|
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: 974.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 116 QPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 196 SLVFVDKpekaklllegvenklipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFFQGDIRLLMDDL 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 356 KVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 434 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA--EGEGEVCVK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 512 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGE 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 592 SLQAFLIAIVVPDVETLCSWA-QKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1832481836 671 TPTMKAKRPELRNYFRSQIDDLYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-696 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 720.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 86 YDDVTTLYEGFQRGIQVSNNGPCLGSR-KPDQ---PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWV 161
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 162 IIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVdKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQRC 241
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 242 GVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLP 321
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK----FYPSDVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 322 LAHIYEQLLKCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEA 399
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 400 ELRSGiiRNNS-LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAG 478
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 479 HVGAPMPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 556 KKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAI 634
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 635 LEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 696
Cdd:PLN02736 589 LADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| 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: 542.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 86 YDDVTTLYEGFQRGIQVSNNGPCLgSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQ 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 166 GCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENklIPGLKIIVVMDaygselvERGQRCGVEV 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 246 TSMKAMEDLGRANR------RKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATEKALPLSASDTHISY 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSN----ARALLERLPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 320 LPLAHIYEQLLKCVMLCHGAKIGFfQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---S 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 395 KRKEAELRSGiiRNNSLW--------DRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 467 CCLTMPGDWTAGHVGAPMPCNLIKLvdveemnymaAEgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI----------AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 547 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRG-FEGSFEELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832481836 626 RNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 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 ... |
116-681 |
2.58e-173 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 502.90 E-value: 2.58e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 116 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 196 SLVFVDKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICF 275
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAHIYEQLL-KCVMLCHGAKIGFFQgDIRLLMDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRAgLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 355 LKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslGGRVRLMVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 435 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 515 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQ 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 595 AFLIAIVVPDVETLCSWAQKRG-FEGSFEELCRNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPT 673
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1832481836 674 MKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-698 |
5.77e-159 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 473.95 E-value: 5.77e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 117 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 196
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVN--PGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 197 LVFVDKPEKAKLLleGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPkPPAPEDLAVICFT 276
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 277 SGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLS-----ASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFFQGDIRLL 351
Cdd:PLN02861 229 SGTTGEPKGVILTNRAII----AEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 352 MDDLKVLQPTVFPVVPRLlnrmFDRIFG------QANTTLKRWLLDFASKRKEAELRSGIIRNNS--LWDRLIFHKVQSS 423
Cdd:PLN02861 305 MEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 424 LGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLVDVEEMNYMAA 502
Cdd:PLN02861 381 LGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYDAL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 503 EG--EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRS 580
Cdd:PLN02861 461 SDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRC 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 581 EPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP 660
Cdd:PLN02861 540 PLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEP 619
|
570 580 590
....*....|....*....|....*....|....*...
gi 1832481836 661 ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV 698
Cdd:PLN02861 620 NPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-696 |
6.23e-156 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 466.21 E-value: 6.23e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 88 DVTTLYEGFQRGIQVSNNGPCLGSRKPDQ----PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVII 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAE--PGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 164 EQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV-DKpeKAKLLLEGvENKLIPGLKIIVVMDAYGSELVERGQRCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 243 VEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATEKAL-----PLSASDTHI 317
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAV----ATFVRGVDLFMeqfedKMTHDDVYL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 318 SYLPLAHIYEQLLKCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASK 395
Cdd:PLN02430 271 SFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 396 RKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG 473
Cdd:PLN02430 351 YKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 474 DWTA-GHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTL 550
Cdd:PLN02430 431 EMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVL 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 551 KIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDV 630
Cdd:PLN02430 510 KIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPEL 589
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481836 631 KKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 696
Cdd:PLN02430 590 KEHILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-697 |
5.04e-155 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 464.11 E-value: 5.04e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 87 DDVTTLYEGFQRGIQVSNNGPCLGSR-----KPDQpYEWLSYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWV 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 162 IIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLlegvenKLIPG----LKIIVVMDAYGSELVER 237
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF------KTCPNsteyMKTVVSFGGVSREQKEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 238 GQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSA---FVKATEKALplSASD 314
Cdd:PLN02614 193 AETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGvirLLKSANAAL--TVKD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 315 THISYLPLAHIYEQLLKCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDF 392
Cdd:PLN02614 271 VYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 393 ASKRKEAELRSGI--IRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT 470
Cdd:PLN02614 351 AFSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 471 MPGDW-TAGHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPN 547
Cdd:PLN02614 431 LPDELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPN 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 548 GTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRN 627
Cdd:PLN02614 510 GSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQN 589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 628 KDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIK 697
Cdd:PLN02614 590 EKAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
6.42e-155 |
|
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: 457.83 E-value: 6.42e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 117 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 197 LVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpPAPEDLAVICFT 276
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 277 SGTTGNPKGAMVTHRNIVSDCSAFVKATEKALplSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFfqGDIRLLMD--- 353
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPELL--GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 354 -----DLKVLQPTVFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDRLIFHKVQSSLGG 426
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 427 RVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYM--AAEG 504
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStdKPPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 505 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 585 QVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-EGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELF 663
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 1832481836 664 SIDNGLLTPTMKAKR 678
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-694 |
3.71e-139 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 424.14 E-value: 3.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 62 VEVAGSGG-ARRSALLDsdEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRK---------PDQ---------PYEWLS 122
Cdd:PLN02387 31 VDVGGEPGyAIRNARFP--ELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 123 YKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDK 202
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 203 PEKAKLLleGVENKLiPGLKIIVVMDAYGSELVERG-QRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTG 281
Cdd:PLN02387 187 KQLKKLI--DISSQL-ETVKRVIYMDDEGVDSDSSLsGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 282 NPKGAMVTHRNIVSDCSAFVKATEKalpLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFfqGDIRLLMD-------- 353
Cdd:PLN02387 264 LPKGVMMTHGNIVATVAGVMTVVPK---LGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 354 ---DLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELR------SGIIRnnSLWDRLIFHKVQS 422
Cdd:PLN02387 339 tkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 SLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA 502
Cdd:PLN02387 417 VLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLIS 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 503 EG---EGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN 575
Cdd:PLN02387 497 DKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEA 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 576 IYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVK 654
Cdd:PLN02387 577 ALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPA 656
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1832481836 655 GITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 694
Cdd:PLN02387 657 KIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
112-563 |
2.25e-128 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 386.67 E-value: 2.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQP------YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 185
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALGVG--KGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 186 ITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsMKAMEDLGRANRRKPKPP 265
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEKALPLSASDTHISYLPLAHIYEQLLKC-VMLCHGAKIGFF 344
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 QGDIRL----LMDDLKVLQPTVFPVVPRLLNRMFDrifgqaNTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkv 420
Cdd:pfam00501 233 PGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------AGAPKRALL------------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 421 qsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW---TAGHVGAPMPCNLIKLVDVEEM 497
Cdd:pfam00501 277 -----SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETG 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481836 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
121-693 |
9.45e-102 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 326.55 E-value: 9.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 200
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI-V 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPEKAKLLLEGVENKLIPGLKIIvvmdaYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPE---DLAVICFTS 277
Cdd:PTZ00216 199 CNGKNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 278 GTTGNPKGAMVTHRNIVSDCSAFV-KATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFfqGDIRLLMD--- 353
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 354 ----DLKVLQPTVFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEAELRSGiiRNNSLWDRLIFHK 419
Cdd:PTZ00216 352 rphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 420 VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCC--LTMPGDWTAGHVGAPMPCNLIKLVDVEEM 497
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLLKGVEMKLLDTEEY 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 498 NYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENI 576
Cdd:PTZ00216 499 KHTdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEAL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 577 YMRSEPVAQ----VFVHgeSLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQ 652
Cdd:PTZ00216 579 YGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1832481836 653 VKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 693
Cdd:PTZ00216 657 VRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
9.69e-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: 298.50 E-value: 9.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 116 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 196 SLVFVdkpekaklllegvENklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppAPEDLAVICF 275
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVSDcsafVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFfqGDIRLLMDDL 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQ----IRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 356 KVLQPTVFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDRLIFHKVQSslGGRVRLMV 432
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 433 TGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKG 512
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 513 PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGES 592
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 593 lQAFLIAIVVPDVETLCSWAQKRG--FEGSFEELCRNKDVKKAI-LEDMVRLGKDSGLKPFEQVKGITLHPELFsIDNGL 669
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 1832481836 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 |
2.19e-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: 259.32 E-value: 2.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 118 YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSL 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLE--PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 198 VFVDKPEKAKLLLEGVenkliPGlKIIVVMDAYGSELvergqRCGVEVTSMKAMedlGRANRRKPkPPAPEDLAVICFTS 277
Cdd:cd05932 82 LFVGKLDDWKAMAPGV-----PE-GLISISLPPPSAA-----NCQYQWDDLIAQ---HPPLEERP-TRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 278 GTTGNPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAHIYEQllkcVMLCHGAKIG----FFQGDIRLLMD 353
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGIEH----IGTEENDRMLSYLPLAHVTER----VFVEGGSLYGgvlvAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 354 DLKVLQPTVFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRKEAELRsgIIRNNSLWDRLIFHKVQSSLG-GRVRLMV 432
Cdd:cd05932 219 DVQRARPTLFFSVPRLWTKFQQGVQ---------------DKIPQQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRLAG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 433 TGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKG 512
Cdd:cd05932 282 CGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 513 PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGES 592
Cdd:cd05932 350 PALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 593 LQAFLIAIVVPDVETLCSWAQKRG-FEGSFeelcrnkdvkKAILEDMvrlgkDSGLKPFEQVKGITLHPELFSIDNGLLT 671
Cdd:cd05932 430 LPAPLALVVLSEEARLRADAFARAeLEASL----------RAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILT 494
|
....*..
gi 1832481836 672 PTMKAKR 678
Cdd:cd05932 495 PTLKIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
112-615 |
3.40e-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: 249.34 E-value: 3.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQP-----YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 187 TYIVNKAELSLVFVdkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppa 266
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 pedlAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVM-LCHGAKI---- 341
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLL----ANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllp 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdrlifhkvq 421
Cdd:COG0318 175 RF---DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------ 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 422 sslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNY 499
Cdd:COG0318 217 ------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 579
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1832481836 580 SEPVAQVFV-------HGESLQAFLI--AIVVPDVETLCSWAQKR 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 |
1.29e-74 |
|
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: 251.19 E-value: 1.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 122 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIE---QGCFAYSMvivPLYDTLGNEAITYIVNKAELSLV 198
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAElaaQAIGALSL---GIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 199 FVDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQrcgveVTSMKAMEDLGRA-NRRKPK-------PPAPEDL 270
Cdd:cd17641 88 IAEDEEQVDKLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 271 AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATekalPLSASDTHISYLPLAHIYEQLLKCVM-LCHGAKIGFFQgDIR 349
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAAD----PLGPGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 350 LLMDDLKVLQPTVFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDRLIFH 418
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 419 KVQSSLG-GRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVeem 497
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 498 nymaaegeGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIY 577
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 578 MRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDsgLKPFEQV-KG 655
Cdd:cd17641 464 KFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIrRF 540
|
570 580
....*....|....*....|...
gi 1832481836 656 ITLHPELfSIDNGLLTPTMKAKR 678
Cdd:cd17641 541 LLLYKEL-DADDGELTRTRKVRR 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
1.62e-74 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 251.51 E-value: 1.62e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 113 KPDQPYEWLSYKQVAELseCIGSAliqKGF-KTAPDQF--IGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYI 189
Cdd:cd05933 1 KRGDKWHTLTYKEYYEA--CRQAA---KAFlKLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 190 VNKAELSLVFVDKPEKAKLLLEgVENKLiPGLKIIVvmdAYGSELVERGQRcgveVTSMKAMEDLGR-----ANRRKPKP 264
Cdd:cd05933 76 AETSEANILVVENQKQLQKILQ-IQDKL-PHLKAII---QYKEPLKEKEPN----LYSWDEFMELGRsipdeQLDAIISS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEKALPLSASDTHISYLPLAHIYEQLLKcVMLC--HGAKIG 342
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 343 FFQGDIR--LLMDDLKVLQPTVFPVVPRLLNRMFDRI--FGQANTTLKRWLLDFAsKRKEAE-------LRSGIIRNNSL 411
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 412 WDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIK 490
Cdd:cd05933 305 AKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 491 LVDVEemnymaAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 570
Cdd:cd05933 384 IHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 571 EKIEN-IYMRSEPVAQVFVHGESLQaFLIAIVV----PDVET----------LCSWAQKRGFEGS-FEELCRNKD--VKK 632
Cdd:cd05933 458 VPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTlkceVNPETgepldelteeAIEFCRKLGSQATrVSEIAGGKDpkVYE 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832481836 633 AILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 693
Cdd:cd05933 537 AIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
1.75e-68 |
|
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: 231.56 E-value: 1.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKTAPDqfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICFTSGTT 280
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVSDCsAFVKATEkalPLSASDTHISYLPLAHIYEQLLKCVM-LCHGAKIGFFQGDIRLLMDDLKVLQ 359
Cdd:cd05914 102 GNSKGVMLTYRNIVSNV-DGVKEVV---LLGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 360 PTVFPVVPRLLNRMFDRIFGQAN-TTLKRWLLDFASKRKEAELRSgiirnnslwdrLIFHKVQSSLGGRVRLMVTGAAPV 438
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMDIIPkLTLKKFKFKLAKKINNRKIRK-----------LAFKKVHEAFGGNIKEFVIGGAKI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 439 SATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPmpcnlIKLVDVEEMNYMAAEGEGEVCVKGPNVFQG 518
Cdd:cd05914 247 NPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 519 YLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA--QVFVHGESLQAf 596
Cdd:cd05914 321 YYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA- 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 597 lIAIVVPDvetlcswaqkrgFEGSFEELCRNKdvKKAILEDmVRLGKDSGLKPFEQVKGITLHPELFSidnglLTPTMKA 676
Cdd:cd05914 400 -LAYIDPD------------FLDVKALKQRNI--IDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE-----KTPKGKI 458
|
..
gi 1832481836 677 KR 678
Cdd:cd05914 459 KR 460
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
89-671 |
1.14e-67 |
|
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: 233.12 E-value: 1.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 89 VTTLYEGF-QRgiqvsnngPCLGSRK---PDQPYE-WLSYKQVAELSECIGSALIQKGFKTA----------PDQFIGIF 153
Cdd:cd17632 28 IATVMTGYaDR--------PALGQRAtelVTDPATgRTTLRLLPRFETITYAELWERVGAVAaahdpeqpvrPGDFVAVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 154 AQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDK---PEKAKLLLEGvenkliPGLKIIVVMDaY 230
Cdd:cd17632 100 GFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAehlDLAVEAVLEG------GTPPRLVVFD-H 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 231 GSEL----------VERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPED---LAVICFTSGTTGNPKGAMVTHRNiVSDC 297
Cdd:cd17632 173 RPEVdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERL-VATF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 298 SAFVKATEKALPLSASDTHisYLPLAHIYEQLLKCVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTVFPVVPRLLNRMFD 375
Cdd:cd17632 252 WLKVSSIQDIRPPASITLN--FMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 376 RIfgQAntTLKRWLLDFA-----SKRKEAELRsgiirnnslwdrlifhkvQSSLGGRVRLMVTGAAPVSATVLTFLRAAL 450
Cdd:cd17632 329 RY--QA--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 451 GCQFYEGYGQTEctAGCCLTmpgdwtAGHVGAPmPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTA 527
Cdd:cd17632 387 DLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 528 EALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVET 607
Cdd:cd17632 458 EVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDA 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832481836 608 LCSWAQKRgfegsfeelcrnkdVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLT 671
Cdd:cd17632 538 LAGEDTAR--------------LRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-615 |
6.26e-65 |
|
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: 218.31 E-value: 6.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKI----GFF 344
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 QGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdrlifhkvqssl 424
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 ggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT--AGHVGAPMPCNLIKLVDVEEmNYMAA 502
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 503 EGEGEVCVKGPNVFQGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEP 582
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832481836 583 VAQVFVHG---ESLQAFLIAIVVP------DVETLCSWAQKR 615
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-590 |
4.81e-63 |
|
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: 217.85 E-value: 4.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPEKAKLLleGVENKLIPGLKIIVvMDAYGSELVERGQrcGVEVTSMKAMEDlgranRRKPKPPAPEDLAVICFTSGTT 280
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIV-LDDKPDGVLSIED--LLSPTLGEEDED-----LPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVSDCSaFVKATEKaLPLSASDTHISYLPLAHIYEQLLKCVMLCHGAK-IGFFQGDIRLLMDDLKVLQ 359
Cdd:cd05911 159 GLPKGVCLSHRNLIANLS-QVQTFLY-GNDGSNDVILGFLPLYHIYGLFTTLASLLNGATvIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 360 PTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRlifHKVQSslggrVRLMVTGAAPVS 439
Cdd:cd05911 237 ITFLYLVPPIAAALA---------------------------------KSPLLDK---YDLSS-----LRVILSGGAPLS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 440 ATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQG 518
Cdd:cd05911 276 KELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKG 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 519 YLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd05911 356 YYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
110-615 |
1.91e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 214.00 E-value: 1.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 110 GSRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqGCFAYSM---VIVPLYDTL 181
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIG--KGDRVAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 182 GNEAITYIVNKAELSLVFVdkpekAKLLLeGVENKL---IPGLKIIVVMDaygselVERGQRCGVEVTSMKAMedLGRAN 258
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFL-GVDYSAttrLPALEHVVICE------TEEDDPHTEKMKTFTDF--LAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 259 RRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAHIY---EQLLKCVM 334
Cdd:PRK07656 156 PAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEY----LGLTEGDRYLAANPFFHVFgykAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 335 lcHGAKIgffqgDIRLLMDDLKVLQ------PTVFPVVPrllnrmfdrifgqantTLKRWLLDFAsKRKEAELRSgiirn 408
Cdd:PRK07656 232 --RGATI-----LPLPVFDPDEVFRlieterITVLPGPP----------------TMYNSLLQHP-DRSAEDLSS----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 409 nslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLTMPGD---WTAGHVGAPM 484
Cdd:PRK07656 283 -------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 485 PCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 563
Cdd:PRK07656 344 AGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832481836 564 QGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVP------DVETLCSWAQKR 615
Cdd:PRK07656 421 GGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
122-591 |
3.23e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 213.51 E-value: 3.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 122 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqgC-FAYSM---VIVPLYDTLGNEAITYIVNKAELSL 197
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLE----AyFAVPKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 198 VFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSElvergqRCGVEVTSMKAMedLGRANRRKPKPPAPE-DLAVICFT 276
Cdd:PRK06187 107 VLVD-SEFVPLL-AAILPQL-PTVRTVIVEGDGPAA------PLAPEVGEYEEL--LAAASDTFDFPDIDEnDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 277 SGTTGNPKGAMVTHRNIVSDcsafVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKI---GFFqgDIRLLMD 353
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLH----SLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPENLLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 354 DLKVLQPTVFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrkeaelrsgiirnnslwdrlifhkvqsslgGRVRLMVT 433
Cdd:PRK06187 250 LIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF------------------------------------SSLRLVIY 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 434 GAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLT----MPGDWT-AGHVGAPMPCNLIKLVDvEEMNYMAAEGE-- 505
Cdd:PRK06187 289 GGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDGGev 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 506 GEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQ 585
Cdd:PRK06187 368 GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPAVAE 445
|
....*.
gi 1832481836 586 VFVHGE 591
Cdd:PRK06187 446 VAVIGV 451
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
112-603 |
1.81e-60 |
|
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: 210.11 E-value: 1.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 187 TYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkaMEDLGRANRRKPKPPA 266
Cdd:cd05936 89 EHILNDSGAKALIVAVS-----------------------------------------------FTDLLAAGAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 --PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfVKATEKALpLSASDTHISYLPLAHIYEQLLKCV-MLCHGAKIGF 343
Cdd:cd05936 122 ltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWLEDL-LEGDDVVLAALPLFHVFGLTVALLlPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 FQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiirnnslwdrlifhkvqs 422
Cdd:cd05936 200 IPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 slggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMA 501
Cdd:cd05936 244 -----LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 581
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHP 395
|
490 500
....*....|....*....|....*....
gi 1832481836 582 PVAQVFV-------HGESLQAFliaiVVP 603
Cdd:cd05936 396 AVAEAAVvgvpdpySGEAVKAF----VVL 420
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
269-615 |
1.78e-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: 162.46 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAHIYEQLLK--CVMLCHGAKI--GFF 344
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWR----WTEDDVLLHVLPLHHVHGLVNAllCPLFAGASVEflPKF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 ---QGDIRLLMDDLkvlqpTVFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdrlifhkvq 421
Cdd:cd05941 166 dpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 422 sslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMP--GDWTAGHVGAPMPCNLIKLVDVEEMNY 499
Cdd:cd05941 212 ----ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIENIYM 578
Cdd:cd05941 286 LPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLL 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1832481836 579 RSEPVAQVFVHGESLQAF---LIAIVVP-------DVETLCSWAQKR 615
Cdd:cd05941 365 AHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
111-604 |
9.31e-43 |
|
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: 160.47 E-value: 9.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 111 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 185
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVA--KGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 186 ITYIVNKAElslvfvdkpekAKLLLEgvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpp 265
Cdd:cd17631 84 VAYILADSG-----------AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 apeDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVM-LCHGAKI--- 341
Cdd:cd17631 99 ---DLALLMYTSGTTGRPKGAMLTHRNLL----WNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvil 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 -GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTlkrwllDFASkrkeaelrsgiirnnslwdrlifhkv 420
Cdd:cd17631 172 rKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS-------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 421 qsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLVDvEEMN 498
Cdd:cd17631 215 -------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGR 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 499 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYM 578
Cdd:cd17631 286 EVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLY 363
|
490 500 510
....*....|....*....|....*....|...
gi 1832481836 579 RSEPVAQVFV-------HGESlqafLIAIVVPD 604
Cdd:cd17631 364 EHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
267-691 |
1.66e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 158.73 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFVKATEKalplsasdTHISYLPLAHIYEQLLKCVMLCHGAK 340
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKKYNPK--------THLSYLPISHIYERVIAYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 341 IGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLdfaskRKEAELRSGiiRNNSLWDRL--- 415
Cdd:PTZ00342 375 INIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLV-----KKILSLRKS--NNNGGFSKFleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 416 IFH---KVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPM-PCNLIKL 491
Cdd:PTZ00342 448 ITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 492 VDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 571
Cdd:PTZ00342 528 RTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 572 KIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-------EGSFEELCRNKDVKKAILEDMVR---- 640
Cdd:PTZ00342 608 MLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginEKNYLEKLTDETINNNIYVDYVKgkml 687
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 641 -LGKDSGLKPFEQVKGITLHPELFSIDNgLLTPTMKAKRPELRNYFRSQIDD 691
Cdd:PTZ00342 688 eVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
115-615 |
1.37e-39 |
|
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: 152.47 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 115 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI-----IEQGCfaysmVIVPLYDTLGNEAITYI 189
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIK--KGDRVAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 190 VNKAELSLVFVDKPEkaklLLEGVENKLIPGLKII-VVMDAYGSELVERGQRCGVEvtsmkameDLGRANRRKPKPPAPE 268
Cdd:cd05926 82 LADLGSKLVLTPKGE----LGPASRAASKLGLAILeLALDVGVLIRAPSAESLSNL--------LADKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATEKALPLSASDTHISYLPLAHIYEQLlkCVMLC---HGAKI---- 341
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLV--ASLLStlaAGGSVvlpp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 GFfqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvq 421
Cdd:cd05926 224 RF---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP-------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 422 sslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgcclTM------PGDWTAGHVGAPMPcNLIKLVDvE 495
Cdd:cd05926 265 ----PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH----QMtsnplpPGPRKPGSVGKPVG-VEVRILD-E 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:cd05926 335 DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDG 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1832481836 576 IYMRSEPVAQ--VF-----VHGESLQAFliaiVVP------DVETLCSWAQKR 615
Cdd:cd05926 414 VLLSHPAVLEavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-608 |
5.79e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 151.84 E-value: 5.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfVKATEKALPLSASDTHISYLPLAHIYEQLLKCV 333
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CRALMGSNLNEGCEILIAPLPLYHIYAFTFHCM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 334 MLchgakigffqgdirLLMDDLKVLQPTvfpvvPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRNNSLWD 413
Cdd:PRK05677 272 AM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNTLFV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 414 RLI----FHKVQSSlggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLI 489
Cdd:PRK05677 313 ALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLC 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 490 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:PRK05677 390 KVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVY 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481836 570 PEKIENIYMRSEPVAQVFV-------HGESLQAFliaIVVPDVETL 608
Cdd:PRK05677 468 PNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-615 |
7.08e-39 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 149.52 E-value: 7.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 123 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 202
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 203 pekAKLLLEGVENKLIPGLKiivvmdAYGselvergqRCGVEVTSMKAMEDLgranrrkpkppapedlAVICFTSGTTGN 282
Cdd:TIGR01923 79 ---SLLEEKDFQADSLDRIE------AAG--------RYETSLSASFNMDQI----------------ATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 283 PKGAMVTHRNIvsdcSAFVKATEKALPLSASDTHISYLPLAHI--YEQLLKCVMlcHGAKIGFFQGDIRLLmDDLKVLQP 360
Cdd:TIGR01923 126 PKAVPHTFRNH----YASAVGSKENLGFTEDDNWLLSLPLYHIsgLSILFRWLI--EGATLRIVDKFNQLL-EMIANERV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 361 TVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvrlmvtGAAPVSA 440
Cdd:TIGR01923 199 THISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 441 TVLTFLRAaLGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHVGAPMPCNLIKL-VDveemnymAAEGEGEVCVKGPNVFQG 518
Cdd:TIGR01923 234 PLIEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVD-------NKEGHGEIMVKGANLMKG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 519 YLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGE 591
Cdd:TIGR01923 306 YL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQ 383
|
490 500
....*....|....*....|....
gi 1832481836 592 SLQAFLIAIVVPDVETLCSWAQKR 615
Cdd:TIGR01923 384 VPVAYIVSESDISQAKLIAYLTEK 407
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-616 |
1.16e-38 |
|
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: 149.79 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAeLSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05909 8 LTYRKLL-TGAIALARKLAKM--TKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKP--EKAKLL-------------LEGVENKLIPGLKIIVVMDAYgselvergqrcgveVTSMKAMEDLGRANRRkpkpp 265
Cdd:cd05909 85 SKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK--------------FPPKWLLRIFGVAPVQ----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 aPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATEKALPLSASDTHISYLPLAHIYeqllkcvmlchgakiGFFQ 345
Cdd:cd05909 146 -PDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFHSF---------------GLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 346 GDIRLLMDDLKVLQ---PTVFPVVPRLLNRMFDRIFGQANTTLKRWLldfasKRKEAELRSGIirnnslwdrlifhkvqs 422
Cdd:cd05909 206 CLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 slggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMA 501
Cdd:cd05909 264 ------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSE 581
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEIL 415
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1832481836 582 P----VAQVFV----HGESLQAFLIAIvVPDVETLCSWAQKRG 616
Cdd:cd05909 416 PedneVAVVSVpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
232-576 |
3.49e-38 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 148.92 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 232 SELVERGQRCGVEVTSMKAMEDLGRANRR------KPKPPAPE----DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV 301
Cdd:cd05904 112 AELAEKLASLALPVVLLDSAEFDSLSFSDllfeadEAEPPVVVikqdDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 302 KATEKALPLSasDTHISYLPLAHIYE-QLLKCVMLCHGAKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMfdr 376
Cdd:cd05904 192 AGEGSNSDSE--DVFLCVLPMFHIYGlSSFALGLLRLGATVvvmpRF---DLEELLAAIERYKVTHLPVVPPIVLAL--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 377 ifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFY 455
Cdd:cd05904 264 ------------------------VKSPIVDKYDL----------SSL----RQIMSGAAPLGKELIEAFRAKFpNVDLG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 456 EGYGQTECTAGCCLTMPGDWTAGHVG-----APMPCnlIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL 530
Cdd:cd05904 306 QGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481836 531 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:cd05904 384 DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-590 |
1.81e-37 |
|
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: 147.01 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 111 SRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIV 190
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVK--PGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 191 NKAELSLVFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSELVERGQRCGvevtsmkAMEDL-GRANRRKPKPPAPE- 268
Cdd:cd12119 94 NHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAGVGVL-------AYEELlAAESPEYDWPDFDEn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATEKALPLSASDTHISYLPLAHI------YeqllKCVMLchGAKI- 341
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESDVVLPVVPMFHVnawglpY----AAAMV--GAKLv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 ---GFFQGDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRkeaelrsgiirnnslwdrlif 417
Cdd:cd12119 236 lpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLDH--------LEANGRDLSSLR--------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 418 hkvqsslggrvRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHV----------GAPMPC 486
Cdd:cd12119 284 -----------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 487 NLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 564
Cdd:cd12119 351 VELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG- 427
|
490 500
....*....|....*....|....*.
gi 1832481836 565 GEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd12119 428 GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
267-599 |
2.11e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 147.51 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCH-GAKigffq 345
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-AKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIElGGQ----- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 346 gdirllmdDLKVLQPTVFP-VVPRLLNRMFDRIFGqANTTLKRWLldfaskrkeaelrsgiirNNSLwdrliFHKVQSSl 424
Cdd:PRK08974 279 --------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEE-----FQELDFS- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 ggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCcltmPGDWT--AGHVGAPMPCNLIKLVDvEEMNY 499
Cdd:PRK08974 326 --SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVN----PYDLDyySGSIGLPVPSTEIKLVD-DDGNE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMR 579
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340
....*....|....*....|....*..
gi 1832481836 580 SEPVAQVF-------VHGESLQAFLIA 599
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
254-559 |
6.47e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 146.30 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCsAFVKATEKALPLSAsDTHISYLPLAHIYeQLLKCV 333
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWVPGLGDGP-ERVLAALPMFHAY-GLTLCL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 334 ---MLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIfgqanttlkrwlldfaskRKEAELRsGIirnns 410
Cdd:PRK05605 282 tlaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 411 lwdrlifhkvqsSLGGrVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMPCN 487
Cdd:PRK05605 334 ------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFPDT 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832481836 488 LIKLVDVEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK05605 399 EVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-599 |
1.89e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 144.58 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 247 SMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD------CSAFVKATEKALPLSASDTHISYL 320
Cdd:PRK12492 186 PFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAPL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 321 PLAHIYEQLLKCVMLchgakigFFQGDIRLLMDDlkvlqptvfpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkeae 400
Cdd:PRK12492 266 PLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF---------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 401 lrSGIIRNNSLWDRLIFHKVQSSLGGRvRLMVT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLTMPGDWTA 477
Cdd:PRK12492 309 --SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELAR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 478 -GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK12492 385 lGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRK 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1832481836 557 KHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------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 |
1.65e-35 |
|
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: 137.25 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAHIYEQLLKCVM-LCHGAKI---GFF 344
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCAD----LTEDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 qgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdrlifhkvqSSL 424
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 ggrvRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTagcCLTM--PGD---WTAGHVGAPMPcnliklvDVEemn 498
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG---VATMcrPGDdaeTVATTCGRACP-------GFE--- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 499 yMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 578
Cdd:cd17638 181 -VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALA 258
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481836 579 RSEPVAQVFV-------HGESLQAFLIA--IVVPDVETLCSWAQKR 615
Cdd:cd17638 259 EHPGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-608 |
6.99e-35 |
|
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: 137.42 E-value: 6.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 122 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 201
Cdd:cd05934 5 TYAELLRESARIAAALAALGIR--PGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 202 kpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapedLAVICFTSGTTG 281
Cdd:cd05934 83 --------------------------------------------------------------------PASILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 282 NPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAHIYEQLLKC-VMLCHGAKI--------GFFQGDIRllm 352
Cdd:cd05934 95 PPKGVVITHANLTFAGYYSARR----FGLGEDDVYLTVLPLFHINAQAVSVlAALSVGATLvllprfsaSRFWSDVR--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 353 ddlkVLQPTVF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggRVR 429
Cdd:cd05934 168 ----RYGATVTnylGAMLSYLLAQPPSPDDRAH--------------------------------------------RLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 430 LmVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVC 509
Cdd:cd05934 200 A-AYGAPNPPELHEEFEER-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 510 VK---GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQV 586
Cdd:cd05934 277 IRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREA 354
|
490 500
....*....|....*....|....*.
gi 1832481836 587 FVHG----ESLQAFLIAIVVPDVETL 608
Cdd:cd05934 355 AVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-628 |
1.11e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 135.10 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFVKateKALPLSASDTHISYLPLAHIYEQLLKcVMLC--HGAKIGFf 344
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIG---ERLGLTEQDRLCIPVPLFHCFGSVLG-VLACltHGATMVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 qgdIRLLMDDLKVLQP------TVFPVVPRllnrMFDRIFGQAnttlKRWLLDFASkrkeaeLRSGIIrnnslwdrlifh 418
Cdd:cd05917 75 ---PSPSFDPLAVLEAiekekcTALHGVPT----MFIAELEHP----DFDKFDLSS------LRTGIM------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 419 kvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMPGD---WTAGHVGAPMPCNLIKLVDv 494
Cdd:cd05917 126 ---------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHTEAKIVD- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 495 EEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 573
Cdd:cd05917 190 PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREI 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 574 ENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQ-KRGFEGSFEEL---CRNK 628
Cdd:cd05917 269 EEFLHTHPKVSDVQVVG-----------VPDErygEEVCAWIRlKEGAELTEEDIkayCKGK 319
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
266-574 |
1.58e-34 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 138.57 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEKALPLSASDTHISYLPLAHIYEqlLKCVMLCH---GAKIG 342
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 343 FFQG-DIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdrlifhkvq 421
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 422 SSlggrVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTM-------PGDWTAGHVGAPMPCNLIKLVD 493
Cdd:PLN02246 298 SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 494 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:PLN02246 372 PETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAEL 450
|
.
gi 1832481836 574 E 574
Cdd:PLN02246 451 E 451
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
254-683 |
3.76e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.70 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATEKALPlsASDTHISYLPLAHIYEQLL 330
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKLEE--GCEVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 331 KCVMLchgAKIGFFQG------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsg 404
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 405 iirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT-MPGDWTAGHVGAP 483
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 484 MPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 562
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 563 AQGEYIAPEKIENIYMRSEPVAQVfvhgeslqaflIAIVVPDvetlcswaQKRGfegsfeELCRNKDVKK--AILEDMVR 640
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1832481836 641 LGKDSGLKPFEQVKGITLHPELFSIDNGlltptmKAKRPELRN 683
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-628 |
7.71e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 136.83 E-value: 7.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYSMV------IVPLYDTlgnEAITYIVNKAE 194
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQ--PGDRVGIWAPNCAEWLLTQ---FATARIgailvnINPAYRA---SELEYALGQSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 195 LSLVFVDK---------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGS-------ELVERGqrcgvEVTSMKAME 252
Cdd:PRK12583 118 VRWVICADafktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPPpgflawhELQARG-----ETVSREALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 253 DLGRANRRkpkppapEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFVKateKALPLSASDTHISYLPLAHIYEQLLKc 332
Cdd:PRK12583 193 ERQASLDR-------DDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVA---ESLGLTEHDRLCVPVPLYHCFGMVLA- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 333 VMLC--HGAKIgFFQGDirlLMDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwlLDFASkrk 397
Cdd:PRK12583 261 NLGCmtVGACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLSS--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 398 eaeLRSGIIrnnslwdrlifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMPGD-- 474
Cdd:PRK12583 319 ---LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdl 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 475 -WTAGHVGAPMPCNLIKLVDVEemNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PRK12583 369 eRRVETVGRTQPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 553 IDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQKR-GFEGSFEEL---C 625
Cdd:PRK12583 447 VGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEELrefC 514
|
...
gi 1832481836 626 RNK 628
Cdd:PRK12583 515 KAR 517
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-607 |
9.28e-34 |
|
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: 134.58 E-value: 9.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVG--PGDLVAVLLERSLEMVvailaVLKAGA-AY----VPLDPSYPAERLAYILEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 196 SLVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICF 275
Cdd:cd05930 86 KLVLTD-----------------------------------------------------------------PDDLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLAHI--YEQLLkcVMLCHGAKI----GFFQGDIR 349
Cdd:cd05930 101 TSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFDvsVWEIF--GALLAGATLvvlpEEVRKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 350 LLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvr 429
Cdd:cd05930 175 ALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL------------------------------------------ 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 430 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT--MPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGE 505
Cdd:cd05930 213 VLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 506 GEVCVKGPNVFQGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 579
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLA 370
|
490 500 510
....*....|....*....|....*....|.
gi 1832481836 580 SEPVAQVFV---HGESLQAFLIAIVVPDVET 607
Cdd:cd05930 371 HPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
111-603 |
1.91e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 135.11 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 111 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPE-WVIIEQGCFAySMVIVPLYDTLGNE 184
Cdd:PRK06188 23 KRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALGL--GTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 185 AITYIVNKAELSLVFVDK---PEKAKLLLEGVenkliPGLKIIVVMDA--YGSELvergqrcgvevtsmkamedLGRANR 259
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDL-------------------LAAAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 260 RKPKPP----APEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATEKALPlsasdTHISYL---PLAH-----IYE 327
Cdd:PRK06188 156 FGPAPLvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIAT--MAQIQLAEWEWP-----ADPRFLmctPLSHaggafFLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 328 QLLK--CVMLCHGAKIGFFqgdIRLLMDDlkvlQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFASKRKeAELrsgi 405
Cdd:PRK06188 229 TLLRggTVIVLAKFDPAEV---LRAIEEQ----RITATFLVPTMIYA----------------LLDHPDLRT-RDL---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 406 irnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV----- 480
Cdd:PRK06188 281 ----------------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrlts 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 481 -GAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:PRK06188 341 cGRPTPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKD 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 559 IFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQafliAIVVP 603
Cdd:PRK06188 418 MI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-628 |
1.93e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 135.71 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 114 PDQPYEWlSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYS-----MV-IVPLYDTlgNEaIT 187
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIE--KGDRVGIWAPNVPEWVLTQ---FATAkigaiLVtINPAYRL--SE-LE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 188 YIVNKAELS-LVFVDK--------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGSelveRGQRCGVEVTSMKAME 252
Cdd:PRK08315 109 YALNQSGCKaLIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKH----PGMLNFDELLALGRAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 253 DLGRANRRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFVKateKALPLSASDTHISYLPLAHIYeqllKC 332
Cdd:PRK08315 185 DDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNN-GYFIG---EAMKLTEEDRLCIPVPLYHCF----GM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 333 VM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwl 389
Cdd:PRK08315 256 VLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 390 LDFASkrkeaeLRSGI-------IRnnslwdrlIFHKVQSSLGgrvrlM--VTGAapvsatvltflraalgcqfyegYGQ 460
Cdd:PRK08315 312 FDLSS------LRTGImagspcpIE--------VMKRVIDKMH-----MseVTIA----------------------YGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 461 TECTAGCCLTMPGD------WTaghVGAPMPCNLIKLVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD 533
Cdd:PRK08315 351 TETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 534 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCS 610
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDEkygEEVCA 494
|
570 580
....*....|....*....|..
gi 1832481836 611 WAQKR-GFEGSFEEL---CRNK 628
Cdd:PRK08315 495 WIILRpGATLTEEDVrdfCRGK 516
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-576 |
3.02e-33 |
|
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: 134.58 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 122 SYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 201
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 202 KPEKAKLLleGVENKLiPGLKIIVVMDaygSELVERGQRCgveVTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSG 278
Cdd:cd17642 124 KKGLQKVL--NVQKKL-KIIKTIIILD---SKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 279 TTGNPKGAMVTHRNIVSDCSAFVKATEKALPLSASdTHISYLPLAHIYEQLLKCVMLCHGAKIGF---FQGDIRL-LMDD 354
Cdd:cd17642 195 STGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDT-AILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrSLQD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 355 LKV----LQPTVFPVVPRllnrmfdrifgqanttlkrwlldfaskrkeaelrSGIIRNNSLwdrlifhkvqSSLggrvRL 430
Cdd:cd17642 274 YKVqsalLVPTLFAFFAK----------------------------------STLVDKYDL----------SNL----HE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 431 MVTGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVC 509
Cdd:cd17642 306 IASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELC 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832481836 510 VKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI 451
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
220-588 |
3.44e-32 |
|
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: 129.31 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 220 GLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsA 299
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLV----N 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 300 FVKATEKALPLSASDTHISYLPLAH--IYEQLLKCvmLCHGAK--------IGFFQGDIRLLMDDLKVlqpTVFPVVPrl 369
Cdd:TIGR01733 148 LLAWLARRYGLDPDDRVLQFASLSFdaSVEEIFGA--LLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLTP-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 370 lnrmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGgrVRLMVTGA-APVSATVLTFLRA 448
Cdd:TIGR01733 221 ----------------------------------------SLLALLAAALPPALAS--LRLVILGGeALTPALVDRWRAR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 449 ALGCQFYEGYGQTECTAGCCLT-----MPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDP 523
Cdd:TIGR01733 259 GPGARLINLYGPTETTVWSTATlvdpdDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRP 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832481836 524 AKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:TIGR01733 338 ELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
264-615 |
2.64e-31 |
|
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: 127.43 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLAH--IYEQLLKCvmLCHGAKI 341
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIAFdaCIGEIFST--LCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 gFFQGDIRLLMDDLKVLqpTVFPVVPRLLnrmfdrifgqanTTLKRWLLDfaskrkeaelrsgiirnnslwdrlifhkvq 421
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSIL------------STLSPQDFP------------------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 422 sslggRVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLT--MPGDWTagHVGAPMPCNLIKLVDVEEMNY 499
Cdd:cd17653 210 -----NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 500 MAAEgEGEVCVKGPNVFQGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:cd17653 281 PEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832481836 574 ENIYMRSEPVAQ---VFVHGEslqaFLIAIVVP---DVETLCSWAQKR 615
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-578 |
3.84e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 128.71 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 113 KPDQPYEWlSYKQVAELSECIGSALIQKGFKTApdqfiGIFAQNRPEW---VIIEQGCFAYSMVIVPLYDTLGNEAITYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 190 VNKAElSLVF-----VDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVErgqrcgveVTSMKAMEDLGRANrrKPKP 264
Cdd:PRK06087 117 LNKCQ-AKMFfaptlFKQTRPVDLILPLQNQ--LPQLQQIVGVDKLAPATSS--------LSLSQIIADYEPLT--TAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAHiyeqllkcvmlchgaKIGFF 344
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN----LTWQDVFMMPAPLGH---------------ATGFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 QGDIR-LLMDDLKVLQPTVFPVVP-RLLNRmfDRIFGQANTTlkRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqS 422
Cdd:PRK06087 245 HGVTApFLIGARSVLLDIFTPDAClALLEQ--QRCTCMLGAT--PFIYDLLNLLEKQPADL------------------S 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 SLggrvRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMN 498
Cdd:PRK06087 303 AL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-EARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 499 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 578
Cdd:PRK06087 375 TLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-616 |
5.34e-31 |
|
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: 126.34 E-value: 5.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELslvfv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVG--PGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 dkpekaklllegvenklipglKIIVVMDAYGSelvergqrcgvevTSMKAMedlgranrrkpkppaPEDLAVICFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERFRQ-------------FDPAAM---------------PDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAHIYEQLlkcvmlcHGAKIGFFQGDIRLLMDdlkVLQP 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAER----LGLGPGDVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQD---IWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 361 TVfpvVPRLLNRmfDRI-FGQANTTLKRWLLDfaskrkeAELRSGiirnnslwDRLifhkvqsslgGRVRLMVTGAAPVS 439
Cdd:cd05903 172 DK---ALALMRE--HGVtFMMGATPFLTDLLN-------AVEEAG--------EPL----------SRLRTFVCGGATVP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 440 ATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQ 517
Cdd:cd05903 222 RSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 518 GYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQ 594
Cdd:cd05903 301 GYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLG 378
|
490 500
....*....|....*....|....*...
gi 1832481836 595 AFLIAIVV------PDVETLCSWAQKRG 616
Cdd:cd05903 379 ERACAVVVtksgalLTFDELVAYLDRQG 406
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
255-637 |
6.81e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 126.64 E-value: 6.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 255 GRANRRKPKPPaPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAHIyeqllkcvm 334
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQ----WTADDVLVHGLPLFHV--------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 335 lcHGAKIGffqgdirllmddlkVLQPTvfpvvprllnrmfdRIFGQANTTLKrwlldFASKRKEAELRSGiirnNSL--- 411
Cdd:PRK07787 182 --HGLVLG--------------VLGPL--------------RIGNRFVHTGR-----PTPEAYAQALSEG----GTLyfg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 412 ----WDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCN 487
Cdd:PRK07787 223 vptvWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 488 LIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHI 559
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 560 FKLAQGEyiapekIENIYMRSEPVAQVFVHGE---SLQAFLIAIVVPD-----------VETLCSwAQKRGFEGSF-EEL 624
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGAddvaadelidfVAQQLS-VHKRPREVRFvDAL 454
|
410
....*....|....*.
gi 1832481836 625 CRN---KDVKKAILED 637
Cdd:PRK07787 455 PRNamgKVLKKQLLSE 470
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-603 |
1.22e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 126.59 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLK--KGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DkPEKAKLLLEGVENKlipglkiivVMDAYGSELVERGQrcgVEVTSMKAMEDLGRANRRKPKPPAP--EDLAVICFTSG 278
Cdd:PRK08316 115 D-PALAPTAEAALALL---------PVDTLILSLVLGGR---EAPGGWLDFADWAEAGSVAEPDVELadDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 279 TTGNPKGAMVTHRNIVSD-CSAFVkatekALPLSASDTHISYLPLahiYeqllkcvmlcHGAKIGFFqgdirlLMDDLKV 357
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEyVSCIV-----AGDMSADDIPLHALPL---Y----------HCAQLDVF------LGPYLYV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 358 LQPTVFPVVPRlLNRMFDRIFGQANTTLkrwlldFASKrkeaelrsgiirnnSLWDRLIFHKV-----QSSLggrvRLMV 432
Cdd:PRK08316 238 GATNVILDAPD-PELILRTIEAERITSF------FAPP--------------TVWISLLRHPDfdtrdLSSL----RKGY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 433 TGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLTMPGDwTAGHVG-APMPC-NL-IKLVDvEEMNYMAAeGE-GE 507
Cdd:PRK08316 293 YGASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVlNVeTRVVD-DDGNDVAP-GEvGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 508 VCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVF 587
Cdd:PRK08316 370 IVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVA 447
|
490 500
....*....|....*....|
gi 1832481836 588 V----HGESLQAfLIAIVVP 603
Cdd:PRK08316 448 ViglpDPKWIEA-VTAVVVP 466
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
1.99e-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: 125.48 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 119 EWLSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 199 FVDkpekaklllegvenklipglkiivvmdaygSELVERGQRCGVevTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSG 278
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLP--VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 279 TTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLA---HIYEQLLKcvmLCHGAKIGFFQGDI----RLL 351
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYAfdiSLLELLLP---LLAGARVVIAPRETqrdpEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 352 MDDLKVLQPTVFpvvprllnrmfdrifgQANTTLKRWLLDfaskrkeaelrSGiirnnslWDRLifhkvqsslgGRVRLM 431
Cdd:cd12116 210 ARLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR----------AGLTAL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 432 VTGAA--PVSATVLTflraALGCQFYEGYGQTECT--AGCCLTMPGDwTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGE 507
Cdd:cd12116 246 CGGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 508 VCVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRS 580
Cdd:cd12116 320 LYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAH 398
|
490 500
....*....|....*....|....*.
gi 1832481836 581 EPVAQ--VFVHGESLQAFLIAIVVPD 604
Cdd:cd12116 399 PGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-628 |
3.62e-30 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 124.72 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 120 WLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 200 VDKPekakLLLEgvenklipglkiivvmdaygsELVERGQRcgvevtsmkamedlgranRRKPKPPAPE-DLAVICFTSG 278
Cdd:cd12118 107 VDRE----FEYE---------------------DLLAEGDP------------------DFEWIPPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 279 TTGNPKGAMVTHRnivsdcSAFVKATEKALpLSASDTHISYL---PLAHiyeqllkCVMLCHGAKIGFFQG--------D 347
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANIL-EWEMKQHPVYLwtlPMFH-------CNGWCFPWTVAAVGGtnvclrkvD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 348 IRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSlwdrlifHKVQSSLGGR 427
Cdd:cd12118 210 AKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAP-------PSDARPLPHR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 428 VRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDWTAGHV----------GAPMPCNL-IKLVD 493
Cdd:cd12118 250 VHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAWKP-EWDELPTeerarlkarqGVRYVGLEeVDVLD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 494 VEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 571
Cdd:cd12118 326 PETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSV 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832481836 572 KIENIymrsepvaqVFVHGESLQAFLIAivVPD---VETLCSW-AQKRGFEGSFEEL---CRNK 628
Cdd:cd12118 404 EVEGV---------LYKHPAVLEAAVVA--RPDekwGEVPCAFvELKEGAKVTEEEIiafCREH 456
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
255-598 |
9.37e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 124.36 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 255 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC---SAFVKATEKALPLSASDTHISYLPLAHIYeQLLK 331
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmEAWLQPAFEKKPRPDQLNFVCALPLYHIF-ALTV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 332 CVMLchGAKIGffqG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelr 402
Cdd:PRK07059 270 CGLL--GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL---------------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 403 sgiirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYG--QTECTAGCCLTMPGDWTaGHV 480
Cdd:PRK07059 317 -----NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDATEFS-GTI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 481 GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:PRK07059 383 GLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481836 561 kLAQGEYIAPEKIENIyMRSEP----VAQVFVH----GESLQAFLI 598
Cdd:PRK07059 462 -LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-557 |
2.82e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 122.29 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAIT-----YIVNKAEL 195
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVK--PGDRVAVQVEKSPEALALYLATLRAGAVFLPL-----NTAYTlaeldYFIGDAEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 196 SLVFVDkPEKAKLLLEGVENKlipGLKIIVVMDAYGS-ELVERGQrcgvevtsmkamedlGRANRRKPKPPAPEDLAVIC 274
Cdd:PRK07514 102 ALVVCD-PANFAWLSKIAAAA---GAPHVETLDADGTgSLLEAAA---------------AAPDDFETVPRGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 275 FTSGTTGNPKGAMVTHRNIVSDCSAFVKA---TEKalplsasDTHISYLPLAHIYEQLLKC-VMLCHGAKIGFFQG-DIR 349
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYwrfTPD-------DVLIHALPIFHTHGLFVATnVALLAGASMIFLPKfDPD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 350 LLMDDLKvlQPTVFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsSL 424
Cdd:PRK07514 236 AVLALMP--RATVMMGVPtfytRLLqEPRLTR----------------------------------------------EA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 GGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaGCCLTM-P--GDWTAGHVGAPMPCNLIKLVDVEEMNYMA 501
Cdd:PRK07514 268 AAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMNTSnPydGERRAGTVGFPLPGVSLRVTDPETGAELP 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481836 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK07514 345 PGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-588 |
4.28e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 122.40 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSD-CSAFVKATEKALplsASDTHISYLPLAHIYEQLLKC--VMLCHGAKIGFFQ 345
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMI---GQVVTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 346 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRLIFHKVqsslg 425
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 426 gRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagcCLTMP-GDWTAGH-------VGAPMPCNLIKLVDVEE 496
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1832481836 577 YMRSEPVAQVFV 588
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-576 |
7.61e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 121.87 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 262 PKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVK--ATEKALPlSASDTHISYLPLAHIYEQLLKCV-MLCH 337
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeASQYEYP-GSDNVYLAALPMFHIYGLSLFVVgLLSL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 338 GAKI----GFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwd 413
Cdd:PLN02574 270 GSTIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK--------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 414 rlifhkvqsSLggrvRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA----GCCLTMPGDWTAghVGAPMPCNL 488
Cdd:PLN02574 320 ---------SL----KQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 489 IKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:PLN02574 385 AKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQI 463
|
....*...
gi 1832481836 569 APEKIENI 576
Cdd:PLN02574 464 APADLEAV 471
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
268-591 |
1.17e-28 |
|
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: 118.99 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 268 EDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATEKALPLSASDTHISYLPLAHI--YEQLLKCVMLCHGAKI--GF 343
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH----WWSAIGSALNLGLTEDDNWLCALPLFHIsgLSILMRSVIYGMTVYLvdKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 FQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqss 423
Cdd:cd05912 153 DAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL-------------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 424 lggrvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPMPCNLIKLVDveemNYM 500
Cdd:cd05912 192 -----RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIED----DGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 501 AAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRS 580
Cdd:cd05912 261 PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSH 338
|
330
....*....|.
gi 1832481836 581 EPVAQVFVHGE 591
Cdd:cd05912 339 PAIKEAGVVGI 349
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
267-604 |
2.29e-28 |
|
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: 119.18 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSaSDTHI----SYLPLAHIYEQLLkcvMLCHGAKIG 342
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALST----SALAHGRALGLT-SESRVlqfaSYTFDVSILEIFT---TLAAGGCLC 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 343 ffqgdI---RLLMDDLkvlqptvfpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdrLIFHK 419
Cdd:cd05918 177 -----IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDPE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 420 VQSSLggrvRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIkLVDVEEMN 498
Cdd:cd05918 213 DVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-VVDPDNHD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 499 YMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLaQ 564
Cdd:cd05918 286 RLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-R 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481836 565 GEYIAPEKIENIYMRSEP-----VAQVFVH-GESLQAFLIAIVVPD 604
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
127-574 |
3.43e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 118.76 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 127 AELSECIG-SALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFvdkpek 205
Cdd:PRK09088 26 AELDALVGrLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 206 aklllegvenklipglkiivvmdayGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPapEDLAVICFTSGTTGNPKG 285
Cdd:PRK09088 100 -------------------------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 286 AMVTHRNIVSDCSAFVKatekalpLSASDTHISYL---PLAHIYeQLLKCV--MLCHGAKIGFFQGdirllmddlkvLQP 360
Cdd:PRK09088 153 VMLSERNLQQTAHNFGV-------LGRVDAHSSFLcdaPMFHII-GLITSVrpVLAVGGSILVSNG-----------FEP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 361 TvfpvvpRLLNRMFDRIFGQANTtlkrwlldFASKRKEAELRSGIIRNNSLWDRLIfhkvqsslggrvrLMVTGAAP-VS 439
Cdd:PRK09088 214 K------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhAA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 440 ATVLTFLraALGCQFYEGYGQTEctAGCCLTMPGDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCVKGPN 514
Cdd:PRK09088 267 EDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPAGV-PGELLLRGPN 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 515 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09088 342 LSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
6.39e-28 |
|
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: 115.06 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFvkATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAK---IGFFQ 345
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 346 GDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdrlifhkvqssl 424
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 ggrvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 503
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 504 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYMRSE 581
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1832481836 582 PVAQVFVHGeslqafliaivVPDVE 606
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-603 |
1.56e-27 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 117.46 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAElSLVFV 200
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLG--VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 --------DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERgqrcgveVTSMKAME---DLGR--ANRRkpkpPAP 267
Cdd:PRK13295 133 vpktfrgfDHAAMARRLRPE-----LPALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAH----IYEQLLKcVMLchGAKIgf 343
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER----LGLGADDVILMASPMAHqtgfMYGLMMP-VML--GATA-- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 fqgdirllmddlkVLQPTVFPVvprllnRMFDRI------FGQANTTlkrWLLDFASKRKEAElrsgiirnnslwdrlif 417
Cdd:PRK13295 268 -------------VLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESG----------------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 418 hKVQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLTMPGD---WTAGHVGAPMPCNLIKLVDV 494
Cdd:PRK13295 309 -RPVSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 495 EEMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK13295 383 DGAPLPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIE 458
|
490 500 510
....*....|....*....|....*....|..
gi 1832481836 575 NIYMRSEPVAQVFVHG---ESLQAFLIAIVVP 603
Cdd:PRK13295 459 ALLYRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-575 |
1.74e-27 |
|
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: 116.39 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 173 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaYGSELVERGQRCGVEVTSMKAME 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG--------------------------AADRLRDALPASPDPGTVLDADG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 253 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAHIY--EQLL 330
Cdd:cd05922 102 IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY----LGITADDRALTVLPLSYDYglSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 331 kcVMLCHGAKIgFFQGDIRL---LMDDLKVLQPTVFPVVPRLLNrMFDRIfgqanttlkrwlldfasKRKEAELrsgiir 407
Cdd:cd05922 178 --THLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKL------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 408 nNSLwdRLIfhkvqSSLGGRVRlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTA---GHVGAPM 484
Cdd:cd05922 231 -PSL--RYL-----TQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMT-YLPPERILekpGSIGLAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 485 PCNLIKLVDVEEMNYmaAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:cd05922 293 PGGEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF 370
|
410
....*....|..
gi 1832481836 564 qGEYIAPEKIEN 575
Cdd:cd05922 371 -GNRISPTEIEA 381
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-590 |
1.96e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.50 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 119 EWLSYKQVAELSECIGSALIQKgFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAITyivnKAELSLV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL-----NIRLT----ENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 199 FVDKpekaklllegvenklipGLKIIVVMDAYGSELVERGQRCGVE----VTSMKAMEDLGRANRrkpKPPAPEDLAVIC 274
Cdd:PRK06839 96 LKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrvisITSLKEIEDRKIDNF---VEKNESASFIIC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 275 FTSGTTGNPKGAMVTHRNIvsdcsaFVKATEK--ALPLSASDTHISYLPLAHIyeqllkcvmlchgAKIGFFQgdirllm 352
Cdd:PRK06839 156 YTSGTTGKPKGAVLTQENM------FWNALNNtfAIDLTMHDRSIVLLPLFHI-------------GGIGLFA------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 353 ddlkvlQPTVFP----VVPRLLN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdrlifh 418
Cdd:PRK06839 210 ------FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS--------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 419 kvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLVDvEE 496
Cdd:PRK06839 266 ---------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-EN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 576
Cdd:PRK06839 335 KNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV 412
|
490
....*....|....
gi 1832481836 577 YMRSEPVAQVFVHG 590
Cdd:PRK06839 413 INKLSDVYEVAVVG 426
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-624 |
2.34e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 117.13 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVK--KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 D----KPEKAKLLLEGVEN--KLIPGLKIIVVMDAYGSELVERGQRcgvevtsmkAMEDLgRANRRKPKPPAP---EDLA 271
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGDL---------DWDEL-LAAASAEFEPEPtdaDDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 272 VICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEKALP----LSASD----THISYL---PLAH-----IYEqllkcvml 335
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPgdvfWCTADigwaTGHSYIvygPLLNgatvvLYE-------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 336 chgAKIGFFQGDiRL--LMDDLKVlqpTVFPVVPRLLnRMfdrifgqanttLKRWLLDFASKrkeaelrsgiirnnslWD 413
Cdd:COG0365 260 ---GRPDFPDPG-RLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAGDEPLKK----------------YD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 414 RlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLV 492
Cdd:COG0365 305 L-------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 493 DvEEMNYMAAEGEGEVCVKG--PNVFQGYLKDPAKTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 568
Cdd:COG0365 374 D-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRI 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 569 APEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPdvetlcswaqKRGFEGSfEEL 624
Cdd:COG0365 452 GTAEIESALVSHPAVAEAAVvgvpDEIRGQV-VKAFVVL----------KPGVEPS-DEL 499
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-608 |
3.16e-27 |
|
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: 118.42 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 86 YDDVTTLYEGFQRgiQVSnngpclgsRKPDQP-----YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEW 160
Cdd:COG1020 472 YPADATLHELFEA--QAA--------RTPDAVavvfgDQSLTYAELNARANRLAHHLRALGVG--PGDLVGVCLERSLEM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 161 VIIEQGCF----AYsmviVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVEnklipglkiIVVMDAygselve 236
Cdd:COG1020 540 VVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVP---------VLALDA------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 237 rgqrcgvevtsmkamEDLGRANRRKPKPPA-PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDT 315
Cdd:COG1020 600 ---------------LALAAEPATNPPVPVtPDDLAYVIYTSGSTGRPKGVMVEHRALV----NLLAWMQRRYGLGPGDR 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 316 HISYLPLAH---IYEQLLkcvMLCHGAKIGFFQGDIRLLMDDLKVL----QPTVFPVVPRLLNRMFDrifgqanttlkrw 388
Cdd:COG1020 661 VLQFASLSFdasVWEIFG---ALLSGATLVLAPPEARRDPAALAELlarhRVTVLNLTPSLLRALLD------------- 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 389 lldfaskrkeaelrsgiirnnSLWDRLifhkvqsslgGRVRLMVTG--AAPVsATVLTFLRAALGCQFYEGYGQTECTAG 466
Cdd:COG1020 725 ---------------------AAPEAL----------PSLRLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPTETTVD 772
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 467 CCL--TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDG--W 535
Cdd:COG1020 773 STYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarL 851
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481836 536 LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQ--VFVHGESLQA-FLIAIVVPDVETL 608
Cdd:COG1020 852 YRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAA 926
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-615 |
4.97e-27 |
|
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: 112.42 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATEKALPLSASDTHISYLPLAHI--YEQLLKCVMLchGAKIGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 347 DiRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 427 rVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEG 506
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 507 EVCVKGPNVFQGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQV 586
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350
....*....|....*....|....*....|....*.
gi 1832481836 587 FVHG---ESLQAFLIAIVV----PDVETLCSWAQKR 615
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVgrgpADPAELRAWLKDK 292
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
114-557 |
5.34e-27 |
|
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: 115.84 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 114 PDQPYEWLSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNRpEWVIIEQGC----FAYSMVIVPLYDTLGNEAITYI 189
Cdd:cd05906 33 ADGSEEFQSYQDLLEDARRLAAGLRQLGLR-PGDSVILQFDDNE-DFIPAFWACvlagFVPAPLTVPPTYDEPNARLRKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 190 VNKAELslvfVDKPekakLLLegVENKLIPGLKiivvmdaygsELVERGQRCGVEVTSMkamEDLGRANRRKPKPPA-PE 268
Cdd:cd05906 111 RHIWQL----LGSP----VVL--TDAELVAEFA----------GLETLSGLPGIRVLSI---EELLDTAADHDLPQSrPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDCsafvKATEKALPLSASDTHISYLPLAHIyeqllkcvmlchgAKIGFFQ-GD 347
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARS----AGKIQHNGLTPQDVFLNWVPLDHV-------------GGLVELHlRA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 348 IRLLMDDLKVLQPTVFPVVPRLLnRMFDRIfgQANTTlkrWLLDFA-SKRKEAELRsgiiRNNSLWDrlifhkvQSSLgg 426
Cdd:cd05906 231 VYLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDLLEE----IEDGTWD-------LSSL-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 427 rvRLMVTGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGC--CLTMP-GDWTAGH----VGAPMPCNLIKLVD 493
Cdd:cd05906 292 --RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVD 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832481836 494 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 557
Cdd:cd05906 370 -DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
264-598 |
8.12e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 115.52 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 264 PPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEKALplSASDTHISYLPLAHIYEqlLKCVM---LCHGA 339
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCK--EGEEVVLGVLPFFHVYG--MTAVMnlsIMQGY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 340 KIGFF-QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdrlifh 418
Cdd:PRK06710 277 KMVLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS--------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 419 kvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPgdW---TAGHVGAPMPCNLIKLVDVE 495
Cdd:PRK06710 325 ---------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFL--WekrVPGSIGVPWPDTEAMIMSLE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK06710 394 TGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEE 471
|
330 340 350
....*....|....*....|....*....|
gi 1832481836 576 IYMRSEPVAQVFV-------HGESLQAFLI 598
Cdd:PRK06710 472 VLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
152-615 |
8.48e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 115.26 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 152 IFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAklLLEGVENkLIPGLKIIVVMDAYG 231
Cdd:PRK07786 72 ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 232 SELVergqrcgvevtsmKAMEDLGRANRrKPKPPA--PEDL-AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEKAL 308
Cdd:PRK07786 149 DDSV-------------LGYEDLLAEAG-PAHAPVdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 309 PlsaSDTHISYLPLAHIYEQLLKCVMLCHGAKIgffqgdirllmddlkVLQPTvfpvvprllnRMFDrifgqANTTLKRW 388
Cdd:PRK07786 215 N---SDVGFVGVPLFHIAGIGSMLPGLLLGAPT---------------VIYPL----------GAFD-----PGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 389 lldfaskrkEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGC 467
Cdd:PRK07786 262 ---------EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 468 CLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWL 545
Cdd:PRK07786 333 CMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 546 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAF---LIAIVVPD-------VETLCSWAQKR 615
Cdd:PRK07786 411 EEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
173-604 |
1.01e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.95 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 173 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDaygseLVERgqrcgveVTSMKAME 252
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLED-----LKAK-------ISKVDKLT 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 253 DLGRA--------NRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATEKALPLSASDTHISYLPLAH 324
Cdd:PRK08633 759 ALLAArllparllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFH 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 325 --------IYEQLLKCVMLCH-----GAKIG--FFQGDIRLLmddlkVLQPTVFpvvprllnRMFDRifgqaNTTLKRwl 389
Cdd:PRK08633 835 sfgltvtlWLPLLEGIKVVYHpdptdALGIAklVAKHRATIL-----LGTPTFL--------RLYLR-----NKKLHP-- 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 390 LDFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL 469
Cdd:PRK08633 895 LMFAS---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASV 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 470 TMP-----GDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL---DKDGWL 536
Cdd:PRK08633 942 NLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWY 1021
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832481836 537 HTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniymrsEPVAQVFvHGESLQafLIAIVVPD 604
Cdd:PRK08633 1022 VTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD 1079
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-604 |
2.66e-26 |
|
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: 113.19 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 111 SRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTL 181
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVG--PDTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 182 GNEAITYIVNKAELSLVFVDKPEKAKLLLEGvenklipglkIIVVMDAygselvergqrcgvEVTSMKAMEDLGRANRrk 261
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 262 pkppaPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLA------HIYEQLLKCVML 335
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASISfdasvtEIFASLLSGNTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 336 CHGAKIGffQGDIRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwLLDfaskrkeaelrsgiirnnslwdrl 415
Cdd:cd17655 207 YIVRKET--VLDGQALTQYIRQNRITIIDLTPAHLK-----------------LLD------------------------ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 416 ifhKVQSSLGGRVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCC--LTMPGDWTAGHV--GAPMPCNLI 489
Cdd:cd17655 244 ---AADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 490 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:cd17655 321 YILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI- 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1832481836 564 QGEYIAPEKIENIYMRSEPVAQ--VFVH-GESLQAFLIAIVVPD 604
Cdd:cd17655 399 RGYRIELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-598 |
2.83e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 112.19 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKTApdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAelslvfv 200
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 dkpekaklllegvenklipGLKIIVVmdayGSELvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 280
Cdd:cd05935 73 -------------------GAKVAVV----GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAHI--YEQLLKCVMLCHGAKIGFFQGDIRLLMDDLKVL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTG----LTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 359 QPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPV 438
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--------ATPEFKTRDLSS---------------------------------LKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 439 SATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 519 YLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 1832481836 589 HGESLQAFLI 598
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-671 |
4.29e-26 |
|
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: 113.30 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 107 PCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF---AYSMVIVPLYDTLGN 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLS--AERPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 184 E--AITYIVNKAELSLVFVDKPEKAKLLLEGVenkLIPGLKIIVVmdaygselveRGQRCGVEVTSMK---AMEDLGRAN 258
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVS----------RNAVAGRGAISFAelaATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 259 RRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATEKALPLSASDTHISYLPLAHIYeqllkcvmlchG 338
Cdd:cd05921 157 AAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCA--NQAMLEQTYPFFGEEPPVLVDWLPWNHTF-----------G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 339 AKIGF-----------------FQGDIRLLMDDLKVLQPTVFPVVPR----LLNRMfdrifgQANTTLKRWLLdfasKRK 397
Cdd:cd05921 223 GNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVPAgwemLVAAL------EKDEALRRRFF----KRL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 398 EAELRSGIIRNNSLWDRLIFHKVQSSlGGRVRlmvtgaapvsatvltflraalgcqFYEGYGQTECTAGCCLTMPGDWTA 477
Cdd:cd05921 293 KLMFYAGAGLSQDVWDRLQALAVATV-GERIP------------------------MMAGLGATETAPTATFTHWPTERS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 478 GHVGAPMPCNLIKLVdveemnymAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKII 553
Cdd:cd05921 348 GLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 554 DRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLcsWAQKRGFEGSFEELCRNKDVK 631
Cdd:cd05921 420 GRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLAC--RRLVGLQEASDAEVLRHAKVR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1832481836 632 KAILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLT 671
Cdd:cd05921 497 AAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-615 |
9.46e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 111.21 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 123 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 202
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 203 pekaklllEGVENKLIPGLKIIVvmdaygSELVErgqrcgvevtsmkamedlGRANRRKPKPPAPED-LAVICFTSGTTG 281
Cdd:PRK03640 107 --------DDFEAKLIPGISVKF------AELMN------------------GPKEEAEIQEEFDLDeVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 282 NPKGAMVTHRNivsdcsAFVKATEKALPL--SASDTHISYLPLAHI--YEQLLKCVMlcHGAKI----GFFQGDI-RLLM 352
Cdd:PRK03640 155 KPKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHIsgLSILMRSVI--YGMRVvlveKFDAEKInKLLQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 353 DDlKVlqpTVFPVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdrlifhkvqsslggrvRLMV 432
Cdd:PRK03640 227 TG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF-----------------RCML 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 433 TGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPM-PCNlIKLVDveEMNYMAAEGEGEV 508
Cdd:PRK03640 261 LGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEEGEI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 509 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:PRK03640 336 VVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGV 413
|
490 500 510
....*....|....*....|....*....|....
gi 1832481836 589 HGESLQ-------AFLIAIVVPDVETLCSWAQKR 615
Cdd:PRK03640 414 VGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-682 |
1.14e-25 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 110.50 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAqNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLR-KGDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 280
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVS---DCSAFVKATEKALPLSASDTHISYLPLAHIYEQLLK--CVMLCHGAKIgffqgDIRLLMDDL 355
Cdd:cd05972 94 GLPKGVLHTHSYPLGhipTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLgaTVFVYEGPRF-----DAERILELL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 356 KVLQPTVFPVVPrllnrmfdrifgqanTTLKRWL-LDFASKRKeaelrsgiirnnslwdrlifhkvqsslgGRVRLMVTG 434
Cdd:cd05972 169 ERYGVTSFCGPP---------------TAYRMLIkQDLSSYKF----------------------------SHLRLVVSA 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 435 AAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLTMPgdWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKG 512
Cdd:cd05972 206 GEPLNPEVIEWWRAATGLPIRDGYGQTETGLtvGNFPDMP--VKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 513 PNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV-- 588
Cdd:cd05972 283 PPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAEAAVvg 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 589 -----HGESLQAFLIAivvpdvetlcswaqKRGFEGSfEELcrnkdvkkaiLEDMVRLGKdSGLKPFEQVKGITLHPELf 663
Cdd:cd05972 361 spdpvRGEVVKAFVVL--------------TSGYEPS-EEL----------AEELQGHVK-KVLAPYKYPREIEFVEEL- 413
|
570
....*....|....*....
gi 1832481836 664 sidngLLTPTMKAKRPELR 682
Cdd:cd05972 414 -----PKTISGKIRRVELR 427
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
1.21e-25 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 113.41 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 89 VTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVR--PGDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 169 AYSMVIVPLYDTlgNEAITYIVNKAELSLVFVDKPEKAKLL------LEGVENklipglkiivVMDAYGSELVERGQRCG 242
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILtcrsrkLETVVY----------THSFYDEDDHAVARDLN 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 243 VEVTSMKAMEDLGRANRRKPKPPAPED----LAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATekALPLS-ASDTHI 317
Cdd:PTZ00297 572 ITLIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLVMTG--VLPSSfKKHLMV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 318 SYLPLAHIYEQLLKCVMLCHGAKIGffQGDIRLLMDDLKVLQPTVFPVVPRLlnrmfdriFGQANTTLKR---------- 387
Cdd:PTZ00297 650 HFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavys 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 388 WLLDfaskrKEAELRSGII---RNNSLWDRLIFHK-VQSSLGGRVRLMVTGAAPVSATvltflraalgcqfyegYGQTEC 463
Cdd:PTZ00297 720 WLFE-----RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLEH 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 464 TAGCCltmpgdwtaghvgapMPCnliklvdVEEMNYMAAegEGEVCVKG---PNVfQGYLK---DPAKTAE----ALDKD 533
Cdd:PTZ00297 779 ISVCY---------------VPC-------LREVFFLPS--EGVFCVDGtpaPSL-QVDLEpfdEPSDGAGigqlVLAKK 833
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 534 GWL-HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAfLIAIVVPDVETL-CS 610
Cdd:PTZ00297 834 GEPrRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVeFE 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 611 WAQKRGFE---GSFEELCRNKDVKKA---ILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNY 684
Cdd:PTZ00297 913 WRQSHCMGeggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSY 992
|
650
....*....|
gi 1832481836 685 FRSQIDDLYS 694
Cdd:PTZ00297 993 FSSVIERFYS 1002
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-646 |
3.09e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 110.74 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQPY--------EW--LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---Y 178
Cdd:PRK08180 51 EAPDRVFlaergadgGWrrLTYAEALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 179 DTLGN--EAITYIVNKAELSLVFVDKPEKAKLLLEGVEnklIPGLKIIVVmdaygselveRGQRCGVEVTSMKAMEDLGR 256
Cdd:PRK08180 129 SLVSQdfGKLRHVLELLTPGLVFADDGAAFARALAAVV---PADVEVVAV----------RGAVPGRAATPFAALLATPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 257 ANRRKPKPPA--PEDLAVICFTSGTTGNPKGAMVTHRNIVS------DCSAFVKATEKALplsasdthISYLPLAH---- 324
Cdd:PRK08180 196 TAAVDAAHAAvgPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEPPVL--------VDWLPWNHtfgg 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 325 -----IyeqllkcvMLCHGAKI---------GFFQGDIRllmdDLKVLQPTVFPVVPR--------------LLNRMFDR 376
Cdd:PRK08180 268 nhnlgI--------VLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpalerdaaLRRRFFSR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 377 ifgqanttLKrwLLDFASkrkeAELRSgiirnnSLWDRLifHKV-QSSLGGRVRLMVtgaapvsatvltflraalgcqfy 455
Cdd:PRK08180 336 --------LK--LLFYAG----AALSQ------DVWDRL--DRVaEATCGERIRMMT----------------------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 456 eGYGQTEcTAGCCL--TMPGDwTAGHVGAPMPCNLIKLVDVEemnymaaeGEGEVCVKGPNVFQGYLKDPAKTAEALDKD 533
Cdd:PRK08180 371 -GLGMTE-TAPSATftTGPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 534 GWLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVEt 607
Cdd:PRK08180 440 GYYRSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITGHD-RDEIGLLVFPNLD- 517
|
570 580 590
....*....|....*....|....*....|....*....
gi 1832481836 608 LCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSG 646
Cdd:PRK08180 518 ACRRLAGLLADASLAEVLAHPAVRAAFRERLARLNAQAT 556
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
184-584 |
6.81e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 110.04 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 184 EAITYIVNKAELSLVFVDKPE-------KAKLLLEGVenkliPGLKIIVVMDayGSELVERGQRCGVEVTSMKAME---D 253
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVD--LARYLPGPKRLAVPLIRRKAHArilD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 254 LGRANRRKP-------KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC---SAFVKATEkalplsaSDTHISYLPLA 323
Cdd:PRK07529 192 FDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLGP-------GDTVFCGLPLF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 324 HIYEQLLKC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL---QPTVFPVVPRLLNRMFDRIFGQANTtlkrwlldfask 395
Cdd:PRK07529 265 HVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDI------------ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 396 rkeaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GD 474
Cdd:PRK07529 333 --------------------------SSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 475 WTAGHVGAPMPCNLIKLVDVEEM-NYM--AAEGE-GEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTL 550
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYF 461
|
410 420 430
....*....|....*....|....*....|....
gi 1832481836 551 KIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:PRK07529 462 WLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
266-607 |
2.61e-24 |
|
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: 106.56 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLAHiyeQLlkCVM-----LCHGAk 340
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSF---DL--SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 341 igffqgdirllmddlkvlqpTVFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDRLIFHK 419
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 420 --VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTmpgDWT----AGH----VGAPMPCNLI 489
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYI---EVTpevlDGYdrlpIGYAKPGAKL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 490 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd05945 284 VILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGY 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1832481836 567 YIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDVET 607
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-682 |
2.78e-24 |
|
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: 107.07 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DkPEKAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgqrcgvevtsmKAMEDL--GRANRRKPKPPAPEDLAVICFTSG 278
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 279 TTGNPKGAMVTHRNIVSDCSAFVKATekaLPLSASDTHISYLPLAHIYEqllkcvmLCHGAKIGFFQGDIRLLM------ 352
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 353 ----DDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWdrlifhkvQSSLGGRV 428
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAPNL--------PSRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 429 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 509 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 589 HGESLQAFLI---AIVVPdvetlcswaqKRGFEGSfeelcrnkdvkkAILEDMVRLGKDSGLKPFEQVKGITLHPELFSi 665
Cdd:cd05959 440 VGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRLAPYKYPRWIVFVDELPK- 496
|
570
....*....|....*..
gi 1832481836 666 dngllTPTMKAKRPELR 682
Cdd:cd05959 497 -----TATGKIQRFKLR 508
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
111-615 |
1.35e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 105.51 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 111 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPlydtlgnea 185
Cdd:PRK06178 44 RERPQRPaIIFyghvITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVP--------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 186 ITYIVNKAELSLVFVDKpekaklllegvenklipGLKIIVVMDAYgSELVER-GQRCGVE---VTSMKAM---------- 251
Cdd:PRK06178 113 VSPLFREHELSYELNDA-----------------GAEVLLALDQL-APVVEQvRAETSLRhviVTSLADVlpaeptlplp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 252 -------------EDLGRANRRKPKP-----PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtekALPLSAS 313
Cdd:PRK06178 175 dslraprlaaagaIDLLPALRACTAPvplppPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV---AVVGGED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 314 DTHISYLPLAHIyeqllkcvmlchgakigffQGDirllmdDLKVLQPTVF--PVVprLLNRmfdrifgqanttlkrwlld 391
Cdd:PRK06178 252 SVFLSFLPEFWI-------------------AGE------NFGLLFPLFSgaTLV--LLAR------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 392 faskrkeaelrsgiirnnslWDRLIF------HKVQSSLG---GRVRLMVTGAapVSATVLTFL---------------- 446
Cdd:PRK06178 286 --------------------WDAVAFmaaverYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdy 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 447 ----RAALGCQFYEG-YGQTEcTAGCcltmpGDWTAG-------------HVGAPMPCNLIKLVDVEEMNYMAAEGEGEV 508
Cdd:PRK06178 344 rqrwRALTGSVLAEAaWGMTE-THTC-----DTFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 509 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAV 495
|
570 580 590
....*....|....*....|....*....|....*.
gi 1832481836 589 HG---ESLQAFLIAIVVP------DVETLCSWAQKR 615
Cdd:PRK06178 496 VGrpdPDKGQVPVAFVQLkpgadlTAAALQAWCREN 531
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
119-583 |
4.04e-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: 103.86 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 119 EWLSYKQVAELSECIGSALIQKGfktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA---ITYIVNKAEL 195
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 196 SLVFVDKPEKAKLLLEGVENKLIPGLKIIVVmDAYGSELVERGQrcgvevtsmkamedlgranrrkPKPPAPEDLAVICF 275
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV-DLLPDTSAADWP----------------------PPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVSDCSAFVkateKALPLSASDTHISYLPLAHiyeqllkcvmlchgaKIGFFQGdirllmddl 355
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIR----RAYGLDPGDVVVSWLPLYH---------------DMGLIGG--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 356 kVLQPTV--FPVV---PR-LLNRMFdrifgqanttlkRWL-----------------LDFASKRKEAELRSGIirnnslw 412
Cdd:cd05931 209 -LLTPLYsgGPSVlmsPAaFLRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 413 dRLifhkvqsslgGRVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLTMPGDWT 476
Cdd:cd05931 269 -DL----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 477 AGHV----------------GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE------ALDKDG 534
Cdd:cd05931 338 AGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGG 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1832481836 535 WLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 583
Cdd:cd05931 418 WLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-626 |
1.14e-22 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 102.20 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF- 199
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 200 -VDKPekakllleGVENKLIPGLKIIVVMDAYGSelvergqrcGVEVTSMKAMEDlgranrrkpKPPAPEDLAVICFTSG 278
Cdd:cd05923 107 aVDAQ--------VMDAIFQSGVRVLALSDLVGL---------GEPESAGPLIED---------PPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 279 TTGNPKGAMVTHRNIVSdcSAFVKATEKALPLSASDTHISYLPLAHIyeqllkcvmlchgakIGFFQgdirLLMDDLkVL 358
Cdd:cd05923 161 TTGLPKGAVIPQRAAES--RVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-AL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 359 QPTVFPVvprllnRMFDRIFgqanttlkrwlldfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGAAP 437
Cdd:cd05923 219 DGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 438 VSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMPgDWTAGHVGAPMPCNLIKLVDV-EEMNYMAAEG-EGEVCVK--GP 513
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 514 NVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG--- 590
Cdd:cd05923 356 AAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvad 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 1832481836 591 ESLQAFLIAIVVPDVETLCswaqkrgfEGSFEELCR 626
Cdd:cd05923 434 ERWGQSVTACVVPREGTLS--------ADELDQFCR 461
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
268-599 |
1.60e-22 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 101.00 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateKALPLSASDTHISYLPLAHIYEqllkcvmLCHGAKIGFFQGD 347
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFSSAKMFFGYG-------LGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 348 IRLLMDD----------LKVLQPTVFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdrlif 417
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 418 hkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEM 497
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 1832481836 578 MRSEPVAQVFV------HGES-LQAFLIA 599
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-604 |
3.96e-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: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGV--GPGDVVGVLAERSPELVvallaVLKAGA-AY----VPLDPELPAERLAFMLADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 196 SLVFVDKPEKAklllegvenkLIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrrkpkPPAPEDLAVICF 275
Cdd:cd12117 96 KVLLTDRSLAG----------RAGGLEVAVVIDEALDAGPAGNPAV----------------------PVSPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVSdcsaFVKATeKALPLSASDTHISYLPLA------HIYEQLLkcvmlcHGAKIgffqgdir 349
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLAfdastfEIWGALL------NGARL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 350 llmddlkVLQPtvfPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkeaelrsgiirNNSLWdRLIFHKVQSSLGGrVR 429
Cdd:cd12117 205 -------VLAP---KGTLLDPDALGALIAEEGVTVL--WL------------------TAALF-NQLADEDPECFAG-LR 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 430 LMVTGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCCLTMPGDWTAGHV--GAPMPcNLIKLVdVEEMNYMAAEG 504
Cdd:cd12117 253 ELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIA-NTRVYV-LDEDGRPVPPG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 505 E-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 577
Cdd:cd12117 331 VpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAAL 409
|
490 500 510
....*....|....*....|....*....|
gi 1832481836 578 MRSEPVAQVFV---HGESLQAFLIAIVVPD 604
Cdd:cd12117 410 RAHPGVREAVVvvrEDAGGDKRLVAYVVAE 439
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
173-590 |
4.37e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 100.35 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 173 VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekaklllegvENKLIPGLKI-IVVMDAYGSELVERGQRCGVEVTSMKam 251
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 252 edlgranrrkpkPPAPEDLAVICFTSGTTGNPKGAMVTHRNIvsdcsaFVKATEK--ALPLSASDTHISYLPLAHIYE-Q 328
Cdd:PRK06145 145 ------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHviALGLTASERLLVVGPLYHVGAfD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 329 LLKCVMLCHGAKIGFFQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASKRkeaelrsgiir 407
Cdd:PRK06145 207 LPGIAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA----------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 408 nnslWdrlifhkvqsSLGGrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMP 485
Cdd:PRK06145 268 ----W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRALA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 486 CNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 565
Cdd:PRK06145 327 HVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGG 403
|
410 420
....*....|....*....|....*
gi 1832481836 566 EYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK06145 404 ENIASSEVERVIYELPEVAEAAVIG 428
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
121-603 |
4.82e-22 |
|
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: 100.24 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALiqKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 200
Cdd:TIGR03098 26 LTYAALSERVLALASGL--RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRrkPKPPAPEDLAVICFTSGTT 280
Cdd:TIGR03098 103 TSSERLDLLHPA-----LPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADP--PHPVIDSDMAAILYTSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIY--EQLLKCVMlcHGAKIgffqgdirLLMDDLkvl 358
Cdd:TIGR03098 176 GRPKGVVLSHRNLV----AGAQSVATYLENRPDDRLLAVLPLSFDYgfNQLTTAFY--VGATV--------VLHDYL--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 359 qptvfpvVPRllnrmfDRIfgqanTTLKRwlldfaskrkeaELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPV 438
Cdd:TIGR03098 239 -------LPR------DVL-----KALEK------------HGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 439 SATVLTFLRAALG-CQFYEGYGQTECTAGCCLTmPG--DWTAGHVGAPMPcNLIKLVDVEEMNYMAAEGEGEVCVKGPNV 515
Cdd:TIGR03098 289 PRATLSRLRSFLPnARLFLMYGLTEAFRSTYLP-PEevDRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGELVHRGALV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 516 FQGYLKDPAKTAEALDK----DGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVA 584
Cdd:TIGR03098 367 AMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVA 445
|
490 500
....*....|....*....|...
gi 1832481836 585 QVFVHG----ESLQAfLIAIVVP 603
Cdd:TIGR03098 446 EAVAFGvpdpTLGQA-IVLVVTP 467
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-603 |
4.89e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 100.35 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGL--LPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKpekaklllEGVENKLIPGLKIIVVMDAYGSElveRGQRCG-VEVTsmkamedLGRANRRKPKPPAPEDL----AVICF 275
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGtLSVH-------LDAATEPTPATSTPEGLrpddAMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAH---IYEQLLKcvMLCHGAKI-----GFFQGd 347
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVRAIITGYR----LSPRDATVAVMPLYHghgLIAALLA--TLASGGAVllparGRFSA- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 348 iRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKEAELRsgIIRNNSlwdrlifhkvqss 423
Cdd:PRK05852 257 -HTFWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKPAALR--FIRSCS------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 424 lggrvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT----------AGCCLTmPGDWT--AGHVGAPMpcnlIKL 491
Cdd:PRK05852 305 ------------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQTEN-PVVSTglVGRSTGAQ----IRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 492 VDVEEMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPE 571
Cdd:PRK05852 368 VGSDGLPLPAGA-VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPE 444
|
490 500 510
....*....|....*....|....*....|....*
gi 1832481836 572 KIENIYMRSEPVAQVFVHGESLQAF---LIAIVVP 603
Cdd:PRK05852 445 RVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
1.72e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 100.04 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGsALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKN--TPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKP--EKAKL--LLEGVENklipGLKIIVVMDaygselVERGQRCGVEVTSMKAmedlGRANRRKPKPPAPEDLAVICFT 276
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 277 SGTTGNPKGAMVTHRNIVSDCsAFVKATekaLPLSASDTHISYLPLAHIYeqllkcvmlchgakiGFFQGDIRLLMDDLK 356
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANR-AQVAAR---IDFSPEDKVFNALPVFHSF---------------GLTGGLVLPLLSGVK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 357 VL---QPTVFPVVPRLlnrmfdrIFgQANTTL----KRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqsslggrVR 429
Cdd:PRK06814 863 VFlypSPLHYRIIPEL-------IY-DTNATIlfgtDTFLNGYARYAHPYDFRS------------------------LR 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 430 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNymaaEGeGEVC 509
Cdd:PRK06814 911 YVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRLF 985
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832481836 510 VKGPNVFQGYLK-DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:PRK06814 986 VRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
266-682 |
2.07e-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: 97.50 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHRNIvsdcsafvkatekalplsasdthISYLPLAHIYEQLLKcvmlcHGAKIGFFQ 345
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVL-----------------------LGHLPGVQFPFNLFP-----RDGDLYWTP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 346 GD---IRLLMDdlkVLQPTVFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdrliFHKV 420
Cdd:cd05971 138 ADwawIGGLLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 421 QSSLGG-RVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCCLTMPGDwtAGHVGAPMPCNLIKLVDvEE 496
Cdd:cd05971 201 QLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 497 MNYMAAEGEGEVCVKGPN--VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 574
Cdd:cd05971 278 GTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 575 NIYMRSEPVAQVFV-------HGESLQAFliaIVVpdvetlcswaqKRGFEGSfEELCRNkdvkkaiLEDMVRlgkdSGL 647
Cdd:cd05971 356 ECLLKHPAVLMAAVvgipdpiRGEIVKAF---VVL-----------NPGETPS-DALARE-------IQELVK----TRL 409
|
410 420 430
....*....|....*....|....*....|....*
gi 1832481836 648 KPFEQVKGITLHPELfsidngLLTPTMKAKRPELR 682
Cdd:cd05971 410 AAHEYPREIEFVNEL------PRTATGKIRRRELR 438
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
266-696 |
2.81e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 98.33 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtekaLPLSASDTHISYLPLAHI--YEQLLKCVML--CHGAKI 341
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAI----VGYGEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 GFfqgDIRLLMDDLKVLQPTVFPVVPRLL------NRMfdRIFGQANTTLKRWLldfaskrkeaelrSGiirNNSLWDRL 415
Cdd:PLN02860 246 KF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRKIL-------------NG---GGSLSSRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 416 IfhKVQSSLGGRVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLTMPGDWTAGH-VGAPMPcnliklvDV 494
Cdd:PLN02860 305 L--PDAKKLFPNAKLFSAYGMTEACSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP-------HV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 495 EEMNYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 573
Cdd:PLN02860 374 ELKIGLdESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 574 ENIYMRSEPVAQVFVHGeSLQAFLIAIVVPDVETLCSW--------AQKRGFEGSFEEL---CRNKdvkkailedmvrlg 642
Cdd:PLN02860 453 EAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK-------------- 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1832481836 643 kdsGLKPFEQVKGITLHPELFSidnglLTPTMKAKRPELRNYFRSQIDDLYSTI 696
Cdd:PLN02860 518 ---NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
112-588 |
6.12e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.14 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVK--RGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 187 TYIVNKAELSLVFVDkpekAKLL--LEGVENKLIPgLKIIVVMDAYGSELVERGQRcgveVTSMKAMedlgrANRRKPKP 264
Cdd:PRK06155 111 EHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAGWS----TAPLPPL-----DAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 265 PAPEDLAVICFTSGTTGNPKGAMVTH-------RNIVSDcsafvkatekaLPLSASDTHISYLPLAHIYEQLLKCVMLCH 337
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED-----------LEIGADDVLYTTLPLFHTNALNAFFQALLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 338 GAKI---------GFFqgdirllmDDLKVLQPTVF----PVVPRLLnrmfdrifgqanttlkrwlldfaSKRKEAELRSg 404
Cdd:PRK06155 246 GATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARESDRA- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 405 iirnnslwdrlifHKVQSSLGGrvrlmvtgaaPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDwTAGHVGAPM 484
Cdd:PRK06155 294 -------------HRVRVALGP----------GVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 485 PCNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVF-QGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 561
Cdd:PRK06155 350 PGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR 427
|
490 500
....*....|....*....|....*...
gi 1832481836 562 lAQGEYIAPEKIENIyMRSEP-VAQVFV 588
Cdd:PRK06155 428 -RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
264-604 |
8.02e-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: 96.26 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGF 343
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 FQGDIRllMDDlkvlqptvfpvvprllnrmfdrifgqanTTLKRWLldfaskrkeAELR-SGIIRNNSLWDRLIFH-KVQ 421
Cdd:cd17651 208 PPEEVR--TDP----------------------------PALAAWL---------DEQRiSRVFLPTVALRALAEHgRPL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 422 SSLGGRVRLMVTGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLTMPGD---WTA-GHVGAPMPCNLIKLVDvE 495
Cdd:cd17651 249 GVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD-A 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:cd17651 328 ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIE 406
|
330 340 350
....*....|....*....|....*....|....*...
gi 1832481836 570 PEKIENIYMRSEPVAQ--VFVHGE-SLQAFLIAIVVPD 604
Cdd:cd17651 407 LGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGD 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
70-604 |
8.91e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.11 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 70 ARRS----ALLDSDEplvyfYDDVTTLY----EGFQRGIQVSNNGPCLGSRKPDQPY-----EWLSYKQVAELSECIGSA 136
Cdd:PRK12316 1970 AQAAlgelALLDAGE-----RQRILADWdrtpEAYPRGPGVHQRIAEQAARAPEAIAvvfgdQHLSYAELDSRANRLAHR 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 137 LIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGvenk 216
Cdd:PRK12316 2045 LRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA---- 2118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 217 lipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVS 295
Cdd:PRK12316 2119 -------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 296 DCsafvKATEKALPLSASDTHISYLPLAH--IYEQLLkcVMLCHGAkigffqgdiRLLMDDLKVLQPtvfpvvprllNRM 373
Cdd:PRK12316 2174 HC----QAAGERYELSPADCELQFMSFSFdgAHEQWF--HPLLNGA---------RVLIRDDELWDP----------EQL 2228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 374 FDRIFGQANTtlkrwLLDFASkrkeaelrsgiirnnSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQ 453
Cdd:PRK12316 2229 YDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 454 F-YEGYGQTECTA-----GCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTA 527
Cdd:PRK12316 2289 YlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTA 2367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 528 EALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV---HGESLQAfL 597
Cdd:PRK12316 2368 ERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ-L 2445
|
....*..
gi 1832481836 598 IAIVVPD 604
Cdd:PRK12316 2446 VAYVVPD 2452
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
2.16e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 95.41 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQPYEW-----LSYKQVAELSECIGSAL-----IQKGfktapDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTL 181
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLqqecgVRKG-----DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 182 GNEAITYIVNKAELSLVFVdkpekAKLLLEGVEnKLI--PGLKIIVV------MDAYGSE-----LVERGQRCGVEVTSM 248
Cdd:PRK08314 96 REEELAHYVTDSGARVAIV-----GSELAPKVA-PAVgnLRLRHVIVaqysdyLPAEPEIavpawLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 249 KAMEDLGRANRRkpkPPA----PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAH 324
Cdd:PRK08314 170 VAWKEALAAGLA---PPPhtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSN----STPESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 325 IYEqlLKCVMlcHGAkigFFQGDIRLLMddlkvlqptvfpvvPR----LLNRMFDR---IFGQANTTLkrwLLDFaskrk 397
Cdd:PRK08314 243 VTG--MVHSM--NAP---IYAGATVVLM--------------PRwdreAAARLIERyrvTHWTNIPTM---VVDF----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 398 eaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG----------- 466
Cdd:PRK08314 294 ---LASPGLAERDL----------SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpkl 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 467 CCLTMPgdwTAGhVGApmpcnliKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA---LDKDGWLHTGDIGK 543
Cdd:PRK08314 357 QCLGIP---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGR 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 544 WLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVPDVE 606
Cdd:PRK08314 426 MDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
138-598 |
4.00e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 94.36 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 138 IQKGFKTApdqfigIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfVDKPEKAKLLLEGVENKL 217
Cdd:PRK08008 59 IRKGDKVA------LHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLL-VTSAQFYPMYRQIQQEDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 218 IPgLKIIVVMDAYGSElvERGqrcgveVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdc 297
Cdd:PRK08008 132 TP-LRHICLTRVALPA--DDG------VSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 298 SAFVKATEKALplSASDTHISYLPLAHIYEQllkcvmlCHGAkigffqgdirllMddlkvlqpTVFPVVPRLLnrmfdri 377
Cdd:PRK08008 201 AGYYSAWQCAL--RDDDVYLTVMPAFHIDCQ-------CTAA------------M--------AAFSAGATFV------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 378 fgqanttlkrwLLDFASKRKeaelrsgiirnnsLWDRLIFHK--VQSSLGGRVR-LMVTgaaPVSAT--------VLTFL 446
Cdd:PRK08008 245 -----------LLEKYSARA-------------FWGQVCKYRatITECIPMMIRtLMVQ---PPSANdrqhclreVMFYL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 447 RAA----------LGCQFYEGYGQTECTAGCCLTMPGD---WTAghVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKG 512
Cdd:PRK08008 298 NLSdqekdafeerFGVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 513 ---PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVH 589
Cdd:PRK08008 374 vpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVV 452
|
490
....*....|....*.
gi 1832481836 590 G-------ESLQAFLI 598
Cdd:PRK08008 453 GikdsirdEAIKAFVV 468
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
168-590 |
4.53e-20 |
|
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: 94.48 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 168 FAYSM--------VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgQ 239
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIE-KAAPECPSKPKLVWVGDPVPE--G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 240 RCGVEVTSMKAMEDLGRanRRKPKPPAPEDLAVICFTSGTTGNPKgaMVTHRNI-----VSDCSAFVKATEKALPLSASD 314
Cdd:cd05970 159 WIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTyplghIVTAKYWQNVREGGLHLTVAD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 315 THISYLPLAHIYEQLLKcvmlchGAKI---GFFQGDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLd 391
Cdd:cd05970 235 TGWGKAVWGKIYGQWIA------GAAVfvyDYDKFDPKALLEKLSKYGVTTFCAPP----------------TIYRFLI- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 392 faskrkeaelRSGIIRNNslwdrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLTM 471
Cdd:cd05970 292 ----------REDLSRYD-----------LSSL----RYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 472 PG-DWTAGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCV---KGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWL 545
Cdd:cd05970 346 PWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWMD 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1832481836 546 PNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd05970 424 EDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
184-626 |
6.00e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.86 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 184 EAITYIVNKAELSLVFVDkPEKAKLLLEGVEnkLIPGLKIIVV---MDAYGselveRGQRCG-VEVTSMKAMEDLGRAnr 259
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP-----GGRFIGaLDYEAFLASGDPDFA-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 260 rkPKPPAPE-DLAVICFTSGTTGNPKGAMVTHR----NIVSDcsafvkATEKALPlsasdTHISYL---PLAHiyeqllk 331
Cdd:PRK08162 175 --WTLPADEwDAIALNYTSGTTGNPKGVVYHHRgaylNALSN------ILAWGMP-----KHPVYLwtlPMFH------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 332 CVMLCH--------GAKIGFFQGDIRLLMDDLKVLQPTVF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAE 400
Cdd:PRK08162 235 CNGWCFpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 401 LRSGIirnnslwdrlifhkvqsslGGRVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLTMPGdWTA- 477
Cdd:PRK08162 291 WRAGI-------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAl 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 478 ---------GHVGAPMPC-NLIKLVDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWL 545
Cdd:PRK08162 349 plderaqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLH 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 546 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRsepvaqvfvHgeslQAFLIAIVV--PDV---ETLCSWAQ-KRGFEG 619
Cdd:PRK08162 428 PDGYIKIKDRSKDII-ISGGENISSIEVEDVLYR---------H----PAVLVAAVVakPDPkwgEVPCAFVElKDGASA 493
|
490
....*....|
gi 1832481836 620 SFEEL---CR 626
Cdd:PRK08162 494 TEEEIiahCR 503
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-624 |
8.18e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 91.77 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsAFVKAtekALPLSAS-DTHISYLPLAHI---YEQLLkcVMLCHGAKIg 342
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLA---LNSLFDPdDVLLCGLPLFHVngsVVTLL--TPLASGAHV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 343 ffqgdirLLMDDLKVLQPTVFPVVPRLLNRMfdRIfgQANTTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqS 422
Cdd:cd05944 73 -------VLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------S 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 SLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GDWTAGHVGAPMPCNLIKLVDVE-EMNYM 500
Cdd:cd05944 122 SL----RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 501 --AAEGE-GEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:cd05944 198 rdCAPDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEAL 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1832481836 578 MRSEPVaqvfvhgeslqAFLIAIVVPDV---ETLCSWAQ-KRGFEGSFEEL 624
Cdd:cd05944 276 LRHPAV-----------AFAGAVGQPDAhagELPVAYVQlKPGAVVEEEEL 315
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-626 |
8.61e-20 |
|
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: 93.29 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKTA-------PdqfigifaqNRPEWVIIeqgCFAYSMV-IVPLYdTL----GNEaITY 188
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGdrvvvqlP---------NVAEFVIV---FFALFRAgAIPVF-ALpahrRAE-ISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 189 IVNKAELS-LVFVDKPEK------AKLLLEGVenkliPGLKIIVVMDAYGSELvergqrcgvevtsmkAMEDLGRANRRK 261
Cdd:COG1021 117 FAEQSEAVaYIIPDRHRGfdyralARELQAEV-----PSLRHVLVVGDAGEFT---------------SLDALLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 262 PKP-PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSafVKATEKALPLSASDTHISYLPLAHIYeqllkcVMLCHGAk 340
Cdd:COG1021 177 SEPrPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--YS--VRASAEICGLDADTVYLAALPAAHNF------PLSSPGV- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 341 IGFFQ--GDIRL-----------LMDDLKVlqpTVFPVVPRLLNRMfdrifgqanttlkrwlLDFASKRKeAELrsgiir 407
Cdd:COG1021 246 LGVLYagGTVVLapdpspdtafpLIERERV---TVTALVPPLALLW----------------LDAAERSR-YDL------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 408 nnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGD---WTAGHVGAP 483
Cdd:COG1021 300 --------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeeVILTTQGRP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 484 M-PCNLIKLVDVEEMNymAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIF 560
Cdd:COG1021 359 IsPDDEVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQIN 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 561 KlaQGEYIAPEKIENIYMRSEPVAQVfvhgeslqafliAIV-VPDV---ETLCSWAQKRGFEGSFEELCR 626
Cdd:COG1021 437 R--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPDEylgERSCAFVVPRGEPLTLAELRR 492
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-605 |
2.08e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 93.69 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 55 CDLSMQSVEvagsggARRSALLDSD-EPLVYFYDDVTTLyegFQRGIQVSNNGPCLGSRKpdqpyEWLSYKQVAELSECI 133
Cdd:PRK12467 485 GELPLLDAE------ERARELVRWNaPATEYAPDCVHQL---IEAQARQHPERPALVFGE-----QVLSYAELNRQANRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 134 GSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLL 209
Cdd:PRK12467 551 AHVLIAAG--VGPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVRLLLTQ-SHLLAQL 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 210 legvenKLIPGLKIIVvMDAYGSELVergqrcgvevtsmkamedlGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVT 289
Cdd:PRK12467 624 ------PVPAGLRSLC-LDEPADLLC-------------------GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 290 HRNIVSdcsaFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIgffqgdirLLMDDLKVLQPTVFpvvprl 369
Cdd:PRK12467 678 HGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF------ 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 370 lnrmFDRIFGQANTTLKrwlldfaskrkeaelrsgiiRNNSLWDRLIFHKVQSSLGGRVRLMVTGAA-PVSATVLTFlRA 448
Cdd:PRK12467 740 ----AALMADQGVTVLK--------------------IVPSHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-AL 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 449 ALGCQFYEGYGQTECTAGC----CLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPA 524
Cdd:PRK12467 795 GPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPA 873
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 525 KTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV--HGESLQA 595
Cdd:PRK12467 874 LTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGL 952
|
570
....*....|
gi 1832481836 596 FLIAIVVPDV 605
Cdd:PRK12467 953 QLVAYLVPAA 962
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
268-576 |
2.27e-19 |
|
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: 90.01 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtekALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFFQGD 347
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKE---GLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 348 IRL--LMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaskrkeaELRSGIIRNNSLwdRLIfhkvqsslg 425
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKLVS------------------------ELKSANATVPSL--RLI--------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 426 grvrlMVTGAAPVSATVLTFLRAALgCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAeG 504
Cdd:cd17635 123 -----GYGGSRAIAADVRFIEATGL-TNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 505 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-671 |
4.81e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 91.65 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 107 PCLGSRKPDQ-PYEWLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---YDTLG 182
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 183 NE--AITYIVNKAELSLVFVDKPEK-----AKLLLEGVEnklipglkiIVVMDAYG--------SELVERGQRCGVEvts 247
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT---------VVHVTGPGegiasiafADLAATPPTAAVA--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 248 mKAMEDLGranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFVKATEKALPLSASDTHISYLPLAHIYe 327
Cdd:PRK12582 212 -AAIAAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMMCAN-IAMQEQLRPREPDPPPPVSLDWMPWNHTM- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 328 qllkcvmlchGAKIGFfQGDIR----LLMDDLKVLqPTVFPVVPRLLNRMFDRIFGQANTTLKrwLLDFASKRKEAELRS 403
Cdd:PRK12582 278 ----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDALRRS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 404 giirnnslwdrliFHKvqsslggRVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGccLTMPGDWTA 477
Cdd:PRK12582 344 -------------FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP--TTTGTHWDT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 478 ---GHVGAPMPCNLIKLVDVEEmNYmaaegegEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTL 550
Cdd:PRK12582 401 ervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 551 KIIDRKKHIFKLAQGEYIAPEKIE-NIYMRSEPVAQ-VFVHGESlQAFLIAIVVPDVETLCSWAQKRGfeGSFEELCRNK 628
Cdd:PRK12582 473 IFDGRVAEDFKLSTGTWVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVVKHP 549
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1832481836 629 DVKKAILEDMVRLGKDSGlKPFEQVKGITLHPELFSIDNGLLT 671
Cdd:PRK12582 550 AVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
115-583 |
4.89e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 91.01 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 115 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPlydtlgneaityivnkae 194
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIK--PGQEVVFQITHNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 195 lslVFVDKPEKAKLLLEGVENKLI-PGLkiivvmdaygselvergqrcgveVTSMKAMEDLgranrrkpkppaPEDLAVI 273
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 274 CFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAHiyeqllkcvmlchgaKIGFFQGDIRLLMD 353
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTE----WKTKDRILSWMPLTH---------------DMGLIAFHLAPLIA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 354 DLK-VLQPT-VFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLM 431
Cdd:cd05908 173 GMNqYLMPTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMI 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 432 VTGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCCL----------------------------TMPGDWTA 477
Cdd:cd05908 234 LNGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSECLTF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 478 GHVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRK 556
Cdd:cd05908 314 VEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGRE 390
|
490 500
....*....|....*....|....*..
gi 1832481836 557 KHIFkLAQGEYIAPEKIENIYMRSEPV 583
Cdd:cd05908 391 KDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-585 |
6.74e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 91.31 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 259 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIYeqllkcvmlchG 338
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSF-----------G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 339 AKIGFFQGdirlLMDDLKVL---QPTVFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgii 406
Cdd:PRK08043 421 LTVGLFTP----LLTGAEVFlypSPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 407 rnnslwdrlifhkvqsslggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 486
Cdd:PRK08043 480 --------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 487 NLIKLVDVEEMnymaaEGEGEVCVKGPNVFQGYLK--DP-------AKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK08043 540 MDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAK 614
|
330 340
....*....|....*....|....*...
gi 1832481836 558 HIFKLAqGEYIAPEKIENIYMRSEPVAQ 585
Cdd:PRK08043 615 RFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-583 |
1.01e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 90.06 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 220 GLKIIVV---MDAYGSELVERGQRcGVEVTSMKAMEDLgranrrKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD 296
Cdd:PRK07768 108 GAKAVVVgepFLAAAPVLEEKGIR-VLTVADLLAADPI------DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 297 CSAFVKATEKALplsASDTHISYLPLAHIyeqllkcvMlchgAKIGFFQGDIRLLMDDLKVlQPTVFPVVPRLLNRMFDR 376
Cdd:PRK07768 181 AEAMFVAAEFDV---ETDVMVSWLPLFHD--------M----GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELISK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 377 IFGQ-------ANTTLKRwLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVS-ATVLTFLRA 448
Cdd:PRK07768 245 YRGTmtaapnfAYALLAR-RLRRQAKPGAFDL--------------------SSL----RFALNGAEPIDpADVEDLLDA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 449 ---------ALGCqfyeGYGQTECTAGCCLTMPGD--------------------WTAGHV------GAPMPCNLIKLVD 493
Cdd:PRK07768 300 garfglrpeAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 494 vEEMNYMAAEGEGEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 573
Cdd:PRK07768 376 -EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDI 452
|
410
....*....|
gi 1832481836 574 ENIYMRSEPV 583
Cdd:PRK07768 453 ERAAARVEGV 462
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
147-590 |
1.55e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 89.84 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 147 DQFIGIFAQNRPEW--VIIEQGCFAysMVIVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLLLEGVENklIPGLKII 224
Cdd:PRK05620 64 DQRVGSMMYNCAEHleVLFAVACMG--AVFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 225 VVMDAYGSELVERGQRCGVEVTSMKAMEDlGRANRRkPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVSDCsafvka 303
Cdd:PRK05620 139 VFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQS------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 304 tekaLPLSASDThisyLPLAHiYEQLLKCVMLCH----GAKIGFFQGDIRLLMDDLKVLQPTVFPVVprllnrmfdrifg 379
Cdd:PRK05620 211 ----LSLRTTDS----LAVTH-GESFLCCVPIYHvlswGVPLAAFMSGTPLVFPGPDLSAPTLAKII------------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 380 qaNTTLKRwlldfaskrkeaeLRSGIirnNSLWDRLIFHKVQSSlGGRVRL--MVTGAAPVSATVLTFLRAALGCQFYEG 457
Cdd:PRK05620 269 --ATAMPR-------------VAHGV---PTLWIQLMVHYLKNP-PERMSLqeIYVGGSAVPPILIKAWEERYGVDVVHV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 458 YGQTECTAGCCLTMPGDWTAGHVGAP-------MPCNLIKLVdVEEMNYMAA--EGEGEVCVKGPNVFQGYLKDPAKT-- 526
Cdd:PRK05620 330 WGMTETSPVGTVARPPSGVSGEARWAyrvsqgrFPASLEYRI-VNDGQVMEStdRNEGEIQVRGNWVTASYYHSPTEEgg 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832481836 527 --------------AEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK05620 409 gaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-604 |
1.93e-18 |
|
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: 88.87 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPEKAKLllegvenklipglkiivvmdaygselvergqRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTT 280
Cdd:cd17646 102 TADLAARL-------------------------------PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLA---HIYEQLLKcvmLCHGAKIGFFQGD-------IRL 350
Cdd:cd17646 151 GRPKGVMVTHAGIVN----RLLWMQDEYPLGPGDRVLQKTPLSfdvSVWELFWP---LVAGARLVVARPGghrdpayLAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 351 LMDDLKVlqpTVFPVVPRLLnrmfdRIFGQanttlkrwlldfaskrkeaELRSGIIRNnslwdrlifhkvqsslggrVRL 430
Cdd:cd17646 224 LIREHGV---TTCHFVPSML-----RVFLA-------------------EPAAGSCAS-------------------LRR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 431 MVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGE 507
Cdd:cd17646 258 VFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 508 VCVKGPNVFQGYLKDPAKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 581
Cdd:cd17646 337 LYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHP 415
|
490 500
....*....|....*....|....*.
gi 1832481836 582 PVAQVFV---HGESLQAFLIAIVVPD 604
Cdd:cd17646 416 AVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-615 |
5.58e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.88 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 dKPEKAKL----LLEGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICFT 276
Cdd:PRK06164 114 -WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 277 -SGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLahiyeqllkCVMLCHGAKIGFFQGDIRLLMDDl 355
Cdd:PRK06164 189 tSGTTSGPKLVLHRQATLL----RHARAIARAYGYDPGAVLLAALPF---------CGVFGFSTLLGALAGGAPLVCEP- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 356 kvlqptVF--PVVPRLL-----------NRMFDRIFGQANTTLkrwllDFASKRkeaelrsgiirnnslwdRLIFHKVQS 422
Cdd:PRK06164 255 ------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----------------LFGFASFAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 SLGGRVRLMVTGAAPvsatvLTFLraalgcqfyegYGQTECTA-GCCLTMPGDWTAGHV--GAPM-PCNLIKLVDVEEMN 498
Cdd:PRK06164 307 ALGELAALARARGVP-----LTGL-----------YGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARVRARDPQDGA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 499 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYM 578
Cdd:PRK06164 371 LLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALE 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1832481836 579 RSEPVAQVFVHGESLQ------AFLIAI--VVPDVETLCSWAQKR 615
Cdd:PRK06164 450 ALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-604 |
6.12e-18 |
|
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: 87.33 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAG--VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPekakllleGVENKLIPGLKIIVVMDAygselvergqrcgvevtsmkamedLGRANRRKPKPPAPEDLAVICFTSGTT 280
Cdd:cd12114 91 DGP--------DAQLDVAVFDVLILDLDA------------------------LAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNivsdCSAFVKATEKALPLSASDTHISYLPLAH---IYEQLlkcVMLCHGAKIGFFQGDIR----LLMD 353
Cdd:cd12114 139 GTPKGVMISHRA----ALNTILDINRRFAVGPDDRVLALSSLSFdlsVYDIF---GALSAGATLVLPDEARRrdpaHWAE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 354 DLKVLQPTVFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSLwdRLIFHK---VQSSLGGRVRL 430
Cdd:cd12114 212 LIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL--RLVLLSgdwIPLDLPARLRA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 431 MVTGAAPVSatvltflraaLGcqfyegyGQTECTAGCCL----TMPGDWTAGHVGAPMPCNLIKLVDveemnymaAEGE- 505
Cdd:cd12114 266 LAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLD--------PRGRd 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 506 ------GEVCVKGPNVFQGYLKDPAKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 575
Cdd:cd12114 321 cpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEA 399
|
490 500 510
....*....|....*....|....*....|.
gi 1832481836 576 IYMRSEPVAQ--VFVHGESLQAFLIAIVVPD 604
Cdd:cd12114 400 ALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-617 |
6.68e-18 |
|
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: 86.75 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsafvkatekalplsasdthiSYLPLAHIYEQLLKCVMLCHGAKIGF--F 344
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAH----------------------AAHAWRREYELDSFPVRLLQMASFSFdvF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 QGDI-RLLM---------DDLKVLQPTVFpvvpRLLNRMFDRIFgQANTTLKRWLLDFASKRKE--AELRSGIIRNNSLW 412
Cdd:cd17650 150 AGDFaRSLLnggtlvicpDEVKLDPAALY----DLILKSRITLM-ESTPALIRPVMAYVYRNGLdlSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 413 DRLiFHKVQSSLGGRVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcclTMPgdwtaghVGAPMPCNLIKLV 492
Cdd:cd17650 225 AQD-FKTLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 493 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd17650 285 D-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGF 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1832481836 567 YIAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETlcSWAQKRGF 617
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAELRAF 414
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
184-658 |
1.33e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 86.68 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 184 EAITYIVNKAELSLVFVD---KPekaklLLEGVENKLiPGLKIIVVM-DAygselvergQRCGVEVTSMKAMEDL-GRAN 258
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMtDA---------AHLPAGSTPLLCYETLvGAQD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 259 RRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCH 337
Cdd:PRK07008 166 GDYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 338 GAKIgffqgdirllmddlkvlqptVFPvvprllnrmfdrifGQAnttlkrwlLDFASKRK--EAELRSGIIRNNSLWDRL 415
Cdd:PRK07008 244 GAKL--------------------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPTVWLGL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 416 IFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLT-----MPGD------WTAGHV 480
Cdd:PRK07008 282 LNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkllEKQGRV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 481 --GAPMpcnliKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK07008 362 iyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 557 KHIFKlAQGEYIAPEKIENIYMRSEPVAqvfvhgeslQAFLIAIVVP--DVETLCSWAQKRGFEGSFEELCRNKDVKKA- 633
Cdd:PRK07008 432 KDVIK-SGGEWISSIDIENVAVAHPAVA---------EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAFYEGKVAk 501
|
490 500 510
....*....|....*....|....*....|....*
gi 1832481836 634 --ILEDMVRL--------GKDSGLKPFEQVKGITL 658
Cdd:PRK07008 502 wwIPDDVVFVdaiphtatGKLQKLKLREQFRDYVL 536
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
121-607 |
1.54e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 86.27 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKTAPDQFiGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK07867 29 TSWREHIRGSAARAAALRARLDPTRPPHV-GVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPEKAklLLEGVEnkliPGLKIIVVMDAYGSELVergqrcgvevtsmkameDLGRANRRKPKPPAPEDLAVICFTSGTT 280
Cdd:PRK07867 108 ESAHAE--LLDGLD----PGVRVINVDSPAWADEL-----------------AAHRDAEPPFRVADPDDLFMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVSdcsAFVKATEKaLPLSASDTHISYLPLAHIYEQLLK-CVMLCHGAKI---------GFfqgdirl 350
Cdd:PRK07867 165 GDPKAVRCTHRKVAS---AGVMLAQR-FGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 351 lMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrWLLDFASKRKEAElrsgiirnNSLwdRLIFhkvqsslggrvrl 430
Cdd:PRK07867 234 -LPDVRRYGATYANYVGKPLS----------------YVLATPERPDDAD--------NPL--RIVY------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 431 mvtGAAPVSATVLTFlRAALGCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAPMPCnlIKLVDVE--------------E 496
Cdd:PRK07867 274 ---GNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 497 MNYMAAEGEgEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:PRK07867 346 LNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERI 422
|
490 500 510
....*....|....*....|....*....|.
gi 1832481836 577 YMRSEPVAQVFVHGeslqafliaivVPDVET 607
Cdd:PRK07867 423 LLRYPDATEVAVYA-----------VPDPVV 442
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-607 |
1.80e-17 |
|
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: 85.44 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASD-----THISY--------LPLAHiyeqllkcv 333
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDvwtlfHSYAFdfsvweiwGALLH--------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 334 mlchGAKIGFFQGDIRLLMDDLkvlqptvfpvvPRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwd 413
Cdd:cd17643 159 ----GGRLVVVPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR----------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 414 rliFHKVQSSLggrvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL-----TMPGDWTAGHVGAPMP 485
Cdd:cd17643 205 ---DGRDPLAL----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaADLPAAAASPIGRPLP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 486 CNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:cd17643 278 GLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 559 IFKLaQGEYIAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVET 607
Cdd:cd17643 357 QVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
269-599 |
2.35e-17 |
|
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: 85.46 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRnivsDCSAFVKATEKALPLSASDTHISYLPLAHIYeqLLKC-----VMLChGAKIGF 343
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHN----DYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 FQ----GDIRLLMDDLKVlqpTVFPVVPRLLnrmfdrifgqanttlKRWLlDFASKRKEAElrsgiirnnslwdrlifhk 419
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 420 vqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTM---PGDWTAGHVGAPM-PCNLIKLVDv 494
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE---GlLNYTRlddPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 495 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 574
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 1832481836 575 NIYMRSEPVAQVFV-------HGESLQAFLIA 599
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
150-638 |
5.54e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.69 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 150 IGIFAQNRPEwviIEQGCFAYSM---VIVPLYDTLGNEAITYIVNKAELSLVFVDKP-----EKAKLLLEGVENKLIPGL 221
Cdd:PLN03102 67 VSVLAPNTPA---MYEMHFAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 222 KIIVVMD----AYGSE-----LVERGQRCGVEVTSMKAMEDlgranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRN 292
Cdd:PLN03102 144 IFIHEIDfpkrPSSEEldyecLIQRGEPTPSLVARMFRIQD-------------EHDPISLNYTSGTTADPKGVVISHRG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 293 I-VSDCSAFVKATEKALPLsasdtHISYLPLAHiyeqllkcvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTVFPVVpr 368
Cdd:PLN03102 211 AyLSTLSAIIGWEMGTCPV-----YLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 369 llnRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiiRNNSLwdrlifhkVQSSLGGRVRLMVTGAAPVSATVLTFLRa 448
Cdd:PLN03102 271 ---EMHNVTHMCCVPTVFNILL----------------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 449 aLGCQFYEGYGQTECTAGCCLTMPGD-WT------AGHVGAPMPCNLIKLVDVEEMNYMAAEGE-------GEVCVKGPN 514
Cdd:PLN03102 323 -LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADVDVKNKETQESVprdgktmGEIVIKGSS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 515 VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIymrsepvaqVFVHGESLQ 594
Cdd:PLN03102 402 IMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLE 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1832481836 595 AFLIAIVVPDV-ETLCSW-AQKRGFEGSFEE----LCRNKDVKKAILEDM 638
Cdd:PLN03102 471 TAVVAMPHPTWgETPCAFvVLEKGETTKEDRvdklVTRERDLIEYCRENL 520
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-603 |
2.57e-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: 82.03 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATEKALPLSASDTHISYLPL----AHiyEQLLkcVMLCHGAki 341
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPL----AAHCQATAERYGLTPGDRELQFASFnfdgAH--EQLL--PPLICGA-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 gffqgdiRLLMDDLKVLQPtvfpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlif 417
Cdd:cd17649 162 -------CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADR----------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 418 hkVQSSLGGRVRLMVTGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLTMPGDWTAGH---VGAPMPCNLIK 490
Cdd:cd17649 206 --TGDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 491 LVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:cd17649 281 ILD-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI- 358
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832481836 564 QGEYIAPEKIENIYMRSEPVAQVFVHGES--LQAFLIAIVVP 603
Cdd:cd17649 359 RGFRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVL 400
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-615 |
9.64e-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: 79.99 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATEKALPLSASDTHISYLPL---AHIYEQllkCVMLCHGAkigf 343
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGL----ANLAAAQIAAFDVGPGSRVLQFASPsfdASVWEL---LMALLAGA---- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 fqgdiRLLMDDLKVLQPtvfpvvprllnrmfdrifGQAnttlkrwLLDFaskrkeaelrsgiirnnsLWDRLIFHKVQS- 422
Cdd:cd17652 161 -----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPp 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 ---------SLGGRVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAgcCLTMPGDWTAGHV---GAPMPCNLIK 490
Cdd:cd17652 193 aalaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTV--CATMAGPLPGGGVppiGRPVPGTRVY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 491 LVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:cd17652 268 VLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI- 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832481836 564 QGEYIAPEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVV------PDVETLCSWAQKR 615
Cdd:cd17652 346 RGFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHLAER 406
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
264-606 |
2.34e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 79.15 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD----CSAFvkatekalPLSASDTHISYLPLAHIYEQ------LLKcv 333
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASaegvLSLM--------PFTAQDSWLLSLPLFHVSGQgivwrwLYA-- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 334 mlchGAKIGFfqGDIRLLMDDLkvLQPTVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwd 413
Cdd:PRK09029 201 ----GATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL----------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 414 rlifhkvqsslGGrvrlmvtGAAPVSatvLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTAGhVGAPMPCNLIKLVD 493
Cdd:PRK09029 248 -----------GG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEMASTVC-AKRADGLAG-VGSPLPGREVKLVD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 494 veemnymaaegeGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKI 573
Cdd:PRK09029 305 ------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEI 369
|
330 340 350
....*....|....*....|....*....|...
gi 1832481836 574 ENIYMRSEPVAQVFVhgeslqafliaIVVPDVE 606
Cdd:PRK09029 370 ERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-614 |
7.28e-15 |
|
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: 77.59 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkatEKALPLSASDTHISYLPL---AHIYEQLlkcVMLCHGAKIGF 343
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH----RPYFGVTPADKSLVYASFsfdASAWEIF---PHLTAGAALHV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 FQGDIRLLMDDLkvlqptvfpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdrlifhkvqss 423
Cdd:cd17645 176 VPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL------------ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 424 lggrvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAE 503
Cdd:cd17645 218 -----RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 504 G-EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:cd17645 286 GvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPF 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1832481836 577 YMRSEPVAQVFV-------HGESLQAFLIAIVVPDVETLCSWAQK 614
Cdd:cd17645 365 LMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
252-604 |
1.26e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 77.00 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 252 EDLGRANRRKPKPPAPEDLAVIC---FTSGTTGNPKGAMVTHRNIvsdcsAFVKATEKA--LP-LSASDTHISYLPLAH- 324
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFVITNHLAdlMPgTTEQDASLVVAPLSHg 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 325 --IYeQLLKcvmLCHGAKigffqgDIRLLMDDLKVlqPTVFPVVPRL-LNRMFdrifgQANTTLKRWLLDFASKRKEael 401
Cdd:PRK07470 219 agIH-QLCQ---VARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD--- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 402 rsgiirnnslwdrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGC------CLTMPGDW 475
Cdd:PRK07470 279 -------------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNitvlppALHDAEDG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 476 TAGHVGapmPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGT 549
Cdd:PRK07470 335 PDARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGF 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1832481836 550 LKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPD 604
Cdd:PRK07470 410 LYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD 452
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
234-587 |
1.50e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.86 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 234 LVERGQRCGvevTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPL 310
Cdd:PRK09274 140 LVTVGGRLL---WGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 311 SASDTHISYLPLahiyeqllkcvMLCHGAKIGFfqGDIRLLMDDLKVLQptvfpVVPRllnRMFDRIFGQANTTLkrwll 390
Cdd:PRK09274 213 EPGEIDLPTFPL-----------FALFGPALGM--TSVIPDMDPTRPAT-----VDPA---KLFAAIERYGVTNL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 391 dFASKrkeaelrsgiirnnSLWDRLIFHKVQS--SLGGrVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC--- 463
Cdd:PRK09274 267 -FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpi 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 464 ---TAGCCLTMPGDWT---AGH-VGAPMPCNLIKLVDVEEM-------NYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAE 528
Cdd:PRK09274 331 ssiESREILFATRAATdngAGIcVGRPVDGVEVRIIAISDApipewddALRLATGEiGEIVVAGPMVTRSYYNRPEATRL 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832481836 529 A--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniymrSEPVAQVF 587
Cdd:PRK09274 411 AkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIF 462
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
2.28e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 74.65 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 457 GYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGW 535
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832481836 536 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyMRSEP-VAQVFVhgeslqafliaIVVPDVetlcSWAQ 613
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPDP----RWAQ 280
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-617 |
2.37e-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: 75.93 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATEKALPLSASDTHISYLPLAH--IYEQLLkcVMLCHGAKIgff 344
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVN----LSHGLIKEYGITSSDRVLQFASIAFdvAAEEIY--VTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 qgdirllmddlkVLQPtvfpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDRLIFHKVQSSL 424
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 GG--RVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLTMPGDWTAGH-----VGAPMPCNLIKLVDvE 495
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832481836 568 IAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETLCSWAQKRGF 617
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
184-590 |
3.76e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.56 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 184 EAITYIVNKAELSLVFVDK---PekaklLLEGVENKLiPGLKIIVVMdaygselverGQRCGVEVTSMK---AMED-LGR 256
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVVL----------TDAAHMPQTTLKnavAYEEwIAE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 257 ANRRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATEKALPLSASDTHISYLPLAHIYEQLL----- 330
Cdd:PRK06018 165 ADGDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHRSNV--LHALMANNGDALGTSAADTMLPVVPLFHANSWGIafsap 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 331 ----KCVMlcHGAKIGffQGDIRLLMDDLKVlqpTVFPVVPrllnrmfdrifgqantTLKRWLLDF--ASKRKEAELRSG 404
Cdd:PRK06018 243 smgtKLVM--PGAKLD--GASVYELLDTEKV---TFTAGVP----------------TVWLMLLQYmeKEGLKLPHLKMV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 405 IIrnnslwdrlifhkvqsslGGrvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECT---AGCCLTMPGDWTAGH 479
Cdd:PRK06018 300 VC------------------GG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSplgTLAALKPPFSKLPGD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 480 V--------GAPMPCNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDKDGWLHTGDIGKWLPNGT 549
Cdd:PRK06018 350 ArldvlqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1832481836 550 LKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK06018 426 MRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
268-598 |
5.82e-14 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 75.19 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 268 EDLAVICFTSGTTGNPKgaMVTHrnivSDCSAFVKA----------TEKALPLSASDTHISYLPLAHIYEQLLK--CVML 335
Cdd:cd05928 174 QEPMAIYFTSGTTGSPK--MAEH----SHSSLGLGLkvngrywldlTASDIMWNTSDTGWIKSAWSSLFEPWIQgaCVFV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 336 CHGAKIgffqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLL--DFASkrkeaelrsgiirnnslwd 413
Cdd:cd05928 248 HHLPRF-----DPLVILKTLSSYPITTFCGAP----------------TVYRMLVqqDLSS------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 414 rlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG-DWTAGHVGAPMPCNLIKLV 492
Cdd:cd05928 288 ----YKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGmKIKPGSMGKASPPYDVQII 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 493 DvEEMNYMAAEGEGEVCVK-GPN----VFQGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 567
Cdd:cd05928 358 D-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYR 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 1832481836 568 IAPEKIENIYMRSEPVAQVFV-------HGESLQAFLI 598
Cdd:cd05928 435 IGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-590 |
7.60e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.54 E-value: 7.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL-YDTLGNEaITYIVNKAELSLVF 199
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLG--PGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 200 VDK---PEKAKLLLEgvenklIPGLKIIVVMDAYGSELVERGqrcGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICfT 276
Cdd:PRK07798 106 YERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-T 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 277 SGTTGNPKGAMVTHRNI--VS------DCSAFVKATEKALPLSASDTHISYLPLAHiyeqllkcvmLCHGAK-----IGF 343
Cdd:PRK07798 172 GGTTGMPKGVMWRQEDIfrVLlggrdfATGEPIEDEEELAKRAAAGPGMRRFPAPP----------LMHGAGqwaafAAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 FQGdirllmddlkvlQPTVFPVVPRL-------------LNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnns 410
Cdd:PRK07798 242 FSG------------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL--------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 411 lwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAP--MPCN 487
Cdd:PRK07798 296 -----------SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 488 LIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 564
Cdd:PRK07798 359 RTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG- 437
|
490 500
....*....|....*....|....*..
gi 1832481836 565 GEYIAPEKIENIyMRSEP-VAQVFVHG 590
Cdd:PRK07798 438 GEKVFPEEVEEA-LKAHPdVADALVVG 463
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-604 |
1.01e-13 |
|
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: 73.89 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVS--DCSAFVKATEKALPLSASdTHISYlPLAhIYEQLlkcVMLCHGAKIgffqgdirllmddlkVL 358
Cdd:cd12115 118 GRPKGVAIEHRNAAAflQWAAAAFSAEELAGVLAS-TSICF-DLS-VFELF---GPLATGGKV---------------VL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 359 QPTVFPvvprllnrmfdrifgqanttlkrwLLDFASkRKEAELrsgIIRNNSLWDRLIFHkvqSSLGGRVRLMVTGAAPV 438
Cdd:cd12115 177 ADNVLA------------------------LPDLPA-AAEVTL---INTVPSAAAELLRH---DALPASVRVVNLAGEPL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 439 SATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNV 515
Cdd:cd12115 226 PRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 516 FQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQ--VF 587
Cdd:cd12115 305 ARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVREavVV 383
|
490
....*....|....*...
gi 1832481836 588 VHGESL-QAFLIAIVVPD 604
Cdd:cd12115 384 AIGDAAgERRLVAYIVAE 401
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
261-586 |
4.68e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 72.35 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 261 KPKPPAPEDLAVIcFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEKALPLSASDTHISYLPLAHI--YEQLLKCVMlcHG 338
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIggLWWILTCLM--HG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 339 AKI---GFFQGDIRLLMDDLKVLQPTVfpvVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRSGIIRNNSLwdrl 415
Cdd:PRK05857 240 GLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 416 ifhkvqsslggrvRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 490
Cdd:PRK05857 289 -------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 491 LVDVEEMNYMAAEGE-----GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 565
Cdd:PRK05857 355 LAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGG 432
|
330 340
....*....|....*....|.
gi 1832481836 566 EYIAPEKIENIymrSEPVAQV 586
Cdd:PRK05857 433 VNIAPDEVDRI---AEGVSGV 450
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
101-608 |
1.23e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 70.83 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 101 QVSNNGPCLGSRkpDQPYEWlsyKQVAELSECIGSALIQKGFKTAPDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT 180
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTW---REVLAEAAARAAALIALADPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLNTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 181 LGNEAITYIVNKAELSLVFVDKPEKAklLLEGVEnklIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrr 260
Cdd:PRK13388 86 RRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTPAYAELVAAAGAL------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 261 KP-KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfvkATEKaLPLSASDTHISYLPLAH---IYEqlLKCVMLC 336
Cdd:PRK13388 142 TPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRA---LTER-FGLTRDDVCYVSMPLFHsnaVMA--GWAPAVA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 337 HGAKI---------GFfqgdirllMDDLKVLQPTVFPVVPRLL-------NRMFDrifgqANTTLKRWLLDFASKRKEAE 400
Cdd:PRK13388 216 SGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRDIAE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 401 lrsgiirnnslwdrlifhkvqsslggrvrlmvtgaapvsatvltFLRAaLGCQFYEGYGQTEctAGCCLTMPGDWTAGHV 480
Cdd:PRK13388 283 --------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGSI 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 481 GAPMPCnlIKLVDVEEM---------------NymAAEGEGE-VCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKW 544
Cdd:PRK13388 316 GRGAPG--VAIYNPETLtecavarfdahgallN--ADEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYR 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832481836 545 LPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG----ESLQAFLIAIVVPDVETL 608
Cdd:PRK13388 391 DADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATF 457
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
264-608 |
1.42e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.53 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAkigf 343
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGA---- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 fqgdiRLLMDDLKVLQPtvfpvvprllNRMFDRIFGQANTTLkrwllDFASkrkeaelrsgiirnnSLWDRLIFHKVQSS 423
Cdd:PRK12316 4762 -----SVVIRDDSLWDP----------ERLYAEIHEHRVTVL-----VFPP---------------VYLQQLAEHAERDG 4806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 424 LGGRVRLMVTG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLTMPGDWTAG----HVGAPMPCNLIKLVDVEe 496
Cdd:PRK12316 4807 EPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDGQ- 4884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:PRK12316 4885 LNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIE 4963
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481836 570 PEKIEnIYMRSEP-------VAQVFVHGeslqAFLIAIVVPDVETL 608
Cdd:PRK12316 4964 LGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPQDPAL 5004
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
1.60e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 70.62 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATEkalplsaSDTHISYLPLAHIYeqllkcvmlchgakiGF 343
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANqraCLKFFSPKE-------DDVMMSFLPPFHAY---------------GF 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 FQGDIRLLMDDLkvlqPTVF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDR 414
Cdd:PRK06334 240 NSCTLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 415 LiFHKVQSslggrvrlmvtgaapvsatvlTFLRAALgcqfYEGYGQTECTAgcCLTMPGDWTAGH---VGAPMPCNLIKL 491
Cdd:PRK06334 315 L-YQEALK---------------------TFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVLI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 492 VDvEEMNYMAAEGE-GEVCVKGPNVFQGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 569
Cdd:PRK06334 367 VS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVS 444
|
....*....
gi 1832481836 570 PEKIENIYM 578
Cdd:PRK06334 445 LEALESILM 453
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
410-588 |
1.60e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 69.90 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 410 SLWdRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLI 489
Cdd:cd05974 185 TVW-RMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 490 KLVDVEEmnymAAEGEGEVCV-----KGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 564
Cdd:cd05974 264 ALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SS 337
|
170 180
....*....|....*....|....
gi 1832481836 565 GEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAV 361
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-598 |
2.54e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 69.47 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNrPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05973 1 LTFGELRALSARFANALQELGVG-PGDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 DKPEKAKLllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 280
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 281 GNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDthiSYLPLAH------IYEQLLKCVMLCHGAKI---GFFQGDIRLL 351
Cdd:cd05973 101 GLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAADpgwaygLYYAITGPLALGHPTILlegGFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 352 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkeaeLRSGIirnnslwdrlifhKVQSSLGGRVRLM 431
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLL------------------------------MAAGA-------------EVPARPKGRLRRV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 432 VTGAAPVSATVLTFLRAALGCQFYEGYGQTEctagccLTMP--GDWTAGHV------GAPMP---CNLIKLVDVEemnym 500
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAALGVPIHDHYGQTE------LGMVlaNHHALEHPvhagsaGRAMPgwrVAVLDDDGDE----- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 501 AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:cd05973 280 LGPGEpGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
490 500 510
....*....|....*....|....*....|
gi 1832481836 576 IYMRSEPVAQVFV-------HGESLQAFLI 598
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
265-639 |
3.61e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.19 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLA---HIYEQLLKcvmLCHGAKI 341
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFAfdvSVWELFWP---LINGARL 1787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 GFFQGDIRL----LMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFAskrkEAELRSGIIRnnslwdRLIF 417
Cdd:PRK12467 1788 VIAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ----------------LLQMD----EQVEHPLSLR------RVVC 1841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 418 hkvqsslGGRvrlmvtgAAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLTMPGDWTAGHVGAPMPcNLIKL 491
Cdd:PRK12467 1842 -------GGE-------ALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIA-NLSTY 1904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 492 VDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 564
Cdd:PRK12467 1905 ILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-R 1983
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832481836 565 GEYIAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPDVETLCSWAQKRGfeGSFEELcrnKDVKKAILED-MV 639
Cdd:PRK12467 1984 GFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV--ALRAIL---KNHLKASLPEyMV 2056
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
118-597 |
4.53e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 69.10 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 118 YEWL-SYKQVAELSecigSALIQKGFktAPDQFIGIFAQNRPEwviIEQGCFAYSM---VIVPLYDTLGNEAITYIVNKA 193
Cdd:PLN02479 46 YTWAqTYQRCRRLA----SALAKRSI--GPGSTVAVIAPNIPA---MYEAHFGVPMagaVVNCVNIRLNAPTIAFLLEHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 194 ELSLVFVDKP------EKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQRCG-VEVTSMKAMEDLGRAnrrkPKPPA 266
Cdd:PLN02479 117 KSEVVMVDQEfftlaeEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKGaIEYEKFLETGDPEFA----WKPPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PE-DLAVICFTSGTTGNPKGAMVTHRnivsdcSAFVKATEKALPLSASD--THISYLPLAHiyeqllkCVMLCH------ 337
Cdd:PLN02479 193 DEwQSIALGYTSGTTASPKGVVLHHR------GAYLMALSNALIWGMNEgaVYLWTLPMFH-------CNGWCFtwtlaa 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 338 --GAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSLWDRL 415
Cdd:PLN02479 260 lcGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLN---------------------------------TIVNAPKSETI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 416 IfhkvqsSLGGRVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDW------TAGHVGAPMPC 486
Cdd:PLN02479 307 L------PLPRVVHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstVCAWKP-EWdslppeEQARLNARQGV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 487 NLIKL-----VDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PLN02479 377 RYIGLegldvVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1832481836 560 FkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFL 597
Cdd:PLN02479 456 I-ISGGENISSLEVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
266-603 |
5.97e-12 |
|
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: 68.27 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateKALPLSASDTHISYLPLAHIYEQ-LLKCVMLCHGAKIGFF 344
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 QGDI-RLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfASKRKEAELRSGiirnnslwdrlifhkvqss 423
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 424 lggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 503
Cdd:cd05958 215 ----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 504 GEGEVCVKGPNvfqGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 583
Cdd:cd05958 290 TIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340
....*....|....*....|...
gi 1832481836 584 AQVFVHGESLQAFLI---AIVVP 603
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVL 388
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
435-603 |
2.00e-11 |
|
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: 66.63 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 435 AAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTmPGDWTA--GHVGAPMPCNLiKLVDvEEMNYMAAEGEGEVCVKG 512
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGKV-HILD-EDGNEVPPGEIGEVYFAN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 513 PNVFQgYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG-- 590
Cdd:cd05929 330 GPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvp 407
|
170
....*....|....
gi 1832481836 591 -ESLQAFLIAIVVP 603
Cdd:cd05929 408 dEELGQRVHAVVQP 421
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-587 |
6.69e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 65.17 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIYEQLLkcvmlchgakigff 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFA----AQIDALRQLYGIRPGEVDLATFPLFALFGPAL-------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 qgdirllmdDLKVLQPTVFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDRLIFHKVQSSL 424
Cdd:cd05910 144 ---------GLTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 G-GRVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LTMPGDWTAGH----VGAPMPCNLIKL 491
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 492 VDVEEMNYMAAEGE--------GEVCVKGPNVFQGYLKDPAKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*...
gi 1832481836 560 FKLAQGEYIapekieniymrSEPVAQVF 587
Cdd:cd05910 357 VITTGGTLY-----------TEPVERVF 373
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-604 |
6.90e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.40 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 429 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGDwTAGHV----GAPM-PCNLIKLVDvEEMNYMAa 502
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GlVNYTRLDD-SDERIfttqGRPMsPDDEVWVAD-ADGNPLP- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 503 EGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIY 577
Cdd:PRK10946 377 QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLL 451
|
170 180
....*....|....*....|....*..
gi 1832481836 578 MRsepvaqvfvHGESLQAFLIAIvvPD 604
Cdd:PRK10946 452 LR---------HPAVIHAALVSM--ED 467
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-606 |
1.12e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.36 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 187 TYIVNKAELsLVFVDKPEKAKLLLEGVENKLipglkiivvmdaygselVERGQrcgvevtsmkamEDLGRANrrKPKPPA 266
Cdd:PRK12316 3147 AYMLEDSGA-QLLLSQSHLRLPLAQGVQVLD-----------------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHrnivSDCSAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIgffqg 346
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRH----SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV----- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 347 dirllmddlkVLQPTVFPVVPRLLNRMFDRifGQANTTLKRWlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGG 426
Cdd:PRK12316 3266 ----------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS 3312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 427 RVRLMVTGAAPVSATVltfLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGH--VGAPMPCNLIKLVDVeEMNYMAAEG 504
Cdd:PRK12316 3313 LKRIVCGGEALPADLQ---QQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 505 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYM 578
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*...
gi 1832481836 579 RSEPVAQVFVHGESLQAfLIAIVVPDVE 606
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-590 |
1.19e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 64.33 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 112 RKPDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNE 184
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLK--RGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 185 AITYIVNKAELSLVF--VDKPEKAKLLLegvenKLIPGLKIIVVMDAYGSelvergqrcgvevtsMKAMEDLGRANRRKP 262
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 263 KPPAPEDL--AVICFTSGTTGNPKGamvthrnivsdcsafVKAtekALPLSASDTHisyLPLAHIYEQLLK----CVMLC 336
Cdd:PRK13391 147 ATPIADESlgTDMLYSSGTTGRPKG---------------IKR---PLPEQPPDTP---LPLTAFLQRLWGfrsdMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 337 -----HGAKIGFFQGDIRL-----LMDD------LKVLQP---TVFPVVPRllnrMFDRIFGQANTTLKRWLLdfaskrk 397
Cdd:PRK13391 206 paplyHSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPT----MFSRMLKLPEEVRDKYDL------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 398 eaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA 477
Cdd:PRK13391 275 ------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 478 --GHVGAPMpCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDG-WLHTGDIGKWLPNGTLKIID 554
Cdd:PRK13391 326 hpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTD 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 1832481836 555 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK13391 403 RAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
229-586 |
2.13e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.63 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 229 AYGSELvergQRCGVEVTSMkAMEDL---GRANRRKPKPPAP-EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAT 304
Cdd:PRK05851 114 SHGSHL----ERLRAVDSSV-TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 305 EKALPlsaSDTHISYLPLAHIyeqlLKCVMLCHGAKIGFfqgdirllmdDLKVLQPTVFPVVP-RLLNrmfdrifgqant 383
Cdd:PRK05851 189 GLDAA---TDVGCSWLPLYHD----MGLAFLLTAALAGA----------PLWLAPTTAFSASPfRWLS------------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 384 tlkrWLLDF-ASKRKEAELRSGIIRNNSlwdrlifHKVQSSLGGRVRLMVTGAAPVSATVLT-FLRAALGCQFYEG---- 457
Cdd:PRK05851 240 ----WLSDSrATLTAAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaap 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 458 -YGQTECTagCCLTMP---------------GDWTAGH--VGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGY 519
Cdd:PRK05851 309 sYGLAEST--CAVTVPvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832481836 520 LKDPAktaeaLDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIymrsepVAQV 586
Cdd:PRK05851 387 LGQAP-----IDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
422-606 |
2.40e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.38 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 422 SSLggrvRLMVTGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNlIKLVDvEE 496
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
170 180 190
....*....|....*....|....*....|.
gi 1832481836 576 IYMRSEPVAQVFVHGeslqafliaivVPDVE 606
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-608 |
2.73e-10 |
|
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: 63.19 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkatEKALPLSASDTHI-----SYLpLAHIYEQLLKCVMlcHGAKI 341
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL----SERYFGRDNGDEAvlffsNYV-FDFFVEQMTLALL--NGQKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 342 GFFQGDIRL-------LMDDLKVlqpTVFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnns 410
Cdd:cd17648 166 VVPPDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV-------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 411 lwdrliFHKVQSSLGGRVrlmVTGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIk 490
Cdd:cd17648 224 ------FEKLRSRFAGLI---INAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 491 lvdveemnymaaegeGEVCVKGPNVFQGYLKDPAKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRK 556
Cdd:cd17648 288 ---------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRN 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 557 KHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV--------HGESLQAFLIAIVVPDVETL 608
Cdd:cd17648 353 DFQVKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
267-614 |
4.92e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.26 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGFFQG 346
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYE----LDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDN 3311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 347 DIRllmDDLKVLQptvfpvvprLLNRmfDRIfgqanTTlkrwlLDFASkrkeaelrsgiirnNSLWDRLIFHKVQSslGG 426
Cdd:PRK12467 3312 DLW---DPEELWQ---------AIHA--HRI-----SI-----ACFPP--------------AYLQQFAEDAGGAD--CA 3351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 427 RVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKL---VDVEEMNYMA 501
Cdd:PRK12467 3352 SLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNPVP 3431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 574
Cdd:PRK12467 3432 VGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIE 3510
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832481836 575 NIYMRSEPVAQVFVHGESLQA--FLIAIVVPDVETlCSWAQK 614
Cdd:PRK12467 3511 ARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWRET 3551
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
184-604 |
5.26e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 62.41 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 184 EAITYIVN--KAELSLVFVDkpekaklLLEGVENKLIPGLKIIVV------MDAYGSELVERGQRCGvevtsMKAMEDLG 255
Cdd:PRK12406 73 EEIAYILEdsGARVLIAHAD-------LLHGLASALPAGVTVLSVptppeiAAAYRISPALLTPPAG-----AIDWEGWL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 256 RANRRKPKPPAPEDLAVIcFTSGTTGNPKGamvthrnivsdcsafVKATEKALPLSASDTHIsylpLAHIYEQLLKCVML 335
Cdd:PRK12406 141 AQQEPYDGPPVPQPQSMI-YTSGTTGHPKG---------------VRRAAPTPEQAAAAEQM----RALIYGLKPGIRAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 336 C-----HGAKIGFFQGDIRLlmDDLKVLQP-----------------TVFpVVPRllnrMFDRifgqanttlkrwLLDFA 393
Cdd:PRK12406 201 LtgplyHSAPNAYGLRAGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 394 SKRKEAelrsgiirnnslWDrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG 473
Cdd:PRK12406 262 EEVRAK------------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 474 DWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNV--FQgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGT 549
Cdd:PRK12406 318 DALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832481836 550 LKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 604
Cdd:PRK12406 395 LFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-590 |
6.23e-10 |
|
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: 61.99 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 269 DLAVICFTSGTTGNPKGAMVTHRNIVSdCSAFVKATEKALPlsaSDTHISYLPLAHIYEQLLK-CVMLCHGAKIGF---F 344
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWR-GGAFFAGSGGALP---SDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 QGdiRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdrlifHKVQSSL 424
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 425 GGRVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGCCLTMPGDWTAGHVGA----PMPCNLIKlVDVEEMN- 498
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSGFINFFGKPGAIGRNPSllrkVAPLALVK-YDLESGEp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 499 ------YMAAEGEGEV--CV-----KGPnvFQGYLkDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd05940 272 irdaegRCIKVPRGEPglLIsrinpLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDT 348
|
330 340 350
....*....|....*....|....*....|.
gi 1832481836 560 FKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd05940 349 FRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
113-638 |
6.58e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 62.22 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 113 KPDQP-YEWL----SYKQVAELSECIGSALIQKGF-KTAPdqfIGIFAQNRPEWVI-----IEQGCfAYsmviVPLYDTL 181
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLpDKSP---IIVFGHMSPEMLAtflgaVKAGH-AY----IPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 182 GNEAITYIVNKAELSLVFvdkpEKAKLLLEGVENKLIpglkiivvmdayGSELVERGQRCGVEVTSMKAMEDlgranrrk 261
Cdd:PRK04813 87 PAERIEMIIEVAKPSLII----ATEELPLEILGIPVI------------TLDELKDIFATGNPYDFDHAVKG-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 262 pkppapEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFvkaTEKALPLSASDTHISYLPLA---------HIYEQLL-- 330
Cdd:PRK04813 143 ------DDNYYIIFTSGTTGKPKGVQISHDNLVS----F---TNWMLEDFALPEGPQFLNQApysfdlsvmDLYPTLAsg 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 331 -KCVMLCHgAKIGffqgDIRLLMDDLKVLQPTVFPVVPR-----LLNRMFDrifGQANTTLKRWLLDfaskrKEaELRsg 404
Cdd:PRK04813 210 gTLVALPK-DMTA----NFKQLFETLPQLPINVWVSTPSfadmcLLDPSFN---EEHLPNLTHFLFC-----GE-ELP-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 405 iirnnslwdrlifHKVQSSLGGRVrlmvtgaaPvSATVltflraalgcqfYEGYGQTECTAGC------------CLTMP 472
Cdd:PRK04813 274 -------------HKTAKKLLERF--------P-SATI------------YNTYGPTEATVAVtsieitdemldqYKRLP 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 473 gdwtaghVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDGW--LHTGDIGKwLPNGT 549
Cdd:PRK04813 320 -------IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGL 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 550 LKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDvetlcswaqkrgfEGSFEelc 625
Cdd:PRK04813 391 LFYQGRIDFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVPK-------------EEDFE--- 452
|
570
....*....|...
gi 1832481836 626 RNKDVKKAILEDM 638
Cdd:PRK04813 453 REFELTKAIKKEL 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-585 |
7.66e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNrPEWVIIEQGCFaYSMVI-VPLYDTLGN-----EAITYIVNKAE 194
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQARA--SFGDRAVLLFPSG-PDYVAAFFGCL-YAGVIaVPAYPPESArrhhqERLLSIIADAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 195 LSLVFVDkpekAKLL--LEGVENKLIPGLKIIVVMDAYGSELVERGQrcgvevtsmkamedlgranrrKPKPPaPEDLAV 272
Cdd:PRK05691 117 PRLLLTV----ADLRdsLLQMEELAAANAPELLCVDTLDPALAEAWQ---------------------EPALQ-PDDIAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 273 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATekALPLSASDTHISYLPLAHiyeqllkcvmlchgaKIGFFQGdirllm 352
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVANEQLIRHGF--GIDLNPDDVIVSWLPLYH---------------DMGLIGG------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 353 ddlkVLQPtVFPVVPRLLnrMFDRIFGQANTtlkRWLldfaskrkEA--ELRSGIIRNNSLWDRLIFHKV-QSSLGG--- 426
Cdd:PRK05691 228 ----LLQP-IFSGVPCVL--MSPAYFLERPL---RWL--------EAisEYGGTISGGPDFAYRLCSERVsESALERldl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 427 -RVRLMVTGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT---AGC-------CLTMPGDWTAGHV--------- 480
Cdd:PRK05691 290 sRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgipALELDAEALARNRaepgtgsvl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 481 ---GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-LDKDG--WLHTGDIGkWLPNGTLKIID 554
Cdd:PRK05691 370 mscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTG 448
|
490 500 510
....*....|....*....|....*....|.
gi 1832481836 555 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQ 585
Cdd:PRK05691 449 RLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-606 |
8.23e-10 |
|
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: 61.72 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSdcsafvkatekalplsasdthisylPLAHIYEQLLkcvmlchgakIGFFQGd 347
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVN-------------------------LLHFEREKTN----------INFSDK- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 348 irllmddlkVLQPTVFPvvprllnrmFDRIFGQANTTL----KRWLLDFASKRKEAELRSGIIRNN--------SLWdRL 415
Cdd:cd17656 172 ---------VLQFATCS---------FDVCYQEIFSTLlsggTLYIIREETKRDVEQLFDLVKRHNievvflpvAFL-KF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 416 IFHKVQ--SSLGGRVRLMVTGAAP--VSATVLTFLRAAlGCQFYEGYGQTEC-TAGCCLTMPGDWTAGH--VGAPMPCNL 488
Cdd:cd17656 233 IFSEREfiNRFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSEThVVTTYTINPEAEIPELppIGKPISNTW 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 489 IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:cd17656 312 IYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1832481836 563 aQGEYIAPEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVVPDVE 606
Cdd:cd17656 391 -RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
114-606 |
1.01e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 114 PDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPE-----WVIIEQGcfaysmvivpLYDTl 181
Cdd:PRK13390 11 PDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLR--TGDVVALLSDNSPEalvvlWAALRSG----------LYIT- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 182 gneAITYIVNKAELSLVFVDKPEK---AKLLLEGVENKLIPGLKIIVvmdAYGSELVERGQrcgVEVTsmkamedLGRAN 258
Cdd:PRK13390 78 ---AINHHLTAPEADYIVGDSGARvlvASAALDGLAAKVGADLPLRL---SFGGEIDGFGS---FEAA-------LAGAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 259 RRKPKPPAPedlAVICFTSGTTGNPKGAM--VTHRNIVSDCSAFVKATEKALPLSASDTHISYLPLAHIyEQLLKCVMLc 336
Cdd:PRK13390 142 PRLTEQPCG---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHA-APLRWCSMV- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 337 H---GAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskRKEAELRSGiirnnslwd 413
Cdd:PRK13390 217 HalgGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR--------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 414 rlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNLiKL 491
Cdd:PRK13390 267 ----YDVSS-----LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDL-HI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 492 VDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:PRK13390 336 CD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIY 413
|
490 500 510
....*....|....*....|....*....|....*..
gi 1832481836 570 PEKIENIYMRSEPVAQVFVHGeslqafliaivVPDVE 606
Cdd:PRK13390 414 PQETENALTMHPAVHDVAVIG-----------VPDPE 439
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-607 |
2.07e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 60.71 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRpEWVIIEQGCFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 199
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVR--AGDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 200 VDKpEKAKLLlEGVENKLIPGLKIIVVMDAygselvERGQRCGVEVtsmkaMEDLGRANRRKPKPPAPEDLAVICFTSGT 279
Cdd:PRK07788 152 YDD-EFTDLL-SALPPDLGRLRAWGGNPDD------DEPSGSTDET-----LDDLIAGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 280 TGNPKGAMVTHRNIVSDCSAFVkateKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAKIGF---FqgDIRLLMDDLK 356
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLL----SRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLrrrF--DPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 357 VLQPTVFPVVPRLLNRMFDrifgqanttlkrwLLDFASKRKEAelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAA 436
Cdd:PRK07788 293 KHKATALVVVPVMLSRILD-------------LGPEVLAKYDT----------------------SSL----KIIFVSGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 437 PVSATVLTFLRAALGCQFYEGYGQTECtAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPN 514
Cdd:PRK07788 334 ALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 515 VFQGYLKDPAKTAealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslq 594
Cdd:PRK07788 412 PFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIG---- 482
|
490
....*....|...
gi 1832481836 595 afliaivVPDVET 607
Cdd:PRK07788 483 -------VDDEEF 488
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
506-574 |
9.18e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.48 E-value: 9.18e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832481836 506 GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09192 412 GHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-615 |
1.06e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELS 196
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVallaILKAGGAY----VPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 197 LVFVDKPEKAKL-LLEGVENklipglkiiVVMDAYGSELveRGQRCGVEVTSMkamedlgranrrkpkppAPEDLAVICF 275
Cdd:PRK12316 611 LLLSQSHLGRKLpLAAGVQV---------LDLDRPAAWL--EGYSEENPGTEL-----------------NPENLAYVIY 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 276 TSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAHIYEQLLKCVMLCHGAkigffqgdiRLLmddl 355
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALS----NRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGA---------RLV---- 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 356 kvlqptvfpVVPRLLNRMFDRIFGQANTTLKRwLLDFASKRKEAELRSGiirnnslwdrlifhKVQSSLGgrVRLMVTGA 435
Cdd:PRK12316 726 ---------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE--------------DVASCTS--LRRIVCSG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 436 APVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCltmpgDWTAGH-------VGAPMPCNLIKLVDVeEMNYMAAEGEGE 507
Cdd:PRK12316 780 EALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVT-----HWTCVEeggdsvpIGRPIANLACYILDA-NLEPVPVGVLGE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 508 VCVKGPNVFQGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 581
Cdd:PRK12316 854 LYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHP 932
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1832481836 582 PVAQVFVHGESLQAfLIAIVVPD------VETLCSWAQKR 615
Cdd:PRK12316 933 WVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
273-604 |
1.32e-08 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 57.03 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 273 ICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATEKALPLSASDTHISYLPLAH---IYEQLLkcVMLCHGAKIGFFQGDIR 349
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHslfLYGAIS--ALYLGGTFIGQRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 350 LLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkEAELRSGIIRnnslwdrlifHKVQSSLGGrvr 429
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTML---------------------------QALARTLEPE----------SKIKSIFSS--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 430 lmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCnliklVDVEEMNymAAEGE-GEV 508
Cdd:cd17633 119 ----GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN--ADGGEiGKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 509 CVKGPNVFQGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:cd17633 188 FVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIV 261
|
330
....*....|....*....
gi 1832481836 589 HGESLQAF---LIAIVVPD 604
Cdd:cd17633 262 VGIPDARFgeiAVALYSGD 280
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
246-601 |
2.02e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 246 TSMKAMEDLGRANRRKP---KPPAPEDLAVICFTSGTTGNPKGAMvtHRNivSDCSAFVKAT-EKALPLSASDthisylp 321
Cdd:PRK06060 120 RVAEAAELMSEAARVAPggyEPMGGDALAYATYTSGTTGPPKAAI--HRH--ADPLTFVDAMcRKALRLTPED------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 322 lahiyeqllkcVMLChGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPrllnrmfdrIFGQANTTLkrwlldfaSKRKEAEL 401
Cdd:PRK06060 189 -----------TGLC-SARMYFAYGLGNSVWFPLATGGSAVINSAP---------VTPEAAAIL--------SARFGPSV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 402 RSGIirnNSLWDRLIFHKVQSSLGGrVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHV 480
Cdd:PRK06060 240 LYGV---PNFFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 481 GAPMPCNLIKLVdVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTaeaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIf 560
Cdd:PRK06060 316 GRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832481836 561 KLAQGEYIAPEKIENIYMRSEPVAQVFVHG-------ESLQAFLIAIV 601
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
2.63e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCsAFVKATEKalpLSASDTHISYLPLA---HIYEQLLKCVMLCHGAKIGff 344
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERL-QWMQATYA---LDDSDVLMQKAPISfdvSVWECFWPLITGCRLVLAG-- 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 345 QGDIRllmDDLKVLQ------PTVFPVVPRLLNRMFDRIFGQANTTLKRwlLDFASKRKEAELRsgiirnnslwDRLIFH 418
Cdd:PRK05691 1347 PGEHR---DPQRIAElvqqygVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR----------NRVLQR 1411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 419 KVQSSLGGRvrlmvtgaapvsatvltflraalgcqfyegYGQTE----CTAGCCLTMPGDWTAghVGAPMPCNLIKLVDv 494
Cdd:PRK05691 1412 LPQVQLHNR------------------------------YGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD- 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 495 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:PRK05691 1459 AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFR 1537
|
330 340 350
....*....|....*....|....*....|....
gi 1832481836 568 IAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIA 599
Cdd:PRK05691 1538 VEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
243-324 |
2.67e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 53.79 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 243 VEVTSMkameDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC----SAFVKATEKALPLSAsdTHIS 318
Cdd:PRK05850 139 IEVDLL----DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGVPPPDT--TVVS 212
|
....*.
gi 1832481836 319 YLPLAH 324
Cdd:PRK05850 213 WLPFYH 218
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
254-589 |
3.67e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 53.89 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIV---------------------SDCSAFVKATEKALPLSA 312
Cdd:PRK10252 584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwmqnhypltaddvvlqkTPCSFDVSVWEFFWPFIA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 313 SDTHISYLPLAHIYEQLLkcvmlchgakigffqgdiRLLMDDLKVlqpTVFPVVPRLL----NRMFDRIFGQANTTLKRW 388
Cdd:PRK10252 664 GAKLVMAEPEAHRDPLAM------------------QQFFAEYGV---TTTHFVPSMLaafvASLTPEGARQSCASLRQV 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 389 lldFASKRK-EAELRsgiirnnSLWDRLIfhkvqsslggrvrlmvtgAAPVsatvltflraalgcqfYEGYGQTECT--- 464
Cdd:PRK10252 723 ---FCSGEAlPADLC-------REWQQLT------------------GAPL----------------HNLYGPTEAAvdv 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 465 ----AGccltmpGDWTAGHVGAPMPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG 534
Cdd:PRK10252 759 swypAF------GEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADP 831
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832481836 535 WL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVH 589
Cdd:PRK10252 832 FApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
113-290 |
6.95e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.59 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 113 KPDQPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIgiFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNK 192
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 193 AElSLVFVDKPEkaklLLEGVENKLIPGLKIIVVMDAYGSELvergqrcGVEVTSMKAMEDlgrANRRKPKPP-APEDLA 271
Cdd:PRK04319 144 SE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDVEEG-------PGTLDFNALMEQ---ASDEFDIEWtDREDGA 208
|
170 180
....*....|....*....|....*
gi 1832481836 272 VICFTSGTTGNPKG------AMVTH 290
Cdd:PRK04319 209 ILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-290 |
1.10e-06 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 51.72 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKTApDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 201 -------DKP-------EKAKLLLEGVEnklipglKIIVVmdaygselvergQRCGVEVTSMKAmEDLGRANRRKPKPPA 266
Cdd:cd05968 170 adgftrrGREvnlkeeaDKACAQCPTVE-------KVVVV------------RHLGNDFTPAKG-RDLSYDEEKETAGDG 229
|
170 180
....*....|....*....|....*....
gi 1832481836 267 -----PEDLAVICFTSGTTGNPKGAMVTH 290
Cdd:cd05968 230 aerteSEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-590 |
1.43e-06 |
|
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: 50.84 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 265 PAPEDLAVICfTSGTTGNPKGAMVTHRNI------VSDCSAFVKATEK-ALPLSASDTHISYLPLAHiyeqllkcvmLCH 337
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIfrmlmgGADFGTGEFTPSEdAHKAAAAAAGTVMFPAPP----------LMH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 338 GAK-----IGFFQGDiRLLMDDLKVLQPTVFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNNSL 411
Cdd:cd05924 70 GTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPYDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 412 wdrlifhkvqSSLggrvRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMPcnLI 489
Cdd:cd05924 134 ----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP--DT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 490 KLVDvEEMNYM--AAEGEGEVCVKGpNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 564
Cdd:cd05924 198 VVLD-DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG- 274
|
330 340
....*....|....*....|....*..
gi 1832481836 565 GEYIAPEKIENIyMRSEP-VAQVFVHG 590
Cdd:cd05924 275 GEKVFPEEVEEA-LKSHPaVYDVLVVG 300
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
261-654 |
2.17e-06 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 50.89 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 261 KPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATE---KALPLsasdtHISYLPLAHiyeqllkCVMLC 336
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGtalSEKDV-----VLPVVPMFH-------VNAWC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 337 HGAKIGFFQGDIRLLMDdlkVLQPTVfpvvprllnrMFDRIFGQANTTL--KRWLLDFASKRKEAelrsgiirnnslwdr 414
Cdd:cd05915 213 LPYAATLVGAKQVLPGP---RLDPAS----------LVELFDGEGVTFTagVPTVWLALADYLES--------------- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 415 lifhkVQSSLGGRVRLMVTGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPgDWT------AGHVGAPMPC 486
Cdd:cd05915 265 -----TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEslseeeKLTLKAKTGL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 487 N-LIKLVDVEEMNYMAAEGEGE----VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 561
Cdd:cd05915 337 PiPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 562 LAqGEYIAPEKIENIYMRSEPVAQVFVHGEslqafliaivvPDV---ETLCSWAQKRGFEGSFEEL---CRNKDVKKAIL 635
Cdd:cd05915 417 SG-GEWISSVDLENALMGHPKVKEAAVVAI-----------PHPkwqERPLAVVVPRGEKPTPEELnehLLKAGFAKWQL 484
|
410
....*....|....*....
gi 1832481836 636 EDMVRLGKDSGLKPFEQVK 654
Cdd:cd05915 485 PDAYVFAEEIPRTSAGKFL 503
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
265-608 |
2.18e-06 |
|
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: 50.55 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 265 PAPEDLAVICFTSGTTGNPKGAMVTHR----NIVSDCSAFvKATEKALPLSAS----DTHISYLPLAhiyeqllkcvmLC 336
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLF-NITSEDILFLTSpltfDPSVVEIFLS-----------LS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 337 HGAKIgffqgdirllmddlkVLQPTVFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGIirnnslw 412
Cdd:cd17654 183 SGATL---------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 413 drlifhkvqSSLggRVrLMVTGAAPVSATVLTFLRAA-LGCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIK 490
Cdd:cd17654 238 ---------SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAyKVPEEDSPVQLGSPLLGTVIE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 491 LVDVEemnymAAEGEGEVCVKGPNVfQGYLKDPAKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAP 570
Cdd:cd17654 306 VRDQN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINL 373
|
330 340 350
....*....|....*....|....*....|....*...
gi 1832481836 571 EKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETL 608
Cdd:cd17654 374 DLIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSR 411
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
261-604 |
7.33e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 48.89 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 261 KPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsafvkatekalplSASDTH---------ISYLPLAHI--YEQL 329
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTA---------------SADATHdrlggpgqwLLALPAHHIagLQVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 330 LKCVMlchgakigffQGDIRLLMDDLKVLQPTVFpvvPRLLNRM-FDRIF-GQANTTLKRWLLDFASKRKEAELRSGIIr 407
Cdd:PRK07824 93 VRSVI----------AGSEPVELDVSAGFDPTAL---PRAVAELgGGRRYtSLVPMQLAKALDDPAATAALAELDAVLV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 408 nnslwdrlifhkvqsslggrvrlmvtGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLtmpgdwtagHVGAPMPC 486
Cdd:PRK07824 159 --------------------------GGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 487 NLIKLVDveemnymaaegeGEVCVKGPNVFQGY--LKDPAKTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAq 564
Cdd:PRK07824 201 VRVRVED------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG- 262
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1832481836 565 GEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 604
Cdd:PRK07824 263 GLTVLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGD 305
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-599 |
5.63e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 266 APEDLAVICFTSGTTGNPKGAMVTHR----NIVSDCSAFVKATEKALPLSASDT-HISYLplahiyeQLLKCVMLchGAK 340
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRgmlnNQLSKVPYLALSEADVIAQTASQSfDISVW-------QFLAAPLF--GAR 3937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 341 IGFFQGDI----RLLMDDLKVLQPTVFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnslwdr 414
Cdd:PRK05691 3938 VEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP----------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 415 lifhkvqsslggrvrlmvTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGH---VGAPMPCNLIK 490
Cdd:PRK05691 3991 ------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRLY 4052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 491 LVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIFKLa 563
Cdd:PRK05691 4053 LLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI- 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832481836 564 QGEYIAPEKIENIYMRSEPV------AQVFVHGESLQAFLIA 599
Cdd:PRK05691 4131 RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
7.47e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 46.02 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGcFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 199
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVG--KGDVVALLMENRPEYLAAWLG-LAKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 200 VDkPEKAKLLlEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsmkAMEDLGRANRRKPKPPAP-------EDLAV 272
Cdd:PRK08279 140 VG-EELVEAF-EEARADLARPPRLWVAGGDTLDDPE--------------GYEDLAAAAAGAPTTNPAsrsgvtaKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1832481836 273 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAH 324
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLR----LTPDDVLYCCLPLYH 251
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
505-590 |
8.51e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 505 EGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:PRK07638 333 IGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVD 410
|
....*.
gi 1832481836 585 QVFVHG 590
Cdd:PRK07638 411 EIVVIG 416
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-594 |
9.01e-05 |
|
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: 45.50 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkatEKALPLSASDTHISYLPLAHIYEQLL-KCVMLCHGAKIGF-- 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYHGTAAFLgACNCLMSGGTLALsr 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 344 -FQgdIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfaskrkeaelrSGIIrnnSLWDRLifHKVQS 422
Cdd:cd05937 162 kFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLL------------STPP---SPYDRD--HKVRV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 423 SLGGRVRLMVTGAapvsatvltfLRAALGC-QFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVE------ 495
Cdd:cd05937 207 AWGNGLRPDIWER----------FRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvlvkmd 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 496 ---EMNYM---------AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEALDK------DGWLHTGDIGKWLPNGTLKI 552
Cdd:cd05937 277 petDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRWYF 356
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832481836 553 IDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGESLQ 594
Cdd:cd05937 357 LDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
233-324 |
1.41e-04 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.97 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 233 ELVERGQRCGV--EVTSMKAMEDLGRANRRKPKPPAPEDL---------AVICFTSGTTGNPKGAMVTHRNIVSdCSAFv 301
Cdd:cd05938 98 ALRADGVSVWYlsHTSNTEGVISLLDKVDAASDEPVPASLrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGF- 175
|
90 100
....*....|....*....|....*.
gi 1832481836 302 katekaLPLS---ASDTHISYLPLAH 324
Cdd:cd05938 176 ------LSLCgvtADDVIYITLPLYH 195
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
261-324 |
7.25e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 42.79 E-value: 7.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832481836 261 KPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEkalpLSASDTHISYLPLAH 324
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE----GQEGDRGVSWLPFFH 232
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-562 |
8.12e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkateKALPLSASDTHIsylplaHIYEqllkcvmlchgakIGFFQG 346
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVI----ERFGMRADDCEL------HFYS-------------INFDAA 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 347 DIRLLmddlkvlqptvfpvVPRLLN-RMFDRIFGQanttlkrWlldfaskrkEAELRSGIIRNNSLwDRLIFHKVQSS-- 423
Cdd:PRK05691 2389 SERLL--------------VPLLCGaRVVLRAQGQ-------W---------GAEEICQLIREQQV-SILGFTPSYGSql 2437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 424 ---LGGR-----VRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTE-------CTAGccLTMPGDWTAGHVGAPMPCN 487
Cdd:PRK05691 2438 aqwLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGAR 2515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 488 LIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:PRK05691 2516 VAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQV 2594
|
..
gi 1832481836 561 KL 562
Cdd:PRK05691 2595 KI 2596
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
259-590 |
1.06e-03 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 42.18 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 259 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHrnivsdcsafvkateKALPLSASDThisylpLAHIYEQLLKCVMLChG 338
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT---------------GGYLVYAATT------MKYVFDYGPGDIYWC-T 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 339 AKIGFFQGDIRLLMDDLkVLQPTVF-----PV--VPRLLNRMFDR----IFGQANTTLkRWLLDFASKRKEAELRSGIir 407
Cdd:cd17634 281 ADVGWVTGHSYLLYGPL-ACGATTLlyegvPNwpTPARMWQVVDKhgvnILYTAPTAI-RALMAAGDDAIEGTDRSSL-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 408 nnslwdrlifhKVQSSLGGRVRlmvtgaaPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG--DWTAGHVGAPMP 485
Cdd:cd17634 357 -----------RILGSVGEPIN-------PEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVF 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481836 486 CNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVFQGYLKDPAKTAEALDK--DGWLHTGDIGKWLPNGTLKIIDRKKHIFK 561
Cdd:cd17634 419 GVQPAVVD-NEGHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVIN 497
|
330 340
....*....|....*....|....*....
gi 1832481836 562 LAqGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd17634 498 VA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| |
