF 300
Cdd:PRK05620 136 RAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRST-VYDWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLSL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 301 vkMTENVFIPTPDDTLISFLPLAHmfervvectMLCHGAKIGFFQGDIRLLMDDLKALRPTVFPVVprllnrmfdrifgq 380
Cdd:PRK05620 214 --RTTDSLAVTHGESFLCCVPIYH---------VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKII-------------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 381 aNTTLKRwlldfaskrkeaeLRSGIirnNSLWDKLIFHKIQSSlGGRVKL--MITGAAPVSATVLTFLRAALGCQFYEGY 458
Cdd:PRK05620 269 -ATAMPR-------------VAHGV---PTLWIQLMVHYLKNP-PERMSLqeIYVGGSAVPPILIKAWEERYGVDVVHVW 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 459 GQTECTA-GcclTVAGDwTAGHVGAP----------MPCSL-IKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKT 526
Cdd:PRK05620 331 GMTETSPvG---TVARP-PSGVSGEArwayrvsqgrFPASLeYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 527 ----------------AEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFVHG 590
Cdd:PRK05620 407 gggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
150-609 |
2.42e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 82.42 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 150 IGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDKPEKAnlLLDGVEnkliPGLKTIVLMDS 229
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAE--LLDGLD----PGVRVINVDSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 230 FGSSLLeqgqkcgveiismkaleDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSdcsAFVKMTENvFI 309
Cdd:PRK07867 131 AWADEL-----------------AAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS---AGVMLAQR-FG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 310 PTPDDTLISFLPLAHMFERVVE-CTMLCHGAKI---------GFfqgdirllMDDLKALRPTVFPVVPRLLNrmfdrifg 379
Cdd:PRK07867 190 LGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGKPLS-------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 380 qanttlkrWLLDFASKRKEAElrsgiirnNSLwdklifhkiqsslggRVKLMITGAAPVSATvltfLRAALGCQFYEGYG 459
Cdd:PRK07867 254 --------YVLATPERPDDAD--------NPL---------------RIVYGNEGAPGDIAR----FARRFGCVVVDGFG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 460 QTEctAGCCLTVAGDWTAGHVGAPMPCslIKLVDVE--------------EMNYLAAKGEgEVCVKGPNVFQGYLKDPAK 525
Cdd:PRK07867 299 STE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGFEGYYNDPEA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 526 TAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHGeslqafliaivVPDa 605
Cdd:PRK07867 374 DAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA-----------VPD- 439
|
....
gi 970702926 606 ETVG 609
Cdd:PRK07867 440 PVVG 443
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
150-626 |
4.16e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.99 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 150 IGIFAQNRPEwviIEQGCFAYSM---VVIPLYDTLGTEAITYIINKAELSLVFVDKP-----EKANLLLDGVENKLIPGL 221
Cdd:PLN03102 67 VSVLAPNTPA---MYEMHFAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 222 KTIVLMDSfgsslleqgqkcgVEIISMKALEDLGRANRQKPKPPA---------PEDIAVICFTSGTTGNPKGAVITHRN 292
Cdd:PLN03102 144 IFIHEIDF-------------PKRPSSEELDYECLIQRGEPTPSLvarmfriqdEHDPISLNYTSGTTADPKGVVISHRG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 293 V-VSDCSAFVKMTENVFiptpdDTLISFLPLAHmfervvectmlCHGAKIGF---FQGDIRLLMDDLKAlrPTVFPVVpr 368
Cdd:PLN03102 211 AyLSTLSAIIGWEMGTC-----PVYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMRHVTA--PEIYKNI-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 369 llnRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiiRNNSLwdklifhkIQSSLGGRVKLMITGAAPVSATVLTFLRa 448
Cdd:PLN03102 271 ---EMHNVTHMCCVPTVFNILL----------------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 449 aLGCQFYEGYGQTECTAGCCLTVAGD-WT------AGHVGAPMPCSLIKLVDVEEMNYLA-------AKGEGEVCVKGPN 514
Cdd:PLN03102 323 -LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADVDVKNKETqesvprdGKTMGEIVIKGSS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 515 VFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFV----H- 589
Cdd:PLN03102 402 IMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYPKVLETAVvampHp 479
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 970702926 590 --GESLQAFliaIVVPDAETvGPWARKRGF---EGSFEELCR 626
Cdd:PLN03102 480 twGETPCAF---VVLEKGET-TKEDRVDKLvtrERDLIEYCR 517
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
264-606 |
1.21e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 79.92 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPEDIAVICFTSGTTGNPKGAVITHRN------VVSDCSAFvkmtenvfipTPDDT-LISfLPLAH-----MFERvve 331
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAhlasaeGVLSLMPF----------TAQDSwLLS-LPLFHvsgqgIVWR--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 332 ctMLCHGAKIGFfqGDIRLLMDDLK-----ALRPTVfpvVPRLLNRmfdrifGQANTTLKRWLLdfaskrkeaelrsgii 406
Cdd:PRK09029 197 --WLYAGATLVV--RDKQPLEQALAgcthaSLVPTQ---LWRLLDN------RSEPLSLKAVLL---------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 407 rnnslwdklifhkiqsslGGRvklMItgaapvsATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAgDWTAGhVGAPMPC 486
Cdd:PRK09029 248 ------------------GGA---AI-------PVELTEQAEQQGIRCWCGYGLTEMASTVCAKRA-DGLAG-VGSPLPG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 487 SLIKLVDveemnylaakgeGEVCVKGPNVFQGYLKDpAKTAEVLDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK09029 298 REVKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGE 362
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 970702926 567 YIAPEKIENIYLRSEPVAQVFVhgeslqafliaIVVPDAE 606
Cdd:PRK09029 363 GIQPEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-576 |
2.48e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 79.47 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMtenvFIPTPDDTLISFLPLAHMFervvectmlchgakiGFFQG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 DIRLLMDDLkalrPTVF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDKLif 417
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDSL-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 418 hkiqsslggrvklmitgaapVSATVLTFLRAALgcqfYEGYGQTECTAgcCLTVAGDWTAGH---VGAPMPCSLIKLVDv 494
Cdd:PRK06334 316 --------------------YQEALKTFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVLIVS- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 495 EEMNYLAAKGE-GEVCVKGPNVFQGYL-KDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:PRK06334 369 EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEA 447
|
....
gi 970702926 573 IENI 576
Cdd:PRK06334 448 LESI 451
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-606 |
2.58e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 77.73 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 457 GYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAkGE-GEVCVKGPNVFQGYLKDPAKTAEVLdKDGW 535
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970702926 536 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyLRSEP-VAQVFVHG-------ESLQAflIAIVVPDAE 606
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAVIGvpdprwaQSVKA--IVVLKPGAS 293
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
266-610 |
2.72e-15 |
|
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: 78.67 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKmteNVFIPTPDDTLISFLPLAHMFER-VVECTMLCHGAKIGFF 344
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGDI-RLLMDDLKALRPTVFPVVPRLLNRMfdrifgqanttlkrwlldFASKRKEAELRSGIIRNNSLWDKLifhkiqss 423
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAM------------------LAHPDAAGPDLSSLRKCVSAGEAL-------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 424 lggrvklmitgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAK 503
Cdd:cd05958 226 ---------------PAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 504 GEGEVCVKGPNVFQgYLKDPAKTAEVldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPV 583
Cdd:cd05958 290 TIGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340 350
....*....|....*....|....*....|
gi 970702926 584 AQVFVHGESLQAFLI---AIVVPDAEtVGP 610
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVLRPG-VIP 394
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
252-605 |
3.18e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 78.93 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 252 EDLGRANRQKPKPPAPEDIAVIC---FTSGTTGNPKGAVITHRNVvsdcsAFVkMTENV--FIP--TPDDTLISFLPLAH 324
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFV-ITNHLadLMPgtTEQDASLVVAPLSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 325 MfERVVECTMLCHGAKIGFFQGDiRLLMDDLKAL----RPTVFPVVPrllnrmfdrifgqanTTLKRWLLDFASKRKEae 400
Cdd:PRK07470 218 G-AGIHQLCQVARGAATVLLPSE-RFDPAEVWALverhRVTNLFTVP---------------TILKMLVEHPAVDRYD-- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 401 lrsgiirnnslwdklifhkiQSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgcCLTV-------AG 473
Cdd:PRK07470 279 --------------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTG--NITVlppalhdAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 474 DWTAGHVGapmPCSL------IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPN 547
Cdd:PRK07470 333 DGPDARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDAR 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 970702926 548 GTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHGeslqafliaivVPDA 605
Cdd:PRK07470 408 GFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPDP 453
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
269-599 |
5.15e-15 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 78.14 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRnvvsDCSAFVKMTENVFIPTPDDTLISFLPLAHMFervvecTMLCHGAKIGFFQGDI 348
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHN----DYAYNVRASAEVCGLDQDTVYLAVLPAAHNF------PLACPGVLGTLLAGGR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 349 RLLMDDLKALrpTVFPVVPRllnrmfdriFGQANTTL-----KRWLlDFASKRKEAElrsgiirnnslwdklifhkiqSS 423
Cdd:cd05920 210 VVLAPDPSPD--AAFPLIER---------EGVTVTALvpalvSLWL-DAAASRRADL---------------------SS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 424 LggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTVAGD---WTAGHVGAPM-PCSLIKLVDvEEMN 498
Cdd:cd05920 257 L----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE---GlLNYTRLDDpdeVIIHTQGRPMsPDDEIRVVD-EEGN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 499 YLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYL 578
Cdd:cd05920 329 PVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLL 407
|
330 340
....*....|....*....|....*...
gi 970702926 579 RSEPVAQVFV-------HGESLQAFLIA 599
Cdd:cd05920 408 RHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
156-615 |
9.22e-15 |
|
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: 77.42 E-value: 9.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 156 NRPEWVIIEQGCFAYSMVVIplyDTLGTEAITYIINKAELSLVFVDKPEKANLLLDgvenKLIPGLKTIVLMDSFGSSll 235
Cdd:cd05929 34 AAAEGVWIADGVYIYLINSI---LTVFAAAAAWKCGACPAYKSSRAPRAEACAIIE----IKAAALVCGLFTGGGALD-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 236 eqgqkcgveiismkALEDLGRANRQKPKPPAPEDIA--VICFTSGTTGNPKGAVITHRNVvsdcsafvkmtenvfiPTPD 313
Cdd:cd05929 105 --------------GLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGLPGG----------------PPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 314 DTLISF-LPLAHMFERVVECTM-LCHGAKIGFFQGDIRL-----LMDDLKAL---------RPTVFPVVPRLLNRMFdri 377
Cdd:cd05929 155 DTLMAAaLGFGPGADSVYLSPApLYHAAPFRWSMTALFMggtlvLMEKFDPEeflrlieryRVTFAQFVPTMFVRLL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 378 fgqanttlkrwlldfasKRKEAElrsgiiRNNslWDklifhkiQSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEG 457
Cdd:cd05929 232 -----------------KLPEAV------RNA--YD-------LSSL----KRVIHAAAPCPPWVKEQWIDWGGPIIWEY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 458 YGQTECTAGCCLTvAGDWTA--GHVGAPMPcSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQgYLKDPAKTAEVLDKDGW 535
Cdd:cd05929 276 YGGTEGQGLTIIN-GEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 536 LHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG---ESLQAFLIAIVVP--------- 603
Cdd:cd05929 352 STLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQPapgadagta 430
|
490
....*....|..
gi 970702926 604 DAETVGPWARKR 615
Cdd:cd05929 431 LAEELIAFLRDR 442
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-590 |
2.66e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 76.08 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPL---YdtlgTEA-ITYIINKAELS 196
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLG--PGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrY----VEDeLRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 197 LVFVDK---PEKANLLLDgvenklIPGLKTIVLMDSFGSSLLEQGqkcGVEIISMKALEDLGRAnrqkPKPPAPEDIAVI 273
Cdd:PRK07798 103 ALVYERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 274 CfTSGTTGNPKGAVITHRNV-VSDCSAFVKMTENvFIPTPDDtlisflplahMFERVVECT-----MLC---HGAK---- 340
Cdd:PRK07798 170 Y-TGGTTGMPKGVMWRQEDIfRVLLGGRDFATGE-PIEDEEE----------LAKRAAAGPgmrrfPAPplmHGAGqwaa 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 341 -IGFFQGDIRLLMDDLKaLRPT-VFPVVPR-LLNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnnslwdklif 417
Cdd:PRK07798 238 fAALFSGQTVVLLPDVR-FDADeVWRTIEReKVNVIT--IVGDA---MARPLLDALEARGPYDL---------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 418 hkiqSSLggrvKLMITGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTVAGDWTAGHVGAP--MPCSLIKLVDv 494
Cdd:PRK07798 296 ----SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPRTVVLD- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 495 EEMNYLAAkGEGEVCV--KGPNVFQGYLKDPAKTAEVL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 569
Cdd:PRK07798 365 EDGNPVEP-GSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVF 442
|
490 500
....*....|....*....|..
gi 970702926 570 PEKIENIyLRSEP-VAQVFVHG 590
Cdd:PRK07798 443 PEEVEEA-LKAHPdVADALVVG 463
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-617 |
3.65e-14 |
|
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: 75.55 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMtenVFIPTPDDTLIsFLPLAhmFERVVE--CTMLCHGAKIgff 344
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKE---YGITSSDRVLQ-FASIA--FDVAAEeiYVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 qgdirllmddlkALRPtvfpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDKLIFHKIQSSL 424
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 GG--RVKLMITGAAPVSATVLTFLRAALG--CQFYEGYGQTECT--AGCCLTVAGDWTAGH---VGAPMPCSLIKLVDvE 495
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATiaATVCRLTQLTERNITsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 496 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 970702926 568 IAPEKIENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDAETVGPWARKRGF 617
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
255-626 |
1.12e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.38 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 255 GRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDTLISFLPLAhmFERVVECTM 334
Cdd:PRK12316 4681 GFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFS--FDGSHEGLY 4754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 335 --LCHGAkigffqgdiRLLMDDLKALRPtvfpvvprllNRMFDRIFGQANTTLkrwllDFASkrkeaelrsgiirnnSLW 412
Cdd:PRK12316 4755 hpLINGA---------SVVIRDDSLWDP----------ERLYAEIHEHRVTVL-----VFPP---------------VYL 4795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 413 DKLIFHKIQSSLGGRVKLMITG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLTVAGDWTAG----HVGAPMP 485
Cdd:PRK12316 4796 QQLAEHAERDGEPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLG 4874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 486 CSLIKLVDVEeMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE-----VLDKDG--WLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:PRK12316 4875 NRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDH 4953
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970702926 559 IFKLaQGEYIAPEKIEnIYLRSEP-------VAQVFVHGeslqAFLIAIVVPDAETVGPW-ARKRGFEGSFEELCR 626
Cdd:PRK12316 4954 QVKI-RGFRIELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPQDPALADAdEAQAELRDELKAALR 5023
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
432-598 |
1.36e-13 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 74.04 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 432 ITGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTVAG-DWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCV 510
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGmKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 511 K-GPN----VFQGYLKDPAKTAEVLDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQ 585
Cdd:cd05928 375 RvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVE 452
|
170 180
....*....|....*....|
gi 970702926 586 VFV-------HGESLQAFLI 598
Cdd:cd05928 453 SAVvsspdpiRGEVVKAFVV 472
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
420-632 |
2.73e-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: 72.60 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 IQSSLGG-RVKLM-ITGAA-PVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEE 496
Cdd:cd05974 191 IQQDLASfDVKLReVVGAGePLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 mnylAAKGEGEVCV-----KGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPE 571
Cdd:cd05974 271 ----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISPF 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970702926 572 KIENIYLRSEPVAQVFV----HGESLQAFLIAIVVPDAETVGPWARKRGFEGSFEELCRNKDVRK 632
Cdd:cd05974 345 ELESVLIEHPAVAEAAVvpspDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRR 409
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-608 |
5.69e-13 |
|
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: 71.66 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCsafVKMTENVFIPTPDDTLISFLPlAHMFERVVE--CTMLCHGAKIGFF 344
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLR---TSLSERYFGRDNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGDIRLLMDDLKAL----RPTVFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnnslwdkli 416
Cdd:cd17648 169 PDEMRFDPDRFYAYinreKVTYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV-------------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 417 FHKIQSSLGGRVklmITGAAPVSATVLTFLRaalgcqFYEGYGQTECTagccltvagdwtaghVGAPMPCSLIKLVDvEE 496
Cdd:cd17648 224 FEKLRSRFAGLI---INAYGPTETTVTNHKR------FFPGDQRFDKS---------------LGRPVRNTKCYVLN-DA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVL-------DKDGWL-------HTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:cd17648 279 MKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqtEQERARgrnarlyKTGDLVRWLPSGELEYLGRNDFQVKI 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 970702926 563 aQGEYIAPEKIENIYLRSEPVAQVFV--------HGESLQAFLIAIVVPDAETV 608
Cdd:cd17648 359 -RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-607 |
6.21e-13 |
|
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: 71.34 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 265 PAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFvkmtENVFIPTPDDTLISFLPLAHMFervvectmlchGAKIGff 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL----RQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 qgdirllmddLKALRPTVFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDKLIFHKIQSSL 424
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 G-GRVKLMITGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LTVAGDWTAGH----VGAPMPCSLIKL 491
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 492 VDVEEMNY--------LAAKGEGEVCVKGPNVFQGYLKDPAKTA--EVLDKDG--WLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd05910 277 IEIDDEPIaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 970702926 560 FKLAQGEYIapekieniylrSEPVAQVF-VHGESLQAFLIAIVVPDAET 607
Cdd:cd05910 357 VITTGGTLY-----------TEPVERVFnTHPGVRRSALVGVGKPGCQL 394
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-606 |
1.03e-12 |
|
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: 70.85 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 269 DIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVfiptPDDTLISFLPLAHMFERVVE-CTMLCHGAKIGF---F 344
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL----PSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 345 QGdiRLLMDDLKALRPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdklifHKIQSSL 424
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 425 GGRVKLMITGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGCCLTVAGDWTAGHVGA----PMPCSLIKlVDVEEMNY 499
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSGFINFFGKPGAIGRNPSllrkVAPLALVK-YDLESGEP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 500 L---------AAKGE-----GEVCVKGPnvFQGYLkDPAKTAEVL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd05940 272 IrdaegrcikVPRGEpglliSRINPLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDT 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 970702926 560 FKLaQGEYIAPEKIENIYLRSEPVAQVFVHGESL-----QAFLIAIVVPDAE 606
Cdd:cd05940 349 FRW-KGENVSTTEVAAVLGAFPGVEEANVYGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-615 |
1.14e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 71.11 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRpEWVIIEQGCFAYSMVVIPLYDT-LGTEAITYIINKAELSLVF 199
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVR--AGDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 200 VDkpEKANLLLDGVENKLiPGLKTIVlmdsfGSSLLEQGQKCGVEiismkALEDLGRANRQKPKPPAPEDIAVICFTSGT 279
Cdd:PRK07788 152 YD--DEFTDLLSALPPDL-GRLRAWG-----GNPDDDEPSGSTDE-----TLDDLIAGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 280 TGNPKGAVITHRNVVSDCSAFV-----KMTENVFIPTPddtlisflplahMFervvectmlcHG-----AKIGFFQG--- 346
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPAP------------MF----------HAtgwahLTLAMALGstv 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 347 ------DIRLLMDDLKALRPTVFPVVPRLLNRMFDrifgqanttlkrwLLDFASKRKEAelrsgiirnnslwdklifhki 420
Cdd:PRK07788 277 vlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT--------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGcclTVAG--DWTA--GHVGAPMPCSLIKLVDvEE 496
Cdd:PRK07788 323 -SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFA---TIATpeDLAEapGTVGRPPKGVTVKILD-EN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAevldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 576
Cdd:PRK07788 394 GNEVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDL 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 970702926 577 YLRSEPVAQVFVHG---ESLQAFLIAIVVP------DAETVGPWARKR 615
Cdd:PRK07788 469 LAGHPDVVEAAVIGvddEEFGQRLRAFVVKapgaalDEDAIKDYVRDN 516
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-605 |
3.47e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 69.25 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 429 KLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEctaGCCLTVAGDWTAGHV----GAPM-PCSLIKLVDvEEMNYLAAK 503
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GLVNYTRLDDSDERIfttqGRPMsPDDEVWVAD-ADGNPLPQG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 504 GEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIYLR 579
Cdd:PRK10946 379 EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLR 453
|
170 180
....*....|....*....|....*.
gi 970702926 580 sepvaqvfvHGESLQAFLIAIvvPDA 605
Cdd:PRK10946 454 ---------HPAVIHAALVSM--EDE 468
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-627 |
4.20e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.95 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 112 RKPDQPY-------EWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTE 184
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLK--RGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 185 AITYIINKAELSLVF--VDKPEKANLLLdgvenKLIPGLKTIVLMDSFGSSlleqgqkcgveiismKALEDLGRANRQKP 262
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDGEL---------------EGFVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 263 KPPAPEDI--AVICFTSGTTGNPKGavithrnvvsdcsafvkmtenVFIPTPDDTLISFLPLAHMFERVV----ECTMLC 336
Cdd:PRK13391 147 ATPIADESlgTDMLYSSGTTGRPKG---------------------IKRPLPEQPPDTPLPLTAFLQRLWgfrsDMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 337 -----HGAKIGFFQGDIRL-----LMDDLKA---------LRPTVFPVVPRllnrMFDRIFGQANTTLKRWLLdfaskrk 397
Cdd:PRK13391 206 paplyHSAPQRAVMLVIRLggtviVMEHFDAeqylalieeYGVTHTQLVPT----MFSRMLKLPEEVRDKYDL------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 398 eaelrsgiirnnslwdklifhkiqSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTVAGDWTA 477
Cdd:PRK13391 275 ------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 478 --GHVGAPMpCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQgYLKDPAKTAEVLDKDG-WLHTGDIGKWLPNGTLKIID 554
Cdd:PRK13391 326 hpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTD 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970702926 555 RKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG---ESLQAFLIAIVVPdAETVGPWArkrGFEGSFEELCRN 627
Cdd:PRK13391 403 RAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFGvpnEDLGEEVKAVVQP-VDGVDPGP---ALAAELIAFCRQ 473
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
265-608 |
8.04e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.03 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 265 PAPEDIAVICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDTLISFLPLAhmFERVVECTM--LCHGAKIG 342
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 343 FFQGDIRL----LMDDLKALRPTVFPVVPRLLNRMFDRIFGQAN-TTLKRWLldfaskrkeaelrsgiirnnslwdklif 417
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHpLSLRRVV---------------------------- 1840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 418 hkiqssLGGRvklmitgAAPVSATVLTFlrAALG-CQFYEGYGQTECTAGCCLtvagdWTAGH----------VGAPMPC 486
Cdd:PRK12467 1841 ------CGGE-------ALEVEALRPWL--ERLPdTGLFNLYGPTETAVDVTH-----WTCRRkdlegrdsvpIGQPIAN 1900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 487 SLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--VLDKDGWL-----HTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK12467 1901 LSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAErfVADPFGTVgsrlyRTGDLARYRADGVIEYLGRIDHQ 1979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 970702926 560 FKLaQGEYIAPEKIENiYLRSEPV---AQVFVHGESLQAFLIAIVVPDAETV 608
Cdd:PRK12467 1980 VKI-RGFRIELGEIEA-RLREQGGvreAVVIAQDGANGKQLVAYVVPTDPGL 2029
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-606 |
1.32e-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: 67.19 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFvkmtENVFIPTPDD-----TLISFLPLA-HMFervvecTMLCHGAK 340
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH----RPYFGVTPADkslvyASFSFDASAwEIF------PHLTAGAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 341 IGFFQGDIRLlmdDLKALrptvfpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdklifhki 420
Cdd:cd17645 173 LHVVPSERRL---DLDAL----------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL--------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 421 qsslggrvKLMITGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEMNYL 500
Cdd:cd17645 218 --------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 501 AAKG-EGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:cd17645 283 QPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEI 361
|
330 340 350
....*....|....*....|....*....|....*.
gi 970702926 574 ENIYLRSEPV---AQVFVHGESLQAFLIAIVVPDAE 606
Cdd:cd17645 362 EPFLMNHPLIelaAVLAKEDADGRKYLVAYVTAPEE 397
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
245-607 |
1.61e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 67.27 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 245 IISMKALeDLGRANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDC----SAFVKMTENVfiPTPDDTLISFL 320
Cdd:PRK05850 138 VIEVDLL-DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 321 PLAHMFERV--VECTMLC-HGAK----IGFFQGDIRLLmdDLKALRPTVFPVVPrllNRMFdrifgqanttlkrwllDFA 393
Cdd:PRK05850 215 PFYHDMGLVlgVCAPILGgCPAVltspVAFLQRPARWM--QLLASNPHAFSAAP---NFAF----------------ELA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 394 SKRKEAELRSGIirnnslwdklifhkiqsSLGGrVKLMITGAAPV-SATVLTFLR--AALGcqFYE-----GYGQTECTa 465
Cdd:PRK05850 274 VRKTSDDDMAGL-----------------DLGG-VLGIISGSERVhPATLKRFADrfAPFN--LREtairpSYGLAEAT- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 466 gccLTVA-GDW--------------TAGHV--------------GAPMPcSLIKLVDVEEMNYLAAKGEGEVCVKGPNVF 516
Cdd:PRK05850 333 ---VYVAtREPgqppesvrfdyeklSAGHAkrcetgggtplvsyGSPRS-PTVRIVDPDTCIECPAGTVGEIWVHGDNVA 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 517 QGYLKDPAKT-----AEVLDK-----DG-WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENiylrsepVAQ 585
Cdd:PRK05850 409 AGYWQKPEETertfgATLVDPspgtpEGpWLRTGDLG-FISEGELFIVGRIKDLL-IVDGRNHYPDDIEA-------TIQ 479
|
410 420
....*....|....*....|..
gi 970702926 586 VFVHGEslqafLIAIVVPDAET 607
Cdd:PRK05850 480 EITGGR-----VAAISVPDDGT 496
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
264-574 |
1.62e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.34 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVfipTPDDTLISFLPLAH-MfervvectmlchgAKIG 342
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKV---RPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 343 FFQGDI--RLLMDDLK----ALRPTVFPvvpRLLNR-----MFDRIFG------------QANTTLKRW----------- 388
Cdd:PRK09192 236 FLLTPVatQLSVDYLPtrdfARRPLQWL---DLISRnrgtiSYSPPFGyelcarrvnskdLAELDLSCWrvagigadmir 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 389 ---LLDFASK------RKEAELRSGIIRNNSLwdKLIFHKIQSslGGRVKLmitgaapVSATVLTFLRAALGCQfyEGYG 459
Cdd:PRK09192 313 pdvLHQFAEAfapagfDDKAFMPSYGLAEATL--AVSFSPLGS--GIVVEE-------VDRDRLEYQGKAVAPG--AETR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 460 QTECTAGCcltvagdwtaghvGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAkTAEVLDKDGWLHTG 539
Cdd:PRK09192 380 RVRTFVNC-------------GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTG 444
|
330 340 350
....*....|....*....|....*....|....*
gi 970702926 540 DIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09192 445 DLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
263-597 |
1.88e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.18 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 263 KPPAPE--DIAvICFTSGTTGNPKGAVITHRnvvsdcSAFVKMTENVFIPTPDDTLISF--LPLAHmfervveCTMLCHG 338
Cdd:PLN02479 189 KPPADEwqSIA-LGYTSGTTASPKGVVLHHR------GAYLMALSNALIWGMNEGAVYLwtLPMFH-------CNGWCFT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 339 AKIGFFQG-DIRLLMDDLKALRP-------TVFPVVPRLLNRMFDrifgqanttlkrwlldfaSKRKEAELrsgiirnns 410
Cdd:PLN02479 255 WTLAALCGtNICLRQVTAKAIYSaianygvTHFCAAPVVLNTIVN------------------APKSETIL--------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 411 lwdklifhkiqsSLGGRVKLMITGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAGCCLTVA--GDW------TAGHVGA 482
Cdd:PLN02479 308 ------------PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGPSTVCAwkPEWdslppeEQARLNA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 483 PMPCSLIKL-----VDVEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PLN02479 373 RQGVRYIGLegldvVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDR 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 970702926 556 KKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFL 597
Cdd:PLN02479 452 SKDII-ISGGENISSLEVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
184-576 |
2.00e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 67.04 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 184 EAITYIINKAELSLVFVD---KPekanlLLDGVENKLiPGLKTIVLM-DSfgsslleqgQKCGVEIISMKALEDL-GRAN 258
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMtDA---------AHLPAGSTPLLCYETLvGAQD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 259 RQKPKPPAPEDIAV-ICFTSGTTGNPKGAVITHRNVVsdCSAFVKMTENVFIPTPDDTLisfLPLAHMFErvVECTMLCH 337
Cdd:PRK07008 166 GDYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 338 -----GAKIgFFQG---DIRLLMDDLKALRPTVFPVVPR----LLNRMfdrifgqanttlkrwlldfaskrKEAELRSGI 405
Cdd:PRK07008 239 sapltGAKL-VLPGpdlDGKSLYELIEAERVTFSAGVPTvwlgLLNHM-----------------------REAGLRFST 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 406 IRnnslwdklifhkiqsslggrvKLMITGAAPVSATVLTFlRAALGCQFYEGYGQTECT---AGCCLTVAGDWTA----- 477
Cdd:PRK07008 295 LR---------------------RTVIGGSACPPAMIRTF-EDEYGVEVIHAWGMTEMSplgTLCKLKWKHSQLPldeqr 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 478 ------GHV--GAPMpcsliKLVDVE--EMNYlAAKGEGEVCVKGPNVFQGYLKdpaKTAEVLDkDGWLHTGDIGKWLPN 547
Cdd:PRK07008 353 kllekqGRViyGVDM-----KIVGDDgrELPW-DGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDAD 422
|
410 420
....*....|....*....|....*....
gi 970702926 548 GTLKIIDRKKHIFKlAQGEYIAPEKIENI 576
Cdd:PRK07008 423 GFMQITDRSKDVIK-SGGEWISSIDIENV 450
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
422-606 |
2.52e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 66.47 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 422 SSLggrvKLMITGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLTVAGDWTA--GHVGAPMpCSLIKLVDvEE 496
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAV-LGEVRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 497 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
170 180 190
....*....|....*....|....*....|.
gi 970702926 576 IYLRSEPVAQVFVHGeslqafliaivVPDAE 606
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
184-590 |
3.84e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 65.93 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 184 EAITYIINKAELSLVFVDK---PekanlLLDGVENKLiPGLKTIVLMDsfGSSLLEQgqkcgVEIISMKALED-LGRANR 259
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVVLT--DAAHMPQ-----TTLKNAVAYEEwIAEADG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 260 QKPKPPAPEDIAV-ICFTSGTTGNPKGAVITHR-NVVSdcsAFVKMTENVFIPTPDDTLISFLPLAH-------MFERVV 330
Cdd:PRK06018 168 DFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHRsNVLH---ALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAPSM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 331 ECTMLCHGAKIGffQGDIRLLMDDLK----ALRPTVfpvvprllnrmfdrifgqanttlkrWLLDFASKRKEAElrsgii 406
Cdd:PRK06018 245 GTKLVMPGAKLD--GASVYELLDTEKvtftAGVPTV-------------------------WLMLLQYMEKEGL------ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 407 rnnslwdKLIFHKiqsslggrvKLMITGAAPVSATVLTFLRaaLGCQFYEGYGQTECTA-GcclTVAG------------ 473
Cdd:PRK06018 292 -------KLPHLK---------MVVCGGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPlG---TLAAlkppfsklpgda 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 474 --DWTAGHVGAPMPCSLiKLVDvEEMNYLAAKGE--GEVCVKGPNVFQGYLKdpaKTAEVLDKDGWLHTGDIGKWLPNGT 549
Cdd:PRK06018 351 rlDVLQKQGYPPFGVEM-KITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 970702926 550 LKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFVHG 590
Cdd:PRK06018 426 MRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
114-626 |
1.24e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 64.26 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 114 PDQPY-------EWLSYKQVEEMSECVGSGLIQKGFKaaPDQFIGIFAQNRPE-----WVIIEQGcfaysmvvipLYDTl 181
Cdd:PRK13390 11 PDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLR--TGDVVALLSDNSPEalvvlWAALRSG----------LYIT- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 182 gteAITYIINKAELSLVFVDKPEK---ANLLLDGVENKLIPGLKtivLMDSFGSslleqgqkcgvEIISMKALEdlgrAN 258
Cdd:PRK13390 78 ---AINHHLTAPEADYIVGDSGARvlvASAALDGLAAKVGADLP---LRLSFGG-----------EIDGFGSFE----AA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 259 RQKPKPPAPEDI--AVICFTSGTTGNPKGAV--ITHRNVVSDCSAFVKMTENVFIPTPDDTLISFLPLAHMfERVVECTM 334
Cdd:PRK13390 137 LAGAGPRLTEQPcgAVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHA-APLRWCSM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 335 LcH---GAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskRKEAELRSgiirnnsL 411
Cdd:PRK13390 216 V-HalgGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT-------R 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 412 WDklifhkiQSSLGGrvklMITGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTVAGDWTA--GHVGAPMPCSLi 489
Cdd:PRK13390 267 YD-------VSSLRA----VIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDL- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 490 KLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 567
Cdd:PRK13390 334 HICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVN 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970702926 568 IAPEKIENIYLRSEPVAQVFVHGeslqafliaivVPDAEtVGPWARK-----RGFEGSfEELCR 626
Cdd:PRK13390 412 IYPQETENALTMHPAVHDVAVIG-----------VPDPE-MGEQVKAviqlvEGIRGS-DELAR 462
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
261-614 |
1.25e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.64 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 261 KPKPPAPEDIAVIcFTSGTTGNPKGAVITHRNvvsdcsafvkmtenvFIPTPD---------------DTLISFLPLAHM 325
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRT---------------FFAVPDilqkeglnwvtwvvgETTYSPLPATHI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 326 --FERVVECTMlcHGAKIGFFQGDIRLLMDDLKALRPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRS 403
Cdd:PRK05857 227 ggLWWILTCLM--HGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLV------------------------SELKS 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 404 GIIRNNSLwdklifhkiqsslggrvKLMITGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCCLTVAGDWT---AG 478
Cdd:PRK05857 281 ANATVPSL-----------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 479 HVGAPMPCSLIKLVDVEEMNYLAAKGE-----GEVCVKGPNVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PRK05857 343 AVGRPYPGVDVYLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIK 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970702926 554 DRKKHIFkLAQGEYIAPEKIENIylrSEPVAQVF------VHGESLQAFLIAIVVPDAETVGPWARK 614
Cdd:PRK05857 422 GRSSEMI-ICGGVNIAPDEVDRI---AEGVSGVReaacyeIPDEEFGALVGLAVVASAELDESAARA 484
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
113-638 |
1.83e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 63.76 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 113 KPDQP-YEWL----SYKQVEEMSECVGSGLIQKGF-KAAPdqfIGIFAQNRPEWVI-----IEQGCfAYsmvvIPLYDTL 181
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLpDKSP---IIVFGHMSPEMLAtflgaVKAGH-AY----IPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 182 GTEAITYIINKAELSLVF--VDKPekanllldgVENKLIPGLKTIVLMDSFgsslleqgqKCGVEIISMKALEDlgranr 259
Cdd:PRK04813 87 PAERIEMIIEVAKPSLIIatEELP---------LEILGIPVITLDELKDIF---------ATGNPYDFDHAVKG------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 260 qkpkppapEDIAVICFTSGTTGNPKGAVITHRNVVS----DCSAFVKMTENVFIPTPddtLISFlPLAHMFerVVECtmL 335
Cdd:PRK04813 143 --------DDNYYIIFTSGTTGKPKGVQISHDNLVSftnwMLEDFALPEGPQFLNQA---PYSF-DLSVMD--LYPT--L 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 336 CHGAKIGFFQGDI----RLLMDDLKALRPTVFPVVPR-----LLNRMFDrifGQANTTLKRWLLDfaskrKEaELRsgii 406
Cdd:PRK04813 207 ASGGTLVALPKDMtanfKQLFETLPQLPINVWVSTPSfadmcLLDPSFN---EEHLPNLTHFLFC-----GE-ELP---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 407 rnnslwdklifHKIQSSLGGRVklmitgaaPvSATVltflraalgcqfYEGYGQTECTagccltVAgdWTAGH------- 479
Cdd:PRK04813 274 -----------HKTAKKLLERF--------P-SATI------------YNTYGPTEAT------VA--VTSIEitdemld 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 480 ------VGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVL-DKDGW--LHTGDIGKwLPNGTL 550
Cdd:PRK04813 314 qykrlpIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLL 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 551 KIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVAQVFV----HGESLQAfLIAIVVPDaetvgpwarkrgfEGSFEelcR 626
Cdd:PRK04813 392 FYQGRIDFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVPK-------------EEDFE---R 453
|
570
....*....|..
gi 970702926 627 NKDVRKAILEDM 638
Cdd:PRK04813 454 EFELTKAIKKEL 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
98-606 |
2.20e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.59 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 98 RGMrVSNNGACLGSRKPDQPYEW------LSYKQVEEMSECVGSGLIQKGFKAAPDQFIGIFAQ------------NRPE 159
Cdd:PRK12316 3018 RGM-VENPQRSVDELAMLDAEERgqlleaWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEqrlsyaelnrraNRLA 3096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 160 WVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDKPEKANLLLDGVENKLIPGLKTivlmdsfgSSLLEQGQ 239
Cdd:PRK12316 3097 HRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS--------QSHLRLPL 3168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 240 KCGVEIISMKA-LEDLGRANrqKPKPPAPEDIAVICFTSGTTGNPKGAVITHrnvvSDCSAFVKMTENVFIPTPDDTLIS 318
Cdd:PRK12316 3169 AQGVQVLDLDRgDENYAEAN--PAIRTMPENLAYVIYTSGSTGKPKGVGIRH----SALSNHLCWMQQAYGLGVGDRVLQ 3242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 319 FLPLAHMFERVVECTMLCHGAKIgffqgdirllmddlkALRPTVFPVVPRLLNRMFDRifGQANTTLKRWlldfaskrke 398
Cdd:PRK12316 3243 FTTFSFDVFVEELFWPLMSGARV---------------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------- 3295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 399 aelrsgiirnnSLWDKLIFHKIQSSLGGrVKLMITGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLTVAGDWTAG 478
Cdd:PRK12316 3296 -----------SMLQAFLEEEDAHRCTS-LKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 479 H--VGAPMPCSLIKLVDVeEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGW------LHTGDIGKWLPNGTL 550
Cdd:PRK12316 3362 AvpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVI 3440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 970702926 551 KIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAfLIAIVVPDAE 606
Cdd:PRK12316 3441 EYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
264-606 |
2.37e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.56 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPEDIAVIcFTSGTTGNPKGavithrnvvsdcsafVKMtenvFIPTPDDTLISFLPLAHMF-----ERVVECTMLCHG 338
Cdd:PRK12406 149 PPVPQPQSMI-YTSGTTGHPKG---------------VRR----AAPTPEQAAAAEQMRALIYglkpgIRALLTGPLYHS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 339 AKIGFFQGDIRL-----LM-----DDLKAL----RPTVFPVVPRllnrMFDRifgqanttlkrwLLDFASKRKEAelrsg 404
Cdd:PRK12406 209 APNAYGLRAGRLggvlvLQprfdpEELLQLierhRITHMHMVPT----MFIR------------LLKLPEEVRAK----- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 405 iirnnslWDklifhkiQSSLggrvKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgccLTVAG--DWTA--GHV 480
Cdd:PRK12406 268 -------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGA---VTFATseDALShpGTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 481 GAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNV--FQgYLKDPAKTAEVlDKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:PRK12406 327 GKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRD 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 970702926 559 IFkLAQGEYIAPEKIENIYLRSEPVAQVFVHGeslqafliaivVPDAE 606
Cdd:PRK12406 404 MV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFG-----------IPDAE 439
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
250-586 |
5.73e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 62.48 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 250 ALEDL---GRANRQKPKPPAP-EDIAVICFTSGTTGNPKGAVITHRNVVSDCSAfvkMTENVFIPTPDDTLISFLPLAHM 325
Cdd:PRK05851 130 TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRG---LNARVGLDAATDVGCSWLPLYHD 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 326 FERVVECTMLCHGAKIGffqgdirllmddlkaLRPT-VFPVVP-RLLNrmfdrifgqanttlkrWLLDF-ASKRKEAELR 402
Cdd:PRK05851 207 MGLAFLLTAALAGAPLW---------------LAPTtAFSASPfRWLS----------------WLSDSrATLTAAPNFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 403 SGIIRNNSlwdklifHKIQSSLGGRVKLMITGAAPVSATVLT-FLRAALGCQFYEG-----YGQTECTagCCLTV----- 471
Cdd:PRK05851 256 YNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAEST--CAVTVpvpgi 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 472 ----------AGDWTAGH--VGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAktaevLDKDGWLHTG 539
Cdd:PRK05851 327 glrvdevttdDGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTG 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 970702926 540 DIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIylrsepVAQV 586
Cdd:PRK05851 402 DLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
112-614 |
9.87e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.49 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 112 RKPDQPY-----EWLSYKQVEEMSECVGSGLIQKGfkAAPDQFIGIfAQNRPewviIEqgcfaysmVVIPLYDTLgteai 186
Cdd:PRK12467 3107 RTPEAPAlvfgdQQLSYAELNRRANRLAHRLIAIG--VGPDVLVGV-AVERS----VE--------MIVALLAVL----- 3166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 187 tyiinKAELSLVFVDKPEKANLLLDGVENKlipGLKTIVLMdsfgSSLLEQ-GQKCGVEIISMkaleDLGRANRQKPKPP 265
Cdd:PRK12467 3167 -----KAGGAYVPLDPEYPRERLAYMIEDS---GVKLLLTQ----AHLLEQlPAPAGDTALTL----DRLDLNGYSENNP 3230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 A----PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPLAhmFERVVE--CTMLCHGA 339
Cdd:PRK12467 3231 StrvmGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYE----LDANDRVLLFMSFS--FDGAQErfLWTLICGG 3304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 340 KIGFFQGDIRllmdDLKALRptvfpvvpRLLNRmfDRIfgqanTTlkrwlLDFASkrkeaelrsgiirnNSLWDKLIFHK 419
Cdd:PRK12467 3305 CLVVRDNDLW----DPEELW--------QAIHA--HRI-----SI-----ACFPP--------------AYLQQFAEDAG 3346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 IQSslGGRVKLMITGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCL-TVAGDWTAGHVGAPMPCSLIKL---VDV 494
Cdd:PRK12467 3347 GAD--CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLD 3424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 495 EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:PRK12467 3425 GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFR 3503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 970702926 568 IAPEKIENIYLRSEPVAQVFVHGESLQA--FLIAIVVPDAETvGPWARK 614
Cdd:PRK12467 3504 IELGEIEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWRET 3551
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
244-585 |
1.11e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.11 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 244 EIISMKALEDLGRANRQKPKPPaPEDIAVICFTSGTTGNPKGAVITHRNVVSDcSAFVKMTENVFIpTPDDTLISFLPLA 323
Cdd:PRK05691 143 ELLCVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVAN-EQLIRHGFGIDL-NPDDVIVSWLPLY 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 324 HmfervvectmlchgaKIGFFQGdirllmddlkALRPtVFPVVPRLLnrMFDRIFGQANTtlkRWLldfaskrkEA--EL 401
Cdd:PRK05691 220 H---------------DMGLIGG----------LLQP-IFSGVPCVL--MSPAYFLERPL---RWL--------EAisEY 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 402 RSGIIRNNSLWDKLIFHKI-QSSLGG----RVKLMITGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECTagccLT 470
Cdd:PRK05691 261 GGTISGGPDFAYRLCSERVsESALERldlsRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEAT----LF 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 471 VAG------------DWTA----------GHV----GAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPA 524
Cdd:PRK05691 337 VSGgrrgqgipalelDAEAlarnraepgtGSVlmscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPE 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970702926 525 KTAEV-LDKDG--WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQ 585
Cdd:PRK05691 417 ASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
273-604 |
4.30e-09 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 58.57 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 273 ICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDTLISFLPLAH-MFERVVECTMLCHGAKIGFFQGDIRLL 351
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 352 MDDLKALRPTVFPVVPRLLNRMfdrifgqANTtlkrwlldfasKRKEAELRSgIIRNNSLWDKLIFHKIQSslggrvklm 431
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQAL-------ART-----------LEPESKIKS-IFSSGQKLFESTKKKLKN--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 432 itgAAPVSatvltflraalgcQFYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVEEmnylaaKGEGEVCVK 511
Cdd:cd17633 133 ---IFPKA-------------NLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 512 GPNVFQGYLKdpaktAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHGE 591
Cdd:cd17633 191 SEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
330
....*....|....*.
gi 970702926 592 SLQAF---LIAIVVPD 604
Cdd:cd17633 265 PDARFgeiAVALYSGD 280
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
257-598 |
9.32e-09 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 58.30 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 257 ANRQKpkppAPEDIAVICFTSGTTGNPKGAVITHRNVVsdcsAFVKMTENVFIPTPDDtliSFLPLAhmfervvectmlc 336
Cdd:cd05973 81 ANRHK----LDSDPFVMMFTSGTTGLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAA------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 337 hgaKIGFFQGDIRLLMDDLKALRPTVF---PVVPRLLNRMFDRiFG----QANTTLKRWLLdfaSKRKEAELRsgiirnn 409
Cdd:cd05973 137 ---DPGWAYGLYYAITGPLALGHPTILlegGFSVESTWRVIER-LGvtnlAGSPTAYRLLM---AAGAEVPAR------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 410 slwdklifhkiqssLGGRVKLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTagccLTVAGDWTAGHV------GAP 483
Cdd:cd05973 203 --------------PKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELG----MVLANHHALEHPvhagsaGRA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 484 MPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNV----FQGYLKDPAKTAEvldkDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd05973 265 MPGWRVAVLD-DDGDELGPGEPGRLAIDIANSplmwFRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRADDV 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 970702926 560 FKLAqGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFLI 598
Cdd:cd05973 340 ITMS-GYRIGPFDVESALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
250-341 |
1.56e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 57.96 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 250 ALEDLGRANRQKPKPPAP-------EDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTEnvfiPTPDDTLISFLPL 322
Cdd:PRK08279 174 GYEDLAAAAAGAPTTNPAsrsgvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPL 249
|
90 100
....*....|....*....|
gi 970702926 323 AH-MFERVVECTMLCHGAKI 341
Cdd:PRK08279 250 YHnTGGTVAWSSVLAAGATL 269
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
150-610 |
2.72e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.96 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 150 IGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLVFVDKPEKAnlLLDGVEnklIPGLkTIVLMDS 229
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGV-RVLDVDT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 230 fgsslleqgqkcgveiisMKALEDLGRANRQKP-KPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAfvkMTENvF 308
Cdd:PRK13388 129 ------------------PAYAELVAAAGALTPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRA---LTER-F 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 309 IPTPDDTLISFLPLAH----MFERVVectMLCHGAKI---------GFfqgdirllMDDLKALRPTVFPVVPRLL----- 370
Cdd:PRK13388 187 GLTRDDVCYVSMPLFHsnavMAGWAP---AVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayila 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 371 --NRMFDrifgqANTTLKRWLLDFASKRKEAElrsgiirnnslwdklifhkiqsslggrvklmitgaapvsatvltFLRA 448
Cdd:PRK13388 256 tpERPDD-----ADNPLRVAFGNEASPRDIAE--------------------------------------------FSRR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 449 aLGCQFYEGYGQTEctAGCCLTVAGDWTAGHVGAPMPCslIKLVDVEEM---------------NYLAAKGEgEVCVKGP 513
Cdd:PRK13388 287 -FGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAPG--VAIYNPETLtecavarfdahgallNADEAIGE-LVNTAGA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 514 NVFQGYLKDPAKTAEVLdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHG--- 590
Cdd:PRK13388 361 GFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpd 438
|
490 500
....*....|....*....|.
gi 970702926 591 -ESLQAFLIAIVVPDAETVGP 610
Cdd:PRK13388 439 eRVGDQVMAALVLRDGATFDP 459
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
232-599 |
3.16e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.49 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 232 SSLLEQ-GQKCGVEIISMKALEdlgrANRQKPKPPA----PEDIAVICFTSGTTGNPKGAVITHRNVVSDcsafVKMTEN 306
Cdd:PRK05691 1236 SHLLERlPQAEGVSAIALDSLH----LDSWPSQAPGlhlhGDNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 307 VFIPTPDDTLISFLPLAhmFE-RVVECTM-LCHGAKIGFF----QGDIRLLMDDLKALRPTVFPVVPRLLNRMFDRIFGQ 380
Cdd:PRK05691 1308 TYALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAgpgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 381 ANTTLKRwlldfaskrkeaelrsgiirnnslwdklifhkiqsslggrvklMITGAAPVSATVLTFLRAAL-GCQFYEGYG 459
Cdd:PRK05691 1386 ACTSLRR-------------------------------------------LFSGGEALPAELRNRVLQRLpQVQLHNRYG 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 460 QTE----CTAGCCLtvAGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--VLDKD 533
Cdd:PRK05691 1423 PTEtainVTHWQCQ--AEDGERSPIGRPLGNVLCRVLD-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfVPDPL 1499
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970702926 534 G-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQ--VFVHGESLQAFLIA 599
Cdd:PRK05691 1500 GedgarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
260-606 |
9.62e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 55.15 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 260 QKPkPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMT-----ENVFIPTPDDTLISFLPLAhmFERVVECTM 334
Cdd:PRK13382 189 QRP-EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTpwraeEPTVIVAPMFHAWGFSQLV--LAASLACTI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 335 LchgAKIGFFQGDIRLLMDdlkALRPTVFPVVPRllnrMFDRIFGQANTTLKRWL---LDFASKRKEAeLRSGIIRnnSL 411
Cdd:PRK13382 266 V---TRRRFDPEATLDLID---RHRATGLAVVPV----MFDRIMDLPAEVRNRYSgrsLRFAAASGSR-MRPDVVI--AF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 412 WDK---LIFHKIQSSLGGrvklMITGAAPVSatvltfLRAALGcqfyegygqtectagccltvagdwTAGHvgaPMPCSL 488
Cdd:PRK13382 333 MDQfgdVIYNNYNATEAG----MIATATPAD------LRAAPD------------------------TAGR---PAEGTE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 489 IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYlkDPAKTAEVldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 568
Cdd:PRK13382 376 IRILD-QDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENV 449
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 970702926 569 APEKIENIyLRSEP-VAQVFVHGESLQAF---LIAIVVPDAE 606
Cdd:PRK13382 450 YPIEVEKT-LATHPdVAEAAVIGVDDEQYgqrLAAFVVLKPG 490
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-590 |
1.42e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 54.31 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 265 PAPEDIAVICfTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVFIPTPD-------DTLISFLPLAHmfervvectmLCH 337
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDahkaaaaAAGTVMFPAPP----------LMH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 338 GAK-----IGFFQGDIRLLMDDlkALRP-TVFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNNS 410
Cdd:cd05924 70 GTGswtafGGLLGGQTVVLPDD--RFDPeEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPYD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 411 LwdklifhkiqSSLggrvKLMITGAAPVSATVLT-FLRAALGCQFYEGYGQTECTAGCCLTVAGdwtAGHVGAP--MPCS 487
Cdd:cd05924 133 L----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPftRANP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 488 LIKLVDvEEMNYLAAK--GEGEVCVKGpNVFQGYLKDPAKTAEVL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:cd05924 196 DTVVLD-DDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT 273
|
330 340
....*....|....*....|....*....
gi 970702926 563 AqGEYIAPEKIENIyLRSEP-VAQVFVHG 590
Cdd:cd05924 274 G-GEKVFPEEVEEA-LKSHPaVYDVLVVG 300
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
175-603 |
1.54e-07 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 54.40 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 175 IPLYDTLGTEAITYIINKAELSLVFVdkPEKANLLldgvenkliPGLKTIVLMDSFGSSLLEQGQKCgveiismKALEDL 254
Cdd:cd17654 44 IGLRCDRGTESPVAILAILFLGAAYA--PIDPASP---------EQRSLTVMKKCHVSYLLQNKELD-------NAPLSF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 255 GRANRQKPKPpAPEDIAVICFTSGTTGNPKGAVITHR----NVVSDCSAFVKMTENVFIPTPddtLISFLPlahmfeRVV 330
Cdd:cd17654 106 TPEHRHFNIR-TDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLFNITSEDILFLTS---PLTFDP------SVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 331 ECTM-LCHGAKigffqgdirLLMDdlkalrPTVFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGI 405
Cdd:cd17654 176 EIFLsLSSGAT---------LLIV------PTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 406 irnnslwdklifhkiqSSLggRVkLMITGAAPVSATVLTFLRAA-LGCQFYEGYGQTECTAGCCLTVAGDWTAG-HVGAP 483
Cdd:cd17654 238 ----------------SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAYKVPEEDSPvQLGSP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 484 MPCSLIKLVDVEemnylAAKGEGEVCVKGPNVfQGYLKDPAKTAEVLdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLA 563
Cdd:cd17654 299 LLGTVIEVRDQN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR 367
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 970702926 564 qGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVP 603
Cdd:cd17654 368 -GKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGE 406
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-606 |
1.56e-07 |
|
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: 54.40 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 268 EDIAVICFTSGTTGNPKGAVITHRNVVsdcsafvkmteNVFIPTPDDTLISFlplahmFERVVECTMLChgakigffqgd 347
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMV-----------NLLHFEREKTNINF------SDKVLQFATCS----------- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 348 irllmddlkalrptvFPVVprllnrmFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNN--------SLWdKLIFHK 419
Cdd:cd17656 180 ---------------FDVC-------YQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNievvflpvAFL-KFIFSE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 420 IQ--SSLGGRVKLMITGAAP--VSATVLTFLRAAlGCQFYEGYGQTECTagccltVAGDWTAGH---------VGAPMPC 486
Cdd:cd17656 237 REfiNRFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETH------VVTTYTINPeaeipelppIGKPISN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 487 SLIKLVDVEEMnyLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEVLDKDGW------LHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd17656 310 TWIYILDQEQQ--LQPQGIvGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQ 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 970702926 560 FKLaQGEYIAPEKIENIYLRSEPVAQ--VFVHGESL-QAFLIAIVVPDAE 606
Cdd:cd17656 388 VKI-RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
261-582 |
2.66e-07 |
|
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: 53.59 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 261 KPKPPAPE-DIAVICFTSGTTGNPKGAVITHRNVVSDCSAFVKMTENVFIPTPddTLISFLPLAHmfervveCTMLCHGA 339
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 340 KIGFFQGDI---------RLLMDDLKALRPTVFPVVPRLLNrmfdrIFGQANTTLKRwlldfaskrkeaelrsgiirnns 410
Cdd:cd05915 216 AATLVGAKQvlpgprldpASLVELFDGEGVTFTAGVPTVWL-----ALADYLESTGH----------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 411 lwdklifhkiqsSLGGRVKLMITGAAPvsATVLTFLRAALGCQFYEGYGQTECTAgccLTVAGDWTAGHVGAPMPCSL-- 488
Cdd:cd05915 268 ------------RLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETSP---VVVQNFVKSHLESLSEEEKLtl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 489 ---------IKLVDVEEMNYLAAKGEGE----VCVKGPNVFQGYLKDPAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:cd05915 331 kaktglpipLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDR 410
|
330 340
....*....|....*....|....*..
gi 970702926 556 KKHIFKLAqGEYIAPEKIENIyLRSEP 582
Cdd:cd05915 411 LKDLIKSG-GEWISSVDLENA-LMGHP 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
267-606 |
3.08e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.19 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAF-----VKMTENVFIPTPDDTLIS----FLPLAHMFERVVECtmlch 337
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMqqaygLGVGDTVLQKTPFSFDVSvwefFWPLMSGARLVVAA----- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 338 gakigffQGDIRLLmDDLKAL----RPTVFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwd 413
Cdd:PRK12316 729 -------PGDHRDP-AKLVELinreGVDTLHFVPSMLQAFLQDEDVASCTSLRR-------------------------- 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 414 klifhkiqsslggrvkLMITGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTVAGDWTAGHV--GAPMPCSLIKL 491
Cdd:PRK12316 775 ----------------IVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYI 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 492 VDVeEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE------VLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 565
Cdd:PRK12316 839 LDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RG 916
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 970702926 566 EYIAPEKIENIYLRSEPVAQVFVHGESLQAfLIAIVVPDAE 606
Cdd:PRK12316 917 LRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLESE 956
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
59-601 |
4.44e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 53.11 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 59 MQSVEVAGSDGARRSAILDSDEPlVYFYDDVTT---LYEGFQR-GMRVSNNGACLGSR----KPDQPyewlsyKQVEEMS 130
Cdd:PRK06060 1 MRNGNLAGLLAEQASEAGWYDRP-AFYAADVVThgqIHDGAARlGEVLRNRGLSSGDRvllcLPDSP------DLVQLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 131 ECVGSGLIqkGFKAAPDQfigifaqNRPEWVIIEQgcfaysmvviplyDTlgteaityiinkaELSLVFVDKPekanlll 210
Cdd:PRK06060 74 ACLARGVM--AFLANPEL-------HRDDHALAAR-------------NT-------------EPALVVTSDA------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 211 dgvenklipglktivLMDSFGSSLLeqgqkcgveiisMKALEDLGRANRQKP---KPPAPEDIAVICFTSGTTGNPKGAV 287
Cdd:PRK06060 112 ---------------LRDRFQPSRV------------AEAAELMSEAARVAPggyEPMGGDALAYATYTSGTTGPPKAAI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 288 itHRNvvSDCSAFVK-MTENVFIPTPDDTLIS--------------FLPLAHMFERVVecTMLCHGAKIGFFqgdirllm 352
Cdd:PRK06060 165 --HRH--ADPLTFVDaMCRKALRLTPEDTGLCsarmyfayglgnsvWFPLATGGSAVI--NSAPVTPEAAAI-------- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 353 ddLKA-LRPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFASKRKEAELRSGIIRNNSLwdklifhkiQSSLGGRVkLM 431
Cdd:PRK06060 231 --LSArFGPSVLYGVPNFFAR----------------VIDSCSPDSFRSLRCVVSAGEAL---------ELGLAERL-ME 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 432 ITGAAPVsatvltflraalgcqfYEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVdVEEMNYLAAKGEGEVCVK 511
Cdd:PRK06060 283 FFGGIPI----------------LDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVR 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 512 GPNVFQGYLKDPAKtaeVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENIYLRSEPVAQVFVHG- 590
Cdd:PRK06060 346 GPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAv 421
|
570
....*....|....*..
gi 970702926 591 ------ESLQAFLIAIV 601
Cdd:PRK06060 422 restgaSTLQAFLVATS 438
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
113-294 |
7.71e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.20 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 113 KPDQPYEWLSYKQVEEMSECVGSGLIQKGFKAAPDQFIgiFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINK 192
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 193 AElSLVFVDKPEkanLLLDGVENKLiPGLKTIVLMDSFGSSlleqgqkcGVEIISMKALedLGRANRQKPKPP-APEDIA 271
Cdd:PRK04319 144 SE-AKVLITTPA---LLERKPADDL-PSLKHVLLVGEDVEE--------GPGTLDFNAL--MEQASDEFDIEWtDREDGA 208
|
170 180
....*....|....*....|...
gi 970702926 272 VICFTSGTTGNPKGAVITHRNVV 294
Cdd:PRK04319 209 ILHYTSGSTGKPKGVLHVHNAML 231
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-594 |
1.57e-06 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 51.28 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 267 PEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAFvkmtENVFIPTPDDTLISFLPLAHMFERVV-ECTMLCHGAKIGF-- 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYHGTAAFLgACNCLMSGGTLALsr 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 344 -FQgdIRLLMDDLKALRPTVFPVVPRLLnrmfdrifgqanttlkRWLLDFASKRKEAELRSGIIRNNSL----WDKliFH 418
Cdd:cd05937 162 kFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLLSTPPSPYDRDHKVRVAWGNGLrpdiWER--FR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 419 KiqsslggRVKLMITGaapvsatvltflraalgcqfyEGYGQTECTAGCCLTVAGDWTAGHVGAPMPCSLIKLVDVE--- 495
Cdd:cd05937 222 E-------RFNVPEIG---------------------EFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvlv 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 496 ------EMNYL---------AAKGE-GEVCVKGPNV----FQGYLKDPAKTA-----EVLDK-DGWLHTGDIGKWLPNGT 549
Cdd:cd05937 274 kmdpetDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATEsklvrDVFRKgDIYFRTGDLLRQDADGR 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 970702926 550 LKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHGESLQ 594
Cdd:cd05937 354 WYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
233-325 |
3.06e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 50.37 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 233 SLLEQGQKCGV--EIISMKALEDLGRANRQKPKPPAPEDI---------AVICFTSGTTGNPKGAVITHRNVVSdCSAFV 301
Cdd:cd05938 98 ALRADGVSVWYlsHTSNTEGVISLLDKVDAASDEPVPASLrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 970702926 302 KmtenVFIPTPDDTLISFLPLAHM 325
Cdd:cd05938 177 S----LCGVTADDVIYITLPLYHS 196
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
257-607 |
3.38e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 49.66 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 257 ANRQKPKPPAPEDIAVICFTSGTTGNPKGAVITHRNVVSDCSAfvkmtENVFIPTPDDTLISfLPLAHmfervvectmlc 336
Cdd:PRK07824 24 RDALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADA-----THDRLGGPGQWLLA-LPAHH------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 337 hgakIGFFQGDIRLLmddLKALRPTVFPVvprllNRMFDrifgqanttlkrwLLDFAskRKEAELRSGiIRNNSLWD-KL 415
Cdd:PRK07824 86 ----IAGLQVLVRSV---IAGSEPVELDV-----SAGFD-------------PTALP--RAVAELGGG-RRYTSLVPmQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 416 IfhKIQSSLGGRVKL-----MITGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLtvagdwtagHVGAPMPCSLI 489
Cdd:PRK07824 138 A--KALDDPAATAALaeldaVLVGGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 490 KLVDveemnylaakgeGEVCVKGPNVFQGY--LKDPAKTAEvldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEY 567
Cdd:PRK07824 204 RVED------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLT 265
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 970702926 568 IAPEKIENIYLRSEPVAQVFVHG---ESLQAFLIAIVVPDAET 607
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDGGP 308
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
264-614 |
4.37e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.43 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 264 PPAPEDIAVICFTSGTTGNPKGAVITHRNVVsdcSAFVKMTENVFIpTPDDTLIS-------------FLPlahmfervv 330
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV---NRLLWMQNHYPL-TADDVVLQktpcsfdvsvwefFWP--------- 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 331 ectMLChGAKigffqgdirLLMDDLKALRPtvfpvvPRLLNRMFDRifgQANTTLkrwlldfaskrkeaelrsgiirnns 410
Cdd:PRK10252 661 ---FIA-GAK---------LVMAEPEAHRD------PLAMQQFFAE---YGVTTT------------------------- 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 411 lwdklifHKIQSSLGGRVKLMITGAAPVSATVLT--F-----LRAALgCQFYEG---------YGQTECTAGCCLTVA-G 473
Cdd:PRK10252 694 -------HFVPSMLAAFVASLTPEGARQSCASLRqvFcsgeaLPADL-CREWQQltgaplhnlYGPTEAAVDVSWYPAfG 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 474 DWTAGHVGAPMPCSL------IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGWL------HTGDI 541
Cdd:PRK10252 766 EELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDV 844
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970702926 542 GKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHgeslqafliAIVVPDAETVGPWARK 614
Cdd:PRK10252 845 ARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTH---------ACVINQAAATGGDARQ 907
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
275-590 |
8.62e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.01 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 275 FTSGTTGNPKGAVITHRNVVS--DCSA---FVKMTENVFIPtpdDTLISFLPLahmfervvectmlcHGAKIGFFQGDIR 349
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHsfDCNVhdfHMKREDSVLIA---GTLVHSLFL--------------YGAISTLYVGQTV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 350 LLMddlkalrPTVFPvvprllNRMFDRIFGQANT---TLKRWLLDFASKRKEAELRSGIIRNNSLWDKLIFHKIQSslgg 426
Cdd:PRK07638 213 HLM-------RKFIP------NQVLDKLETENISvmyTVPTMLESLYKENRVIENKMKIISSGAKWEAEAKEKIKN---- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 427 rvklmitgaapvsatvlTFLRAalgcQFYEGYGQTECTAGCCLtVAGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGE- 505
Cdd:PRK07638 276 -----------------IFPYA----KLYEFYGASELSFVTAL-VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEi 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 506 GEVCVKGPNVFQGYLKDpAKTAEVLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQ 585
Cdd:PRK07638 334 GTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDE 411
|
....*
gi 970702926 586 VFVHG 590
Cdd:PRK07638 412 IVVIG 416
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-599 |
1.20e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.93 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 266 APEDIAVICFTSGTTGNPKGAVITHRNVVSDCSA---FVKMTENVFIPTP-----DDTLISFLPlAHMFervvectmlch 337
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSkvpYLALSEADVIAQTasqsfDISVWQFLA-APLF----------- 3934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 338 GAKIGFFQGDI----RLLMDDLKALRPTVFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnsl 411
Cdd:PRK05691 3935 GARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP-------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 412 wdklifhkiqsslggrvklmiTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TVAGDWTAGH---VGAPMPCS 487
Cdd:PRK05691 3991 ---------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNN 4049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 488 LIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEVLDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:PRK05691 4050 RLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQV 4128
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 970702926 561 KLaQGEYIAPEKIENIYLRSEPV------AQVFVHGESLQAFLIA 599
Cdd:PRK05691 4129 KI-RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
262-324 |
2.96e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.96 E-value: 2.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970702926 262 PKPPAPEDIAVICFTSGTTGNPKGAVITHRNVvsdCSAFVKMTENVFIPTPDDTLISFLPLAH 324
Cdd:PRK12476 187 PVELDTDDVSHLQYTSGSTRPPVGVEITHRAV---GTNLVQMILSIDLLDRNTHGVSWLPLYH 246
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
245-324 |
3.59e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 43.95 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 245 IISMKALEDLGRANRQKPkPPAPEDIAVICFTSGTTGNPKGAVITHRNVvsdCSAFVKMTENVFIPTpDDTLISFLPLAH 324
Cdd:PRK07769 158 VIAVDAVPDEVGATWVPP-EANEDTIAYLQYTSGSTRIPAGVQITHLNL---PTNVLQVIDALEGQE-GDRGVSWLPFFH 232
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
58-290 |
4.46e-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: 43.33 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 58 AMQSVEVAGSDGARRSAILDSDEPLVYFYDDVT--TLYEGFQRGMRVSNNGACLGSRKPDQPY-EWLSYKQVEEMSECVG 134
Cdd:cd17634 19 AGKILDWITPYQKVKNTSFAPGAPSIKWFEDATlnLAANALDRHLRENGDRTAIIYEGDDTSQsRTISYRELHREVCRFA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 135 SGLIQKGFKAApdQFIGIFAQNRPEWVIIEQGCFAYSMVVIPLYDTLGTEAITYIINKAELSLV-----FVDKPEKANLL 209
Cdd:cd17634 99 GTLLDLGVKKG--DRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLitadgGVRAGRSVPLK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 210 --LDGVENKLIPGLKTIVLMDSFGSSLLEQGqkcGVEIISMKALEDlgRANRQKPKPPAPEDIAVICFTSGTTGNPKGAV 287
Cdd:cd17634 177 knVDDALNPNVTSVEHVIVLKRTGSDIDWQE---GRDLWWRDLIAK--ASPEHQPEAMNAEDPLFILYTSGTTGKPKGVL 251
|
...
gi 970702926 288 ITH 290
Cdd:cd17634 252 HTT 254
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
121-324 |
5.09e-04 |
|
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: 43.18 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 121 LSYKQVEEMSECVGSGLIQKGFKAApdQFIGIFAQNRPEWVIIEQGcFAYSMVVIPLYDT-LGTEAITYIINKAELSLVF 199
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSG--DVVALFMENRLEFVALWLG-LAKIGVETALINSnLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970702926 200 VDkpekanlLLDgvenklipglktivlmdsfgsSLLEQGQKcgveiiSMKALEDLGRanrqkpkppapEDIAVICFTSGT 279
Cdd:cd05939 81 FN-------LLD---------------------PLLTQSST------EPPSQDDVNF-----------RDKLFYIYTSGT 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 970702926 280 TGNPKGAVITHrnvvsdcSAFVKMTENV---FIPTPDDTLISFLPLAH 324
Cdd:cd05939 116 TGLPKAAVIVH-------SRYYRIAAGAyyaFGMRPEDVVYDCLPLYH 156
|
|
| |
